Gene
KWMTBOMO00190 Validated by peptides from experiments
Pre Gene Modal
BGIBMGA000622
Annotation
kettin_protein_[Danaus_plexippus]
Full name
Titin
+ More
Muscle M-line assembly protein unc-89
Titin homolog
Palladin
Hemicentin-2
Basement membrane-specific heparan sulfate proteoglycan core protein
Myosin light chain kinase, smooth muscle
Obscurin
Hemicentin-1
Twitchin
Peroxidasin homolog
Striated muscle preferentially expressed protein kinase
Immunoglobulin superfamily member 10
Peroxidasin
Striated muscle-specific serine/threonine-protein kinase
Protein sax-3
Roundabout homolog 2
Obscurin-like protein 1
Down syndrome cell adhesion molecule homolog
Peroxidasin-like protein
Down syndrome cell adhesion molecule
Roundabout homolog 1
Netrin receptor DCC
Matrix-remodeling-associated protein 5
Roundabout homolog 3
Immunoglobulin superfamily DCC subclass member 3
Contactin-4
ADAMTS-like protein 1
Contactin-3
Protogenin
Muscle M-line assembly protein unc-89
Titin homolog
Palladin
Hemicentin-2
Basement membrane-specific heparan sulfate proteoglycan core protein
Myosin light chain kinase, smooth muscle
Obscurin
Hemicentin-1
Twitchin
Peroxidasin homolog
Striated muscle preferentially expressed protein kinase
Immunoglobulin superfamily member 10
Peroxidasin
Striated muscle-specific serine/threonine-protein kinase
Protein sax-3
Roundabout homolog 2
Obscurin-like protein 1
Down syndrome cell adhesion molecule homolog
Peroxidasin-like protein
Down syndrome cell adhesion molecule
Roundabout homolog 1
Netrin receptor DCC
Matrix-remodeling-associated protein 5
Roundabout homolog 3
Immunoglobulin superfamily DCC subclass member 3
Contactin-4
ADAMTS-like protein 1
Contactin-3
Protogenin
Alternative Name
D-Titin
Kettin
Connectin
Rhabdomyosarcoma antigen MU-RMS-40.14
Obscurin
Uncoordinated protein 89
SIH002
Sarcoma antigen NY-SAR-77
Perlecan
Kinase-related protein
Telokin
Muscle M-line assembly protein Unc-89
Fibulin-6
Uncoordinated protein 22
Melanoma-associated antigen MG50
Vascular peroxidase 1
p53-responsive gene 2 protein
Obscurin-RhoGEF
Obscurin-myosin light chain kinase
Aortic preferentially expressed protein 1
Sensory axon guidance 3
Calvaria mechanical force protein 608
Cardiac peroxidase
Vascular peroxidase 2
polysomal ribonuclease 1
CHD2
Deleted in U twenty twenty
H-Robo-1
Tumor suppressor protein DCC
Adhesion protein with leucine-rich repeats and immunoglobulin domains related to perlecan
Colorectal cancer suppressor
Immunoglobulin superfamily DCC subclass member 1
Roundabout-like protein 3
Retinoblastoma-inhibiting gene 1 protein
Putative neuronal cell adhesion molecule
Brain-derived immunoglobulin superfamily protein 2
Punctin-1
Brain-derived immunoglobulin superfamily protein 1
Plasmacytoma-associated neuronal glycoprotein
Protein Shen-Dan
Kettin
Connectin
Rhabdomyosarcoma antigen MU-RMS-40.14
Obscurin
Uncoordinated protein 89
SIH002
Sarcoma antigen NY-SAR-77
Perlecan
Kinase-related protein
Telokin
Muscle M-line assembly protein Unc-89
Fibulin-6
Uncoordinated protein 22
Melanoma-associated antigen MG50
Vascular peroxidase 1
p53-responsive gene 2 protein
Obscurin-RhoGEF
Obscurin-myosin light chain kinase
Aortic preferentially expressed protein 1
Sensory axon guidance 3
Calvaria mechanical force protein 608
Cardiac peroxidase
Vascular peroxidase 2
polysomal ribonuclease 1
CHD2
Deleted in U twenty twenty
H-Robo-1
Tumor suppressor protein DCC
Adhesion protein with leucine-rich repeats and immunoglobulin domains related to perlecan
Colorectal cancer suppressor
Immunoglobulin superfamily DCC subclass member 1
Roundabout-like protein 3
Retinoblastoma-inhibiting gene 1 protein
Putative neuronal cell adhesion molecule
Brain-derived immunoglobulin superfamily protein 2
Punctin-1
Brain-derived immunoglobulin superfamily protein 1
Plasmacytoma-associated neuronal glycoprotein
Protein Shen-Dan
Location in the cell
Nuclear Reliability : 2.709
Sequence
CDS
ATGGAGAAGCAGTCGAGATGGTCGGAGCAGCGCTCCGAACAACGTTCTGAGCAACGCGTTCAACAACACTCCGAACGACGCGAGCAAGTTGTGCAGCAACAGGAGAGGATCCAACGCACGGAGCAACACTTTACAAGACAAATGACGACACAAGTGGAGAGCTCCGGTGATCGCCAGCCCATCACTGCAGGTCGGCCTGGTGAACCCTCCCCGCCAATATTCGAGCAAATATTCAAAAATGCTAGATTTGCACAAGGTGGCAATGCTAAGTTCGAAGGAAAGCTTAGAGGAAACCCTACACCCGTCGTATCGTGGACGAGAAAGAAGGCGCCTCTTGTTGAATGTAATAAATACAGCATGCGTTACAACGAACAAACTGGCGACGTTTCGCTGCTTATAAAACAAATTGGACCTGGTGATGAGGGCGAGTACACCTGTACAGCTCGTAATCAGTATGGTGAAGCTATCTGCTCCGTATACATTCAACCTGAAGGTGTCCCGGTACCTGCTCAACAAGCTAGTCAGCAACAAAGCTACCGACATGTTAGTGAAACAGTCGAGCACAAAGCCTACGGTACACAAGGATACACAACAGAACAGTCACGACAAACACAGAAAGTAGCATACACTAATGGTACTGACCATTCTTCAACGGACGACTTCAAAGTAGACACCTTTGAGTACAGACTTTTGAGAGAAGTATCATTTAGGGAATCCATCACGAAAAGATACGTAGGAGAAAGCGATGTTCAAATTTCAACAGAAATTGATAGATCTCTAGGACCTGTATCTCCACCGAAAATAGCTCAGAAACCGAGAAACTCTAAACTGCAAGAAGGAGCTGATGCACAGTTCCAAGTACAATTATCGGGTAATCCCAGACCGCGAGTTACTTGGTTCAAAAATGGACAGCGCTTAATCAACTCAAACAAGCACGAAATCATAACGACCCATAATCATACGACGCTAAGGGTAAGAAATACTCAAAAATCAGACTCCGGCCATTACACTTTACTGGCTGAAAATCCCAACGGTTGCATTGTAACCTCAGGATATCTTGCTGTTGAATCTCCGACCGAAAGTTATGTACAGGACCAAAGGTCACAATACATAACTGATACTCAACAAAGAGAGACTGAAGAAAGAATAGAAATAAGTGAAAAAGCTCTTGCTCCGCAATTTGTTAAGGTTTGCCAAGACCGTGATGTAACGGAGGGTAAAATGACGCGATTCGATTGCCGCGTCACAGGCAGACCTTACCCTGAAGTCACGTGGTTCATTAACGATAGACAAATACGAGACGATTATAATCATAAGATATTAGTAAACGAATCCGGTAATCATGCACTTATGATTACAAACGTCACTCTCAGTGATAGTGGTGTGGTTACTTGTGTCGCACGTAATAAGAGCGGCGAGACAGCTTTCCAGTGTCGACTGAATGTTATTGAAAAGGAACAAGTAGTAGCTCCTAAATTCGTGGAGCGTTTCAGCACACTGAATGTTAGAGAAGGCGAACCGGTTGTGTTGAATGCCCGCGCTGTCGGCACACCAACGCCACGAATCACATGGCAGAAGGATGGCGTTCCGATAATACCCAATCCAGAATTACGAATTCATACTGACGGTGGGGCCTCGACGCTAGATATACCGCGAGCCAAGGCGTCGGATGCGGCATGGTACCAATGCACCGCTCAAAACGTCGCAGGTTCCACCGCCACTCGGGCCAGGCTCTATGTCGAAGTTCCGAAAGAGCCTCCGCCCGAGCAGAAGCGTCTACACCTACCCCGGCCTACAAAAGTAATCGAACCAGAGCCTGCTCCTGGACCAGAAATTATTTACTTAAGGCACGTGGAAAGGGCAAGACCGTATATTCCTCCCGGTGAGGAAGACCGCGTCTATCCTCCGCCACAGTTTATTGTGCCACTGAAGAGCGTCACGGCTATGGAGGGTGGCAAAATACACTTTGAGACGAGGATAGAGCCGGTTGGCGACCCCACGATGAAAATTGAATGGTTGAAAAATGGACAGAGTATTGAAGCAAGTTCAAGATTTACGTCAATATTCCGTTTTGGTTACATTTCTCTTGATATGCTCAGTCTGAATATCCAAGACAGTGGTGAGTACACATGCAGAGCGGTGAGCGCAACGGGGGTTGCTGAAACAAAAGCTGTGTTACACGTAACTCCCAGGGCTACTATCGAAAGAACTAGCCAACACCCAGAAACTCTGCAGTACATACAACAATTAGAAGATTATTCAAAATATCAACACCAAGAATCTATCGAAGAACAAACATCTCAGAGGCCACAATTTATAAGACCTCTGCAGGATCTTGGTGAACTTCAGGAAGGCAGAAATGCCCATTTCGAAGCACAACTGACTCCAGTGAGCGACCCCACAATGAGGGTAGAGTGGTATAAAGATGGCAGACCAATTACAGCTAGCTCGCGAATCACGTCAATCTTCAACTTCGGCTACGTCTCCCTTAACATCATGCACCTACGGGCTGAAGATGCAGGTTCGTACACAGTTAGAGCTGTAAATAAATTGGGTGAAGCTATCAGTACCGCTTCTATTAGAGTCGCAGCGAGGAGTACGGTTACCGCAGATCTTGGTATTCCTGAGCAACGTAGATACATCGAAAAAACAGAACAATTAGAAGCTTATCAACAACAGCAACATCAAAAATATTATCAGGAAGTACCGGAAAGTACACAAAAACCAGAATTTAAAACTCCTATCAAAGACCAAATCAGCATCAAAGAAGGAGGATTCGCTCATTTCGAAGCCCGGTTAGAACCAATCGGGGATTCGACTTTAAGAGTTGAATGGTTAAAGGATGGTCGCCCAGTCGAAGCTAGTTCAAGAATAACGACCTTCTTCAACTTTGGATATGTCGCATTAACTATCAAATCAGTTACGGTACACGATGCAGGTCATTACACCTGCCGAGCCTACAATGCTATCGGTCAAGCAACTACAAGTGCCAACTTAACGATCGTAACTAAAAAGGATATTATTGCGGAATCACAGCATCCTGGTGGACTAGAAAAAATTCAATACCTTGAGGACGCTAGTCGCTATTCAAAGAGAACTGAAGAAGAAGTAAAGATCACACAAAAGCCTCGGTTCTTAGGACCCCTTAAAGGCACAAATAAAATTGTTGAAGGACAAAGTGCTCACTTTGAAGCCAGAGTTGAACCTCAAAGCGATTTGACGATGACTGTAGAGTGGTACTTTAATGGAAAACAGATTACAAGTGCTAATCGTATTCAAACATATCATGATTTCGGTTATGTTGCCCTTGACATCGCAAGCGTTAGGGCTGAGGATTCTGGCGTTTATACTGTCGTGGCACGTAATGCAGCCGGCGAAGCGCAGTTAAGCGCGTCAATGACAGTCGAAACACGATCCAGCATTGATACATCTAGTATTCATCGTGGTTTATATGAAAAGACAAGACACATTGAAGAATCCAAATTTGTAGAGCCTATGTATCAGATTGAGGAAATATCCAAGTCAAAACCTGTGTTCGTGCAGCCTCTGTCTAACCCGCCTCCAGTTTCTGAAGGAAAGAACATTCATCTTGAATGCAGACTTGAACCTATGGGTGATCCTACAATGAGAGTAGAGTGGTTCCATAATGGTAGATCAGTCACTGTCGGTTCGCGATTCAAAACTTATTACGACTTTGGCTTTGTTGCTCTTGACATTATACATGCAACTTCTGCTGATACTGGCGAGTATACAGTGAGGGCTGTAAATCATTTAGGATCTGCTCACACTTCAGCAATAGTACGAGTTATCGAGAGATCAGACATCGTTACAGACACGCAAAATGAACAAGCTATAGAACAAATTCAATTATTAGAAGATGCTGCTCGAAGAACCAAACAAGTGCGGGAAGACATAACCGTTATGCAAGCACCACAGTTTTCAAGAGCACTTCATAACATCGAAACTGTTGAAGGTACAAACGTACATTTGGAATGTCGTTTGCAACCCGTTGGTGATCAGACCATGAGAGTCGAATGGTTCTGTAACGGAAAACCAATTAAAACCGGACACCGCTTTAGACCGGCTTACGAATTTGACTATGTAGCTCTTGACCTGTTAAGCGTGTATCCAGAAGACTCTGGTGTTTACACTTGTCAAGCTACAAATCAACTTGGAGAAGCAGTAACGTCTTGTGCGTTACGTGTAATTGCTAAAAAGGATCTAATTCTTGAGTCACAACATCCATCAGGCTTAGAGAAAATTCAATATCTAGAAGACACATCCCGTTACAAGAAAACTGATATAATTGATGAGTCAGTGACTATAAAGCCACGATTCGTAACACGGCCAAAGTCAATTGAAAATGTCATTGAAGGTCAGCATGTCCACTTTGAATGCAAACTTGAACCAGTGACAGATTCAAATCTTAAAGTTGAATGGTTCAAAAACGGTCAACCCGTTACGATAGGACATAGATTCAGACCAATCCATGACTTTGGGTACGTGGCCCTTGATATCATTGACTTGATTGCTGAAGATTCTGGGATTTACACTTGTCGTGCTGTTAACCTTGTTGGTACTGATGAAGTTAGCTGCAGGCTCACATGTCGCAGTACAACCGACATCGTCAGAAGCACTCAAAATGAAGCCGGCTTGGAACAAATTCAAGTTTTAGAAGATCGATCCAAATATCACAGAACTGACATGGTTGATGAAGTCACAACCCAGGCTCCTATATTTACGACATCGTTGAAGAACGTCGAAATCAAGGAAGGACAACGCGCTCACTTCGAATGCAGATTGATACCAGTATCTGATGCTACATTGAAAGTAGAATGGTATCACAACAATAAACCTCTGAAAAGCGGCTCGAGATTTACCGAAACCAACAATTTTGGTTTCGTCGCTTTAGATATCATGTCTTGCTTGCCAGAGGATTCAGGTACTTATACCTGCAGAGCAATAAACGCTCTTGGGGAAGCCGTAACTTCTGGCATCGCAATAGTACATTCCAAAAAATCAATATATTTGGAGTCTCAACATGAAGGAGCTCTTCCAAGGCTTAATCAATTGGAAGATACTTCAAAGTATCAAAGGCACAGCGCACAAGACGAGGTAATTACTCAAGCACCTGTGTTCACTATGCCGATGAAAGACATAAGAGTCGCTGAAAACCAAGCAGCTCACTTTGAAGCCAGACTCATACCTGTTGGCGATCCAAAACTACGCGTAGAATGGTTGCGCAATGGTGTCCCCATAGAAGCATCGAACCGTTTGACTACAATGCACGATTTTGGGTACGTCGCATTAAACATGAAATACGTAAATCCTGAAGATTCTGGCACATACACGTGTCGGGCTATAAATGAGCTGGGTGAAGCCGTAACATCTTCGACGCTGTTCGTGCAGTCGAAAGCATCCCTACAGCTCGAATCACAACACGAAAGCGCTCTTCAGAAAATTCAACAGCTTGAAGACTCTTCGCGGTATCAAAGACGAGAGGACGTAGAAGTGGCTGTAAATCAAGCGCCCAGATTTATAACTCAACTAAATGGACCAACAAAGCTAAGCGAAGGCCAAAGTGCGCATTACGAATGTCGTATCGAACCTTACCCGGATCCGAATATGCGCGTTGAATGGTATTTCAACGGCAAAGTACTCCAAAGTGGACACCGCTACCGGACTTCCAATGACTTCGGCTTTGCAGCACTTGATATTCTCACCGTTTATGGTGAAGATTCTGGTGAATACACATGCAAAGCTATTAATAACTTAGGACAAGCTGTTTCTTCCATTCGGTTGAATGTACAATCAAAGGAATCTATAATTAGAGATTCTCAGCACGAAAGCGCTTTGGAGAAAATCCAATACCTTGAAGATGATAGCAGATATAAACGGGCCGTTCAAGATGATAGCTTTGTAGTTGAGAAACCACAGTTCGGCAAACCGATAAAGAATGCAGAAGTAACAGAAGGTCACCCAGTGCACCTTGAAGCTACGCTAACGCCAGTCAACGACCCTACCATGCGAGTCGAATGGTACTGCAACGGTAGACCTGTACAACAAGGACATAGATTTAAGACGACTTATGATTTCGGCTATGTTGCCTTGGACATTTTGTATGCATATGCAGAAGATACAGGAACTTACATGTGTAAAGCGACAAATGCCGTTGGCGAAGCTGTCACTACCAGCTCAGTAAAAGTAGACGCAAAATCTGGTCTGTATCTCGACACGTTGGATGAACAAAGACTTAAGAAGATACAAGAGTTGGAGAAATACGAAAGACCTAAGCCAATTGAAGAGGAGCAGCCAGGTCAGAGGCCGGTCTTCTTAACTGCTCTGACTAGTCTTGAGAATCTTAAAGAAGGCGATCGTGCGCACTTTGAGTGCAGAGTAGAGCCAATCAACGATCCTCATCTGACAATTGACTGGTTCCATAATGGCCAGAAGATCAGAGCCGGGCATAGGTACAGAACCACACACGATTTCGGCTATGTTGCTCTGGATATCTTGTATACTTATGCTGAAGATTCTGGAACATATATGTGCAAAGCTACCAACAAACTCGGTGAAGCTGTCAACACATGCACGTTGAAGGTTGCAGGACATAGAAACATTATATTGGACACACAACATCCTAACGGCTTGGAAAAGATAAGACAACTTGAAGCTCAAGGTCACTCTACAAGGATCGAAGTTGAAGAGCCAAAGATAAGCCCGCCAAGATTTGTTACGGAGTTACGAGGCACCACACATGTTTTTGAAGGAAAAACAGCTCATTTTGAATGCCAAGTCGAACCAGTACATGATCCTAATCTACGTATTGAATTTTATCACAATGGCAAGGCCCTGCAATCTGCCGCACGATTCCATATCACTTTTGATTTTGGTTACGTGTCATTGGATATTCAACACTGCGTACCTGAAGATGCAGGAGAATATTCGGTTAAGGCAATTAATGCTCTAGGACACTGTACATCAGCAATCTCCATGACAGTAACCGCAAAAGGCAGTATAATATCGGAATCTCAACGTCCAGAAGGTTTAGAGAAAATCCGAGAATTGGAATCAGCTGAACCGTTCAAACGTCCCGAAATTCCGGAACCAGTTACTAGGCAAAGGCCCGTATTCACTCAACCGTTACAGAATATTGATAATATTCAGGAAGGCCAGACTGCACACTTTGACTGCAGATTAATTCCGGTTGGAGATCCAACTTTGAAAGTTGAATGGTTCAGAAACGAGAAACTCATTGAAGACAGTTCCAGAATCACGAAAACGCACGATTTCGGTTATGTATCCATGACCATTTCACACGTACGCGATGAAGATGAAGGCGTTTACATGTGCAGAGCTTCCAACTTACTTGGAGAAGCAGTAACTACGGCTGCAATGAAAATCAAAACAAAAGCAGCAATCCAGTTGGAGACCCAACATCCCGAAGGAATGAAGAAAATTCAGAAACTTGAACAGCCTCATGAGAGACGTTCAGAAGAGCCAGATCGCGAGTTCGAAAAACCGATATTCACTCAGGTTCTTACTGGGCCATCCGAACTGTGGGAAGGACAACACGCACATTATGAAGCTCGCGTAGTTCCTGTCGGTGATCCTAGTCTTCGGTTTGAATGGTACATAAATGGCGTAGAATTGAAAATGGGTTCAAGGTTCCGCACCACTCATGACTTTGGTTTTGTTACTTTAGACATTAATTCAGTCGTGGCAAATGACGCAGGTTTATACATGTGCAAAGCTATTAATAGAGCTGGTAGCACAGTTTCTTCGACATCACTTAAAGTCAAAACTAAATCTACTATTATCGACCAGGCCATGAGACCCGAGTCGTGGGAACAAATTCAATTAAAGGAAGCTGCCATGAACAAGGTTCCCGAAATGTTCGTTGACACTGGTGTTCAACAAGCCCCTATTTTCACTACACATCTAAAAAGCTACGACAAGCTTGTAGAAGGACAGCACGTGTATTTGGAAGCTCAGGTAGAACCACGTACTGATCCAAACCTTAAGATTGAGTGGTTCAAAAATGGAGTCACGCTAACTACTGGAGCTCGATTGAAGAGTACGTTTGACTTTGGTTTAGTTACTCTTTCTATTAATAGCTTGCGAAATGATGATTCGGGTATTTACACATGTAAAGCAACAAATCTTTTGGGTGAAGCTGTATCAACTGCATCGATTAAAATAGAAGATCGTCATTGGTTGCTTGGAGAATCACTTCATCCGGACTCACTCGATCGTATTGGGGCACTTGAGCAGCCCAAGCCTGAAAAACCTGAAGCTCCCGAACCAACTTATGAAACGCCCGTATTCATATCCCATTTAAATAATATTGTATGTAAAGAAGGAGATAATATTCATTTCGAATGTAATGTGGAACCATCTAGAGATCCTACTCTTAAAATCGAGTGGTTCTTTAATAATAAACCTCTACCATCGGGAACTAGGTATAAGAGTACTCATGACTTCAGCTATGTTTCGCTTGATATAACGCATACTTACGAAGAGGATTCCGGTATTTACACTTGTAAAGCAACGAACAGCAAGGGCTCAGCTACAACTTCTGGTTCATTAAGATGCACGGGTGACAAAAACATTTACTTTGATACTCAGCATCCTCAAGGTAAAGCTGGTTTGGAAGCTGTCGAACAAGCTGAGGAAGCTAGATTGGCAAAGGGTAGGAGGCCTTCCGTTCCGGATACAGAATATCCAAAACCAGAATGGATTATACCAATTGCTGCTGAGCATCAACTAGTAGAAGGCCAAGTACTTCATTTGGAAGGCCAAGTAGAACCCAAGAATGATCCAGATCTCAAGATTGAGTGGTATTTCAATGGTAAAGTTTTGGAACAAGGTTCCAGATTCAAACTTACTAGTGATTTCGGATTCGTGACGCTAGATCTCGTGGACGTGTATGAAAGAGATAGTGGCATTTATACGTGCAAAGCTTACAACAAGAGGGGTGAAGCTTTTACTTCATCTACTGTATATTGCACTAGTAAAGATAATCTAATTGAAAGAACTCAACATCCGAAAGGAACTGAAGGTTTAGAAAAGATTCAAAATTTGGAGGATTCTCTTCGCAAAGAACCCGGGCAACAGCCTGATGACGATACAGGTAGACCACCAGAATTTACCACCGTTTTCAAAGACATTGTTGATATTAGTGAAGGACAAATTGCTCACTACGAGGCATCTTTGATACCAACTGGCGACCAAAGTATGGTTATTGAATGGTTCTATAACGGAAAGACCATTGAAGCTAGTCATCGCATCCGCACAGTTTACGCATTTGGGATGGTGGTTTTAGAGATACTAGGAACTAAAACTACTGATTCTGGAACATATTCCTGTCGTGCCACAAATAAATGGGGACAAGCTGAAATAAGCGTGAAACTAGAATGCGTGGATAAGAGTAAAGGACAGAAACCTAGATTCACAACACACATACAAAACATTGAAGGTCTAAAAGACGGACAGTCTGCACACTTCGAATGCACTGTCGTACCAGTCGACGATCCGGATATGAAAATCGAATGGTACCACAATGGTCAACATATGCGTCACTCTACAAGAATCAAAACTGTTTCAGACTTTGGATTCGTCGTTCTCGACATAGCTTACACACAGAATCACGACTCTGGTGAATATGTTTGTCGCGCCTACAACAAATATGGTGAAGACTTTACTCGTGCCACTATAAACTGTTATGGAAAAGGTGGCGTCTACCTGGAAAGCTTACAGCCAGATTCTTTAGCAAAGATAAGGGAATTAGAAAGCTTACAAGGAGCGCAACAACAGACACCATCAACACCATCTGCTGAGCCACCTAAGTTCATAACTCAAATTCAGGATGTTACGAAATTAGTTGAGGGACAGAGTGCTCACTTCGAAGCAAGACTTGTACCAGTAGATGACCCTGACTTAAAGGTTGAATGGTTCTATAATGGGAAAAAGTTGCCTCATGGACATAGGTACAGAACGTTCCATGACTTTGGTATTGTAATTTTGGATATTTTATATTGTTACGAAGAAAATTCTGGTGAATATGAATGTGTCGCCACCAATAAGCTAGGACGTGACTCTACGAAGGCCAATCTTAAGTGCACATCAAAAGAAAACTTAATCCTGGACTCGCAACTTCCGCGGGGCATGGAAGGTGGATTGGAAAAACTTCAAACTTTGGAAGATTCTATGGTTCGAAGGAAAGATACATCTGTAGAAGAAGAAAAGGGCAAAGCTCCAGTGTTTACAGTTCCACTTTCAAACATAGAAAATTTGCGAGAAGGCGAAAATGCTCACTTTGAAGCTAGACTGACACCGACCGATGATCCTAACCTAAAAGTTGAATGGTACTGGAATGGAAAATCACTTAAAGCTGGGTCCAGATTTAGGACATTCTGCGACTTTGGATTCGTTATTCTGGAAATATCTCCGACGTATCCTGAAGATTCTGGAGAATATTTGTGCAGAGCCTACAATAACTATGGTGAAGCCGTTACCACGGCTTCTATGAAGGTACAAGGAAAACGTAATATCATTTTGGAATCACAGCTGCCGAAGGGAATGGAAGGGACCATTGATAAGATTGCAGCTTTAGAAGGTTACTCTGGAACCGTAGATACCTTGACACCAGAAGCTGAAAGTGGAAACCCACCAGAATTCACAACGACTCCTTCGGACCTAATTCTTTCCGAAAACTCATCGGCTCATTTCGAATGTCGCTTGATACCAGTAAACGATTCGAGTATGCGTGTTGAATGGTTCCACAATGGAAAACCGCTATTAACCGGATCTAGGGTTAAGACCATTAATGATTTTGGTTTCGTAATCTTGGAAATCGGCGGAGTGTATCAACGAGATGCCGGTCTGTACACATGCAAGGCAACAAATCGTCACGGTGAAGCAACCGTATCTTGCAAGTTGCAAGTAAAGGGAAGACAGGGCATTATCCTTGAACCTCAGTTGCCTTCACACTTTAAGTCCGGAACTGAGAGTATCCAGAAACTAGAAGAAACGCTTCACAAACGCGAAGAGATTACTATCGAAGACGAAAAACCGAACCCGCCGAGATTCACGGTAGAGATAAAAGATAATATCGACGTACCTGAAGGCGGTCCGGTTCACTTCGATTGTCGTGTTGAACCAGTAGGTGACCCTACCATGAGGATTGATTGGTTCCACAATGGCAGGCCATTTGCTACCGGCTCTCGTGTGCACACGCTTAATGATTTTGGTTTTATTGCTTTAGACATTGATTACATTTATGCTCGTGACGCCGGCGAATATACCTGTCGGGCCACAAACAAATGGGGATCAGCAACTACTACAGCTAAAATAACTTGCAGCGCCAAACGCGATATCGTTCTAGAGTCACAATTGCCGCAAGGTATGAGTGGCGAAAAGATTAAAGAACTGGAAAGAGGCCGCATAAGCGATGCTCCGAAAGAAGAACCGATCGTTAGTACACCGCCTAAGTTTATCACGCAAATCAAATCGCACACAGTAGAAGAATCAGAGGGTGTACGATTTGAGTGTCGCGTCGAACCTAAAGAAGATCCTAAATTACGCATAGAATGGTACCGCAACGGAAAATTGTTACCTTCCGGCCATCGATATAGGACGGTATACGACATGGGCTTTGTTTCTTTGGACATCTTGTATGTTTATGCTGAAGACTCCGGTGAATACATTTGTCGTGCCGTTAACGACTTCGGAGAGGATTTCACAAAGGCTACAATTTCGTGCAAGAAATTACCTGATATTATTCTACAAAATCAAGTTCCTCGTGGAATGAAGAGGTCTGAAGCGCTCACACAGATGGAAGCTACAATAAAAAAATATACATCTGAAGTTTATCTGACGGAGGATGATCTGTATGACGTGGATAAGAAACAACCACCACGCTTCGTTACGCAGATACAAAGCCAAACCAGTTTGGTAGAAATGGAAACTACTAAATTTGAATGTCAACTGGCGCCAGTAGGAGATCCTAATATGAAAGTCGAATGGTTCTTTAACGGAAAACCTTTACTACATAAAAATCGTTTCACACCCATTTACGACTTCGGTTACGTTGCTATGAACTTCGGTTGGGTATATCCTGAAGACAGTGGGGAATACCTTTGCCGCGCTACCAATCTGTATGGAATGGATGAAACCAAAGCAGTCATCAAAACAACAGGAAAACCAGGAATCGTATACGATTCACAATTACCTAAACACATGAAGAGCATTGAAAAAATACGAGAGATGGAAGCATCTTGGCAAGTGACGCCCGAGCAAGTAGTGGAAGAAAGTAAGGCGCGCTGCCCACCTGTCTTCGTTAGTCTTCCGGACGCAGTTACGGTAGAAGAAGGAGAATGGGCTCGTTTCTGCTGTCGCGTAACTGGTCATCCAAAACCACGAGTGATGTGGCTCCTAAACGGCAACACCATCGTCAATGGATCAAGATACAAACTGACTTACGATGGAATGTATCATTTCGACATACCAAAGACAAGGCAATATGATACTGGTAAAATCGAAGTTATTGCAAGAAGCTCAGCCGGCGAGGCGGCGGCATCAGCCGAATTAAAAGTTATTCCCAGACATGACGATTATCGAGGTGTATTGAAGAACGCACCACGTCCGTGGTACGATGAAACGACACAATATCAACGCACTGAAACCGAATTAGAGAAAACATTTGAGGAGCGTCAAGTACTGCAACGCCAGGGCGTTATTGATCACAGACCAGAGTTAAAACCTAAAGTAATCAAAGAACCAGAAACGGAATGGCAACAGTCTGTAAAGAGGAAAAAGAATGAGGAATATTACAATAAACTTCAAGAATTGGAAAACGAACAGGTCATCAAGGAGAGTAGGCTGAGAGAATCGACTCACCAATACGCTATTCCCGGTGATAAAGTTACAAGCAATACTGTAGCTAAAAGCATGGCCCAACGATACGAGGACAACCTTGACCAGACCGAAGAAGTAACGGAACAAAGAGTGCAAAAGAAGGTGACTCAAAAGCCAAGAATACCGGATCCTTCGGAATCGACCGTGCACGGCAAAGAAGTGCACGTTGCGAAACAAAAACAAACTCAGAAAGAGGTCGTCGGGGATAAAGAAATAACACGTAAAATTACTTCTACTGAGACAACGGAGATCGAGCATAAAGCTCAAACACAAGAGAGAGTTGTGGAAGGGCCAGTTAAACCTTCGAAACCACCGATATTCACTAAGAAAATGCAGCCCTGCCGTGTGTTTGAACATGAACAAGCTAGATTCGAAGTTGAGTTCGATGGCGAACCCTTGCCTTTGATTAAATGGTATCGGGAGAATTTCCCTATTAAAAACTCGCCTGACTTCCAAATTCATACATTTAGTACCAAGTCTATATTGATCATAAGACAGGTGTTTGTCGAAGATTCCGCTGTGTTTGCTGCTGTGGCTGAAAATAGAGGTGGGACTGCTAAATGCAGCGCTAACTTGGTGGTGGAAGAAAAAAGACGTCAAGGACGTGGAGGGATCGTTCCTCCTAGTTTTACGTTAACTGCTCAAAACGTTAACGTGACCTCAGGTCAACTTGTGAGGCTTGACACCAAGGTTACCGGAACGAAACCTATTGACGTTTATTGGCTGAAAAACGGTAAGAAAGTCCAACCTGATATAAGGAACAAGATTCTAGAAGAAGATGGAACTTATACCCTGCTTATTCTCGAAGCTTACCCGCAAGATTCTGGTAAATACGAGTGCGTTGCAATTAACAGCGCTGGAGAAGCCAGATGTGATGCTGAATGTGTTGTAAGCCTTCCAGCTACCAAGGACAAGCCTAAACCTCAAACGAAAGCAGCAAATGCCCCACCCGAGATTATCGAACCTTTAAAGGACAAAATTGTCGCTGAAGGACAGGCTATTGAGTTCAGTTGTAAGATCGTTGGGAAACCTCTTCCAACAGTACAGTGGTACAAGGGTGATAAACTGATTAAACCATCAAAATACTTCCAAATGTCGAGGACCGCTGATGAATACACCCTGCGTATATCAGAAGCTTTCCCGGAAGACGAAGGGGACTACAAATGTGTGGCGTATAACTCGGCTGGTCGTGTGACTGTCGCTGCGAAACTGAAAGTGACACAGCCCGACCAGGCTGATAATCTTCCAGCCCTGACACCTCTTCGTGACATCGTGGTCTACGAGGGCCAACCGGCCCAATTTAAAACACAGATCACCAGCAAGATCAAGCCGACCATTCAATGGCTGAGAGAAGGTGCACTAATACCGGAGACTCCCGATTTTCAGATGATTCACGAAGGCAACAACGCTGTGCTGCTAATCGGGAACACATACGAAGAAGACACTGGCACTTTCACATGCCGCGCTACCACGGCTGCGGGTCAAGTCGAGACTTCGGCAAAACTAGTCGTCAAAAAATCTCGGACACGTACTCAGAAGACGTTTGATCACAAAACACAAATTCAGACGACTTCTACAAAGAAAGTGGAACCTACAACAGGAAAAACAAGTTATTCTACCACTGAAGAAACTAATATGTTAAAGGTGGAAAATATTCAAGACACCGAAACAAAAAACATTACTACAGTACCTTGGCGTAAGAGGGAACAACTGGATATGCATTTTAAAAAAGAAGACACCTTAGAAATAAAACACTGGAGAAGATCTCGACCAGAACAAAATAAAGATACCGAGCATACAAGTATGATTGGAACCACTACTTCAACAAAAGAAGATAAAACTAAAGAAGTCTTTGAACGTGGTGTCATTGAAGAACATGTCAAAGTTCAAGAAGTTGTTGAAACAAAGTTATGGCGCAAACCAAAAACTATTTCAGAAAAAAAAGATTTACTTCAGGTTTCTACGCATGAGGATACCAATATTTTAAAGGTCGAAAACTTGCAATCAGTAAATGTTGATACTACAAGCAGTAAACTAGAAACTAAATCATGGCGTAAACCACGGCTTGAAGAATCTTTGGAAGAGGTAGGCCCTACTAAAGGTGTTAACGAGCCTGAAGTATGTCATTGGAGAAAACCAAAAACCTCAGAGATTTTAAAAGATAAGAATGAAGAAGAAATACGTGTTCAAGAGATGAAAAAACAGAGCACGAAAGCTTTGGAAGTTAAAGACGAAAGCAAGCAAAAGATTCCATGGACTCAAGAAGCAATAAAATTGCGGCCAACAAAGGTTGAAAAATCACCCATCGAAAAAGAAAAGATCGAAGATGTAGCTTTGAAACCAGTAAGAAAAGATTCTTTAATGGATGAAAAATCAAGTGAAATAAGTGAACTTCAGAACGAAAGACAAATAACTGAAAAGAAAGAAAGTCTTCAGGAAACTCAACTTCAACCAACCGAGAAAAACAAATTACTTGAAAACATTGTCTCTGAGGAAAGCAAAGAATCAACTGGTAAAAGAAGACAGAGGGAAGAGATTACACAAAAAGAGGTAGCTTTAAAGACTGTACGAAAACAAGAGGAATTCACTGAAGAAAAAACTGAACAAAAATCTCTGAAGCCCGTGTTAACAACAGAAAAAGAATCAAAAGAAACAGAAGATAGAATCAACACTAAAGACACGAGAAAACCATCAATCCCATGGACTCAAGAAGCAATTAAATTGCGCCCAACAAAAATGGAAAAAACTCCGATTGAAAAAGAAAAGTTTGAAGACATAACATTAAAACCAACAAGAAAACAGTCTTTGGTAGACGAAATAACAGAGGAAGTTTGCGCATTAAAATCTGCACTGGACGACATTGAGAAAGAAGAGCACAAACCAGATAAAGTAAGCGAAAATAATGCCCCTGAGGAACGTAAGTGGCCCACCGGAAAAAGACAACCTAAAGAAGAGACCCCACAAGAAGAGGTCGTTTTAAAACCCACACGAAAGCAAAAAGAGCCTGAAGAAGAAAAGTCCGAGGAGCGTAAATGGCCCAGTGGTAAGAGACGACCTAAGGAAGAGACTCCACAAGAAGAGGTCGTTCTCAAACCCATACCAAAGCAAATGGAGCCCGAAGAAGAAAAGCCCGAGGAATTTCAACATAAAGCGGTTAAAAAAGAAAAGAAAATTGAAGATGCAACACCTGAGGAGCATAAATGGCCCAGTGGTAAGAGACGACCAAAGGAAGAAACTCCACAAGAAGAGGTCGTTCTCAAACCCATACCAAAGCAAAAGGAGCCTGAAGAAGAGAAGCCCGAGGAAGTTCAACTTAAACAGGTTAAAAAAGAGAAGCAAATTGAAGATACAACACCTGAGGAGCGTAAATGGCCCAGTGGTAAGAGACGACCTAAGGAAGAAGCTCCGCAAGAAGAGGTCGTTCTCAAACCCGTACCAAAGCAAAAGGAGCCTGAAGAAGAGAAGCCCGAGGAAGTCCAACTTAAACCAGTTAAAAAAGAGAAGCAAGTTGAAGATGTAACACCTGAAGAGCGTAAATGGCCCAGTGGTAAGAGACGACCTAAGGAAGAGACTCCACAAAAAGAGGTTCTACTTGAGCACGTGAAAAAACAAGAAGAAATAGATGAGGAAAAAATTGAACAAAACGTACTGAAGGACGTCTCAGAAACAGAGAAAGAATCAAAAGAAAGAGGAGATAAAATCCAAACTAAAGACACGAGGAAATCATCTATTCCATGGACTCAAGAAGCAATCAAATTGCGACCAACAAAAGTTGAAAAATTACCAATGGAAAAAGAAAAATTGGAAGACATAACACTAAAACCCATAAGAAAAGATTCTATGTTAGGCGAAAAACCAGAAGAAGCTAACACATTAAGAGCACTAGTGGACAAAATCCATACAGAAGAACAAGAACTCAAAGACAAAGAAAGGGTACAGGAAATCCGAGACGAGCAAATGAAAACAGACAAACCAGTAGAAGACGCAATGCCTGAGGAACGCAAGTGGCCTACTGGTAAAAGACGACCTAAAGAAGCGACTTCACAAGAAGAGGTCGTTCTCAAACCCGTACCAAAGCAAAAGGAACCTGAAGAAGAGAAGCCTGAGGAAGTCCAACTTAAACCGGTTAAAAAAGAGAAGCAAATTGAAGATGCAACACCTGAGGAGCGTAAATGGCCCAGTGGTAAGAGACGACCAAAGGAAGAAACTCCACAAGAAGAGGTCGTTCTCAAACCCATACCAAAGCAAAAGGAGCCTGAAGAAGAGAAGCCCGAGGAAGTTCAATTTAAACAGGTTAAAAAAGAGAAGCAAATTGAAGATACAACACCTGAGGAGCGTAAATGGCCCAGTGGTAAGAGACGACCTAAGGAAGAGACTCCACAAGAAGAGGTCGTTCTCAAACCCATACCAAAGCAAAAGGAACCTGAAGAAGAGAAGCCCGATGAAGTCCAACTTAAGCCGGTTAAAAAAGACAAGCAAATTGAAGATGCAACGCCCGAAGAGCGTAAATGGCCCAGTGGTAAGAGACGACCTAAGGAAGAGACTCCACAAGAAGAAGTCGTTCTCAAACCCATACCAAAGCAAAAAGAGCCTGAAGAAGACAAGCCGGAGGAAGTCCAACTCAAACCGGTTAAAAAAGACAAGCAAATTGAAGATGTAACACCTGAAGAGCGTAAATGGCCCAGTGGTAAGAGACGACCTAAGGAAGAGACTCCACAAGAAGAGGTCGTTCTCAAACCCGTACCAAAGCAAAAGGAGCCTGAAGAAGAGAAGCCGGAGGAAGTCCAACTCAAACCGGTTAAAAAAGACAAGCAAATTGAAGATGTGATGCCTGAAGAGCGTAAATGGCCCAGTGGTAAGAGACGACCTAAGGAAGAGACTCCACAAGAAGAGGTCGTTCTCAAACCCGTACCAAAGCAAAAGGAACCTGAAGAAGAGAAGCCCGAGGAAGTCCAACTTAAACCAGTTAAAAAAGAGAAGCAAATTGAAGATGTAACACCTGAAGAGCGTAAATGGCCCAGTGGTAAGAGACGACCTAAGGAAGAGACTCCACAAGAAGAGGTCGTTCTCAAACCCGTACCAAAGCAAAAGGAACCTGAAGAAGAGAAGCCGGAGGAAGTTCAACTTAAACCGGTTAAAAAAGACAAGCAAATTGAAGAAGCAACGCCCGAAGAGCGTAAATGGCCAATTGGGAAGAGACGACCTAAGGAAGAGACTCCACAAGAAGAGGTCGTTCTCAAACCCGTACCAAAGCAAAAGGAACCTGAAGAAGAGAAGCCCGATGAAGTCCAACTTAAGCCGGTTAAAAAAGACAAGCAAATTGAAGATGCAACGCCCGAAGAGCGTAAATGGCCCAGTGGTAAGAGACGACCTAAGGAAGAGACTCCACAAGAAGAGGTCGTTCTCAAACCCATACCAAAGCAAAAGGAACCTGAAGAAGAGAAGCCCGATGAAATCCAACTTAAGCCGGTTAAAAAAGATAAGCAAATTGAAGATGTAACGCCTGAAGAGCGTAAATGGCCCAGTGGTAAGAGACGACCTAAGGAAGAGACTCCACAAGAAGAGGTCGTTCTCAAACCCATACCAAAGCAAAAGGAGCCTGACGAAGAGAAGTCCGAGGAAGTCCAACTTAAGCCGGTTAAAAAAGATAAGCAAATTGAAGATGTAACGCCTGAAGAGCGTAAATGGCCCAGTGGTAAGAGACGACCTAAGGAAGAGACTCCACAAGAAGAGGTCGTTCTCAAACCCGTACCAAAGCAAAAGGAACCTGAAGAAGAGAAGCCCGAGGAAGTCCAACTTAAACCAGTTAAAAAAGAGAAGCAAATTGAAGATGTAACACCTGAAGAGCGTAAATGGCCCAGTGGTAAGAGACGACCTAAGGAAGAGACTCCACAAGAAGAGGTCGTTCTCAAACCCATACCAAAGCAAAAGGAGCCTGACGAAGAGAAGTCCGAGGAAGTCCAACTTAAACCAGTTAAAAAAGAGAAGCAAATTGAAGATGTAACGCCTGAAGAGCGTAAATGGCCTAGTGGTAAGAGACGACCTAAGGAAGAGACTCCACAAGAAGAGGTCGTTCTCAAACCCATACCAAAGCAAAAGGAGCCTGAAGAAGAGAAGCCCGAGGAAGTCCAACTTAAACCAGTTAAAAAAGAGAAGCAAATTGAAGATGTAACGCCTGAAGAGCGTAAATGGCCCAGTGGTAAGAGACGACCTAAGGAAGAGACTCCACAAGAAGAGGTCGTTCTCAAACCCATACCAAAGCAAAAGGAACCTGAAGAAGAGAAGCCCGATGAAGTCCAACTTAAGCCGGTTAAAAAAGACAAGCAAATTGAAGATGCAACGCCCGAAGAGCGTAAATGGCCCAGTGGTAAGAGACGACCTAAGGAAGAGACTCCACAAGAAGAAGTCGTTCTCAAACCCATACCAAAGCAAAAAGAGCCTGAAGAAGACAAGCCGGAGGAAGTCCAACTCAAACCGGTTAAAAAAGACAAGCAAATTGAAGATGTAACACCTGAAGAGCGTAAATGGCCCAGTGGTAAGAGACGACCTAAGGAAGAGACTCCACAAGAAGAGGTCGTTCTCAAACCCGTACCAAAGCAAAAGGAGCCTGAAGAAGAGAAGCCGGAGGAAGTCCAACTCAAACCGGTTAAAAAAGACAAGCAAATTGAAGATGTAACGCCTGAAGAGCGTAAATGGCCCAGTGGTAAGAGACGACCTAAGGAAGAGACTCCACAAGAAGAGGTCGTTCTCAAACCCGTACCAAAGCAAAAGGAACCTGAAGAAGAGAAGCCCGAGGAAGTCCAACTTAAACCAGTTAAAAAAGAGAAGCAAATTGAAGATGTAACACCTGAGGAGCGTAAATGGCCCAGTGGTAAGAGACGACCTAAGGAAGAGACTCCACAAGAAGAAGTCGTTCTCAAACCCGTACCAAAGCAAAAGGAACCTGAAGAAGAGAAGCCCGAGGAAGTCCAACTTAAACCAGTTAAAAAAGAGAAGCAAATTGACGATGTAACGCCTGAAGAACGTAAATGGCCCAGTGGTAAGAGACGACCTAAGGAAGAGACTCCACAAGAAGAGGTCGTTCTCAAACCAATACCAAAGCAAAAGGAGCCTGAAGAAGAGAAGCCCGAGGAAGTCCAACTTAAGCCGGTCAGGAAAGATAAGCCCATCGAAAAAGATTCACATATAATAGAAAAAGACAGTACAGCTTACGAATACGTTCCTAGTGTTTCAGAGGAAGATGTGTTGAGTGACGAAAAAACGAGCGATGTTGAAGAATTTGCACCACGGATAGTAAAGGCACTACCCACTGTGGTCACAACAACTGAAGGAAAATTAATAAGATTGGAGGCGAAAGCTATTGGCATACCTAAACCACAAGTCAGATGGTTAAGACAGGGTACCGAACTTCTTCAATCTACTGAGTATCAAATTGAAGAATTAGACGACGGTACTTCTATTTTAACAATGCCAGAAGTTTATCAAGACGACACAGGAGAAATTGTCTTCGAAGCCTACAATCATCTTGGGGTAACAGCGACAATTGCTGCGTTGTCGGTTGAAAGTATTGTGGGAACACAAGAATATAGAAAGCCCGAATGGGTGACACACATGGAAGAGTTACAAGCAGCTTTGAAAGCAACACAATCTGTGCCTACATTTGTGAAGGAAATTATCCCAGAGCGAGTACACGAAGAAGAAATAGTCACCTTCGAAGCGATTTATAGCGGAAATCCAACGCCAGAAATACTTTGGTATAAAGATAATAAGGTTATACGTACTGATGAACGTTTCATTATTGAAAACAAAGAAAATCGTACCACATGCACAATTAAAAAGGCAACCAAAGACTTAGAAGGCACATATACCTGTAAAGCTGTTAGCGACATTGGTTTAGCAGTAACCAAAGCGAAGCTGCAAGTTTTCCAAAGAGGTTCCAAAATTAAAAAAGGAAAAGAGACGAAAGAAAAAGTTACCAAGCAAAAAGTAATTAAGAGTGAAGAAGAATCTGTAGGTGTTGAAGATACCCTTGATTTTGCTACTGTTTCTGAAGTTCAAGCACTAGATAAACAACATTCTACAGACAAAGTAAAGAAAAGAAAAGCAAAGATTGTCGTGAGTGAATCTGAGCATATAGAAACTGAAGATATAGCACTACAAAAGAAAGTAGATGAAAAAACAAAAGGTATACCAGTCGAAGAAAAAGCAAAACCAATTTTGACTACACATGAACACGTAGTTTTATCCGAACAACAAGAAGGTGAATCTGTTGAACCGTTTGATGAATCCTACCAAACGCAGAAGGGTATCATTAAAATGGTGGAAGCTGATTCAAACCTTGTAGCTGAAGTGAATGAGTTACTGGAAGTTATTAACGCAAAAGAATTTGGACCAGGAGAGACGCCTTTACGAGAGCTTGCTAAAATTGGTTATTTGTTAAGACGAGGTATTACGATTGAACAAATAGAGAGTTTGTATGATTCACAATACTTCCCTTCTCTTCTGATTCCTCAGTCACAATCAGCTCTAGTACAATTAGTTGAAAGACAAGGTCACGGAGCGTTGATCACTGAAGTGCTTACAGAAGAGACGGCACAAGATGAAGATATTATTGCCGCCAAAGTAGGTTTTAAAGCTTTCCTTAAAATGGTCGAAATGAAGCATTCTTCTGTTGAGGAAGTTATTGCTCAGTTTTATCCAGAAGATTTTAAGCCACGTTCCTGGGAACAAAGAGCAGCAAATGAGGTTATTGTGGAAGCGACTGCAGATCATGTAGTCGAAGCACACACCACAAAAGTCATAAAAGATTCAAGTAAGAGGAAAGAAAAAATAAGCAAAGATAAAACAAAAATACAGAAAAATATTATCGAAGAAATTGTAAAACAAGAAGAATCGAGTCAAAAAGCATTAAAAATATTGAAACCTTTACTCAGTGAAGATTGCAATGAGAGTGATGAAGTCCAAGAAATTCACTCTGAAACTATAAAATATATTAAGGAAATTGCCACGGATATACCTGATACTAAAATTGAAGTAATTCCTGCTAATGAAGCCAGTAACATTTTACTAGAAAGACGAGAAGACGTTAAAGCTAACATAAAATTAGATACTTCTTTTCCAATTATTGAAAATGTGCAACTAATTCAAGAAAAAGAAGAATTTCTTCCAATTAAAAAGTTTCCGCATAGCAAAATAAAGTCAACTGTGACAGAATCTGAATCGTTACAAGTAACAGAAGTAGAGCCAGCAGGAGCTATAAACGAATATTTCCAGAATTCGAGCAATGCAACTGAAAACATAGCTAACCGAAAAATAATTTTGTCGGAAAACATTATTACTTCCGAAACTCATGCAGCTGGGATACTGGATGATTTAGATACTCAACATGAAAATAAGCGTATGGAAACAGCAAAATCTACTTTAATTTTAAACAATGCAGTAAACGTCTCTCAGCATATTTTACCCACTGAAGAAAGACCTTTAGATGACTTGAAAATTAATGCATCAAGTGCAGAGATAGCATTTTCTCCACTCATTAGTTTAAATGTAATAGAAGTAAACGAAGATATGAAGGAAAAATACCTGGAAACTCCCGATATTGATAAAGGTCTGGTACCAAATCTAAATTTCAATTTACTTGAGCCAATTGAAGTAGGCGAAGTTTTTGTAGAAGACAAATCAGGTAAATACTACCCTGAACTAATTGTACCAACGGAAACAGCCCGTAAAGATGTTCTTGTATCTAACCAACTCATAACAGAAATTCATGATGTCCAAGAGAAGGAAGGAAATGTTTCAGATTTGAAAGTACCTCCAAAACAGGAAGCTAGAGTAGATATAGCAATAAAAGACAGCTTAATTATATCATTTGAAGAGCTAAATGAAAAAGAAGGCCACCTTCCAGTACAGGAAAAGCCTATACAACAATCAGCCCTTAAGGATGTAACTTTACATTCAAGTCTTGGTAATACTATAACGACAACACATATTAAAGAATCAGATTTTGCTCCATGTGATACTCCTAGTAGAAAAGCAATAATAACCATTAATGAACACCTGCACCAAACTAATTCTGAAACAACTACCGCTGATTCAGAGACGATACTTGAAAAATCAAAACCTACACCTGAAAGTCATGCCGACGTCTCTATAACAGCATTGGACAAAAATACTGTAGAAGAAGTTGATGTTCATGAAAAAGAATTTGAATTAGTGATTAAGGAGGACAAACAAATGGTAAAAGCTGATGTAGATATTAAATCCATTGAACCAATTGTCATGTCCGAAATTTTACATATCACGACCACTGATGAAATGGCTAAGCCTCAAGTAGTGCCGGAAGAGACCGCATCAAAATCTATCGAAATGACCAAGGCTAAAATAATCACTATACCTTTTATACATGAAAAGGAACAAAATGAAAACTTTTTGTCCAAAAAACCCGAAGAATTTGATACATCTTTGATCCCAGTTATGCCAATTACAGTTTTAGAAACACAACTGTCAGAATCGGAAAATAAACTTCATCTCAATAAAATTCCTAGTATTAGTCGCGCGGAATTTACACTCACTCATCAACTTAAAATTCCAGTTAAACAAGAAATTAATACTACTGATCAGATAGATTTCATGACTTTACCTAAAGAGAATACTGGAACAGCATCTATAAGCAGAGATTTACAAAAGGAAATAGCTGTAATTGAAACCACTGTAGAAGAACAATTAAATAAGTTAGAAGAAAATGAAATACAACATAACAAAGTAAAAACTGGTTATATTAGTAACGAAAGCATAAATGTGACTGAAATAATACCAAATATTCATGAAACAAAACTTACGATATCTGAGGAAAAAACAAAGCAGCTTGCTACTTTGGACATTAACTCAGATCATAAATTAGCAATAACTTCGGAGATAAACCTTAAAGAAAGGTTGGGAAACCTTAAGTCCACTATAATGGAAACCGAGGAAGCTAATTTAATATCAACTCATCTACAGTCCATACAAGTACTTGAAAACAATATTTTGGATAGTCAATCTACATTAGAAAATGACATCCACCCGTCCCCTAAAACAATTTCCTCTGAGATTGTTCCGTCTCAGGAAATCCTGAATATTACGGAGATTGTACAACATGAAAAAGAGGAGGAGTATGAATATTATAAGCTGCCTGACACGTCAACTGCTAACCCTTTTATAACTGGACACCTAGTTGCTGTTTCAACAGAAATATCACCGGATGTAGACGTAGGTGACACCGATATTGTTGTAGATGATGTTAAAACAGCTAATGTCAAAAACATAGCTTTTAATGAAATTATTATCAGTACAGTTGATTGGCATGAAAAAGAAGATGAAATTAAAACAACATCAACACCAACAACTGTTACAGCTTCAGTAGGATTAAACTCAAGTCAAGCATTACAAATTGATGAAAGAAGTACAGAAATAAAGCCTACATCACTCATACAAAATAAATTACCTTTTGCAAAAGCAGAACAAGATACTGTGATATCAGAAGCTTTAACTCAACAGGAAATTTTGGTACATTCCTCTGAAGGAATACTTTCCGATATAAACAAAAACCAAAGCGAAATGCCAGTTATATCTGTCAGCACACTACATCTACCACAATGTGATGAGAAGACACTTATTGAAACAGAAGACTATTTAAGAGACACGATATCACCAGAAATGCAGCATGCCGCAGTCGCTTTTAGATCCCAGCAAGGCATACAAACATCCGAAGTGCTATCACAATCACAAAGTCTTGAAGCATCTCAAGATTTTGATATGAAGTATAAAAATGCTGTATCAAAATTAGATGAAAATTATGGCAAAATTGCTAATTCTGAAGAATGTACTGTAAATCAATCAGTAGGAAAATTGCTCGAACCAGCTGTGAAACCGCAACATTCTGACTTAAACGCAATCTGTGAAAATGCCCTTGAAAGAACCGAAATTATTTTTGGGGAACGTGAGAGAGAATTAGATTTATGTAAGCCATTAGCTTCCAATATTACCCCTCATATTACAGAAATCCATGCAGTTGAGACAAACTCTACAATTATAGCAGAAAAAGAACAAGAGTTAGTTTCACAGAAAGCACCAAATGTTTTAGAAGCTTTTATAGAAGTAGTTCCGCACCAGAGTGCTATCGGCATGGAAGTATTAGCCTCGGGGAATATAAGCAAATTGGAAAGTAAAGACACAAAGCTTGTAAGTGCAGAAACAACGCAGGATAATTTACAAAGCTATGTTCAAGAAGAGATAGTACACGGAGAAAAAGAATTTGAATTTGTGGATACTAAGACAATAACTGCAAATGCTTCAGAAATAATTATACAAGAAAAGGCAAAGGAAACTTTAGAAGTTCAACCAATGGAAGCCGAAAAAGATCTTCGAGCAGCAATTCTAGATTCCGAAGTCAATGCCAAACTTGCTTTTAATGAACAGCAATCATTACAAGAGACAGAAATAGTTTCAAGTCAAGAAAGTCAGAGCTTTAGTATTTCAGATATTAATTTAGTAAACGTATCTACTGGTCACGAAATGCAAGAAGCAATAAAAGAATATGAGTTATTCATTGGAGAGGTAGAAAATACTTTTACAATACCGACTGCGGATGAGAAAATTGGTACTGGTACGGTTGAAGAACAAAAACCTTTGAATATAACTGTAATCATTGCAAATGAAAAAGAAAACACAATACAGGATACTCCTGTAGTTAAAAAAGAAACAACACAGCTTATTATTAATGGTAAAAACTACGTCGATGTAACAGAGGTAATGTTTTCTGAAAAAGAACAAACTTTTCATACTCACAATAATTTAGTAGAAGACAAATCAGTGGCACCAAAAACTGATATAATTTTAAAATCCAGTATAAATATTAACGAAACAAATGCAACAGAAGGCGATGTTCCATTTGAATCAGATAAAATCCAATATTTTGAAGCTAGCACAGATATTCACGCTAACGATCACCTACAGATATCAGAAAACATAACAGTTGAAAAAGAAATAGAAATAAAGCCGATGCTTTTCCCAAAAACGACTCTTAGCGAATTCAATATTAGTCCACATATGCATTTAAATGTTGAAATTCACCAATTTAATGAAAATGAAGAAGCACTTGAAGAAACGGAAATCGTTAAACAGGTAAAAAGTGATGTTTCGTTACAGACATTGAAACATCTGGAAGTTAGTGAGATTAATTTCGGAGAACAGTCAGAAAAGTTATTACAAGAACAAAAATCGAAAGATGCTAGCCCACACATTGGTATCGAAACTGGAGAGCATATTTTAATTACTGAAACGAATATTCAAGAATCTGAATCTACGTTGCATAGAAATACATCCAATATGTGCAAGCAAGGCAATTTTTCTGTTGAAAGTATATTACCCCTTCAAATTGAAGAGGCAATCGTTAAGGAAAAAGAAGGCAACTTGGCGGAGTTTGTGATAAAGACATCTGAAAAACCTGAAGTTACCATCAAAACTCAAAATTATTTAGTAATTTCCAATGATATAATTAGGGAATGTGGACGAAATATGGAGGATAGCCTAACTATACCATCCTTATCTTCTCAACAAGGTGTTGAAATAAATCCAGCTACACACATCACAGTAAGTGAGATGGTTCCTGTTGAAGGTACTGTTAGGTTTGCTGACACAACTGACACAAATACAGAAACTAAGGCAACTCCCAAGCAAGTGGTTAATACTGAGGTAGTTAACAATGACCACCAAACTATCGAAACTGTTAATAAGATCGTCCCTGACTATATGACAGAAAATAACAAAGCTCAGGTAGCAATAGAAGCACAAAAAAGCATTGTAACTTCTGAAGATTACCCTCAAGAAACCTCAGGACAAATCTTTACTACTACAGACAATAATTTCAAACAAGCTGCTCTAAATATAATTGAAATGAAACATGTTCAACAAACAGAAATTCTGCTTCACGAAGAAATAGGTAAGTTCGCTAAAAATCATGTTGATAATATACAGAAGGCAGACGAAAGTCACATCATACTATCTGAAATAACTCAAATAAAACCAGATGTGATAGATGACTTACGTGACATGTCTTCCGCAATAAAACCTCAAGTTGGAGAAGTTTCATTAGAAATTGAGGCACATAGATGCTACGAGACGACAGAAAACATAGCTCACGAAACATCGTACTCCATAACGCACGATAAAAACATAACCAAACAAGTTTCTGAATCTGTTTTAGAAGTAAAACCCTTAGAACAAACAGAAATAATAACAAGTGAACATACCGGGACTATAACAGCTAATTCAGTTGAAACACAAACAGTTACATTAAAATCAATAGAATTACAACCACTGAGTCAAAGTGAGGTTTTAGTCAATGAATCCGAAACGAATTTAATAGACATTGACAGAAAGCTTTCACTAAAGGAAAATGCTACTGTCAACTTTAACACTGCGCAAGGCTTAATTGTAGATCAGGTTCTAAATGAGGAGATTCCGTACGATTTTCGACCGAGTAATAATAAGCCATTGGTAGCTCAGCATAATATAACTCCATTAACACACATCGAATGTTCAGAAAACATTGCGGAGGCACGAACTAATCAATTCACCTCTGATAAAGTACATCTTCAAACACCAAAAATTAAATCAACCGAAATGATACCCTTAATAATAACTGACACTCAAAGTATGCAAATGGAAACAGAATTTAAGTCATCAAAACCAGAAGAACAAAAAATTAGAGAAAATTATATTATTGCTAACGAAACAGAAGTTATTTCTGAGTATTTTAATGAACAAACGGCTCCATGCTTTTATGAACCAGTCGATTTATTAAGAGAAGCAGATGAAAAAATTCAACACGATCAATCAAATCGGGTTCTTATCACAGAACAAGATGGGCTTGTTGATGACAAACTCGAGAGAATTTCAATATCTTCACGATCTGATGTTGAGGAAACGGAAGAAATAATCACTAAATTTGTTCAAACACCTGGCTATAGTGAGCCTCAACAAATTAAAACTAAAAGAACCATTCTCCGAAAGAAAAAGAGGGTTGGCGATGAAACAGGCGACGTCGTCATTGAAGAGACATTAGACGACGAAGATCTCAAAAAATCAATTAGGAAAACAAAACATGATCTGAATATTGTTGAATATGAAGGAGATGAATCGCAAATAATTGATGACTTAGAAAAAAGTAAAATTGAAATGCCAGATGAATTTCTACACATACCGAAGATGGCAACACATCTAATAATAGAAGACGTAACTGAACTCACTGAAACACTAAATGAGGTACTTCAAGAATCTGCTAGAAAAGTACACATCACGGAAAAGAAACCGGAAACAGATGATGTTCAAACCGTTAAATCAACTAAGCGCCTAATCAAAAAGAAAAAGGGATTGAATGAGGAAGTAACCGAAATCACCACAGTGCAGAAAGACGACGAGACTCCTATCAAGACGATCACTGTGATAGAAGAAATTACACCCGAAGAAAGCAAGCCAAAAGAAGTTATTGAGCTACCTGAAGAGGTAACAGTTGAGGACAGTAAGACACAAGAAGGTAAGCCAAAACAAAAGAAAATCACAAAGCGTACTATTAAAAAGCGGGTAGGGCCTAAAGTCGAAACTACACAAATCACCACTGAACAAGAAGACGATAAAGAACCTATAGTTTCTATTCAAACCACAGAGGAACTCATAGATGATTCAACTACACCACTCTCAGACATCGAACCTGATACCGCTCAGGTCGTCGAAGAAACCCCAGAGACAGTACAAATTACACAAGTCAAAACTGAAACAGGCGCGGACCAAACTGTCAAAACAACTAAGCGCGTAATCAAAAAAAGAAAAGGATCGAAAAATGAAGTCACCGAAATCACCACAGTCCAAAAAGACGACGACACCCCGCTAACGACGGTCACTGTGGTAGAAGAAACTACCCCTGAAGAGAGCAAGCCAGAAGAAATCATGGAGTTGCCTGAAGAGGTAACAGTTGAGGAAACTAAGACGAAAGAAGGTAAGCTGAAACAAAAGAAAATCATAAAGCGTATTATTAAGAAACGGGTAGGGCCTAAAGTTGAAACAACACAAATCACTACTGAACAAGAAGACGACAAACAACCAGTCGTTTCTATTCAAACCTCAGAGGAACTCATAGATGATACGACTACACCGCTCTCAGAAATCACTCCAGACACTGCTCAGGTCGTTGAAGAAACCCCTGAGAAAGTACACATTACACAAGTCAAAACTGAAACCGGCGATGTCCAAACCGTTAAAACCACTAAGCGAATAATCAAAAAGAGAAAAGGACCTAAGGAAGAAGTCACCGAAATCACTACAGTCCAAAAAGACGACGAGGCCCCTGTGACAAGTGTTACTGTAGTAGAAGAAACTACCCCCGAAGAGAGCAAGCCAGAAGAAGTTGTTGAGTTGCCTGAAGAGGTGACTGTTGAGGAAACTGAGACACCGGAAGGTAAGCCAAAACAAAAGAAAATCACAAAGCGCATTATTAAAAAGCGGAAAGGACCTAAAGTCGAAACTACACAAATTACAACTGAGCAAGAAGACGACAAACAACCAGTCGTTTCAATTCAAACCACAGAGGAAGTCGTAGACGACACGACTACACCACTCTCAGATATTACACCAGACACTGCTCAGGTCGTTGAAGAAACTCCTGAGAAAGTACATATTACACAAGTCAAAACTGAAACCGGCGATGTCCAAACCGTTAAAACCACTAAGCGAATAATCAAAAAGAGAAAAGGACCTAAGGAAGAAGTCACCGAAATCACCACAGTCCAAAAAGACGACGAGGCCCCTGTTACAAGTGTTACTGTAGTAGAAGAATCTACCCCTGAAGAAAGCAAGCCGGAAGAAGTTATTGAGTTGCCTGAAGAGGTGACTGTTGAGGAAACTGAGACGAAAGAAGGTAAGCCGAAACAAAAGAAAATCATAAAGCGTATTATTAAGAAACGGGTAGGGCCTAAAGTTGAAACAACACAAATCACTACTGAGCAAGAAGACGACAAACAACCAGTCGTTTCAATTCAAACCACAGAGGAACTCATAGATGACACGACTACACCGCTCTCAGAAATCACTCCAGACATTGCTCAGGTCGTTGAAGAAACCCCTGAGAAAGTACACATTACACAAGTCAAAACTGAAACCGGCGATGTCCAAATCGTTAAAACCACTAAGCGAATAATCAAAAAGAGAAAAGTACCTAAGGAAGAAGTCACCGAAATCACCACAGTCCAAAAAGACGACGAGGCCCCTGTTACAAGTGTTACTGTAGTAGAAGAAACTACCCCCGAAGAGAGCAAGCCGGAAGAAGTTATTGAGTTGCCTGAAGAGGTGACTGTTGAGGAAACTGAGACGAAAGAAGGTAAGCCGAAACAAAAGAAAATCATAAAGCGTATTATTAAGAAACGGGTAGGGCCTAAAGTTGAAACAACACAAATCACTACTGAGCAAGAAGACGACAAACAACCAGTCGTTTCAATTCAAACCACAGAGGAACTCATAGATGACACGACTACACCGCTCTCAGAAATCACTCCAGACACTGCTCAGGTCGTTGAAGAAACCCCTGAGAAAGTACACATTACACAAGTCAAAACTGAAACCGGCGATGTCCAAACCGTTAAAACCACTAAGCGAATAATCAAAAAGAGAAAAGGACCTAAGGAAGAAGTCACCGAAATCACTACAGTCCAAAAAGACGACGAGGCCCCTGTTACAAGTGTTACTGTAGTAGAAGAAACTACCCCCGAAGAGAGCAAGCCGGAAGAAGTTATTGAGTTGCCTGAAGAGGTAACAGTTGAGGAAACTAAGACGAAAGAAGGTAAGCCAAAACAAAAGAAAATCACAAAGCGCATTATTAAAAAGCGGAAAGGACCTAAAGTCGAAACTACACAAATTACTACTGAGCAAGAAGACGAAAAACAACCAGTCGTTTCAATTCAAACCACAGAGGAACTCATAGATGACACGACTACACCGCTCTCAGAAATCACTCCAGACACTGCTCAGGTCGTTGAAGAAACCCCTGAGAAAGTACACATTACACAAGTCAAAACTGAAACCGGCGATGTCCAAACCGTTAAAACCACTAAGCGAATAATCAAAAAGAGAAAAGGACCTAAGAAAGAAGTCACCGAAATCACCACAGTCCAAAAAGACGACGAGGCCCCTGTTACAAGTGTTACTGTAGTAGAAGAAACTACCCCCGAAGAGAGCAAGCCAGAAGAAGTTGTTGAGTTGCCTGAAGAGGTGACTGTAGAGGAAACTGAGACACATGAAGGTAAGCCAAAAATAAAGAAAATCACAAAGCGCATTATTAAAAAGCGGAAAGGACCTAAAGTCGAAACTACACAAATTACTACTGAGCAAGAAGACGACAAACAACCAGTCGTTTCAATTCAAACCACAGAGGAACTCGTAGATGACACGACTACACCACTCTCAGATATTACACCAGACACTGCTCAGGTCGTTGAAGAAACTCCTGAGAAAGTACACATTACACAAGTCAAAACTGAAACCGGTGATGTCCAAACCGTTAAAACCACTAAGCGAATAATCAAAAAGAGAAAAGGACCTAAGGAAGAAGTCACCGAAATCACCACAGTCCAAAAAGACGACGAGGCCCCTGTTACAAGTGTTACTGTAGTAGAAGAAACTACCCCCGAAGAGAGCAAGCCGGAAGAAGTTATTGAGTTGCCTGAAGAGGTAACAGTTGAGGAAACTGAGACGAAAGAAGGTAAGCCGAAACAAAAGAAAATCATAAAGCGTATTATTAAGAAACGGGTAGGGCCTAAAGTTGAAACAACACAAATCACTACTGAGCAAGAGGATGACAAACAACCAGTCGTTTCAATTCAAACCACAGAGGAACTCATAGATGACACGACTACACCGCTCTCAGACATCACTACAGACACTGCTCAGGTCGTTGAAGAAACCCCTGAGAAAGTACACATTACACAAGTCAAAACTGAAACCGGCGATGTCCAAACCGTTAAAACCACTAAGCGAATAATCAAAAAGAGAAAAGGACCTAAGGAAGAAGTCACCGAAATCACCACAGTCCAAAAAGACGACGAGGCCCCTGTTACAAGTGTTACTGTAGTAGAAGAATCTACCCCTGAAGAAAGCAAGCCGGAAGAAGTTATTGAGTTGCCTGAAGAGGTGACTGTAGAAGAAACTGAGACACAGGAAGGTAAGCCAAAACAAAAGAAAATCACAAAGCGTATTATTAAGAAAAGGGTAGGACCTAAAGTCGAAACTACACAAATCACTACTGAGCAAGAAGACGACAAACAACCAGTCGTTTCAATTCAAACCACAGAGGAACTCATAGATGACACGACTACACCGCTCTCAGAAATCACTCCAGACACTGCTCAGGTCGTTGAAGAAACTCCTGAGAAAGTACACATTACACAAGTCAAAACCGAAACCGGCGATGTCCAAACCGTGAAAACCACTAAGCGAATAATCAAAAAGAGAAAAGGACCTAAGCAAGAAGTCACCGAAATCACCACAGTCCAAAAAGACGACGAGGCCCCTGTTACAAGTGTTACTGTAGTAGAAGAAACTACCCCCGAAGAGAGCAAGCCGGAAGAAGTTATTGAGTTGCCTGAAGAGGTAACAGTTGAGGAAACTGAGACGAAAGAAGGTAAGCCGAAACAAAAGAAAATCGTAAAGCGTATTATTAAGAAACGGGTAGGACCTAAAGTCGAAACTACACAAATCACTACTGAGCAAGAAGACAACAAACAACCAGTCGTTTCTGTTCAAACCACAGAGGAACTATAGATGACACAACTACACAACTCTCAGATATCACACCAGATACTGCTCAGGTCGTTGAAGAAACCCCTGAGAAAGTACACATTACACAAGTCAAAACCGAAACCGGCGATTTTCAAACCATTAAAACCACTAAGCGCATAATCAAAAAGAGAAAAGGACCTAAAGAAGAAGTCACCGAAATCACCACAGTCCAAAAAGACGACGAGGCCCCTGTGACAAGTGTTACTGTAGTAGAAGAAACTACCCCCGAAGAGAGCAAGCCAGAAGAAGTTGTTGAGTTGCCTGAAGAGGTGACTGTAGAGGAAACTGAGACGAAAGAAGGTAAGCCGAAACAAAAGAAAATCACAAAGCGAATCATTAAGAAACGGGTAGGGCCTAAAGTTGAAACAACACAAATCACTACTGAGCAAGAAGACGACAAACAACCAGTCGTTTCTGTTCAAACCACAGAGGAACTCGTAGATGACACAACTACACCACTCTCAGATATCACACCAGATACTGCTCAGGTCGTTGAAGAAACCCCTGAGAAAGTACACATTACACAAGTCAAAACTGAAACCGGCGATGTCCAAACCATTAAAACCACTAAGCGCATAATCAAAAAGAGAAAAGGACCTAAAGAAGAAGTCACCGAAATCACCACAGTCCAAAAAGACGACGAGGCCCCTGTTACAAGTGTTTCTGTGATAGAAGAAACTACCCCCGAAGAGAGCAAGCCAGAAGAAGTTATTGAGTTGCCTGAAGAGGTGACTGTAGAGGAAACTGAGACGAAAGAAGGTAAGCCGAAACAAAAGAAAATCACAAAGCGAATCATTAAGAAACGGGTAGGGCCTAAAGTTGAAACAACACAAATCACTACTGAGCAAGAAGACGACAAACAACCAGTCGTTTCAATTCAAACCACAGAGGAACTCATGGATGACACTACTACACTGCTCTCAGAAATCACTCCAGACACTGCTCAGGTCGTTGAAGAAACCCCTGAGAAAGTACACATTACACAAGTCAAAACTGAAACCGGCGATGTCCAAACCATTAAAACCACTAAGCGCATAATCAAAAAGAGAAAAGGACCTAAAGAAGAAGTCACCGAAATCACCACAGTCCAAAAAGACGACGAGGCCCCTGTTACAAGTGTTTCTGTGATAGAAGAAACTACCCCCGAAGAGAGCAAGCCGGAAGAAGTTATTGAGTTGCCTGAAGAGGTAACAGTTGAGGAAACTAAGACGAAAGAAGGTAAGCCAAAACAAAAGAAAATCACAAAGCGCATTATTAAAAAGCGGAAAGGACCTAAAGTCGAAACTACACAAATTACTACTGAGCAAGAAGACGACAAACAACCAGTCGTTTCAATTCAAACCACAGAGGAACTCATGGATGACACTACTACACTGCTCTCAGAAATCACTCCAGACACTGCTCAGGTCGTTGAAGAAACCCCTGAGAAAGTACACATTACACAAGTCAAAACTGAAACCGGCGATGTCCAAACCATTAAAACCACTAAGCGCATAATCAAAAAGAGAAAAGGACCTAAAGAAGAAGTCACCGAAATCACCACAGTCCAAAAAGACGACGAAGCCCCTGTGACAAGTGTTACTGTAGTAGAAGAAACTACCCCCGAAGAGAGCAAGCCAGAAGAAGTTATTGAGTTGCCTGAAGAGGTGACTGTAGAGGAAACTGAGACGAAAGAAGGTAAGCCGAAACAAAAGAAAATCACAAAGCGAATCATTAAGAAACGGGTAGGGCCTAAAGTTGAAACAACACAAATCACTACTGAGCAAGAAGACGACAAACAACCAGTCGTTTCAATTCAAACCACAGAGGAACTCATGGATGACACTACTACACTGCTCTCAGAAATCACTCCAGACACTGCTCAGGTCGTTGAAGAAACCCCTGAGAAAGTACACATTACACAAGTCAAAACTGAAACCGGCGATGTCCAAACCATTAAAACCACTAAGCGCATAATCAAAAAGAGAAAAGGACCTAAAGAAGAAGTCACCGAAATCACCACAGTCCAAAAAGACGACGAGGCCCCTGTTACAAGTGTTTCTGTGATAGAAGAAACTACCCCCGAAGAGAGCAAGCCAGAAGAAGTTATTGAGTTGCCTGAAGAGGTGACTGTAGAAGAAACTGAGACACAGGAAGGTAAGCCAAAACAAAAGAAAATCACAAAGCGTATTATTAAGAAAAGGGTAGGACCTAAAGTCGAAACTACACAAATCACTACTGAGCAAGAAGACGACAAACAACCAGTCGTTTCTATTCAAACCACAGAGGAACTCGTAGATGACACAACTACACCACTCTCAGATATCACACCAGATACTGCTCAGGTCGTTGAAGAAACCCCTGAGAAAGTACACATTACACAAGTCAAAACCGAAACCGGCGATGTTCAAACCGTTAAAACCACTAAGCGAATAATCAAAAAGAGAAAAGGACCTAAGGAAGAAGTCACCGAAATCACCACAGTCCAAAAAGACGACGAGGCCCCTGTTACAAGTGTTACTGTAGTAGAAGAAACTACCCCCGAAGAGAGCAAGCCGGAAGAAGTTATTGAGTTGCCTGAAGAAGTGACTGTTGAGGAAACTGAGACGAAAGAAGGTAAGCCGAAACAAAAGAAAATCATAAAGCGTATTATTAAGAAACGGGTAGGACCTAAAGTTGAAACAACACAAATCACTACTGAGCAAGAAGACGACAAACAACCAGTCGTTTCTATTCAAACCACAGAGGAACTCGTAGATGACACAACTACACCACTCTCAGATATCACACCAGATACTGCTCAGGTCGTTGAAGAAACCCCTGAGAAAGTACACATTACACAAGTCAAAACTGAAACTGGCGATGTCCAAACCGTTAAAACCACTAAGCGCATAATCAAAAAGAGAAAAGGACCTAAGGAAGAAGTCACCGAAATCACCACAGTCCAAAAAGACGACGAGGCCCCTGTTACAAGTGTTACTGTAGTAGAAGAATCTACCCCTGAAGAAAGCAAGCCGGAAGAAGTTATTGAGTTGCCTGAAGAGGTGACTGTAGAAGAAACTGAGACACAGGAAGGTAAGCCAAAACAAAAGAAAATCACAAAGCGTATTATTAAGAAAAGGGTAGGACCTAAAGTCGAAACTACACAAATCACTACTGAGCAAGAAGACGACAAACAACCAGTCGTTTCAATTCAAACCACAGAGGAACTCGTAGATGACACAACTACACCACTCTCAGATATTACACCAGACACTGCTCAGGTCGTTGAAGAAACCCCTGAGAAAGTACACATTACACAAGTCAAAACCGAAACTGGCGATGTTCAAACCGTTAAAACCACTAAGCGCATAATCAAAAAGAGAAAAGGACCTAAGGAAGAAGTCACCGAAATCACTACAGTCCAAAAAGACGACGAGGCCCCTGTGACAAGTGTTACTGTAGTAGAAGAAACTACCCCCGAAGAGAGCAAGCCGGAAGAAGTTATTGAGTTGCCTGAAGAGGTGACTGTAGAAGAAACTGAGACACCGGAAGGTAAGCCAAAACAAAAGAAAATCACAAAGCGCATTATTAAGAAAAGGGTAGGACCTAAAATCGAAACTACACAAATCACTACTGAACAAGAAGACGACAAACAACCAGTCGTTTCTGTTCAAACCACAGAGGAACTCATAGATGACACAACTACACCACTCTCAGATATCACACCAGATACTGCTCAGGTCGTTGAAGAAACCCCTGAGAAAGTACAAATTACACAAGTCAAAACTGAAACAGGCGATGTCCAAACCGTTAAAACCACTAAGCGCATAATCAAAAAGAGAAGAGGACCTAAGGAAGAAGTCACCGAAATCACCATAGTCCAAAAAGACGACGAGGCCCCTGTTACAAGTGTTACTGTAGTAGAAGAATCTACCCCTGAAGAAAGCAAGCCGGAAGAAGTTATTGAGTTGCCTGAAGAAGTGACTGTTGAGGAAACTGAGACGAAAGAAGGTAAGCCGAAACAAAAGAAAATCACAAAGCGAATCATTAAGAAACGGGTAGGGCCTAAAGTTGAAACAACACAAATCACTACTGAACAAGAAGACGACAAACAACCAGTCGTTTCTATTCAAACCACAGAGGAACTCGTAGATGACACAACTACACCACTCTCAGATATTACACCAGACACTGCTCAGGTCGTTGAAGAAACCCCTGAGAAAGTACACATTACACAAGTCAAAACTGAAACCGGCGATGTCCAAACCATTAAAACCACTAAGCGCATAATCAAAAAGAGAAAAGGACCTAAAGAAGAAGTCACCGAAATCACCACAGTCCAAAAAGACGACGAGGCCCCTGTTACAAGTGTTTCTGTGATAGAAGAAACTACCCCCGAAGAGAGCAAGCCAGAAGAAGTTCTTGAGTTGCCTGAAGAAGTGACTGTTGAGGAAACTGAGACGAAAGAAGGTAAGCCGAAACAAAAGAAAATCACAAAGCGAATCATTAAAAAACGGGTAGGGCCTAAAGTTGAAACAACACAAATCACTACTGAACAAGAAGACGACAAACAACCAGTCGTTTCTATTCAAACCACAGAGGAACTCGTAGATGACACAACTACACCACTCTCAGATATCACACCAGATACTGCTCAGGTCGTTGAAGAAACCCCTGAGAAAGTACAAATTACACAAGTCAAAACTGAAACAGGCGATGTCCAAACCGTTAAAACCACTAAGCGAATAATCAAAAAGAGAAAAGGACCTAAGGAAGAAGTCACCGAAATCACCACAGTCCAAAAAGACGACGAGGCCCCGGTTACGACGGTCACTGTGGTAGAAGAAACTACCCCCGAAGAGAGCAAGGCAGATGAAGTTGTTGAGTTGCCTGAAGAGGTGACTGTAGAGGAAACTGAGACACAGGAAGGTAAGCCAAAACAAAAGAAAATCACGAAGCGTATTATTAAAAAGCGGGTAGGGCCTAAAGTCGAAACTACACAAATCACTACTGAACAAGAAGACGACAAACAACCAGTCGTTTCTATTCAAACCACAGAGGAACTCGTAGATGACACAACTACACCACTCTCAGATATTACACCAGACACTGCTCAGGTCGTTGAAGAAACCCCTGAGAAAGTACACATTACACAAGTCAAAACTGAAACTGGCGATGTCCAAACCGTTAAAACCACTAAGCGCATAATCAAAAAGAGAAAAGGACCTAAGGAAGAAGTCACCGAAATCACCACAGTCCAAAAAGACGACGAGGCCCCTGTGACAAGTGTTACTGTAGTAGAAGAAACTACCCCCGAAGAGAGCAAGCCAGAAGAAATTGTTGAGTTGCCTGAAGAGGTGACTGTTGAGGAAACTGAGACACCGGAAGGTAAGCCAAAACAAAAGAAAATCATAAAGCGTATTATTAAGAAACGGGTAGGACCTAAAGTTGAAACAACACAAATCACTACTGAGCAAGAAGACGACAAACAACCAGTCGTTTCTATTCAAACCACAGAGGAACTCGTAGATGACACAACTACACCACTCTCAGATATCACACCAGATACTGCTCAGGTCGTTGAAGAAACCCCTGAGAAAGTAAACATTACACAAGTCAAAACCGAAACCGGCGATGTCCAAACCGTTAAAACCACTAAGCGCGTTATCAAAAAGAGAAAAGGACCTAAGGAAGAAGTTACGGAAATCACCACAGTCCAAAAAGACGACGAGGCCCCTGTTACAAGTGTTACTGTAGTAGAAGAAACTACCCCCGAAGAGAACAAGCCAGAAGAAGTTGTTGAGTTACCTGAAGAGGTAACTGTAGAGGAAACTGAGACACAGGAAGGTAAGCCAACACAAAAGAAAATCACAAAGCGCATTATTAAGAAAAGGGTGGGACCTAAAATCGAAACTACACAAATCACTACTGAACAAGAAGACGACAAACAACCAGTCGTTTCTGTTCAAACCACAGAGGAACTCATAGATGACACAACTACACCACTCTCAGATATCACACCAGATACTGCTCAGGTCGTTGAAGAAACCCCTGAGAAAGTACACATTACACAAGTCAAAACCGAAACCGGCGATGTTCAAACCGTTAAAACCCTTAAGCGCGTTATCAAAAATAAAAAGGGACCGAAAGAGGAAGTCACCGAAATCACCACAGTCCAAAAAGACGACGAGGCCCCGGTTACGACGGTCACTGTGGTAGAAGAAACTACCCCCGAAGAGAGCAAGGCAGATGAAGTTGTTGAGTTGCCTGAAGAGGTGACTGTAGAGGAAACTGAGACACAGGAAGGTAAGCCAAAACAAAAGAAAATCACGAAGCGTATTATTAAAAAGCGGGTAGGGCCTAAAGTCGAAACTACACAAATCACTACTGAACAAGAAGACGACAAAGAACCAGTCGTTTCTGTTCAAACCACAGAGGAACTCATAGATGACACAACTACACCACTCTCAGATATCACACCAGATACTGCTCAGGTCGTTGAAGAAACCCCTGAGAAAGTACAAATTACACAAGTCAAAACTGAAACCGGCGATGTCCAAACTGTTAAAACCACTAAGCGCATAATCAAAAAGAGAAAAGGACCTAAGGAAGAAGTCACCGAAATCACTACAGTCCAAAAAGACGACGAGGCCCCTGTGACAAGTGTTACTGTAGTAGAAGAAACTACCCCCGAAGAGAGCAAGCCAGAAGAAGTTGTTGAGTTGCCTGAAGAGGTGACTGTTGAGGAAACTGAGACACATGAAGGTAAGCCAAAAATAAAGAAAATCACAAAGCGCATTATTAAGAAACGGGTAGGACCTAAAATCGAAACTACACAAATCACTACTGAACAAGAAGACGACAAACAACCAGTCGTTTCTATTCAAACCACAGAGGAACTCGTAGATGACACAACTACACCACTCTCAGACATTACACCAGATACTGCTCAGGTCGTTGAAGAAACCCCTGAGAAAGTACAAATTACACAAGTCAAAACTGAAACCGGCGATGTCCAAACCGTTAAAACCACTAAGCGCATAATCAAAAAGAGAAGAGGACCTAAGGAAGAAGTCACCGAAATCACCATAGTCCAAAAAGACGACGAGGCCCCTGTGACAAGTGTTACTGTAGTAGAAGAAACTACCCCCGAAGAGAGCAAGCCAGAAGAAGTTGTTGAGTTGCCTGAAGAGGTGACTGTAGAGGAAACTGAGACACCGGAAGGTAAGCCAAAACAAAAGAAAATCATAAAGCGTATTATTAAGAAACGGGTAGGACCTAAAGTTGAAACAACACAAATCACTACTGAGCAAGAAGACGACAAACAACCAGTCGTTTCTATTCAAACCACAGAGGAACTCGTAGATGACACAACTACACCACTCTCAGACATTACACCAGATACTGCTCAGGTCGTTGAAGAAACCCCTGAGAAAGTACACATTACACAAGTCAAAACCAAAACCGGCGATGTTCAAACCGTTAAAACCACTAAGCGCGTTATCAAAAAGAAAAAGGGACCGAAAGAGGAAGTCACCGAAATCACTACAGTCCAAAAAGACGACGAGGCCCCGGTAACGACAGTCACTGTGGTAGAAGAAACTACCCCCCAAGAGAGCAAGCCAGAAGAAGTTGTTGAGTTACCTGAAGAGGTGACTGTGGAGGAAACTGAGACACAGGAAGGTAAGCCAAAACAAAAGAAAATCACGAAGCGTATTATTAAAAAGCGGGTAGGGCCTAAAGTCGAAACTACACAAATCACCACTGAACAAGAAGACGACAAACAACCAGTCGTTTCTGTTCAAACCACAGAGGAACTTATAGATGACACAACTACACCACTCTCAGATATTACACCAGACACTGCTCAGGTCGTTGAAGAAACCCCTGAGAAAGTACACATTACACAAGTCAAAACTGAAACCGGCGATGTCCAAACCGTTAAAACCACTAAGCGAATAATCAAAAAGAGAAAAGGACCTAAGGAAGAAGTCACCGAAATCACCACAGTCCAAAAAGACGACGAGGCCCCTGTGACAAGTGTTACTGTAGTAGAAGAAACTACCCCCGAAGAGAGCAAGCCAGAAGAAATTGTTGAGTTGCCTGAAGAGGTGACTGTTGAGGAAACTGAGACACCGGAAGGTAAGCCAAAACAAAAGAAAATCATAAAGCGTATTATTAAGAAACGGGTAGGACCTAAAGTTGAAACAACACAAATCACTACTGAGCAAGAAGACGACAAACAACCAGTCGTTTCTATTCAAACCACAGAGGAACTCGTAGATGACACAACTACACCACTCTCAGATATTACACCAGACACTGCTCAGGTCGTTGAAGAAACTCCTGAGAAAGTACACATTACACAAGTCAAAACTGAAACCGGCGATGTCCAAACCGTTAAAACCACTAAGCGCGTGATCAAAAAGAGAAAAGGACCTAAGGAAGAAGTCACCGAAATCACCACAGTCCAAAAAGACGACGAGGCCCCTGTGACAAGTGTTACTGTAGTAGAAGAAACTACCCCCGAAGAGAGCAAGCCAGAAGAAGTTGTTGAGTTGCCTGAAGAGGTGACTGTAGAGGAAACTGAGACACCGGAAGGTAAGCCAAAACAAAAGAAAATCATAAAGCGTATTATTAAGAAACGGGTAGGACCTAAAGTTGAAACAACACAAATCACTACTGAGCAAGAAGACGACAAACAACCAGTCGTTTCTATTCAAACCACAGAGGAACTCGTAGATGACACAACTACACCACTCTCAGACATTACACCAGATACTGCTCAGGTCGTTGAAGAAACCCCTGAGAAAGTACACATTACACAAGTCAAAACCAAAACCGGCGATGTTCAAACCGTTAAAACCACTAAGCGCGTTATCAAAAAGAAAAAGGGACCGAAAGAGGAAGTCACCGAAATCACTACAGTCCAAAAAGACGACGAGGCCCCTGTGACAAGTGTTACTGTAGTAGAAGAAACTACCCCCGAAGAGAGCAAGCCAGAAGAAGTTGTTGAGTTGCCTGAAGAGGTGACTGTAGAGGAAACTGAGACGAAAGAAGGTAAGCCGAAACAAAAGAAAATCACAAAGCGAATCATTAAGAAACGGGTAGGGCCTAAAGTTGAAACAACACAAATCACTACTGAACAAGAAGACGACAAACAACCAGTCGTTTCAATTCAAACCACAGAGGAACTCGTAGATGACACAACTACACCACTCTCAGATATTACACCAGACACTGCTCAGGTCGTTGAAGAAACCCCTGAGAAAGTACACATTACACAAGTCAAAACTGAAACCGGCGATGTCCAAACCGTTAAAACCACTAAGCGAATAATCAAAAAGAGAAAAGGACCGAAAGAGGAAGTCACCGAAATCACTACAGTCCAAAAAGACGACGAGGCCCCTGTGACAAGTGTTACTGTAGTAGAAGAAATTACCCCCGAAGAGAGCAAGCCAGAAGAAGTTGTTGAGTTGCCTGAAGAGGTGACTGTAGAGGAAACTGAGACACATGAAGGGCCTAAAATCGAAACTACACAAATCACCACTGAACAAGAAGACGACAAACAACCAGTCGTTTCTATTCAAACCACAGAGGAACTCGTAGATGACACAACTACACCACTCTCAGATATTACACCAGACACTGCTCAGGTCGTTGAAGAAACCCCTGAGAAAGTACACATTACACAAGTCAAAACTGAAACCGGCGATGTCCAAACCGTTAAAACCACTAAGCGAATAATCAAAAAGAGAAAAGGACCTAAGGAAGAAGTCACCGAAATCACAACAGTCCAAAAAGACGATGAGGCCCCTGTGACAAGTGTTACTGTAGTAGAAGAAACTACCCCCGAAGAGAGCAAGCCAGAAGAAGTTGTTGAGTTGCCTGAAGAGGTGACTGTTGAGGAAACTGAGACACCGGAAGGTAAGCCAAAACAAAAGAAAATCATAAAGCGTATTATTAAGAAACGGGTAGGACCTAAAGTTGAAACAACACAAATCACTACTGAGCAAGAAGACGACAAACAACCAGTCGTTTCTATTCAAACCACAGAGGAACTCGTAGATGACACAACTACACCACTCTCAGATATTACACCAGACACTGCTCAGGTCGTTGAAGAAACCCCTGAGAAAGTACACATTACACAAGTCAAAACTGAAACCGGCGATGTCCAAACCGTTAAAACCACTAAGCGAATAATCAAAAAGAGAAAAGGACCTAAGGAAGAAGTCACCGAAATCACAACAGTCCAAAAAGACGATGAGGCCCCTGTGACAAGTGTTAATGTAGTAGAAGAAACTACCCCCGAAGAGAGCAAGCCAGAAGAAGTTGTTGAGTTGCCTGAAGAGGTGACTGTAGAGGAAACTGAGACACCGGAAGGTAAGCCAAAACAAAAGAAAATCATAAAGCGTATTATTAAGAAACGGGTAGGACCTAAAGTTGAAACAACACAAATCACTACTGAGCAAGAAGACGACAAACAACCAGTCGTTTCTATTCAAACCACAGAGGAACTCGTAGATGACACAACTACACCACTCTCAGATATTACACCAGACACTGCTCAGGTCGTTGAAGAAACTCCTGAGAAAGTACACATTACACAAGTCAAAACTGAAACCGGCGATGTCCAAACCGTTAAAACCACTAAGCGCGTGATCAAAAAGAGAAAAGGACCTAAGGAAGAAGTCACCGAAATCACCACAGTCCAAAAAGACGACGAGGCCCCTGTGACAAGTGTTACTGTAGTAGAAGAAACTACCCCCGAAGAGAGCAAGCCAGAAGAAGTTGTTGAGTTGCCTGAAGAGGTGACTGTAGAGGAAACTGAGACACCGGAAGGTAAGCCAAAACAAAAGAAAATCATAAAGCGTATTATTAAGAAACGGGTAGGACCTAAAGTTGAAACAACACAAATCACTACTGAGCAAGAAGACGACAAACAACCAGTCGTTTCTATTCAAACCACAGAGGAACTCGTAGATGACACAACTACACCACTCTCAGACATTACACCAGATACTGCTCAGGTCGTTGAAGAAACCCCTGAGAAAGTACACATTACACAAGTCAAAACCAAAACCGGCGATGTTCAAACCGTTAAAACCACTAAGCGCGTTATCAAAAAGAAAAAGGGACCGAAAGAGGAAGTCACCGAAATCACTACAGTCCAAAAAGACGACGAGGCCCCTGTGACAAGTGTTACTGTAGTAGAAGAAACTACCCCCGAAGAGAGCAAGCCAGAAGAAGTTGTTGAGTTGCCTGAAGAGGTGACTGTAGAGGAAACTGAGACGAAAGAAGGTAAGCCGAAACAAAAGAAAATCACAAAGCGAATCATTAAGAAACGGGTAGGGCCTAAAGTTGAAACAACACAAATCACTACTGAACAAGAAGACGACAAACAACCAGTCGTTTCAATTCAAACCACAGAGGAACTCGTAGATGACACAACTACACCACTCTCAGATATTACACCAGACACTGCTCAGGTCGTTGAAGAAACCCCTGAGAAAGTACACATTACACAAGTCAAAACTGAAACCGGCGATGTCCAAACCGTTAAAACCACTAAGCGAATAATCAAAAAGAGAAAAGGACCGAAAGAGGAAGTCACCGAAATCACTACAGTCCAAAAAGACGACGAGGCCCCTGTGACAAGTGTTACTGTAGTAGAAGAAATTACCCCCGAAGAGAGCAAGCCAGAAGAAGTTGTTGAGTTGCCTGAAGAGGTGACTGTAGAGGAAACTGAGACACATGAAGGTAAGCCAAAACAAAAGAAAATCACAAAGCGTATTATTAAAAAGCGGGTAGGGCCTAAAATCGAAACTACACAAATCACCACTGAACAAGAAGACGACAAACAACCAGTCGTTTCTATTCAAACCACAGAGGAACTCGTAGATGACACAACTACACCACTCTCAGATATTACACCAGACACTGCTCAGGTCGTTGAAGAAACCCCTGAGAAAGTACACATTACACAAGTCAAAACTGAAACCGGCGATGTCCAAACCTGTTACTGTAGTAGAAGAAACTACCCCGAAGAGAGCAAGCCAGAAGAAGTTGTTGAGTTGCCTGAAGAGGTGACTGTTGAGGAAACTGAGACACCGGAAGGTAAGCCAAAACAAAAGAAAATCATAAAGCGTATTATTAAGAAACGGGTAGGACCTAAAGTTGAAACAACACAAATCACTACTGAGCAAGAAGACGACAAACAACCAGTCGTTTCTATTCAAACCACAGAGGAACTCGTAGATGACACAACTACACCACTCTCAGATATTACACCAGACACTGCTCAGGTCGTTGAAGAAACCCCTGAGAAAGTACACATTACACAAGTCAAAACTGAAACTGGCGATGTCCAAACCGTTAAAACCACTAAGCGAATAATCAAAAAGAGAAAAGGACCTAAGGAAGAAGTCACCGAAATCACAACAGTCCAAAAAGACGATGAGGCCCCTGTGACAAGTGTTACTGTAGTAGAAGAAACTACCCCCGAAGAGAGCAAGCCAGAAGAAGTTGTTGAGTTGCCTGAAGAGGTGACTGTAGAGGAAACTGAGACGAAAGAAGGTAAGCCGAAACAAAAGAAAATCACAAAGCGCATTATTAAGAAAAGGGTAGGGCCTAAAGTTGAAACAACACAAATCACTACTGAACAAGAAGACGACAAACAACCAGTCGTTTCTATTCAAACCACAGAGGAACTCGTAGATGACACAACTACACCACTCTCAGATATTACACCAGACACTGCTCAGGTCGTTGAAGAAACCCCAGAGAAAGTACACATTACACAAGTCAAAACTGAAACCGGCGATATTCAAACCGTTAAAACCACTAAGCGCGTTATCAAAAAGAAAAAGGGACCGAAAGAGGAAGTCACCGAAATCACTACAGTCCAAAAAGACGACGAGGCCCCTGTGACAAGTGTTACTGTAGTAGAAGAAACTACCCCCGAAGAGAGCAAGCCAGAAGAAGTTGTTGAGTTGCCTGAAGAGGTGACTGTAGAGGAAACTGAGACACAGGAAGGTAAGCCAAAACAAAAGAAAATCACAAAGCGTATTATTAAAAAGCGGGTAGGGCCTAAAATCGAAACTACACAAATCACCACTGAACAAGAAGACGACAAACAACCAGTCGTTTCTATTCAAACCACAGAGGAACTCGTAGATGACACAACTACACCACTCTCAGATATTACACCAGACACTGCTCAGGTCGTTGAAGAAACCCCAGAGAAAGTACACATTACACAAGTCAAAACTGAAACCGGCGATATTCAAACCGTTAAAACCACTAAGCGCGTTATCAAAAAGAAAAAGGGACCGAAAGAGGAAGTCACCGAAATCACTACAGTCCAAAAAGACGACGAGGCCCCTGTGACAAGTGTTACTGTAGTAGAAGAAACTACCCCCGAAGAGAGCAAGCCAGAAGAAGTTGTTGAGTTGCCTGAAGAGGTGACTGTAGAGGAAACTGAGACACAGGAAGGGCCTAAAATCGAAACTACACAAATCACCACTGAACAAGAAGACGACAAACAACCAGTCGTTTCTATTCAAACCACAGAGGAACTCGTAGATGACACAACTACACCACTCTCAGATATCACACCAGATACTGCTCAGGTCGTTGAAGAAACCCCTGAGAAAGTACAAATTACACAAGTCAAAACTGAAACCGGCGATGTCCAAACCGTTAAAACCACTAAGCGCATAATCAAAAAGAGAAAAGGACCTAAGGAAGAAGTCACCGAAATCACCACAGTCCAAAAAGACGACGAGGCCCCTGTGACAAGTGTTACTGTAGTAGAAGAAACTACCCCCGAAGAGAGCAAGCCAGAAGAAGTTGTTGAGTTGCCTGAAGAGGTGACTGTAGAGGAAACTGAGACGAAAGAAGGTAAGCCGAAACAAAAGAAAATCACAAAGCGAATCATTAAGAAACGGGTAGGGCCTAAAGTTGAAACAACACAAATCACTACTGAACAAGAAGACGACAAACAACCAGTCGTTTCTATTCAAACCACAGAGGAACTCGTAGATGACACAACTACACCACTCTCAGATATTACACCAGACACTGCTCAGGTCGTTGAAGAAACCCCTGAGAAAGTACACATTACACAAGTCAAAACTGAAACCGGCGATATTCAAACCGTTAAAACCACTAAGCGCGTTATCAAAAAGAAAAAGGGACCGAAAGAGGAAGTCACCGAAATCACTACAGTCCAAAAAGACGACGAGGCCCCTGTGACAAGTGTTACTGTAGTAGACGAAATTACCCCCGAAGAGAGCAAGCCAGAAGAAGTTGTTGAGTTGCCTGAAGAGGTGACTGTAGATGAAACTGAGACACCGGAAAGTAAGCCAAAACAAAAGAAAATCACAAAGCGTATTATTAAAAAGCGGGTAGGGCCTAAAATCGAAACTACACAAATCACCACTGAACAAGAAGACGACAAACAACCAGTCGTTTCTATTCAAACCACAGAGGAACTCGTAGATGACACAACTACACCACTCTCAGATATTACACCAGACACTGCTCAGGTCGTTGAAGAAACCCCCGAGAAAGTACACATTACACAAGTCAAAACTGAAACCGGCGATGTCCAAACCGTTAAAACCACTAAGCGCGTGATCAAAAAGAAAAAGGGACCGAAAGAGGAAGTCACCGAAATCACCACCGTCCAAAAAGACGACGAGGCCCCTGTGACAAGTGTTACTGTAGTAGAAGAAACTACCCCCGAAGAGAGCAAGCCAGAAGAAGTTGTTGAGTTGCCTGAAGAGGTGACTGTAGAGGAAACTGAGACACCGGAAGGTAAGCCAAAACAAAAGAAAATCATAAAGCGTATTATTAAGAAACGGGTAGGACCTAAAGTTGAAACAACACAAATCACTACTGAACAAGAAAACGACAAACAACCAGTCGTTTCTATTCAAACCACAGATGAACTCGTAGATGACACAACTACACCACTCTCAGATATTACACCAGACACTGCTCAGGTCGTTGAAGAAACCCCTGAGAAAGTACACATTACACAAGTCAAAACTGAAACCGGCGATGTTCAAACCGTTAAAACCACTAAGCGCGTTATCAAAAAGAAAAAGGGACCGAAAGAGGAAGTCACCGAAATCACCACCGTCCAAAAAGACGACGAGGCCCCTGTGACAAGTGTTACTGTAGTAGAAGAAACTACCCCCGAAGAGAGCAAGCCAGAAGAAGTTGTTGAGTTGCCTGAAGAGGTGACTGTAGAGGAAACTGAGACACCGGAAGGTAAGCCAAAACAAAAGAAAATCACAAAGCGCATTATTAAAAAGCGGAAAGGACCTAAAGTCGAAACTACACAAATTACTACTGAGCAAGAAGACGACAAACAACCAGTCGTTTCAATTCAAACCACAGAGGAACTCATGGATGACACAACTACACCACTCTCAGATATCACACCAGATACTGCTCAGGTCGTTGAAGAAACCCCTGAGAAAGTACACATTACACAAGTCAAAACCGAAACCGGCGATGTTCAAATCGTTAAAACTACTAAGCGCGTCATCAAAAAGAAAAAGGGACCGAAAGAGGAAGTCACCGAAATCACCACCGTCCAAAAAGACGACGAGGCCCCTGTGACAAGTGTTACTGTAGTAGAAGAAATTACCCCCGAAGAGAGCAAGCCAGAAGAAGTTGTTGAGTTGCCTGAAGAGGTGACTGTAGAGGAAACTGAGACACCGGAAGGTAAGCCAAAACAAAAGAAAATCACAAAGCGTATTATTAAAAAGCGGGTAGGGCCTAAAATCGAAACTACACAAATCACCACTGAACAAGAAGACGACAAACAACCAGTCGTTTCTGTTCAAACCACAGAGGAACTCATAGATGACACAACTACACCACTCTCAGACATTACACCAGACACTGCTCAGGTCGTTGAAGAAACCCCTGAGAAAGTACACATTACACAAGTCAAAACCGAAACCGGCGATGTTCAAACCGTTAAAACCACTAAGCGCGTTATCAAAAAGAAAAAGGGACCGAAAGAGGAAGTCACCGAAATCACTACAGTCCAAAAAGACGACGAGGCCCCTGTGACAAGTGTTACTGTAGTAGAAGAAACTACCCCCGAAGAGAGCAAGCCAGAAGAAGTTGTTGAGTTGCCTGAAGAGGTGACTGTAGAGGAAACTGAGACACAGGAAGGTAAGCCAACACAAAAGAAAATCACAAAGCGCATTATTAAAAAGCGGGTAGGGCCTAAAATCGAAACTACACAAATCACTACTGAACAAGAAGACGACAAACAACCTGTCGTTTCTGTTCAAACCACAGAGGAACTCATAGATGACACAACTACACCACTCTCAGATATCACACCAGATACTGCTCAGGTCGTTGAAGAAACCCCTGAGAAAGTACACATTACACAAGTCAAAACCGAAACCGGCGATGTTCAAACCGTTAAAACCACTAAGCGCGTTATCAAAAAGAAAAAGGGACCGAAAGAGGAAGTCACCGAAATCACTACAGTCCAAAAAGACGACGAGGCCCCTGTGACAAGTGTTACTGTAGTAGAAGAAACTACCCCCGAAGAGAGCAAGCCAGAAGAAGTTGTTGAGTTGCCTGAAGAGGTGACTGTAGAGGAAACTGAGACACATGAAGGTAAGCCAAAACAAAAGAAAATCACAAAGCGCATTATTAAAAAGCGGAAAGGACCTAAAGTCGAAACTACACAAATTACAACTGAGCAAGAAGACGACAAACAACCAGTCGTTTCTGTTCAAACCACAGAGGAACTCATAGATGACACAACAACACCACTCTCAGATATCACACCAGATACTGCTCAGGTCGTTGAAGAAACCCCTGAGAAAGTACACATTACACAAGTCAAAACCGAAACCGGCGATGTTCAAATCGTTAAAACTACTAAGCGCGTCATCAAAAAGAAAAAGGGACCGAAAGAGGAAGTCACCGAAATCACCACCGTCCAAAAAGACGACGAGGCCCCTGTGACAAGTGTTACTGTAGTAGAAGAAACTACCCCCGAAGAGAGCAAGCCAGAAGAAGTTGTTGAGTTGCCTGAAGAGGTGACTGTAGAGGAAACTGAGACACCGGAAGGTAAGCCAAAACAAAAGAAAATCACAAAGAGTATTATTAAAAAGCGGGTAGGGCCTAAAATCGAAACTACACAAATCACTACTGAACAAGAAGACGACAAACAACCAGTCGTTTCTGTTCAAACCACAGAGGAACTCATAGATGACACAACTACACCACTCTCAGATATCAGACCAGATACTGCTCAGGTCGTTGAAGAAACCCCTGAGAAAGTACACATTACACAAGTCAAAACCGAAACCGGCGATGTTCAAACCGTTAAAACCACTAAGCGCGTTATCAAAAAGAAAAAGGGACCGAAAGAGGAAGTCACCGAAATCACCACCGTCCAAAAAGACGACGAGGCCCCTGTGACAAGTGTTTCTGTGATAGAAGAAACTACCCCCGAAGAGAGCAAGCCAGAAGAAGTTGTTGAGTTACCTGAAGAGGTAACTGTAGAGGAAACTGAGACACAGGAAGGTAAGCCAACACAAAAGAAAATCACAAAGCGCATTATTAAAAAGCGGGTAGGGCCTAAAATCGAAACTACACAAATCACTACTGAACAAGAAGACGACAAACAACCAGTCGTTTCTGTTCAAACGACAGAGGAACTCATAGATGACACAACTACACCACTCTCAGATATCACACCAGATACTGCTCAGGTCGTTGAAGAAACCCCTGAGAAAGTACACATTACACAAGTCAAAACCAAAACAGGTGATGTTCAAACCGTTAAAACCACTAAACGCGTTATCAAAAAGAAAAAGGGACCGAAAGAGGAAGTCACCGAAATCACCACCGTCCAAAAAGACGACGAGGCCCCTGTGACAAGTGTTTCTGTGATAGAAGAAACTACCCCCGAAGAGAGCAAGCCAGAAGAAGTTGTTGAGATACCTGAAGAGGTAACTGTAGAGGAAACTGAGACACAGGAAGGTAAGCCAACACAAAAGAAAATCACAAAGCGCATTATTAAGAAAAGGGTAGGACCTAAAATTGAAACTACACAAATCACCACTGAAGAAGAAGACGACAAACAACCAGTCGTTTCTATTCAAACCACAGAGGAACTCATAGATGACACAACTACACCACTCTCAGACATTGCACCATATACTGCTCAGGTCGTTGAAGAAACCCCTGAGAAAGTACACATTACACAAGTCAAAACCGAAACCGGCGATGTTCAAACCGTTAAAACCACTAAGCGCGTTATCAAAAAGAAAAAGGGACCGAAAGAGGAAGTCACCGAAATCACTACAGTCCAAAAAGACGACGAGGCCCCTGTGACAAGTGTTACTGTAGTAGAAGAAATTACCCCCGAAGAGAGCAAGCCAGAAGAAGTTGTTGAGTTGCCTGAAGAGGTGACTGTAGATGAAACTGAGACACCGGAAGGTAAGCCAAAACAAAAGAAAATCACAAAGCGTATTATTAAAAAGCGGGTAGGGCCTAAAATCGAAACTACACAAATCACCACTGAACAAGAAGACGACAAACAACCAGTCGTTTCTGTTCAAACCACAGAGGAACTCATTGATGACACAACTACACCACTCTCAGACATTAGACCAGATATTGCTCAGGTCGTTGAAGAAACTCCCGAGAAAGTTCATATTACACAAGTCAAAACCGAAACCGGCGATGTTCAAACCGTTAAAACCACTAAGCGCGTTATCAAAAAGAAAAAGGGACCGAAAGAGGAAGTCACCGAAATCACTACAGTCCAAAAAGACGACGAGGCCCCTGTGACAAGTGTTACTGTAGTAGAAGAAATTACCCCCGAAGAGAGCAAGCCAGAAGAAGTTGTTGAGTTGCCTGAAGAGGTGACTGTAGATGAAACTGAGACACCGGAAGGTAAGCCAAAACAAAAGAAAATCACAAAGCGTATTATTAAAAAGCGGGTAGGGCCTAAAATCGAAACTACACAAATCACTACTGAACAAGAAGATGACAAACAACCAGTCGTTTCTGTTCAAACCACAGAGGAACTCATAGATGACACAACTACACCACTCTCAGATATCACACCAGATACTGCTCAGGTCGTTGAAGAAACCCCTGAGAAAGTAAACATTACACAAGTCAAAACCGAAACCGGCGATGTCCAAACCGTTAAAACCACTAAGCGCGTTATCAAAAAGAGAAAAGGACCTAAGGAAGAAGTTACGGAAATCACCACAGTCCAAAAAGACGACGAGGCCCCTGTTACAAGTGTTACTGTAGTAGAAGAAACTACCCCCGAAGAGAACAAGCCAGAAGAAGTTGTTGAGTTACCTGAAGAGGTAACTGTAGAGGAAACTGAGACACAGGAAGGTAAGCCAACACAAAAGAAAATCACAAAGCGCATTATTAAGAAAAGGGTGGGACCTAAAATCGAAACTACACAAATCACTACTGAACAAGAAGACGACAAACAACCAGTCGTTTCTGTTCAAACCACAGAGGAACTCATAGATGACACAACTACACCACTCTCAGATATCACACCAGATACTGCTCAGGTCGTTGAAGAAACCCCTGAGAAAGTACACATTACACAAGTCAAAACCGAAACCGGCGATGTTCAAACCGTTAAAACCCTTAAGCGCGTTATCAAATATAAAAAGGGACCGAAAGAGGAAGTCACCGAAATCACCACAGTCCAAAAAGACGACGAGGCCCCGGTTACGACGGTCACTGTGGTAGAAGAAACTACCCCTGAAGAGAGCAAGCCAGAAGAAGTTGTTGAGTTACCTCAAGAGGTAACTGTAGAGGAAACTGAGCCACAGGAAGGTAAGCCAACACAAAAGAAAATCACAAAGCGCATTATTAAAAAGCGGGTAGGGCCTAAAATCGAAACTACACAAATCACTACTGAACAAGAAGACGACAAACAACCAGTCGTTTCTGTTCAAACCACAGAGGAACTCATAGATGACACAACTACACCACTCTCAGACATTATACCAGACACTGCTCAGGTCGTTGTAGAAACCCCTGAGAAAGTACACATTACACAAGTCAAAACCAAAACAGGTGATGTTCAAACGGTTAAAACCACTAAGCGCGTTATCAAAAAGAAAAAGGGACCGAAAGAGGAAGTCACCGAAATCACTACAGTCCAAAAAGACGACGAGGCCCCTGTGACAAGTGTTACTGTAGTAGAAGAAACTACCCCCGAAGAGAGCAAGCCAGAAGAAGTTGTTGAGTTGCCTGAAGAGGTGACTGTAGATGAAACTGAGACACATGAAGGTAAGCCAAAACAAAAGAAAATCACAAAGCGCATTATTAAAAAGCGGGTAGGGCCTAAAATCGAAACTACACAAATCACTACTGAACAAGAAGACGACAAACAACCAGTCGTTTCTGTTCAAACCACAGAGGAACTCATAGATGACACAACTACACCACTCTCAGACATTACACCAGACACTGCTCAGTTCGTTGAAGAAACCCCTGAGAAAGTACACATTACACAAGTCAAAACCAAAACCGGCGATATTCAAACCGTTAAAACCACTAAGCGCGTTATCAAAAAGAAAAAGGGACCGAAAGAGGAAGTCACCGAAATCACTACAGTCCAAAAAGACGACGAGGCCCCGGTTACGACGGTCACTGTGGTAGAAGAAACTACCCCCGAAGAGAGCAAGCCAGATGAAGTTGTTGAGTTGCCTGAAGAGGTGACTGTAGAGGAAACTGAGACACAGGAAGGTAAGCCAAAACAAAAGAAAATCACGAAGCGTATTATTAAAAAGCGGGTAGGGCCTAAAGTCGAAACTACACAAATCACCACCGAACAAGAAGACGACAAACAACCAGTCGTTTCTGTTCAAACCACAGAGGAACTCATTGATGACACAACTACACCACTCTCAGACATTACACCAGACACTACTCAGGTCGTTGAAGAAACCCCTGAGAAAGTACACATTACACAAGTCAAAACCGAAACCGGCGATGTCCAAACCGTTAAAACCACTAAGCGCGTTATCAAAAAGAGAAAAGGACCTAAGGAAGAAGTCACCGAAATCACCACAGTCCAAAAAGACGACGAGGCCCCGGTTACGACGGTCACTGTGATAGAAGAAACTACCCCCGAAGAGAGCAAGCCAGATGAAGTTGTTGAGTTGCCTGAAGAGGTGACTGTAGAGGAAACTGAGACACAGGAAGGTAAGCCAAAACAAAAGAAAATCACGAAGCGTATTATTAAAAAGCGGGTAGGGCCTAAAGTCGAAACTACACAAATCACCACCGAACAAGAAGACGACAAACAACCAGTCGTTTCTGTTCAAACCACAGAGGAACTCATAGATGACACAACTACACCACTCTCAGACATTACACCAGATACTGCTCAGGTCGTTGAAGAAACCCCTGAGAAAGTACACATTACACAAGTCAAAACCGAAACCGGCGATGTCCAAACCTTTAAAACCACTAAGCGCGTTATCAAAAAGAGAAAAGGACCTAAAGAAGAAGTCACCGAAATCACCACAGTCCAAAAAGACGACGAGGCCCCGGTTACGACGGTCACTGTGGTAGAAGAAACTACCCCCGAAGAGAGCAAGCCAGATGAAGTTGTTGAGTTGCCTGAAGAGGTGACTGTAGAGGAAACTGAGACACAGGAAGGTAAGCCAAAACAAAAGAAAATCACGAAGCGTATTATTAAAAAGCGGGTAGGGCCTAAAGTCGAAACTACACAAATCACCACTGAACAAGAAGACGACAAACAACCAGTCGTTTTTGTTCAAACCACAAAGGAACTCATTGATGACACAACTACACCACTCTCAGATATCACACCAGATACTGCTCAGGTCGTTGAAGAAACCCCTGAGAAAGTACACATTACACAAGTCAAAACCAAAACCGGCGATGTTCAAACCGTTAAAACCACTAAGCGCGTTATCAAAAAGAAAAAGGGACCGAAAGAGGAAGTCACCGAAATCACCACAGTCCAAAAAGACGACGAGGCCCCGGTTACATCGATTACTGTAGTAGAAGAAACTACCCCCGAAGAGAGCAAGCCAGAAGAAGTTGTTGAGTTGCCTGAAGAGGTGACTGTAGAGGAAACTGAGACACAGGAAGGTAAGCCAAAACAAAAGAAAACCACAAAGCGTATTATTAAAAAGCGGGTAGGGCCTAAAATCGAAACTACACAAATCACCACTGAACAAGAAGACGACAAACAACCAGTCGTTTCTGTTCTAACCACAGAGGAACTCATAGATGACACAACTACACCACTCTCAGATATCACACCAGATACTGCTCAGGTCGTTGAAGAAACCCCTGAGAAAGTACACATTACACAAGTCAAAACCAAAACCGGCGATGTTCAAACCGTTAAAACCACTAAGCGCGTTATCAAAAAGAAAAAGGGACCGAAAGAGGAAGTCACCGAAATCACCACAGTCCAAAAAGACGACGAGGCCCCTGTGACAAGTGTTACTGTAGTAGAAGAATCTACTCCCGAAGAGAGCAAGCCAGAAGAAGTTGTTGAGTTGCCTGAAGAGGTGACTGTAGAGGAAACTGAGACACAGGAAGGTATGCCAAAACAAAAGAAAATCACGAAGCGTATTATTAAAAAGCGGGTAGGGCCTAAAGTCGAAACTACACAAATCACCACCGAACAAGAAGACGACAAACAACCAGTCGTTTCTGTTCAAACCACAGAGGAACTCATTGATGACACAACTACACCACTCTCAGACATTACACCAGACACTACTCAGGTCGTTGAAGAAACCCCTGAGAAAGTACACATTACACAAGTCAAAACCGAAACCGGCGATGTCCAAACCGTTAAAACCACTAAGCGCGTTATCAAAAAGAGAAAAGGACCTAAGGAAGAAGTCACCGAAATCACCACAGTCCAAAAAGACGACGAGGCCCCGGTTACGACGGTCACTGTGATAGAAGAAACTACCCCCGAAGAGAGCAAGCCAGAAGAAGTTGTTGAGTTACCTGAAGAGGTGACTGTAGAGGAAACTGAGACACAGGAAGGTAAGCCAAAACAAAAGAAAATCACGAAGCGTATTATTAAAAAGCGGGTAGGGCCTAAAGTCGAAACCACACAAATCACCACTGAACAAGAAGACGACAAACAACCAGTCGTTTCTGTTCAAACCACAGAGGAACTCATAGATGACACAACTACACCACTCTCAGACATTACACCAGACACTGCTCAGGTTGTTGAAGAAACCCCTGAGAAAGTACACATAACACAAGTCAAAACCAAAACCGGCGATGTTCAAACCGTTAAAACCACTAAGCGCGTTATCAAAAAGAAAAAGGGACCGAAAGAGGAAGTCACCGAAATCACCACAGTCCAAAAAGACGACGAGGCCCCTGTGACAAGTGTTACTGTAGTAGAAGAATCTACTCCCGAAGAGAGCAAGCCAGAAGAAGTTGTTGAGTTGCCTGAAGAGGTGACTGTAGAGGAAACTGAGACACAGGAAGGTATGCCAAAACAAAAGAAAATCACGAAGCGTATTATTAAAAAGCGGGTAGGGCCTAAAGTCGAAACTACACAAATCACCACCGAACAAGAAGACGACAAACAACCAGTCGTTTCTGTTCAAACCACAGAGGAACTCATTGATGACACAACTACACCACTCTCAGACATTACACCAGATACTGCTCAGGTCGTTGAAGAAACCCCTGAGAAAGTACACATTACACAAGTCAAAACCGAAACCGGCGATGTTCAAACCGTTAAAACCACTAAGCGCGTTATCAAAAAGAAAAAGGGACCGAAAGAGGAAGTCACCGAAATCACTACAGTCCAAAAAGACGACGAGGCCCCGGTTACGACGGTCACTGTGGTAGAAGAAACTACTCCCGAAGAGAGCAAGCCAGATGAAGTTGTTGAGTTGCCTGAAGAGGTGACTGTAGAGGAAACTGAGACACAGGAAGGTAAGCCAAAACAAAAGAAAATCACAAAGCGTATTATTAAAAAGCGGGTAGGGCCTAAAGTTGAAACAACACAAATCACCACTGAACAAGAAGACGACAAACAACCAGTCGTTTCTGTTCAAACCACAGATGAACTCATAGATGACACAACTACACCACTCTCAGACATTACACCAGACACTGCTCAGGTCGTTGAAGAAACCCCTGAGAAAGTACACATTACACAAGTCAAAACCGAAACCGGCGATGTTCAAACCGTTAAAACCACTAAGCGCGTTATCAAAAAGAAAAAGGGACCGAAAGAGGAAGTCACCGAAATCACTACAGTCCAAAAAGACGACGAGGCCCCTGTGACAAGTGTTACTGTAGTAGAAGAAACTACCCCCGAAGAGAGCAAGCCAGAAGAAGTTGTAGAGTTGCCTGAAGAGGTGACTGTAGAGGAAACTGAGACACAGGAAGGTAAGCCAAAACAAAAGAAAATCACAAAGCGTATTATTAAAAAGCGGGTAGGGCCTAAAATCGAAACTACACAAATCACCACTGAACAAGAAGACGACAAACAACCAGTCGTTTCTGTTCAAACCACAGAGGAACTCATTGATGACACAACTACACCACTCTCAGACATTACACCAGATACTGCTCAGGTCGTTGAAGAAACCCCTGAGAAAGTACACATTACACAAGTCAAAACCAAAACCGGCGATGTTCAAACCGTTAAAACCACTAAGCGCGTTATCAAAAAGAAAAAGGGACCGAAAGAGGAAGTCACCGAAATCACTACAGTCCAAAAAGACGACGAGGCCCCGGTAACGACAGTCACTGTGGTAGAAGAAACTACCCCCCAAGAGAGCAAGCCAGAAGAAGTTGTTGAGTTACCTGAAGAGGTGACTGTGGAGGAAACTGAGACACAGGAAGGTAAGCCAAAACAAAAGAAAATCACGAAGCGTATTATTAAAAAGCGGGTAGGGCCTAAAGTCGAAACTACACAAATCACCACTGAACAAGAAGACGACAAACAACCAGTCGTTTCTGTTCAAACCACAGAGGAACTTATAGATGACACAACTACACCACTCTCAGACATTACACCAGACACTGCTCAGGTCGTTGAAGAAACCCCTGAGAAAGTACACATTACACAAGTCAAAACCGAAACCGGCGATGTTCAAACCGTTAAAACCACTAAGCGCGTTATCAAAAAGAAAAAGGGACCGAAAGAGGAAGTCACCGAAATCACTACAGTCCAAAAAGACGACGAGGCCCCTGTGACAAGTGTTACTGTAGTAGAAGAAACTACCCCCGAAGAGAGCAAGCCAGAAGAAGTTGTAGAGTTGCCTGAAGAGGTGACTGTAGAGGAAACTGAGACACAGGAAGGTAAGCCAAAACAAAAGAAAATCACAAAGCGTATTATTAAAAAGCGGGTAGGGCCTAAAATCGAAACTACACAAATCACCACTGAACAAGAAGACGACAAACAACCAGTCGTTTCTGTTCAAACCACAGAGGAACTCATTGATGACACAACTACACCACTCTCAGACATTACACCTGATACTGCTCAGGTCGTTGAAGAAACCCCTGAGAAAGTACACATTACACAAGTCAAAACCAAAACCGGCGATGTTCAAACCGTTAAAACCACTAAGCGCGTTATCAAAAAGAAAAAGGGACCGAAAGAGGAAGTCACCGAAATCACTACAGTCCAAAAAGACGACGAGGCCCCGGTAACGACAGTCACTGTGGTAGAAGAAACTACCCCCCAAGAGAGCAAGCCAGAAGAAGTTGTTGAGTTACCTGAAGAGGTGACTGTGGAGGAAACTGAGACACAGGAAGGTAAGCCAAAACAAAAGAAAATCACGAAGCGTATTATTAAAAAGCGGGTAGGGCCTAAAATCGAAACTACACAAATCACCACTGAACAAGAAGACGACAAACAACCAGTCGTTTCTGTTCAAACCACAGATGAACTCATAGATGACACAACTACACCACTCTCAGACATTACACCAGACACTGCTCAGGTCGTTGAAGAAACCCCTGAGAAAGTACACATTACACAAGTCAAAACCAAAACAGGTGATGTTCAAACCGTTAAAACCACTAAGCGCGTTATCAAAAAGAAAAAGGGACCGAAAGAGGAAGTCACCGAAATCACTACAGTCCAAAAAGACGACGAGGCCCCGGTTACATCGATTACTGTAGTAGAAGAAACTACCCCCGAAGAGAGCAAGCCAGAAGAAGTTGTTGAGTTGCCTGAAGAGGTGACTGTAGAGGAAACTGAGACACCGGAAGGTAAGCCAAAACAAAAGAAAATCACGAAGCGTATTATTAAAAAGCGGGTAGGGCCTAAAATTAAAACTACACAAATCACCACTGAACAAGAAGACGACAAACAACCAGTCGTTTCTGTTCAAACCACAGAGGAACTCATTGATGACACAACTACACCACTCTCAAACATTACACCAGATACTGCTCAGGTCGTTGAAGAAACCCCTGAGAAAGTACACATTACACAAGTCAAAACCAAAACCGGCGATGTTCAAACCGTTAAAACCACTAAGCGCGTTATCAAAAAGAAAAAGGGACCGAAAGAGGAAGTCACCGAAATCACTACAGTCCAAAAAGACGACGAGGCCCCGGTAACGACAGTCACTGTGGTAGAAGAAACTACCCCCCAAGAGAGCAAGCCAGAAGAAGTTGTTGAGTTACCTGAAGAGGTGACTGTGGAGGAAACTGAGACACAGGAAGGTAAGCCAAAACAAAAGAAAATCACGAAGCGTATTATTAAAAAGCGGGTAGGGCCTAAAATCGAAACTACACAAATCACCACTGAACAAGAAGACGACAAACAACCAGTCGTTTCTGTTCAAACCACAGATGAACTCATAGATGACACAACTACACCACTCTCAGACATTACACCAGACACTGCTCAGGTCGTTGAAGAAACCCCTGAGAAAGTACACATTACACAAGTCAAAACCAAAACAGGTGATGTTCAAACCGTTAAAACCACTAAGCGCGTTATCAAAAAGAAAAAGGGACTGAAAGAGGAAGTCACCGAAATCACTACAGTCCAAAAAGACGACGAGGCCCCGGTTACATCGATTACTGTAGTAGAAGAAACTACCCCCGAAGAGAGCAAGCCAGAAGAAGTTGTTGAGTTGCCTGAAGAGGTGACTGTAGAGGAAACTGAGACACAGGAAGGTAAGCCAAAACAAAAGAAAACCACAAAGCGTATTATTAAAAAGCGGGTAGGGCCTAAAATCGAAACTACACAAATCACCATTGAACAAGAAGACGACAAACAACCAGTCGTTTCTATTCAAACCACAGAGGAACTTAAAGATGACACAACTACACCACTCTCAGACATTACACCAAACACTGCTCAGGTCGTTGAAGAAACCCCTGAGAAAGTACACATTACACAAGTCAAAACCAAAACCGGCGATGTTCAAACCGTTAAAACCACTAAGCGCGTTATCAAAAAGAAAAAGGGACCGAAAGAGGAAGTCACCGAAATCACTACAGTCCAAAAAGACGACGAGGCCCCGATTACAACGATTACTGTGGTAGAAGAAACTACCCCCGAAGAGAGCAAGCCAGAAGAAGTTGTTGAGTTGCCTGAAGAGGTGACTGTAGAGGAAACTGAGACACCGGAAGGTAAGCCAAAACAAAAGAAAATCACAAAGCGTACTATTAAAAAGCGGGTAGGGCCTAAAATCGAAACTACACAAATCACCACTGAACAAGAAGACGACAAACAACCAGTCGTTTCTGTTCAAACCATAGAGGAACTCATAGATGACACAACTACACCACTCTCAGACATTACACCAGACACTGCTCAGGTCGTCGAAGAAACCCCTGAGAAAGTACACATTACACAAGTCAAAACCGAAACCGGCGATGTCCAAACCGTTAAAACCACTAAGCGCGTTATAAAAAAGAAAAAAGGACCGAAAGGGGAAGTCACTGAAATCACTACAGTCCAAAAAGACGACGAGGCCCCGATTACAACGATTACTGTGGTAGAAGAAACTACCCCCGAAGAGAGCAAGCCAGAAGAAGTTGTTGAGTTGCCTGAAGAGGTGACTGTAGAGGAAACTGAGACACCGGAAGGTAAGCCAAAACAAAAGAAAATCACAAAGCGTACTATTAAAAAACGGGTAGGGCCTAAAATCGAAACTACACAAATCACCACTGAACAAGAAGACGACCAACAACCAGTCGTTTCTGTTCAAACCACAGAGGAACTCATAGATGACACAACTACACCACTCTCAGATATCACACCAGATACTGCACAGGTCGTTGAAGAAGTCCCTGAGAAAGTACACATTACACAAGTCAAAACTGAGAAAATTGACGTCTAA
Protein
MEKQSRWSEQRSEQRSEQRVQQHSERREQVVQQQERIQRTEQHFTRQMTTQVESSGDRQPITAGRPGEPSPPIFEQIFKNARFAQGGNAKFEGKLRGNPTPVVSWTRKKAPLVECNKYSMRYNEQTGDVSLLIKQIGPGDEGEYTCTARNQYGEAICSVYIQPEGVPVPAQQASQQQSYRHVSETVEHKAYGTQGYTTEQSRQTQKVAYTNGTDHSSTDDFKVDTFEYRLLREVSFRESITKRYVGESDVQISTEIDRSLGPVSPPKIAQKPRNSKLQEGADAQFQVQLSGNPRPRVTWFKNGQRLINSNKHEIITTHNHTTLRVRNTQKSDSGHYTLLAENPNGCIVTSGYLAVESPTESYVQDQRSQYITDTQQRETEERIEISEKALAPQFVKVCQDRDVTEGKMTRFDCRVTGRPYPEVTWFINDRQIRDDYNHKILVNESGNHALMITNVTLSDSGVVTCVARNKSGETAFQCRLNVIEKEQVVAPKFVERFSTLNVREGEPVVLNARAVGTPTPRITWQKDGVPIIPNPELRIHTDGGASTLDIPRAKASDAAWYQCTAQNVAGSTATRARLYVEVPKEPPPEQKRLHLPRPTKVIEPEPAPGPEIIYLRHVERARPYIPPGEEDRVYPPPQFIVPLKSVTAMEGGKIHFETRIEPVGDPTMKIEWLKNGQSIEASSRFTSIFRFGYISLDMLSLNIQDSGEYTCRAVSATGVAETKAVLHVTPRATIERTSQHPETLQYIQQLEDYSKYQHQESIEEQTSQRPQFIRPLQDLGELQEGRNAHFEAQLTPVSDPTMRVEWYKDGRPITASSRITSIFNFGYVSLNIMHLRAEDAGSYTVRAVNKLGEAISTASIRVAARSTVTADLGIPEQRRYIEKTEQLEAYQQQQHQKYYQEVPESTQKPEFKTPIKDQISIKEGGFAHFEARLEPIGDSTLRVEWLKDGRPVEASSRITTFFNFGYVALTIKSVTVHDAGHYTCRAYNAIGQATTSANLTIVTKKDIIAESQHPGGLEKIQYLEDASRYSKRTEEEVKITQKPRFLGPLKGTNKIVEGQSAHFEARVEPQSDLTMTVEWYFNGKQITSANRIQTYHDFGYVALDIASVRAEDSGVYTVVARNAAGEAQLSASMTVETRSSIDTSSIHRGLYEKTRHIEESKFVEPMYQIEEISKSKPVFVQPLSNPPPVSEGKNIHLECRLEPMGDPTMRVEWFHNGRSVTVGSRFKTYYDFGFVALDIIHATSADTGEYTVRAVNHLGSAHTSAIVRVIERSDIVTDTQNEQAIEQIQLLEDAARRTKQVREDITVMQAPQFSRALHNIETVEGTNVHLECRLQPVGDQTMRVEWFCNGKPIKTGHRFRPAYEFDYVALDLLSVYPEDSGVYTCQATNQLGEAVTSCALRVIAKKDLILESQHPSGLEKIQYLEDTSRYKKTDIIDESVTIKPRFVTRPKSIENVIEGQHVHFECKLEPVTDSNLKVEWFKNGQPVTIGHRFRPIHDFGYVALDIIDLIAEDSGIYTCRAVNLVGTDEVSCRLTCRSTTDIVRSTQNEAGLEQIQVLEDRSKYHRTDMVDEVTTQAPIFTTSLKNVEIKEGQRAHFECRLIPVSDATLKVEWYHNNKPLKSGSRFTETNNFGFVALDIMSCLPEDSGTYTCRAINALGEAVTSGIAIVHSKKSIYLESQHEGALPRLNQLEDTSKYQRHSAQDEVITQAPVFTMPMKDIRVAENQAAHFEARLIPVGDPKLRVEWLRNGVPIEASNRLTTMHDFGYVALNMKYVNPEDSGTYTCRAINELGEAVTSSTLFVQSKASLQLESQHESALQKIQQLEDSSRYQRREDVEVAVNQAPRFITQLNGPTKLSEGQSAHYECRIEPYPDPNMRVEWYFNGKVLQSGHRYRTSNDFGFAALDILTVYGEDSGEYTCKAINNLGQAVSSIRLNVQSKESIIRDSQHESALEKIQYLEDDSRYKRAVQDDSFVVEKPQFGKPIKNAEVTEGHPVHLEATLTPVNDPTMRVEWYCNGRPVQQGHRFKTTYDFGYVALDILYAYAEDTGTYMCKATNAVGEAVTTSSVKVDAKSGLYLDTLDEQRLKKIQELEKYERPKPIEEEQPGQRPVFLTALTSLENLKEGDRAHFECRVEPINDPHLTIDWFHNGQKIRAGHRYRTTHDFGYVALDILYTYAEDSGTYMCKATNKLGEAVNTCTLKVAGHRNIILDTQHPNGLEKIRQLEAQGHSTRIEVEEPKISPPRFVTELRGTTHVFEGKTAHFECQVEPVHDPNLRIEFYHNGKALQSAARFHITFDFGYVSLDIQHCVPEDAGEYSVKAINALGHCTSAISMTVTAKGSIISESQRPEGLEKIRELESAEPFKRPEIPEPVTRQRPVFTQPLQNIDNIQEGQTAHFDCRLIPVGDPTLKVEWFRNEKLIEDSSRITKTHDFGYVSMTISHVRDEDEGVYMCRASNLLGEAVTTAAMKIKTKAAIQLETQHPEGMKKIQKLEQPHERRSEEPDREFEKPIFTQVLTGPSELWEGQHAHYEARVVPVGDPSLRFEWYINGVELKMGSRFRTTHDFGFVTLDINSVVANDAGLYMCKAINRAGSTVSSTSLKVKTKSTIIDQAMRPESWEQIQLKEAAMNKVPEMFVDTGVQQAPIFTTHLKSYDKLVEGQHVYLEAQVEPRTDPNLKIEWFKNGVTLTTGARLKSTFDFGLVTLSINSLRNDDSGIYTCKATNLLGEAVSTASIKIEDRHWLLGESLHPDSLDRIGALEQPKPEKPEAPEPTYETPVFISHLNNIVCKEGDNIHFECNVEPSRDPTLKIEWFFNNKPLPSGTRYKSTHDFSYVSLDITHTYEEDSGIYTCKATNSKGSATTSGSLRCTGDKNIYFDTQHPQGKAGLEAVEQAEEARLAKGRRPSVPDTEYPKPEWIIPIAAEHQLVEGQVLHLEGQVEPKNDPDLKIEWYFNGKVLEQGSRFKLTSDFGFVTLDLVDVYERDSGIYTCKAYNKRGEAFTSSTVYCTSKDNLIERTQHPKGTEGLEKIQNLEDSLRKEPGQQPDDDTGRPPEFTTVFKDIVDISEGQIAHYEASLIPTGDQSMVIEWFYNGKTIEASHRIRTVYAFGMVVLEILGTKTTDSGTYSCRATNKWGQAEISVKLECVDKSKGQKPRFTTHIQNIEGLKDGQSAHFECTVVPVDDPDMKIEWYHNGQHMRHSTRIKTVSDFGFVVLDIAYTQNHDSGEYVCRAYNKYGEDFTRATINCYGKGGVYLESLQPDSLAKIRELESLQGAQQQTPSTPSAEPPKFITQIQDVTKLVEGQSAHFEARLVPVDDPDLKVEWFYNGKKLPHGHRYRTFHDFGIVILDILYCYEENSGEYECVATNKLGRDSTKANLKCTSKENLILDSQLPRGMEGGLEKLQTLEDSMVRRKDTSVEEEKGKAPVFTVPLSNIENLREGENAHFEARLTPTDDPNLKVEWYWNGKSLKAGSRFRTFCDFGFVILEISPTYPEDSGEYLCRAYNNYGEAVTTASMKVQGKRNIILESQLPKGMEGTIDKIAALEGYSGTVDTLTPEAESGNPPEFTTTPSDLILSENSSAHFECRLIPVNDSSMRVEWFHNGKPLLTGSRVKTINDFGFVILEIGGVYQRDAGLYTCKATNRHGEATVSCKLQVKGRQGIILEPQLPSHFKSGTESIQKLEETLHKREEITIEDEKPNPPRFTVEIKDNIDVPEGGPVHFDCRVEPVGDPTMRIDWFHNGRPFATGSRVHTLNDFGFIALDIDYIYARDAGEYTCRATNKWGSATTTAKITCSAKRDIVLESQLPQGMSGEKIKELERGRISDAPKEEPIVSTPPKFITQIKSHTVEESEGVRFECRVEPKEDPKLRIEWYRNGKLLPSGHRYRTVYDMGFVSLDILYVYAEDSGEYICRAVNDFGEDFTKATISCKKLPDIILQNQVPRGMKRSEALTQMEATIKKYTSEVYLTEDDLYDVDKKQPPRFVTQIQSQTSLVEMETTKFECQLAPVGDPNMKVEWFFNGKPLLHKNRFTPIYDFGYVAMNFGWVYPEDSGEYLCRATNLYGMDETKAVIKTTGKPGIVYDSQLPKHMKSIEKIREMEASWQVTPEQVVEESKARCPPVFVSLPDAVTVEEGEWARFCCRVTGHPKPRVMWLLNGNTIVNGSRYKLTYDGMYHFDIPKTRQYDTGKIEVIARSSAGEAAASAELKVIPRHDDYRGVLKNAPRPWYDETTQYQRTETELEKTFEERQVLQRQGVIDHRPELKPKVIKEPETEWQQSVKRKKNEEYYNKLQELENEQVIKESRLRESTHQYAIPGDKVTSNTVAKSMAQRYEDNLDQTEEVTEQRVQKKVTQKPRIPDPSESTVHGKEVHVAKQKQTQKEVVGDKEITRKITSTETTEIEHKAQTQERVVEGPVKPSKPPIFTKKMQPCRVFEHEQARFEVEFDGEPLPLIKWYRENFPIKNSPDFQIHTFSTKSILIIRQVFVEDSAVFAAVAENRGGTAKCSANLVVEEKRRQGRGGIVPPSFTLTAQNVNVTSGQLVRLDTKVTGTKPIDVYWLKNGKKVQPDIRNKILEEDGTYTLLILEAYPQDSGKYECVAINSAGEARCDAECVVSLPATKDKPKPQTKAANAPPEIIEPLKDKIVAEGQAIEFSCKIVGKPLPTVQWYKGDKLIKPSKYFQMSRTADEYTLRISEAFPEDEGDYKCVAYNSAGRVTVAAKLKVTQPDQADNLPALTPLRDIVVYEGQPAQFKTQITSKIKPTIQWLREGALIPETPDFQMIHEGNNAVLLIGNTYEEDTGTFTCRATTAAGQVETSAKLVVKKSRTRTQKTFDHKTQIQTTSTKKVEPTTGKTSYSTTEETNMLKVENIQDTETKNITTVPWRKREQLDMHFKKEDTLEIKHWRRSRPEQNKDTEHTSMIGTTTSTKEDKTKEVFERGVIEEHVKVQEVVETKLWRKPKTISEKKDLLQVSTHEDTNILKVENLQSVNVDTTSSKLETKSWRKPRLEESLEEVGPTKGVNEPEVCHWRKPKTSEILKDKNEEEIRVQEMKKQSTKALEVKDESKQKIPWTQEAIKLRPTKVEKSPIEKEKIEDVALKPVRKDSLMDEKSSEISELQNERQITEKKESLQETQLQPTEKNKLLENIVSEESKESTGKRRQREEITQKEVALKTVRKQEEFTEEKTEQKSLKPVLTTEKESKETEDRINTKDTRKPSIPWTQEAIKLRPTKMEKTPIEKEKFEDITLKPTRKQSLVDEITEEVCALKSALDDIEKEEHKPDKVSENNAPEERKWPTGKRQPKEETPQEEVVLKPTRKQKEPEEEKSEERKWPSGKRRPKEETPQEEVVLKPIPKQMEPEEEKPEEFQHKAVKKEKKIEDATPEEHKWPSGKRRPKEETPQEEVVLKPIPKQKEPEEEKPEEVQLKQVKKEKQIEDTTPEERKWPSGKRRPKEEAPQEEVVLKPVPKQKEPEEEKPEEVQLKPVKKEKQVEDVTPEERKWPSGKRRPKEETPQKEVLLEHVKKQEEIDEEKIEQNVLKDVSETEKESKERGDKIQTKDTRKSSIPWTQEAIKLRPTKVEKLPMEKEKLEDITLKPIRKDSMLGEKPEEANTLRALVDKIHTEEQELKDKERVQEIRDEQMKTDKPVEDAMPEERKWPTGKRRPKEATSQEEVVLKPVPKQKEPEEEKPEEVQLKPVKKEKQIEDATPEERKWPSGKRRPKEETPQEEVVLKPIPKQKEPEEEKPEEVQFKQVKKEKQIEDTTPEERKWPSGKRRPKEETPQEEVVLKPIPKQKEPEEEKPDEVQLKPVKKDKQIEDATPEERKWPSGKRRPKEETPQEEVVLKPIPKQKEPEEDKPEEVQLKPVKKDKQIEDVTPEERKWPSGKRRPKEETPQEEVVLKPVPKQKEPEEEKPEEVQLKPVKKDKQIEDVMPEERKWPSGKRRPKEETPQEEVVLKPVPKQKEPEEEKPEEVQLKPVKKEKQIEDVTPEERKWPSGKRRPKEETPQEEVVLKPVPKQKEPEEEKPEEVQLKPVKKDKQIEEATPEERKWPIGKRRPKEETPQEEVVLKPVPKQKEPEEEKPDEVQLKPVKKDKQIEDATPEERKWPSGKRRPKEETPQEEVVLKPIPKQKEPEEEKPDEIQLKPVKKDKQIEDVTPEERKWPSGKRRPKEETPQEEVVLKPIPKQKEPDEEKSEEVQLKPVKKDKQIEDVTPEERKWPSGKRRPKEETPQEEVVLKPVPKQKEPEEEKPEEVQLKPVKKEKQIEDVTPEERKWPSGKRRPKEETPQEEVVLKPIPKQKEPDEEKSEEVQLKPVKKEKQIEDVTPEERKWPSGKRRPKEETPQEEVVLKPIPKQKEPEEEKPEEVQLKPVKKEKQIEDVTPEERKWPSGKRRPKEETPQEEVVLKPIPKQKEPEEEKPDEVQLKPVKKDKQIEDATPEERKWPSGKRRPKEETPQEEVVLKPIPKQKEPEEDKPEEVQLKPVKKDKQIEDVTPEERKWPSGKRRPKEETPQEEVVLKPVPKQKEPEEEKPEEVQLKPVKKDKQIEDVTPEERKWPSGKRRPKEETPQEEVVLKPVPKQKEPEEEKPEEVQLKPVKKEKQIEDVTPEERKWPSGKRRPKEETPQEEVVLKPVPKQKEPEEEKPEEVQLKPVKKEKQIDDVTPEERKWPSGKRRPKEETPQEEVVLKPIPKQKEPEEEKPEEVQLKPVRKDKPIEKDSHIIEKDSTAYEYVPSVSEEDVLSDEKTSDVEEFAPRIVKALPTVVTTTEGKLIRLEAKAIGIPKPQVRWLRQGTELLQSTEYQIEELDDGTSILTMPEVYQDDTGEIVFEAYNHLGVTATIAALSVESIVGTQEYRKPEWVTHMEELQAALKATQSVPTFVKEIIPERVHEEEIVTFEAIYSGNPTPEILWYKDNKVIRTDERFIIENKENRTTCTIKKATKDLEGTYTCKAVSDIGLAVTKAKLQVFQRGSKIKKGKETKEKVTKQKVIKSEEESVGVEDTLDFATVSEVQALDKQHSTDKVKKRKAKIVVSESEHIETEDIALQKKVDEKTKGIPVEEKAKPILTTHEHVVLSEQQEGESVEPFDESYQTQKGIIKMVEADSNLVAEVNELLEVINAKEFGPGETPLRELAKIGYLLRRGITIEQIESLYDSQYFPSLLIPQSQSALVQLVERQGHGALITEVLTEETAQDEDIIAAKVGFKAFLKMVEMKHSSVEEVIAQFYPEDFKPRSWEQRAANEVIVEATADHVVEAHTTKVIKDSSKRKEKISKDKTKIQKNIIEEIVKQEESSQKALKILKPLLSEDCNESDEVQEIHSETIKYIKEIATDIPDTKIEVIPANEASNILLERREDVKANIKLDTSFPIIENVQLIQEKEEFLPIKKFPHSKIKSTVTESESLQVTEVEPAGAINEYFQNSSNATENIANRKIILSENIITSETHAAGILDDLDTQHENKRMETAKSTLILNNAVNVSQHILPTEERPLDDLKINASSAEIAFSPLISLNVIEVNEDMKEKYLETPDIDKGLVPNLNFNLLEPIEVGEVFVEDKSGKYYPELIVPTETARKDVLVSNQLITEIHDVQEKEGNVSDLKVPPKQEARVDIAIKDSLIISFEELNEKEGHLPVQEKPIQQSALKDVTLHSSLGNTITTTHIKESDFAPCDTPSRKAIITINEHLHQTNSETTTADSETILEKSKPTPESHADVSITALDKNTVEEVDVHEKEFELVIKEDKQMVKADVDIKSIEPIVMSEILHITTTDEMAKPQVVPEETASKSIEMTKAKIITIPFIHEKEQNENFLSKKPEEFDTSLIPVMPITVLETQLSESENKLHLNKIPSISRAEFTLTHQLKIPVKQEINTTDQIDFMTLPKENTGTASISRDLQKEIAVIETTVEEQLNKLEENEIQHNKVKTGYISNESINVTEIIPNIHETKLTISEEKTKQLATLDINSDHKLAITSEINLKERLGNLKSTIMETEEANLISTHLQSIQVLENNILDSQSTLENDIHPSPKTISSEIVPSQEILNITEIVQHEKEEEYEYYKLPDTSTANPFITGHLVAVSTEISPDVDVGDTDIVVDDVKTANVKNIAFNEIIISTVDWHEKEDEIKTTSTPTTVTASVGLNSSQALQIDERSTEIKPTSLIQNKLPFAKAEQDTVISEALTQQEILVHSSEGILSDINKNQSEMPVISVSTLHLPQCDEKTLIETEDYLRDTISPEMQHAAVAFRSQQGIQTSEVLSQSQSLEASQDFDMKYKNAVSKLDENYGKIANSEECTVNQSVGKLLEPAVKPQHSDLNAICENALERTEIIFGERERELDLCKPLASNITPHITEIHAVETNSTIIAEKEQELVSQKAPNVLEAFIEVVPHQSAIGMEVLASGNISKLESKDTKLVSAETTQDNLQSYVQEEIVHGEKEFEFVDTKTITANASEIIIQEKAKETLEVQPMEAEKDLRAAILDSEVNAKLAFNEQQSLQETEIVSSQESQSFSISDINLVNVSTGHEMQEAIKEYELFIGEVENTFTIPTADEKIGTGTVEEQKPLNITVIIANEKENTIQDTPVVKKETTQLIINGKNYVDVTEVMFSEKEQTFHTHNNLVEDKSVAPKTDIILKSSININETNATEGDVPFESDKIQYFEASTDIHANDHLQISENITVEKEIEIKPMLFPKTTLSEFNISPHMHLNVEIHQFNENEEALEETEIVKQVKSDVSLQTLKHLEVSEINFGEQSEKLLQEQKSKDASPHIGIETGEHILITETNIQESESTLHRNTSNMCKQGNFSVESILPLQIEEAIVKEKEGNLAEFVIKTSEKPEVTIKTQNYLVISNDIIRECGRNMEDSLTIPSLSSQQGVEINPATHITVSEMVPVEGTVRFADTTDTNTETKATPKQVVNTEVVNNDHQTIETVNKIVPDYMTENNKAQVAIEAQKSIVTSEDYPQETSGQIFTTTDNNFKQAALNIIEMKHVQQTEILLHEEIGKFAKNHVDNIQKADESHIILSEITQIKPDVIDDLRDMSSAIKPQVGEVSLEIEAHRCYETTENIAHETSYSITHDKNITKQVSESVLEVKPLEQTEIITSEHTGTITANSVETQTVTLKSIELQPLSQSEVLVNESETNLIDIDRKLSLKENATVNFNTAQGLIVDQVLNEEIPYDFRPSNNKPLVAQHNITPLTHIECSENIAEARTNQFTSDKVHLQTPKIKSTEMIPLIITDTQSMQMETEFKSSKPEEQKIRENYIIANETEVISEYFNEQTAPCFYEPVDLLREADEKIQHDQSNRVLITEQDGLVDDKLERISISSRSDVEETEEIITKFVQTPGYSEPQQIKTKRTILRKKKRVGDETGDVVIEETLDDEDLKKSIRKTKHDLNIVEYEGDESQIIDDLEKSKIEMPDEFLHIPKMATHLIIEDVTELTETLNEVLQESARKVHITEKKPETDDVQTVKSTKRLIKKKKGLNEEVTEITTVQKDDETPIKTITVIEEITPEESKPKEVIELPEEVTVEDSKTQEGKPKQKKITKRTIKKRVGPKVETTQITTEQEDDKEPIVSIQTTEELIDDSTTPLSDIEPDTAQVVEETPETVQITQVKTETGADQTVKTTKRVIKKRKGSKNEVTEITTVQKDDDTPLTTVTVVEETTPEESKPEEIMELPEEVTVEETKTKEGKLKQKKIIKRIIKKRVGPKVETTQITTEQEDDKQPVVSIQTSEELIDDTTTPLSEITPDTAQVVEETPEKVHITQVKTETGDVQTVKTTKRIIKKRKGPKEEVTEITTVQKDDEAPVTSVTVVEETTPEESKPEEVVELPEEVTVEETETPEGKPKQKKITKRIIKKRKGPKVETTQITTEQEDDKQPVVSIQTTEEVVDDTTTPLSDITPDTAQVVEETPEKVHITQVKTETGDVQTVKTTKRIIKKRKGPKEEVTEITTVQKDDEAPVTSVTVVEESTPEESKPEEVIELPEEVTVEETETKEGKPKQKKIIKRIIKKRVGPKVETTQITTEQEDDKQPVVSIQTTEELIDDTTTPLSEITPDIAQVVEETPEKVHITQVKTETGDVQIVKTTKRIIKKRKVPKEEVTEITTVQKDDEAPVTSVTVVEETTPEESKPEEVIELPEEVTVEETETKEGKPKQKKIIKRIIKKRVGPKVETTQITTEQEDDKQPVVSIQTTEELIDDTTTPLSEITPDTAQVVEETPEKVHITQVKTETGDVQTVKTTKRIIKKRKGPKEEVTEITTVQKDDEAPVTSVTVVEETTPEESKPEEVIELPEEVTVEETKTKEGKPKQKKITKRIIKKRKGPKVETTQITTEQEDEKQPVVSIQTTEELIDDTTTPLSEITPDTAQVVEETPEKVHITQVKTETGDVQTVKTTKRIIKKRKGPKKEVTEITTVQKDDEAPVTSVTVVEETTPEESKPEEVVELPEEVTVEETETHEGKPKIKKITKRIIKKRKGPKVETTQITTEQEDDKQPVVSIQTTEELVDDTTTPLSDITPDTAQVVEETPEKVHITQVKTETGDVQTVKTTKRIIKKRKGPKEEVTEITTVQKDDEAPVTSVTVVEETTPEESKPEEVIELPEEVTVEETETKEGKPKQKKIIKRIIKKRVGPKVETTQITTEQEDDKQPVVSIQTTEELIDDTTTPLSDITTDTAQVVEETPEKVHITQVKTETGDVQTVKTTKRIIKKRKGPKEEVTEITTVQKDDEAPVTSVTVVEESTPEESKPEEVIELPEEVTVEETETQEGKPKQKKITKRIIKKRVGPKVETTQITTEQEDDKQPVVSIQTTEELIDDTTTPLSEITPDTAQVVEETPEKVHITQVKTETGDVQTVKTTKRIIKKRKGPKQEVTEITTVQKDDEAPVTSVTVVEETTPEESKPEEVIELPEEVTVEETETKEGKPKQKKIVKRIIKKRVGPKVETTQITTEQEDNKQPVVSVQTTEELIDDTTTQLSDITPDTAQVVEETPEKVHITQVKTETGDFQTIKTTKRIIKKRKGPKEEVTEITTVQKDDEAPVTSVTVVEETTPEESKPEEVVELPEEVTVEETETKEGKPKQKKITKRIIKKRVGPKVETTQITTEQEDDKQPVVSVQTTEELVDDTTTPLSDITPDTAQVVEETPEKVHITQVKTETGDVQTIKTTKRIIKKRKGPKEEVTEITTVQKDDEAPVTSVSVIEETTPEESKPEEVIELPEEVTVEETETKEGKPKQKKITKRIIKKRVGPKVETTQITTEQEDDKQPVVSIQTTEELMDDTTTLLSEITPDTAQVVEETPEKVHITQVKTETGDVQTIKTTKRIIKKRKGPKEEVTEITTVQKDDEAPVTSVSVIEETTPEESKPEEVIELPEEVTVEETKTKEGKPKQKKITKRIIKKRKGPKVETTQITTEQEDDKQPVVSIQTTEELMDDTTTLLSEITPDTAQVVEETPEKVHITQVKTETGDVQTIKTTKRIIKKRKGPKEEVTEITTVQKDDEAPVTSVTVVEETTPEESKPEEVIELPEEVTVEETETKEGKPKQKKITKRIIKKRVGPKVETTQITTEQEDDKQPVVSIQTTEELMDDTTTLLSEITPDTAQVVEETPEKVHITQVKTETGDVQTIKTTKRIIKKRKGPKEEVTEITTVQKDDEAPVTSVSVIEETTPEESKPEEVIELPEEVTVEETETQEGKPKQKKITKRIIKKRVGPKVETTQITTEQEDDKQPVVSIQTTEELVDDTTTPLSDITPDTAQVVEETPEKVHITQVKTETGDVQTVKTTKRIIKKRKGPKEEVTEITTVQKDDEAPVTSVTVVEETTPEESKPEEVIELPEEVTVEETETKEGKPKQKKIIKRIIKKRVGPKVETTQITTEQEDDKQPVVSIQTTEELVDDTTTPLSDITPDTAQVVEETPEKVHITQVKTETGDVQTVKTTKRIIKKRKGPKEEVTEITTVQKDDEAPVTSVTVVEESTPEESKPEEVIELPEEVTVEETETQEGKPKQKKITKRIIKKRVGPKVETTQITTEQEDDKQPVVSIQTTEELVDDTTTPLSDITPDTAQVVEETPEKVHITQVKTETGDVQTVKTTKRIIKKRKGPKEEVTEITTVQKDDEAPVTSVTVVEETTPEESKPEEVIELPEEVTVEETETPEGKPKQKKITKRIIKKRVGPKIETTQITTEQEDDKQPVVSVQTTEELIDDTTTPLSDITPDTAQVVEETPEKVQITQVKTETGDVQTVKTTKRIIKKRRGPKEEVTEITIVQKDDEAPVTSVTVVEESTPEESKPEEVIELPEEVTVEETETKEGKPKQKKITKRIIKKRVGPKVETTQITTEQEDDKQPVVSIQTTEELVDDTTTPLSDITPDTAQVVEETPEKVHITQVKTETGDVQTIKTTKRIIKKRKGPKEEVTEITTVQKDDEAPVTSVSVIEETTPEESKPEEVLELPEEVTVEETETKEGKPKQKKITKRIIKKRVGPKVETTQITTEQEDDKQPVVSIQTTEELVDDTTTPLSDITPDTAQVVEETPEKVQITQVKTETGDVQTVKTTKRIIKKRKGPKEEVTEITTVQKDDEAPVTTVTVVEETTPEESKADEVVELPEEVTVEETETQEGKPKQKKITKRIIKKRVGPKVETTQITTEQEDDKQPVVSIQTTEELVDDTTTPLSDITPDTAQVVEETPEKVHITQVKTETGDVQTVKTTKRIIKKRKGPKEEVTEITTVQKDDEAPVTSVTVVEETTPEESKPEEIVELPEEVTVEETETPEGKPKQKKIIKRIIKKRVGPKVETTQITTEQEDDKQPVVSIQTTEELVDDTTTPLSDITPDTAQVVEETPEKVNITQVKTETGDVQTVKTTKRVIKKRKGPKEEVTEITTVQKDDEAPVTSVTVVEETTPEENKPEEVVELPEEVTVEETETQEGKPTQKKITKRIIKKRVGPKIETTQITTEQEDDKQPVVSVQTTEELIDDTTTPLSDITPDTAQVVEETPEKVHITQVKTETGDVQTVKTLKRVIKNKKGPKEEVTEITTVQKDDEAPVTTVTVVEETTPEESKADEVVELPEEVTVEETETQEGKPKQKKITKRIIKKRVGPKVETTQITTEQEDDKEPVVSVQTTEELIDDTTTPLSDITPDTAQVVEETPEKVQITQVKTETGDVQTVKTTKRIIKKRKGPKEEVTEITTVQKDDEAPVTSVTVVEETTPEESKPEEVVELPEEVTVEETETHEGKPKIKKITKRIIKKRVGPKIETTQITTEQEDDKQPVVSIQTTEELVDDTTTPLSDITPDTAQVVEETPEKVQITQVKTETGDVQTVKTTKRIIKKRRGPKEEVTEITIVQKDDEAPVTSVTVVEETTPEESKPEEVVELPEEVTVEETETPEGKPKQKKIIKRIIKKRVGPKVETTQITTEQEDDKQPVVSIQTTEELVDDTTTPLSDITPDTAQVVEETPEKVHITQVKTKTGDVQTVKTTKRVIKKKKGPKEEVTEITTVQKDDEAPVTTVTVVEETTPQESKPEEVVELPEEVTVEETETQEGKPKQKKITKRIIKKRVGPKVETTQITTEQEDDKQPVVSVQTTEELIDDTTTPLSDITPDTAQVVEETPEKVHITQVKTETGDVQTVKTTKRIIKKRKGPKEEVTEITTVQKDDEAPVTSVTVVEETTPEESKPEEIVELPEEVTVEETETPEGKPKQKKIIKRIIKKRVGPKVETTQITTEQEDDKQPVVSIQTTEELVDDTTTPLSDITPDTAQVVEETPEKVHITQVKTETGDVQTVKTTKRVIKKRKGPKEEVTEITTVQKDDEAPVTSVTVVEETTPEESKPEEVVELPEEVTVEETETPEGKPKQKKIIKRIIKKRVGPKVETTQITTEQEDDKQPVVSIQTTEELVDDTTTPLSDITPDTAQVVEETPEKVHITQVKTKTGDVQTVKTTKRVIKKKKGPKEEVTEITTVQKDDEAPVTSVTVVEETTPEESKPEEVVELPEEVTVEETETKEGKPKQKKITKRIIKKRVGPKVETTQITTEQEDDKQPVVSIQTTEELVDDTTTPLSDITPDTAQVVEETPEKVHITQVKTETGDVQTVKTTKRIIKKRKGPKEEVTEITTVQKDDEAPVTSVTVVEEITPEESKPEEVVELPEEVTVEETETHEGPKIETTQITTEQEDDKQPVVSIQTTEELVDDTTTPLSDITPDTAQVVEETPEKVHITQVKTETGDVQTVKTTKRIIKKRKGPKEEVTEITTVQKDDEAPVTSVTVVEETTPEESKPEEVVELPEEVTVEETETPEGKPKQKKIIKRIIKKRVGPKVETTQITTEQEDDKQPVVSIQTTEELVDDTTTPLSDITPDTAQVVEETPEKVHITQVKTETGDVQTVKTTKRIIKKRKGPKEEVTEITTVQKDDEAPVTSVNVVEETTPEESKPEEVVELPEEVTVEETETPEGKPKQKKIIKRIIKKRVGPKVETTQITTEQEDDKQPVVSIQTTEELVDDTTTPLSDITPDTAQVVEETPEKVHITQVKTETGDVQTVKTTKRVIKKRKGPKEEVTEITTVQKDDEAPVTSVTVVEETTPEESKPEEVVELPEEVTVEETETPEGKPKQKKIIKRIIKKRVGPKVETTQITTEQEDDKQPVVSIQTTEELVDDTTTPLSDITPDTAQVVEETPEKVHITQVKTKTGDVQTVKTTKRVIKKKKGPKEEVTEITTVQKDDEAPVTSVTVVEETTPEESKPEEVVELPEEVTVEETETKEGKPKQKKITKRIIKKRVGPKVETTQITTEQEDDKQPVVSIQTTEELVDDTTTPLSDITPDTAQVVEETPEKVHITQVKTETGDVQTVKTTKRIIKKRKGPKEEVTEITTVQKDDEAPVTSVTVVEEITPEESKPEEVVELPEEVTVEETETHEGKPKQKKITKRIIKKRVGPKIETTQITTEQEDDKQPVVSIQTTEELVDDTTTPLSDITPDTAQVVEETPEKVHITQVKTETGDVQTCYCSRRNYPEESKPEEVVELPEEVTVEETETPEGKPKQKKIIKRIIKKRVGPKVETTQITTEQEDDKQPVVSIQTTEELVDDTTTPLSDITPDTAQVVEETPEKVHITQVKTETGDVQTVKTTKRIIKKRKGPKEEVTEITTVQKDDEAPVTSVTVVEETTPEESKPEEVVELPEEVTVEETETKEGKPKQKKITKRIIKKRVGPKVETTQITTEQEDDKQPVVSIQTTEELVDDTTTPLSDITPDTAQVVEETPEKVHITQVKTETGDIQTVKTTKRVIKKKKGPKEEVTEITTVQKDDEAPVTSVTVVEETTPEESKPEEVVELPEEVTVEETETQEGKPKQKKITKRIIKKRVGPKIETTQITTEQEDDKQPVVSIQTTEELVDDTTTPLSDITPDTAQVVEETPEKVHITQVKTETGDIQTVKTTKRVIKKKKGPKEEVTEITTVQKDDEAPVTSVTVVEETTPEESKPEEVVELPEEVTVEETETQEGPKIETTQITTEQEDDKQPVVSIQTTEELVDDTTTPLSDITPDTAQVVEETPEKVQITQVKTETGDVQTVKTTKRIIKKRKGPKEEVTEITTVQKDDEAPVTSVTVVEETTPEESKPEEVVELPEEVTVEETETKEGKPKQKKITKRIIKKRVGPKVETTQITTEQEDDKQPVVSIQTTEELVDDTTTPLSDITPDTAQVVEETPEKVHITQVKTETGDIQTVKTTKRVIKKKKGPKEEVTEITTVQKDDEAPVTSVTVVDEITPEESKPEEVVELPEEVTVDETETPESKPKQKKITKRIIKKRVGPKIETTQITTEQEDDKQPVVSIQTTEELVDDTTTPLSDITPDTAQVVEETPEKVHITQVKTETGDVQTVKTTKRVIKKKKGPKEEVTEITTVQKDDEAPVTSVTVVEETTPEESKPEEVVELPEEVTVEETETPEGKPKQKKIIKRIIKKRVGPKVETTQITTEQENDKQPVVSIQTTDELVDDTTTPLSDITPDTAQVVEETPEKVHITQVKTETGDVQTVKTTKRVIKKKKGPKEEVTEITTVQKDDEAPVTSVTVVEETTPEESKPEEVVELPEEVTVEETETPEGKPKQKKITKRIIKKRKGPKVETTQITTEQEDDKQPVVSIQTTEELMDDTTTPLSDITPDTAQVVEETPEKVHITQVKTETGDVQIVKTTKRVIKKKKGPKEEVTEITTVQKDDEAPVTSVTVVEEITPEESKPEEVVELPEEVTVEETETPEGKPKQKKITKRIIKKRVGPKIETTQITTEQEDDKQPVVSVQTTEELIDDTTTPLSDITPDTAQVVEETPEKVHITQVKTETGDVQTVKTTKRVIKKKKGPKEEVTEITTVQKDDEAPVTSVTVVEETTPEESKPEEVVELPEEVTVEETETQEGKPTQKKITKRIIKKRVGPKIETTQITTEQEDDKQPVVSVQTTEELIDDTTTPLSDITPDTAQVVEETPEKVHITQVKTETGDVQTVKTTKRVIKKKKGPKEEVTEITTVQKDDEAPVTSVTVVEETTPEESKPEEVVELPEEVTVEETETHEGKPKQKKITKRIIKKRKGPKVETTQITTEQEDDKQPVVSVQTTEELIDDTTTPLSDITPDTAQVVEETPEKVHITQVKTETGDVQIVKTTKRVIKKKKGPKEEVTEITTVQKDDEAPVTSVTVVEETTPEESKPEEVVELPEEVTVEETETPEGKPKQKKITKSIIKKRVGPKIETTQITTEQEDDKQPVVSVQTTEELIDDTTTPLSDIRPDTAQVVEETPEKVHITQVKTETGDVQTVKTTKRVIKKKKGPKEEVTEITTVQKDDEAPVTSVSVIEETTPEESKPEEVVELPEEVTVEETETQEGKPTQKKITKRIIKKRVGPKIETTQITTEQEDDKQPVVSVQTTEELIDDTTTPLSDITPDTAQVVEETPEKVHITQVKTKTGDVQTVKTTKRVIKKKKGPKEEVTEITTVQKDDEAPVTSVSVIEETTPEESKPEEVVEIPEEVTVEETETQEGKPTQKKITKRIIKKRVGPKIETTQITTEEEDDKQPVVSIQTTEELIDDTTTPLSDIAPYTAQVVEETPEKVHITQVKTETGDVQTVKTTKRVIKKKKGPKEEVTEITTVQKDDEAPVTSVTVVEEITPEESKPEEVVELPEEVTVDETETPEGKPKQKKITKRIIKKRVGPKIETTQITTEQEDDKQPVVSVQTTEELIDDTTTPLSDIRPDIAQVVEETPEKVHITQVKTETGDVQTVKTTKRVIKKKKGPKEEVTEITTVQKDDEAPVTSVTVVEEITPEESKPEEVVELPEEVTVDETETPEGKPKQKKITKRIIKKRVGPKIETTQITTEQEDDKQPVVSVQTTEELIDDTTTPLSDITPDTAQVVEETPEKVNITQVKTETGDVQTVKTTKRVIKKRKGPKEEVTEITTVQKDDEAPVTSVTVVEETTPEENKPEEVVELPEEVTVEETETQEGKPTQKKITKRIIKKRVGPKIETTQITTEQEDDKQPVVSVQTTEELIDDTTTPLSDITPDTAQVVEETPEKVHITQVKTETGDVQTVKTLKRVIKYKKGPKEEVTEITTVQKDDEAPVTTVTVVEETTPEESKPEEVVELPQEVTVEETEPQEGKPTQKKITKRIIKKRVGPKIETTQITTEQEDDKQPVVSVQTTEELIDDTTTPLSDIIPDTAQVVVETPEKVHITQVKTKTGDVQTVKTTKRVIKKKKGPKEEVTEITTVQKDDEAPVTSVTVVEETTPEESKPEEVVELPEEVTVDETETHEGKPKQKKITKRIIKKRVGPKIETTQITTEQEDDKQPVVSVQTTEELIDDTTTPLSDITPDTAQFVEETPEKVHITQVKTKTGDIQTVKTTKRVIKKKKGPKEEVTEITTVQKDDEAPVTTVTVVEETTPEESKPDEVVELPEEVTVEETETQEGKPKQKKITKRIIKKRVGPKVETTQITTEQEDDKQPVVSVQTTEELIDDTTTPLSDITPDTTQVVEETPEKVHITQVKTETGDVQTVKTTKRVIKKRKGPKEEVTEITTVQKDDEAPVTTVTVIEETTPEESKPDEVVELPEEVTVEETETQEGKPKQKKITKRIIKKRVGPKVETTQITTEQEDDKQPVVSVQTTEELIDDTTTPLSDITPDTAQVVEETPEKVHITQVKTETGDVQTFKTTKRVIKKRKGPKEEVTEITTVQKDDEAPVTTVTVVEETTPEESKPDEVVELPEEVTVEETETQEGKPKQKKITKRIIKKRVGPKVETTQITTEQEDDKQPVVFVQTTKELIDDTTTPLSDITPDTAQVVEETPEKVHITQVKTKTGDVQTVKTTKRVIKKKKGPKEEVTEITTVQKDDEAPVTSITVVEETTPEESKPEEVVELPEEVTVEETETQEGKPKQKKTTKRIIKKRVGPKIETTQITTEQEDDKQPVVSVLTTEELIDDTTTPLSDITPDTAQVVEETPEKVHITQVKTKTGDVQTVKTTKRVIKKKKGPKEEVTEITTVQKDDEAPVTSVTVVEESTPEESKPEEVVELPEEVTVEETETQEGMPKQKKITKRIIKKRVGPKVETTQITTEQEDDKQPVVSVQTTEELIDDTTTPLSDITPDTTQVVEETPEKVHITQVKTETGDVQTVKTTKRVIKKRKGPKEEVTEITTVQKDDEAPVTTVTVIEETTPEESKPEEVVELPEEVTVEETETQEGKPKQKKITKRIIKKRVGPKVETTQITTEQEDDKQPVVSVQTTEELIDDTTTPLSDITPDTAQVVEETPEKVHITQVKTKTGDVQTVKTTKRVIKKKKGPKEEVTEITTVQKDDEAPVTSVTVVEESTPEESKPEEVVELPEEVTVEETETQEGMPKQKKITKRIIKKRVGPKVETTQITTEQEDDKQPVVSVQTTEELIDDTTTPLSDITPDTAQVVEETPEKVHITQVKTETGDVQTVKTTKRVIKKKKGPKEEVTEITTVQKDDEAPVTTVTVVEETTPEESKPDEVVELPEEVTVEETETQEGKPKQKKITKRIIKKRVGPKVETTQITTEQEDDKQPVVSVQTTDELIDDTTTPLSDITPDTAQVVEETPEKVHITQVKTETGDVQTVKTTKRVIKKKKGPKEEVTEITTVQKDDEAPVTSVTVVEETTPEESKPEEVVELPEEVTVEETETQEGKPKQKKITKRIIKKRVGPKIETTQITTEQEDDKQPVVSVQTTEELIDDTTTPLSDITPDTAQVVEETPEKVHITQVKTKTGDVQTVKTTKRVIKKKKGPKEEVTEITTVQKDDEAPVTTVTVVEETTPQESKPEEVVELPEEVTVEETETQEGKPKQKKITKRIIKKRVGPKVETTQITTEQEDDKQPVVSVQTTEELIDDTTTPLSDITPDTAQVVEETPEKVHITQVKTETGDVQTVKTTKRVIKKKKGPKEEVTEITTVQKDDEAPVTSVTVVEETTPEESKPEEVVELPEEVTVEETETQEGKPKQKKITKRIIKKRVGPKIETTQITTEQEDDKQPVVSVQTTEELIDDTTTPLSDITPDTAQVVEETPEKVHITQVKTKTGDVQTVKTTKRVIKKKKGPKEEVTEITTVQKDDEAPVTTVTVVEETTPQESKPEEVVELPEEVTVEETETQEGKPKQKKITKRIIKKRVGPKIETTQITTEQEDDKQPVVSVQTTDELIDDTTTPLSDITPDTAQVVEETPEKVHITQVKTKTGDVQTVKTTKRVIKKKKGPKEEVTEITTVQKDDEAPVTSITVVEETTPEESKPEEVVELPEEVTVEETETPEGKPKQKKITKRIIKKRVGPKIKTTQITTEQEDDKQPVVSVQTTEELIDDTTTPLSNITPDTAQVVEETPEKVHITQVKTKTGDVQTVKTTKRVIKKKKGPKEEVTEITTVQKDDEAPVTTVTVVEETTPQESKPEEVVELPEEVTVEETETQEGKPKQKKITKRIIKKRVGPKIETTQITTEQEDDKQPVVSVQTTDELIDDTTTPLSDITPDTAQVVEETPEKVHITQVKTKTGDVQTVKTTKRVIKKKKGLKEEVTEITTVQKDDEAPVTSITVVEETTPEESKPEEVVELPEEVTVEETETQEGKPKQKKTTKRIIKKRVGPKIETTQITIEQEDDKQPVVSIQTTEELKDDTTTPLSDITPNTAQVVEETPEKVHITQVKTKTGDVQTVKTTKRVIKKKKGPKEEVTEITTVQKDDEAPITTITVVEETTPEESKPEEVVELPEEVTVEETETPEGKPKQKKITKRTIKKRVGPKIETTQITTEQEDDKQPVVSVQTIEELIDDTTTPLSDITPDTAQVVEETPEKVHITQVKTETGDVQTVKTTKRVIKKKKGPKGEVTEITTVQKDDEAPITTITVVEETTPEESKPEEVVELPEEVTVEETETPEGKPKQKKITKRTIKKRVGPKIETTQITTEQEDDQQPVVSVQTTEELIDDTTTPLSDITPDTAQVVEEVPEKVHITQVKTEKIDV
Summary
Description
Key component in the assembly and functioning of adult and embryonic striated muscles and muscle tendons. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The size and extensibility of the cross-links are the main determinants of sarcomere extensibility properties of muscle. In non-muscle cells, seems to play a role in chromosome condensation and chromosome segregation during mitosis. Might link the lamina network to chromatin or nuclear actin, or both during interphase.
Key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The size and extensibility of the cross-links are the main determinants of sarcomere extensibility properties of muscle. In non-muscle cells, seems to play a role in chromosome condensation and chromosome segregation during mitosis. Might link the lamina network to chromatin or nuclear actin, or both during interphase.
Structural component of the muscle M line which is involved in assembly and organization of sarcomere myofilaments (PubMed:15313609, PubMed:16453163, PubMed:18801371, PubMed:22621901, PubMed:23283987, PubMed:27009202). The large isoform a, isoform b, isoform d and isoform f play an essential role in maintaining the organization of sarcomeres but not myofilament alignment during body wall muscle development whereas the small isoform c and isoform d appear to have a minor role (PubMed:15313609, PubMed:16453163, PubMed:22768340). Isoform b and isoform f are required for the organization of unc-15/paramyosin into sarcomere thick filaments in body wall muscles (PubMed:27009202). By binding mel-26, a substrate adapter of the cul-3 E3 ubiquitin-protein ligase complex, regulates the organization of myosin thick filaments, likely by preventing the degradation of microtubule severing protein mei-1 (PubMed:22621901). Acts as guanine nucleotide exchange factor (GEF) for Rho GTPase rho-1 but not ced-10, mig-2 and cdc-42 (PubMed:18801371). The large isoforms regulate Ca(2+) signaling during muscle contraction by ensuring the correct localization of sarco-endoplamic reticulum Ca(2+) ATPase sca-1 and ryanodine receptor unc-68 (PubMed:22768340). By controlling the contraction and/or organization of pharyngeal muscles, plays a role in the formation of pharyngeal gland cell extension (PubMed:21868609). In contrast to obscurins in other species, unlikely to have serine/threonine kinase activity as both protein kinase domains are predicted to be catalytically inactive (Probable).
Serine/threonine-protein kinase (PubMed:18390597, PubMed:20346955). Key component in the assembly and functioning of muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The size and extensibility of the cross-links are the main determinants of sarcomere extensibility properties of muscle. In non-muscle cells, seems to play a role in chromosome condensation and chromosome segregation during mitosis. Might link the lamina network to chromatin or nuclear actin, or both during interphase (By similarity).
Cytoskeletal protein required for organization of normal actin cytoskeleton. Roles in establishing cell morphology, motility, cell adhesion and cell-extracellular matrix interactions in a variety of cell types. May function as a scaffolding molecule with the potential to influence both actin polymerization and the assembly of existing actin filaments into higher-order arrays. Binds to proteins that bind to either monomeric or filamentous actin. Localizes at sites where active actin remodeling takes place, such as lamellipodia and membrane ruffles. Different isoforms may have functional differences. Involved in the control of morphological and cytoskeletal changes associated with dendritic cell maturation. Involved in targeting ACTN to specific subcellular foci.
Calcium/calmodulin-dependent myosin light chain kinase implicated in smooth muscle contraction via phosphorylation of myosin light chains (MLC). Also regulates actin-myosin interaction through a non-kinase activity. Phosphorylates PTK2B/PYK2 and myosin light-chains. Involved in the inflammatory response (e.g. apoptosis, vascular permeability, leukocyte diapedesis), cell motility and morphology, airway hyperreactivity and other activities relevant to asthma. Required for tonic airway smooth muscle contraction that is necessary for physiological and asthmatic airway resistance. Necessary for gastrointestinal motility. Implicated in the regulation of endothelial as well as vascular permeability, probably via the regulation of cytoskeletal rearrangements. In the nervous system it has been shown to control the growth initiation of astrocytic processes in culture and to participate in transmitter release at synapses formed between cultured sympathetic ganglion cells. Critical participant in signaling sequences that result in fibroblast apoptosis. Plays a role in the regulation of epithelial cell survival. Required for epithelial wound healing, especially during actomyosin ring contraction during purse-string wound closure. Mediates RhoA-dependent membrane blebbing. Triggers TRPC5 channel activity in a calcium-dependent signaling, by inducing its subcellular localization at the plasma membrane. Promotes cell migration (including tumor cells) and tumor metastasis. PTK2B/PYK2 activation by phosphorylation mediates ITGB2 activation and is thus essential to trigger neutrophil transmigration during acute lung injury (ALI). May regulate optic nerve head astrocyte migration. Probably involved in mitotic cytoskeletal regulation. Regulates tight junction probably by modulating ZO-1 exchange in the perijunctional actomyosin ring. Mediates burn-induced microvascular barrier injury; triggers endothelial contraction in the development of microvascular hyperpermeability by phosphorylating MLC. Essential for intestinal barrier dysfunction. Mediates Giardia spp.-mediated reduced epithelial barrier function during giardiasis intestinal infection via reorganization of cytoskeletal F-actin and tight junctional ZO-1. Necessary for hypotonicity-induced Ca(2+) entry and subsequent activation of volume-sensitive organic osmolyte/anion channels (VSOAC) in cervical cancer cells. Responsible for high proliferative ability of breast cancer cells through anti-apoptosis.
Calcium/calmodulin-dependent myosin light chain kinase implicated in smooth muscle contraction via phosphorylation of myosin light chains (MLC). Also regulates actin-myosin interaction through a non-kinase activity. Phosphorylates PTK2B/PYK2 and myosin light-chains. Involved in the inflammatory response (e.g. apoptosis, vascular permeability, leukocyte diapedesis), cell motility and morphology, airway hyperreactivity and other activities relevant to asthma. Required for tonic airway smooth muscle contraction that is necessary for physiological and asthmatic airway resistance. Necessary for gastrointestinal motility. Implicated in the regulation of endothelial as well as vascular permeability, probably via the regulation of cytoskeletal rearrangements. In the nervous system it has been shown to control the growth initiation of astrocytic processes in culture and to participate in transmitter release at synapses formed between cultured sympathetic ganglion cells. Critical participant in signaling sequences that result in fibroblast apoptosis. Plays a role in the regulation of epithelial cell survival. Required for epithelial wound healing, especially during actomyosin ring contraction during purse-string wound closure. Mediates RhoA-dependent membrane blebbing. Triggers TRPC5 channel activity in a calcium-dependent signaling, by inducing its subcellular localization at the plasma membrane. Promotes cell migration (including tumor cells) and tumor metastasis. PTK2B/PYK2 activation by phosphorylation mediates ITGB2 activation and is thus essential to trigger neutrophil transmigration during acute lung injury (ALI). May regulate optic nerve head astrocyte migration. Probably involved in mitotic cytoskeletal regulation. Regulates tight junction probably by modulating ZO-1 exchange in the perijunctional actomyosin ring. Mediates burn-induced microvascular barrier injury; triggers endothelial contraction in the development of microvascular hyperpermeability by phosphorylating MLC. Essential for intestinal barrier dysfunction. Mediates Giardia spp.-mediated reduced epithelial barrier function during giardiasis intestinal infection via reorganization of cytoskeletal F-actin and tight junctional ZO-1. Necessary for hypotonicity-induced Ca(2+) entry and subsequent activation of volume-sensitive organic osmolyte/anion channels (VSOAC) in cervical cancer cells.
Structural component of the muscle M line which is involved in assembly and organization of sarcomere (PubMed:22467859, PubMed:26251439). Required for the development and organization of indirect flight muscle sarcomeres by regulating the formation of M line and H zone and the correct assembly of thick and thin filaments in the sarcomere (PubMed:22467859, PubMed:26251439). Likely to have serine/threonine-protein kinase activity as one of the two protein kinase domains appears to be functional (Probable).
Promotes cleavage furrow maturation during cytokinesis in preimplantation embryos (PubMed:21215633). May play a role in the architecture of adhesive and flexible epithelial cell junctions (PubMed:17015624). May play a role during myocardial remodeling by imparting an effect on cardiac fibroblast migration (PubMed:24951538).
Promotes cleavage furrow maturation during cytokinesis in preimplantation embryos. May play a role in the architecture of adhesive and flexible epithelial cell junctions. May play a role during myocardial remodeling by imparting an effect on cardiac fibroblast migration.
Regulator of muscle contraction and relaxation. Senses mechanical strain that occurs during muscle activity by unfolding in clearly resolvable steps at differing forces (PubMed:18390597, PubMed:7190524). Plays a role in the organization of sarcomeres in body wall muscles (PubMed:25851606).
Displays low peroxidase activity and is likely to participate in H(2)O(2) metabolism and peroxidative reactions in the cardiovascular system. Plays a role in extracellular matrix formation.
Structural component of striated muscles which plays a role in myofibrillogenesis. Probably involved in the assembly of myosin into sarcomeric A bands in striated muscle (PubMed:11448995, PubMed:16205939). Has serine/threonine protein kinase activity and phosphorylates N-cadherin CDH2 and sodium/potassium-transporting ATPase subunit ATP1B1 (By similarity). Binds (via the PH domain) strongly to phosphatidylinositol 3,4-bisphosphate (PtdIns(3,4)P2) and phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2), and to a lesser extent to phosphatidylinositol 3-phosphate (PtdIns(3)P), phosphatidylinositol 4-phosphate (PtdIns(4)P), phosphatidylinositol 5-phosphate (PtdIns(5)P) and phosphatidylinositol 3,4,5-trisphosphate (PtdIns(3,4,5)P3) (PubMed:28826662).
Structural component of striated muscles which plays a role in myofibrillogenesis. Probably involved in the assembly of myosin into sarcomeric A bands in striated muscle (By similarity). Has serine/threonine protein kinase activity and phosphorylates N-cadherin CDH2 and sodium/potassium-transporting ATPase subunit ATP1B1 (PubMed:23392350). Binds (via the PH domain) strongly to phosphatidylinositol 3,4-bisphosphate (PtdIns(3,4)P2) and phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2), and to a lesser extent to phosphatidylinositol 3-phosphate (PtdIns(3)P), phosphatidylinositol 4-phosphate (PtdIns(4)P), phosphatidylinositol 5-phosphate (PtdIns(5)P) and phosphatidylinositol 3,4,5-trisphosphate (PtdIns(3,4,5)P3) (By similarity).
Isoform 2 and isoform 3: bind phosphatidylinositol bisphosphates (PIP2s) via their PH domains and negatively regulate the PI3K/AKT/mTOR signaling pathway, thus contributing to the regulation of cardiomyocyte size and adhesion.
Displays low peroxidase activity and is likely to participate in H(2)O(2) metabolism and peroxidative reactions in the cardiovascular system (By similarity). Plays a role in extracellular matrix formation.
Involved in the control of early migration of neurons expressing gonadotropin-releasing hormone (GNRH neurons) (PubMed:27137492). May be involved in the maintenance of osteochondroprogenitor cells pool (By similarity).
Required to confine migrating sex myoblasts to the ventral muscle quadrants during their migration through the body and for multiple aspects of sensory, motor, and interneuron axon guidance.
Core component of the 3M complex, a complex required to regulate microtubule dynamics and genome integrity. It is unclear how the 3M complex regulates microtubules, it could act by controlling the level of a microtubule stabilizer (By similarity). Acts as a regulator of the Cul7-RING(FBXW8) ubiquitin-protein ligase, playing a critical role in the ubiquitin ligase pathway that regulates Golgi morphogenesis and dendrite patterning in brain. Required to localize CUL7 to the Golgi apparatus in neurons.
Receptor for SLIT2, and probably SLIT1, which are thought to act as molecular guidance cue in cellular migration, including axonal navigation at the ventral midline of the neural tube and projection of axons to different regions during neuronal development.
Cell adhesion molecule that plays a role in neuronal self-avoidance. Promotes repulsion between specific neuronal processes of either the same cell or the same subtype of cells. Mediates within retinal amacrine and ganglion cell subtypes both isoneuronal self-avoidance for creating an orderly dendritic arborization and heteroneuronal self-avoidance to maintain the mosaic spacing between amacrine and ganglion cell bodies (By similarity). Receptor for netrin required for axon guidance independently of and in collaboration with the receptor DCC (PubMed:18585357). Might also collaborate with UNC5C in NTN1-mediated axon repulsion independently of DCC (By similarity). In spinal cord development plays a role in guiding commissural axons projection and pathfinding across the ventral midline to reach the floor plate upon ligand binding. Enhances netrin-induced phosphorylation of PAK1 and FYN. Mediates intracellular signaling by stimulating the activation of MAPK8 and MAP kinase p38 (By similarity). Adhesion molecule that promotes lamina-specific synaptic connections in the retina: expressed in specific subsets of interneurons and retinal ganglion cells (RGCs) and promotes synaptic connectivity via homophilic interactions (By similarity).
Cell adhesion molecule that plays a role in neuronal self-avoidance. Promotes repulsion between specific neuronal processes of either the same cell or the same subtype of cells. Mediates within retinal amacrine and ganglion cell subtypes both isoneuronal self-avoidance for creating an orderly dendritic arborization and heteroneuronal self-avoidance to maintain the mosaic spacing between amacrine and ganglion cell bodies (PubMed:18216855, PubMed:19196994, PubMed:19945391). Receptor for netrin required for axon guidance independently of and in collaboration with the receptor DCC (PubMed:18585357). Might also collaborate with UNC5C in NTN1-mediated axon repulsion independently of DCC (PubMed:22685302). In spinal cord development plays a role in guiding commissural axons projection and pathfinding across the ventral midline to reach the floor plate upon ligand binding. Enhances netrin-induced phosphorylation of PAK1 and FYN. Mediates intracellular signaling by stimulating the activation of MAPK8 and MAP kinase p38. Adhesion molecule that promotes lamina-specific synaptic connections in the retina: expressed in specific subsets of interneurons and retinal ganglion cells (RGCs) and promotes synaptic connectivity via homophilic interactions (By similarity).
Involved in the control of early migration of neurons expressing gonadotropin-releasing hormone (GNRH neurons) (By similarity). May be involved in the maintenance of osteochondroprogenitor cells pool (PubMed:14962803).
Involved in the control of early migration of neurons expressing gonadotropin-releasing hormone (GNRH neurons) (By similarity). May be involved in the maintenance of osteochondroprogenitor cells pool (By similarity).
Cell adhesion molecule that plays a role in neuronal self-avoidance. Promotes repulsion between specific neuronal processes of either the same cell or the same subtype of cells. Mediates within retinal amacrine and ganglion cell subtypes both isoneuronal self-avoidance for creating an orderly dendritic arborization and heteroneuronal self-avoidance to maintain the mosaic spacing between amacrine and ganglion cell bodies (By similarity). Receptor for netrin required for axon guidance independently of and in collaboration with the receptor DCC (By similarity). Adhesion molecule that promotes lamina-specific synaptic connections in the retina: expressed in specific subsets of interneurons and retinal ganglion cells (RGCs) and promotes synaptic connectivity via homophilic interactions (PubMed:18216854).
Isoform PMR1: Endonuclease selectively degrading some target mRNAs while they are engaged by translating ribosomes, among which albumin and beta-globin mRNAs.
Cell adhesion molecule that plays a role in neuronal self-avoidance. Promotes repulsion between specific neuronal processes of either the same cell or the same subtype of cells. Mediates within retinal amacrine and ganglion cell subtypes both isoneuronal self-avoidance for creating an orderly dendritic arborization and heteroneuronal self-avoidance to maintain the mosaic spacing between amacrine and ganglion cell bodies (PubMed:10925149). Receptor for netrin required for axon guidance independently of and in collaboration with the receptor DCC. Might also collaborate with UNC5C in NTN1-mediated axon repulsion independently of DCC (By similarity). In spinal cord development plays a role in guiding commissural axons projection and pathfinding across the ventral midline to reach the floor plate upon ligand binding (PubMed:18585357, PubMed:19196994). Enhances netrin-induced phosphorylation of PAK1 and FYN (PubMed:15169762). Mediates intracellular signaling by stimulating the activation of MAPK8 and MAP kinase p38 (PubMed:18585357, PubMed:19196994). Adhesion molecule that promotes lamina-specific synaptic connections in the retina: expressed in specific subsets of interneurons and retinal ganglion cells (RGCs) and promotes synaptic connectivity via homophilic interactions (By similarity).
Receptor for SLIT1 and SLIT2 that mediates cellular responses to molecular guidance cues in cellular migration, including axonal navigation at the ventral midline of the neural tube and projection of axons to different regions during neuronal development (PubMed:10102268, PubMed:24560577). Interaction with the intracellular domain of FLRT3 mediates axon attraction towards cells expressing NTN1 (PubMed:24560577). In axon growth cones, the silencing of the attractive effect of NTN1 by SLIT2 may require the formation of a ROBO1-DCC complex (By similarity). Plays a role in the regulation of cell migration via its interaction with MYO9B; inhibits MYO9B-mediated stimulation of RHOA GTPase activity, and thereby leads to increased levels of active, GTP-bound RHOA (PubMed:26529257). May be required for lung development (By similarity).
Integral component of basement membranes. Component of the glomerular basement membrane (GBM), responsible for the fixed negative electrostatic membrane charge, and which provides a barrier which is both size- and charge-selective. It serves as an attachment substrate for cells. Plays essential roles in vascularization. Critical for normal heart development and for regulating the vascular response to injury. Also required for avascular cartilage development (By similarity).
Endorepellin in an anti-angiogenic and anti-tumor peptide that inhibits endothelial cell migration, collagen-induced endothelial tube morphogenesis and blood vessel growth in the chorioallantoic membrane. Blocks endothelial cell adhesion to fibronectin and type I collagen. Anti-tumor agent in neovascularization. Interaction with its ligand, integrin alpha2/beta1, is required for the anti-angiogenic properties. Evokes a reduction in phosphorylation of receptor tyrosine kinases via alpha2/beta1 integrin-mediated activation of the tyrosine phosphatase, PTPN6 (By similarity).
The LG3 peptide has anti-angiogenic properties that require binding of calcium ions for full activity.
Receptor for SLIT1 and SLIT2 that mediates cellular responses to molecular guidance cues in cellular migration, including axonal navigation at the ventral midline of the neural tube and projection of axons to different regions during neuronal development (PubMed:10433822, PubMed:24560577). Interaction with the intracellular domain of FLRT3 mediates axon attraction towards cells expressing NTN1 (PubMed:24560577). In axon growth cones, the silencing of the attractive effect of NTN1 by SLIT2 may require the formation of a ROBO1-DCC complex (By similarity). Plays a role in the regulation of cell migration via its interaction with MYO9B; inhibits MYO9B-mediated stimulation of RHOA GTPase activity, and thereby leads to increased levels of active, GTP-bound RHOA (By similarity). May be required for lung development (PubMed:11734623).
In kidney, has anti-inflammatory and anti-fibrotic properties by limiting the induction of chemokines, fibronectin and collagen expression in response to TGB1 and pro-inflammatory stimuli.
Receptor for SLIT1 and SLIT2 that mediates cellular responses to molecular guidance cues in cellular migration, including axonal navigation at the ventral midline of the neural tube and projection of axons to different regions during neuronal development. Interaction with the intracellular domain of FLRT3 mediates axon attraction towards cells expressing NTN1 (By similarity). In axon growth cones, the silencing of the attractive effect of NTN1 by SLIT2 may require the formation of a ROBO1-DCC complex (By similarity). Plays a role in the regulation of cell migration via its interaction with MYO9B; inhibits MYO9B-mediated stimulation of RHOA GTPase activity, and thereby leads to increased levels of active, GTP-bound RHOA (By similarity). May be required for lung development (By similarity).
Receptor for netrin required for axon guidance. Mediates axon attraction of neuronal growth cones in the developing nervous system upon ligand binding. Its association with UNC5 proteins may trigger signaling for axon repulsion. It also acts as a dependence receptor required for apoptosis induction when not associated with netrin ligand. Implicated as a tumor suppressor gene (By similarity).
Receptor for netrin required for axon guidance. Mediates axon attraction of neuronal growth cones in the developing nervous system upon ligand binding. Its association with UNC5 proteins may trigger signaling for axon repulsion. It also acts as a dependence receptor required for apoptosis induction when not associated with netrin ligand. Implicated as a tumor suppressor gene.
Thought to be involved during neural development in axonal navigation at the ventral midline of the neural tube. In spinal chord development plays a role in guiding commissural axons probably by preventing premature sensitivity to Slit proteins thus inhibiting Slit signaling through ROBO1 (By similarity). Required for hindbrain axon midline crossing.
Thought to be involved during neural development in axonal navigation at the ventral midline of the neural tube. In spinal chord development plays a role in guiding commissural axons probably by preventing premature sensitivity to Slit proteins thus inhibiting Slit signaling through ROBO1. Required for hindbrain axon midline crossing (By similarity).
Contactins mediate cell surface interactions during nervous system development. Has some neurite outgrowth-promoting activity. May be involved in synaptogenesis.
Contactins mediate cell surface interactions during nervous system development. Has some neurite outgrowth-promoting activity (By similarity).
May play a role in anteroposterior axis elongation.
Key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The size and extensibility of the cross-links are the main determinants of sarcomere extensibility properties of muscle. In non-muscle cells, seems to play a role in chromosome condensation and chromosome segregation during mitosis. Might link the lamina network to chromatin or nuclear actin, or both during interphase.
Structural component of the muscle M line which is involved in assembly and organization of sarcomere myofilaments (PubMed:15313609, PubMed:16453163, PubMed:18801371, PubMed:22621901, PubMed:23283987, PubMed:27009202). The large isoform a, isoform b, isoform d and isoform f play an essential role in maintaining the organization of sarcomeres but not myofilament alignment during body wall muscle development whereas the small isoform c and isoform d appear to have a minor role (PubMed:15313609, PubMed:16453163, PubMed:22768340). Isoform b and isoform f are required for the organization of unc-15/paramyosin into sarcomere thick filaments in body wall muscles (PubMed:27009202). By binding mel-26, a substrate adapter of the cul-3 E3 ubiquitin-protein ligase complex, regulates the organization of myosin thick filaments, likely by preventing the degradation of microtubule severing protein mei-1 (PubMed:22621901). Acts as guanine nucleotide exchange factor (GEF) for Rho GTPase rho-1 but not ced-10, mig-2 and cdc-42 (PubMed:18801371). The large isoforms regulate Ca(2+) signaling during muscle contraction by ensuring the correct localization of sarco-endoplamic reticulum Ca(2+) ATPase sca-1 and ryanodine receptor unc-68 (PubMed:22768340). By controlling the contraction and/or organization of pharyngeal muscles, plays a role in the formation of pharyngeal gland cell extension (PubMed:21868609). In contrast to obscurins in other species, unlikely to have serine/threonine kinase activity as both protein kinase domains are predicted to be catalytically inactive (Probable).
Serine/threonine-protein kinase (PubMed:18390597, PubMed:20346955). Key component in the assembly and functioning of muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The size and extensibility of the cross-links are the main determinants of sarcomere extensibility properties of muscle. In non-muscle cells, seems to play a role in chromosome condensation and chromosome segregation during mitosis. Might link the lamina network to chromatin or nuclear actin, or both during interphase (By similarity).
Cytoskeletal protein required for organization of normal actin cytoskeleton. Roles in establishing cell morphology, motility, cell adhesion and cell-extracellular matrix interactions in a variety of cell types. May function as a scaffolding molecule with the potential to influence both actin polymerization and the assembly of existing actin filaments into higher-order arrays. Binds to proteins that bind to either monomeric or filamentous actin. Localizes at sites where active actin remodeling takes place, such as lamellipodia and membrane ruffles. Different isoforms may have functional differences. Involved in the control of morphological and cytoskeletal changes associated with dendritic cell maturation. Involved in targeting ACTN to specific subcellular foci.
Calcium/calmodulin-dependent myosin light chain kinase implicated in smooth muscle contraction via phosphorylation of myosin light chains (MLC). Also regulates actin-myosin interaction through a non-kinase activity. Phosphorylates PTK2B/PYK2 and myosin light-chains. Involved in the inflammatory response (e.g. apoptosis, vascular permeability, leukocyte diapedesis), cell motility and morphology, airway hyperreactivity and other activities relevant to asthma. Required for tonic airway smooth muscle contraction that is necessary for physiological and asthmatic airway resistance. Necessary for gastrointestinal motility. Implicated in the regulation of endothelial as well as vascular permeability, probably via the regulation of cytoskeletal rearrangements. In the nervous system it has been shown to control the growth initiation of astrocytic processes in culture and to participate in transmitter release at synapses formed between cultured sympathetic ganglion cells. Critical participant in signaling sequences that result in fibroblast apoptosis. Plays a role in the regulation of epithelial cell survival. Required for epithelial wound healing, especially during actomyosin ring contraction during purse-string wound closure. Mediates RhoA-dependent membrane blebbing. Triggers TRPC5 channel activity in a calcium-dependent signaling, by inducing its subcellular localization at the plasma membrane. Promotes cell migration (including tumor cells) and tumor metastasis. PTK2B/PYK2 activation by phosphorylation mediates ITGB2 activation and is thus essential to trigger neutrophil transmigration during acute lung injury (ALI). May regulate optic nerve head astrocyte migration. Probably involved in mitotic cytoskeletal regulation. Regulates tight junction probably by modulating ZO-1 exchange in the perijunctional actomyosin ring. Mediates burn-induced microvascular barrier injury; triggers endothelial contraction in the development of microvascular hyperpermeability by phosphorylating MLC. Essential for intestinal barrier dysfunction. Mediates Giardia spp.-mediated reduced epithelial barrier function during giardiasis intestinal infection via reorganization of cytoskeletal F-actin and tight junctional ZO-1. Necessary for hypotonicity-induced Ca(2+) entry and subsequent activation of volume-sensitive organic osmolyte/anion channels (VSOAC) in cervical cancer cells. Responsible for high proliferative ability of breast cancer cells through anti-apoptosis.
Calcium/calmodulin-dependent myosin light chain kinase implicated in smooth muscle contraction via phosphorylation of myosin light chains (MLC). Also regulates actin-myosin interaction through a non-kinase activity. Phosphorylates PTK2B/PYK2 and myosin light-chains. Involved in the inflammatory response (e.g. apoptosis, vascular permeability, leukocyte diapedesis), cell motility and morphology, airway hyperreactivity and other activities relevant to asthma. Required for tonic airway smooth muscle contraction that is necessary for physiological and asthmatic airway resistance. Necessary for gastrointestinal motility. Implicated in the regulation of endothelial as well as vascular permeability, probably via the regulation of cytoskeletal rearrangements. In the nervous system it has been shown to control the growth initiation of astrocytic processes in culture and to participate in transmitter release at synapses formed between cultured sympathetic ganglion cells. Critical participant in signaling sequences that result in fibroblast apoptosis. Plays a role in the regulation of epithelial cell survival. Required for epithelial wound healing, especially during actomyosin ring contraction during purse-string wound closure. Mediates RhoA-dependent membrane blebbing. Triggers TRPC5 channel activity in a calcium-dependent signaling, by inducing its subcellular localization at the plasma membrane. Promotes cell migration (including tumor cells) and tumor metastasis. PTK2B/PYK2 activation by phosphorylation mediates ITGB2 activation and is thus essential to trigger neutrophil transmigration during acute lung injury (ALI). May regulate optic nerve head astrocyte migration. Probably involved in mitotic cytoskeletal regulation. Regulates tight junction probably by modulating ZO-1 exchange in the perijunctional actomyosin ring. Mediates burn-induced microvascular barrier injury; triggers endothelial contraction in the development of microvascular hyperpermeability by phosphorylating MLC. Essential for intestinal barrier dysfunction. Mediates Giardia spp.-mediated reduced epithelial barrier function during giardiasis intestinal infection via reorganization of cytoskeletal F-actin and tight junctional ZO-1. Necessary for hypotonicity-induced Ca(2+) entry and subsequent activation of volume-sensitive organic osmolyte/anion channels (VSOAC) in cervical cancer cells.
Structural component of the muscle M line which is involved in assembly and organization of sarcomere (PubMed:22467859, PubMed:26251439). Required for the development and organization of indirect flight muscle sarcomeres by regulating the formation of M line and H zone and the correct assembly of thick and thin filaments in the sarcomere (PubMed:22467859, PubMed:26251439). Likely to have serine/threonine-protein kinase activity as one of the two protein kinase domains appears to be functional (Probable).
Promotes cleavage furrow maturation during cytokinesis in preimplantation embryos (PubMed:21215633). May play a role in the architecture of adhesive and flexible epithelial cell junctions (PubMed:17015624). May play a role during myocardial remodeling by imparting an effect on cardiac fibroblast migration (PubMed:24951538).
Promotes cleavage furrow maturation during cytokinesis in preimplantation embryos. May play a role in the architecture of adhesive and flexible epithelial cell junctions. May play a role during myocardial remodeling by imparting an effect on cardiac fibroblast migration.
Regulator of muscle contraction and relaxation. Senses mechanical strain that occurs during muscle activity by unfolding in clearly resolvable steps at differing forces (PubMed:18390597, PubMed:7190524). Plays a role in the organization of sarcomeres in body wall muscles (PubMed:25851606).
Displays low peroxidase activity and is likely to participate in H(2)O(2) metabolism and peroxidative reactions in the cardiovascular system. Plays a role in extracellular matrix formation.
Structural component of striated muscles which plays a role in myofibrillogenesis. Probably involved in the assembly of myosin into sarcomeric A bands in striated muscle (PubMed:11448995, PubMed:16205939). Has serine/threonine protein kinase activity and phosphorylates N-cadherin CDH2 and sodium/potassium-transporting ATPase subunit ATP1B1 (By similarity). Binds (via the PH domain) strongly to phosphatidylinositol 3,4-bisphosphate (PtdIns(3,4)P2) and phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2), and to a lesser extent to phosphatidylinositol 3-phosphate (PtdIns(3)P), phosphatidylinositol 4-phosphate (PtdIns(4)P), phosphatidylinositol 5-phosphate (PtdIns(5)P) and phosphatidylinositol 3,4,5-trisphosphate (PtdIns(3,4,5)P3) (PubMed:28826662).
Structural component of striated muscles which plays a role in myofibrillogenesis. Probably involved in the assembly of myosin into sarcomeric A bands in striated muscle (By similarity). Has serine/threonine protein kinase activity and phosphorylates N-cadherin CDH2 and sodium/potassium-transporting ATPase subunit ATP1B1 (PubMed:23392350). Binds (via the PH domain) strongly to phosphatidylinositol 3,4-bisphosphate (PtdIns(3,4)P2) and phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2), and to a lesser extent to phosphatidylinositol 3-phosphate (PtdIns(3)P), phosphatidylinositol 4-phosphate (PtdIns(4)P), phosphatidylinositol 5-phosphate (PtdIns(5)P) and phosphatidylinositol 3,4,5-trisphosphate (PtdIns(3,4,5)P3) (By similarity).
Isoform 2 and isoform 3: bind phosphatidylinositol bisphosphates (PIP2s) via their PH domains and negatively regulate the PI3K/AKT/mTOR signaling pathway, thus contributing to the regulation of cardiomyocyte size and adhesion.
Displays low peroxidase activity and is likely to participate in H(2)O(2) metabolism and peroxidative reactions in the cardiovascular system (By similarity). Plays a role in extracellular matrix formation.
Involved in the control of early migration of neurons expressing gonadotropin-releasing hormone (GNRH neurons) (PubMed:27137492). May be involved in the maintenance of osteochondroprogenitor cells pool (By similarity).
Required to confine migrating sex myoblasts to the ventral muscle quadrants during their migration through the body and for multiple aspects of sensory, motor, and interneuron axon guidance.
Core component of the 3M complex, a complex required to regulate microtubule dynamics and genome integrity. It is unclear how the 3M complex regulates microtubules, it could act by controlling the level of a microtubule stabilizer (By similarity). Acts as a regulator of the Cul7-RING(FBXW8) ubiquitin-protein ligase, playing a critical role in the ubiquitin ligase pathway that regulates Golgi morphogenesis and dendrite patterning in brain. Required to localize CUL7 to the Golgi apparatus in neurons.
Receptor for SLIT2, and probably SLIT1, which are thought to act as molecular guidance cue in cellular migration, including axonal navigation at the ventral midline of the neural tube and projection of axons to different regions during neuronal development.
Cell adhesion molecule that plays a role in neuronal self-avoidance. Promotes repulsion between specific neuronal processes of either the same cell or the same subtype of cells. Mediates within retinal amacrine and ganglion cell subtypes both isoneuronal self-avoidance for creating an orderly dendritic arborization and heteroneuronal self-avoidance to maintain the mosaic spacing between amacrine and ganglion cell bodies (By similarity). Receptor for netrin required for axon guidance independently of and in collaboration with the receptor DCC (PubMed:18585357). Might also collaborate with UNC5C in NTN1-mediated axon repulsion independently of DCC (By similarity). In spinal cord development plays a role in guiding commissural axons projection and pathfinding across the ventral midline to reach the floor plate upon ligand binding. Enhances netrin-induced phosphorylation of PAK1 and FYN. Mediates intracellular signaling by stimulating the activation of MAPK8 and MAP kinase p38 (By similarity). Adhesion molecule that promotes lamina-specific synaptic connections in the retina: expressed in specific subsets of interneurons and retinal ganglion cells (RGCs) and promotes synaptic connectivity via homophilic interactions (By similarity).
Cell adhesion molecule that plays a role in neuronal self-avoidance. Promotes repulsion between specific neuronal processes of either the same cell or the same subtype of cells. Mediates within retinal amacrine and ganglion cell subtypes both isoneuronal self-avoidance for creating an orderly dendritic arborization and heteroneuronal self-avoidance to maintain the mosaic spacing between amacrine and ganglion cell bodies (PubMed:18216855, PubMed:19196994, PubMed:19945391). Receptor for netrin required for axon guidance independently of and in collaboration with the receptor DCC (PubMed:18585357). Might also collaborate with UNC5C in NTN1-mediated axon repulsion independently of DCC (PubMed:22685302). In spinal cord development plays a role in guiding commissural axons projection and pathfinding across the ventral midline to reach the floor plate upon ligand binding. Enhances netrin-induced phosphorylation of PAK1 and FYN. Mediates intracellular signaling by stimulating the activation of MAPK8 and MAP kinase p38. Adhesion molecule that promotes lamina-specific synaptic connections in the retina: expressed in specific subsets of interneurons and retinal ganglion cells (RGCs) and promotes synaptic connectivity via homophilic interactions (By similarity).
Involved in the control of early migration of neurons expressing gonadotropin-releasing hormone (GNRH neurons) (By similarity). May be involved in the maintenance of osteochondroprogenitor cells pool (PubMed:14962803).
Involved in the control of early migration of neurons expressing gonadotropin-releasing hormone (GNRH neurons) (By similarity). May be involved in the maintenance of osteochondroprogenitor cells pool (By similarity).
Cell adhesion molecule that plays a role in neuronal self-avoidance. Promotes repulsion between specific neuronal processes of either the same cell or the same subtype of cells. Mediates within retinal amacrine and ganglion cell subtypes both isoneuronal self-avoidance for creating an orderly dendritic arborization and heteroneuronal self-avoidance to maintain the mosaic spacing between amacrine and ganglion cell bodies (By similarity). Receptor for netrin required for axon guidance independently of and in collaboration with the receptor DCC (By similarity). Adhesion molecule that promotes lamina-specific synaptic connections in the retina: expressed in specific subsets of interneurons and retinal ganglion cells (RGCs) and promotes synaptic connectivity via homophilic interactions (PubMed:18216854).
Isoform PMR1: Endonuclease selectively degrading some target mRNAs while they are engaged by translating ribosomes, among which albumin and beta-globin mRNAs.
Cell adhesion molecule that plays a role in neuronal self-avoidance. Promotes repulsion between specific neuronal processes of either the same cell or the same subtype of cells. Mediates within retinal amacrine and ganglion cell subtypes both isoneuronal self-avoidance for creating an orderly dendritic arborization and heteroneuronal self-avoidance to maintain the mosaic spacing between amacrine and ganglion cell bodies (PubMed:10925149). Receptor for netrin required for axon guidance independently of and in collaboration with the receptor DCC. Might also collaborate with UNC5C in NTN1-mediated axon repulsion independently of DCC (By similarity). In spinal cord development plays a role in guiding commissural axons projection and pathfinding across the ventral midline to reach the floor plate upon ligand binding (PubMed:18585357, PubMed:19196994). Enhances netrin-induced phosphorylation of PAK1 and FYN (PubMed:15169762). Mediates intracellular signaling by stimulating the activation of MAPK8 and MAP kinase p38 (PubMed:18585357, PubMed:19196994). Adhesion molecule that promotes lamina-specific synaptic connections in the retina: expressed in specific subsets of interneurons and retinal ganglion cells (RGCs) and promotes synaptic connectivity via homophilic interactions (By similarity).
Receptor for SLIT1 and SLIT2 that mediates cellular responses to molecular guidance cues in cellular migration, including axonal navigation at the ventral midline of the neural tube and projection of axons to different regions during neuronal development (PubMed:10102268, PubMed:24560577). Interaction with the intracellular domain of FLRT3 mediates axon attraction towards cells expressing NTN1 (PubMed:24560577). In axon growth cones, the silencing of the attractive effect of NTN1 by SLIT2 may require the formation of a ROBO1-DCC complex (By similarity). Plays a role in the regulation of cell migration via its interaction with MYO9B; inhibits MYO9B-mediated stimulation of RHOA GTPase activity, and thereby leads to increased levels of active, GTP-bound RHOA (PubMed:26529257). May be required for lung development (By similarity).
Integral component of basement membranes. Component of the glomerular basement membrane (GBM), responsible for the fixed negative electrostatic membrane charge, and which provides a barrier which is both size- and charge-selective. It serves as an attachment substrate for cells. Plays essential roles in vascularization. Critical for normal heart development and for regulating the vascular response to injury. Also required for avascular cartilage development (By similarity).
Endorepellin in an anti-angiogenic and anti-tumor peptide that inhibits endothelial cell migration, collagen-induced endothelial tube morphogenesis and blood vessel growth in the chorioallantoic membrane. Blocks endothelial cell adhesion to fibronectin and type I collagen. Anti-tumor agent in neovascularization. Interaction with its ligand, integrin alpha2/beta1, is required for the anti-angiogenic properties. Evokes a reduction in phosphorylation of receptor tyrosine kinases via alpha2/beta1 integrin-mediated activation of the tyrosine phosphatase, PTPN6 (By similarity).
The LG3 peptide has anti-angiogenic properties that require binding of calcium ions for full activity.
Receptor for SLIT1 and SLIT2 that mediates cellular responses to molecular guidance cues in cellular migration, including axonal navigation at the ventral midline of the neural tube and projection of axons to different regions during neuronal development (PubMed:10433822, PubMed:24560577). Interaction with the intracellular domain of FLRT3 mediates axon attraction towards cells expressing NTN1 (PubMed:24560577). In axon growth cones, the silencing of the attractive effect of NTN1 by SLIT2 may require the formation of a ROBO1-DCC complex (By similarity). Plays a role in the regulation of cell migration via its interaction with MYO9B; inhibits MYO9B-mediated stimulation of RHOA GTPase activity, and thereby leads to increased levels of active, GTP-bound RHOA (By similarity). May be required for lung development (PubMed:11734623).
In kidney, has anti-inflammatory and anti-fibrotic properties by limiting the induction of chemokines, fibronectin and collagen expression in response to TGB1 and pro-inflammatory stimuli.
Receptor for SLIT1 and SLIT2 that mediates cellular responses to molecular guidance cues in cellular migration, including axonal navigation at the ventral midline of the neural tube and projection of axons to different regions during neuronal development. Interaction with the intracellular domain of FLRT3 mediates axon attraction towards cells expressing NTN1 (By similarity). In axon growth cones, the silencing of the attractive effect of NTN1 by SLIT2 may require the formation of a ROBO1-DCC complex (By similarity). Plays a role in the regulation of cell migration via its interaction with MYO9B; inhibits MYO9B-mediated stimulation of RHOA GTPase activity, and thereby leads to increased levels of active, GTP-bound RHOA (By similarity). May be required for lung development (By similarity).
Receptor for netrin required for axon guidance. Mediates axon attraction of neuronal growth cones in the developing nervous system upon ligand binding. Its association with UNC5 proteins may trigger signaling for axon repulsion. It also acts as a dependence receptor required for apoptosis induction when not associated with netrin ligand. Implicated as a tumor suppressor gene (By similarity).
Receptor for netrin required for axon guidance. Mediates axon attraction of neuronal growth cones in the developing nervous system upon ligand binding. Its association with UNC5 proteins may trigger signaling for axon repulsion. It also acts as a dependence receptor required for apoptosis induction when not associated with netrin ligand. Implicated as a tumor suppressor gene.
Thought to be involved during neural development in axonal navigation at the ventral midline of the neural tube. In spinal chord development plays a role in guiding commissural axons probably by preventing premature sensitivity to Slit proteins thus inhibiting Slit signaling through ROBO1 (By similarity). Required for hindbrain axon midline crossing.
Thought to be involved during neural development in axonal navigation at the ventral midline of the neural tube. In spinal chord development plays a role in guiding commissural axons probably by preventing premature sensitivity to Slit proteins thus inhibiting Slit signaling through ROBO1. Required for hindbrain axon midline crossing (By similarity).
Contactins mediate cell surface interactions during nervous system development. Has some neurite outgrowth-promoting activity. May be involved in synaptogenesis.
Contactins mediate cell surface interactions during nervous system development. Has some neurite outgrowth-promoting activity (By similarity).
May play a role in anteroposterior axis elongation.
Catalytic Activity
ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]
[myosin light chain]-L-serine + ATP = [myosin light chain]-O-phospho-L-serine + ADP + H(+)
[myosin light chain]-L-threonine + ATP = [myosin light chain]-O-phospho-L-threonine + ADP + H(+)
2 a phenolic donor + H2O2 = 2 a phenolic radical donor + 2 H2O
ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]
[myosin light chain]-L-serine + ATP = [myosin light chain]-O-phospho-L-serine + ADP + H(+)
[myosin light chain]-L-threonine + ATP = [myosin light chain]-O-phospho-L-threonine + ADP + H(+)
2 a phenolic donor + H2O2 = 2 a phenolic radical donor + 2 H2O
Cofactor
Mg(2+)
Ca(2+)
heme b
Ca(2+)
heme b
Biophysicochemical Properties
6.5 uM for MLC (isoform 1 at 22 degrees Celsius)
7.2 uM for MLC (isoform 2 at 22 degrees Celsius)
0.15 mM for H(2)O(2)
7.2 uM for MLC (isoform 2 at 22 degrees Celsius)
0.15 mM for H(2)O(2)
Subunit
Interacts with MYOM1, MYOM2, tropomyosin and myosin. Interacts with actin, primarily via the PEVK domains and with MYPN. Interacts with FHL2, NEB, CRYAB, LMNA/lamin-A and LMNB/lamin-B. Interacts with TCAP/telethonin and/or ANK1 isoform Mu17/ank1.5, via the first two N-terminal immunoglobulin domains. Interacts with TRIM63, TRIM55, ANKRD1, ANKRD2, ANKRD23, and CAPN3 through several Ig domains. Interacts with NBR1 through the protein kinase domain (By similarity). Interacts with CMYA5 (By similarity).
Interacts with MYOM1, MYOM2, tropomyosin and myosin. Interacts with actin, primarily via the PEVK domains and with MYPN (By similarity). Interacts with FHL2, NEB, CRYAB, LMNA/lamin-A and LMNB/lamin-B. Interacts with TCAP/telethonin and/or ANK1 isoform Mu17/ank1.5, via the first two N-terminal immunoglobulin domains. Interacts with TRIM63 and TRIM55, through several domains including immunoglobulin domains 141 and 142. Interacts with ANKRD1, ANKRD2 and ANKRD23, via the region between immunoglobulin domains 77 and 78 and interacts with CAPN3, via immunoglobulin domain 79. Interacts with NBR1 through the protein kinase domain. Interacts with CALM/calmodulin. Isoform 6 interacts with OBSCN isoform 3. Interacts with CMYA5.
May interact (via fibronectin type-III domain 1, Ig-like C2-type domain 48/49 and protein kinase domain 1 or C-terminus of the interkinase region) with lim-9 (via LIM zinc-binding domain) (PubMed:19244614). May interact (via fibronectin type-III domain 1, Ig-like C2-type domain 48/49 and kinase protein domain 1 or Ig-like C2-type domain 50, fibronectin type-III domain 2 and kinase protein domain 2) with scpl-1 isoforms a and b (via FCP1 homology domain); the interaction may act as a molecular bridge to bring two unc-89 molecules together or to stabilize a loop between the 2 kinase domains (PubMed:18337465, PubMed:19244614). May interact (via SH3 domain) with unc-15 (PubMed:27009202). May interact (via Ig-like C2-type domain 1-3) with cpna-1 (via VWFA domain) (PubMed:23283987). May interact (via Ig-like C2-type domain 2/3 and, Ig-like C2-type domain 50 and fibronectin type-III domain 2) with mel-26 (via MATH domain) (PubMed:22621901). May interact (via DH and PH domains) with rho-1, ced-10, mig-2 and cdc-42 (PubMed:18801371).
Interacts (via C-terminus) with myosin. Interacts with actin.
Interacts with EPS8 (By similarity). Interacts with LASP1 (By similarity). Interacts with VASP (By similarity). Interacts with ACTN (PubMed:15147863). Interacts with ARGBP2 (PubMed:16125169). Interacts with PFN1 (PubMed:16367745). Interacts with LPP (PubMed:17322171). Interacts with SPIN90 (PubMed:17537434). Interacts with SRC (PubMed:17537434). Interacts with EZR (PubMed:11598191). Interacts with RAI14 (By similarity).
Purified perlecan has a strong tendency to aggregate in dimers or stellate structures. It interacts with other basement membrane components such as laminin, prolargin and collagen type IV. Interacts with COL13A1, FGFBP1 and VWA1. Interacts (via C-terminus) with ECM1 (via C-terminus).
All isoforms including Telokin bind calmodulin. Interacts with SVIL (By similarity). Interacts with CTTN; this interaction is reduced during thrombin-induced endothelial cell (EC) contraction but is promoted by the barrier-protective agonist sphingosine 1-phosphate (S1P) within lamellipodia. A complex made of ABL1, CTTN and MYLK regulates cortical actin-based cytoskeletal rearrangement critical to sphingosine 1-phosphate (S1P)-mediated endothelial cell (EC) barrier enhancement. Binds to NAA10/ARD1 and PTK2B/PYK2.
All isoforms including Telokin bind calmodulin.
All isoforms including Telokin bind calmodulin. Interacts with CTTN; this interaction is reduced during thrombin-induced endothelial cell (EC) contraction but is promoted by the barrier-protective agonist sphingosine 1-phosphate (S1P) within lamellipodia. A complex made of ABL1, CTTN and MYLK regulates cortical actin-based cytoskeletal rearrangement critical to sphingosine 1-phosphate (S1P)-mediated endothelial cell (EC) barrier enhancement. Binds to NAA10/ARD1 (By similarity). Interacts with SVIL and PTK2B/PYK2.
Interacts with myosin (PubMed:22467859). May interact (via protein kinase domain 1) with ball (PubMed:26251439). May interact (via protein kinase domain 1 or 2) with mask (PubMed:26251439). May interact (via protein kinase domain 2) with Tm1/tropomyosin-1 (PubMed:26251439).
May interact (via protein kinase and CRD domains) with mak-1 (via protein kinase domain).
Interacts (via protein kinase domain 2) with CDH2 and (via protein kinase domain 1) with ATP1B1 (By similarity). Isoform 3 interacts with TTN/titin and calmodulin (PubMed:11448995, PubMed:11717165). Isoform 3 interacts with ANK1 isoform Mu17/ank1.5 (PubMed:12527750).
Interacts with MTM1. Isoform 3 is found as a monomer or homodimer.
Interacts (via protein kinase domain 1) with CDH2 and (via protein kinase domain 1) with ATP1B1 (PubMed:23392350). Isoform 2 is found in a complex with DSG2, DESM, GJA1, CDH2 and VCL (PubMed:28826662). Isoform 3 is found in a complex with DSG2, DESM, GJA1, CDH2, ANK3 and VCL (PubMed:28826662).
Interacts with MTM1 (By similarity). Isoform 3 is found as a monomer or homodimer.
Interacts with MTM1 (By similarity).
Interacts with SLIT2.
Component of the 3M complex, composed of core components CUL7, CCDC8 and OBSL1. Interacts with CCDC8. Interacts with CUL7; the interaction is direct. Interacts with FBXW8. Interacts (via N-terminal Ig-like domain) with TTN/titin (via C-terminal Ig-like domain); the interaction is direct (By similarity).
Homodimer; mediates homophilic interactions to promote cell adhesion (By similarity). Interacts with DCC; the interaction is abolished in response to NTN1 (By similarity). Interacts (via extracellular domain) with NTN1 (By similarity). Probably found in a ternary complex composed of DSCAM, PAK1 and RAC1 (By similarity). Interacts (via cytoplasmic domain) with PAK1; the interaction is direct and enhanced in presence of RAC1 (By similarity). Interacts with RAC1; the interaction requires PAK1 (By similarity). Interacts (via extracellular domain) with UNC5C (via Ig-like C2-type domain) (By similarity). Interacts with PTK2 (By similarity). Interacts with FYN (By similarity).
Homodimer; mediates homophilic interactions to promote cell adhesion (By similarity). Interacts with DCC; the interaction is abolished in response to NTN1 (PubMed:18585357). Interacts (via extracellular domain) with NTN1 (PubMed:18585357). Probably found in a ternary complex composed of DSCAM, PAK1 and RAC1 (By similarity). The interaction with PAK1 is direct and enhanced in presence of RAC1 (PubMed:15169762). Interacts with RAC1; the interaction requires PAK1 (By similarity). Interacts (via cytoplasmic domain) with PAK1 (By similarity). Interacts (via extracellular domain) with UNC5C (via Ig-like C2-type domain) (PubMed:22685302). Interacts with PTK2 (PubMed:22685302). Interacts with FYN (PubMed:22685302).
Homodimer; mediates homophilic interactions to promote cell adhesion.
Homodimer; mediates homophilic interactions to promote cell adhesion (By similarity). Interacts with DCC; the interaction is abolished in response to NTN1 (By similarity). Interacts (via extracellular domain) with NTN1 (PubMed:19196994). Probably found in a ternary complex composed of DSCAM, PAK1 and RAC1 (PubMed:15169762). Interacts (via cytoplasmic domain) with PAK1; the interaction is direct and enhanced in presence of RAC1 (PubMed:15169762). Interacts with RAC1; the interaction requires PAK1 (PubMed:15169762). Interacts (via extracellular domain) with UNC5C (via Ig-like C2-type domain) (PubMed:22685302). Interacts with PTK2 (By similarity). Interacts with FYN (By similarity).
Homodimer. Dimerization is mediated by the extracellular domain and is independent of SLIT liganding (PubMed:24673457). Interacts with SLIT1 (By similarity). Interacts with SLIT2 (PubMed:10102268, PubMed:11404413, PubMed:17848514). Interacts with FLRT3 (PubMed:24560577). Interacts with MYO9B (via Rho-GAP domain) (PubMed:26529257).
Purified perlecan has a strong tendency to aggregate in dimers or stellate structures. It interacts with other basement membrane components such as laminin, prolargin and collagen type IV. Interacts with COL13A1, FGFBP1 and VWA1. Interacts (via C-terminus) with ECM1 (via C-terminus) (By similarity).
Homodimer. Dimerization is mediated by the extracellular domain and is independent of SLIT liganding (By similarity). Interacts with SLIT1 (PubMed:10433822) Interacts with SLIT2 (By similarity). Interacts with FLRT3 (PubMed:24560577). Interacts with MYO9B (via Rho-GAP domain) (By similarity).
Interacts with the cytoplasmic part of UNC5A, UNC5B, UNC5C and probably UNC5D. Interacts with MAPK1. Interacts with NTN1 (By similarity). Interacts with DSCAM. Interacts with PTK2/FAK1. Interacts with MYO10. Interacts with CBLN4; this interaction can be competed by NTN1.
Homodimer. Dimerization is mediated by the extracellular domain and is independent of SLIT liganding (By similarity). Interacts with SLIT1 (By similarity). Interacts with SLIT2. Interacts with FLRT3. Interacts with MYO9B (via Rho-GAP domain) (By similarity).
Interacts with the cytoplasmic part of UNC5A, UNC5B, UNC5C and probably UNC5D (By similarity). Interacts with DSCAM. Interacts with PTK2/FAK1. Interacts with MYO10 (By similarity). Interacts with MAPK1. Interacts with NTN1. Interacts with CBLN4; this interaction can be competed by NTN1 (By similarity).
Interacts with the cytoplasmic part of UNC5A, UNC5B, UNC5C and probably UNC5D. Interacts with DSCAM. Interacts with PTK2/FAK1 and MAPK1. Interacts with NTN1 (By similarity). Interacts with MYO10. Interacts with CBLN4; this interaction can be competed by NTN1 (By similarity).
Probably interacts with SLIT2.
Interacts with PTPRG.
Monomer.
Interacts with MYOM1, MYOM2, tropomyosin and myosin. Interacts with actin, primarily via the PEVK domains and with MYPN (By similarity). Interacts with FHL2, NEB, CRYAB, LMNA/lamin-A and LMNB/lamin-B. Interacts with TCAP/telethonin and/or ANK1 isoform Mu17/ank1.5, via the first two N-terminal immunoglobulin domains. Interacts with TRIM63 and TRIM55, through several domains including immunoglobulin domains 141 and 142. Interacts with ANKRD1, ANKRD2 and ANKRD23, via the region between immunoglobulin domains 77 and 78 and interacts with CAPN3, via immunoglobulin domain 79. Interacts with NBR1 through the protein kinase domain. Interacts with CALM/calmodulin. Isoform 6 interacts with OBSCN isoform 3. Interacts with CMYA5.
May interact (via fibronectin type-III domain 1, Ig-like C2-type domain 48/49 and protein kinase domain 1 or C-terminus of the interkinase region) with lim-9 (via LIM zinc-binding domain) (PubMed:19244614). May interact (via fibronectin type-III domain 1, Ig-like C2-type domain 48/49 and kinase protein domain 1 or Ig-like C2-type domain 50, fibronectin type-III domain 2 and kinase protein domain 2) with scpl-1 isoforms a and b (via FCP1 homology domain); the interaction may act as a molecular bridge to bring two unc-89 molecules together or to stabilize a loop between the 2 kinase domains (PubMed:18337465, PubMed:19244614). May interact (via SH3 domain) with unc-15 (PubMed:27009202). May interact (via Ig-like C2-type domain 1-3) with cpna-1 (via VWFA domain) (PubMed:23283987). May interact (via Ig-like C2-type domain 2/3 and, Ig-like C2-type domain 50 and fibronectin type-III domain 2) with mel-26 (via MATH domain) (PubMed:22621901). May interact (via DH and PH domains) with rho-1, ced-10, mig-2 and cdc-42 (PubMed:18801371).
Interacts (via C-terminus) with myosin. Interacts with actin.
Interacts with EPS8 (By similarity). Interacts with LASP1 (By similarity). Interacts with VASP (By similarity). Interacts with ACTN (PubMed:15147863). Interacts with ARGBP2 (PubMed:16125169). Interacts with PFN1 (PubMed:16367745). Interacts with LPP (PubMed:17322171). Interacts with SPIN90 (PubMed:17537434). Interacts with SRC (PubMed:17537434). Interacts with EZR (PubMed:11598191). Interacts with RAI14 (By similarity).
Purified perlecan has a strong tendency to aggregate in dimers or stellate structures. It interacts with other basement membrane components such as laminin, prolargin and collagen type IV. Interacts with COL13A1, FGFBP1 and VWA1. Interacts (via C-terminus) with ECM1 (via C-terminus).
All isoforms including Telokin bind calmodulin. Interacts with SVIL (By similarity). Interacts with CTTN; this interaction is reduced during thrombin-induced endothelial cell (EC) contraction but is promoted by the barrier-protective agonist sphingosine 1-phosphate (S1P) within lamellipodia. A complex made of ABL1, CTTN and MYLK regulates cortical actin-based cytoskeletal rearrangement critical to sphingosine 1-phosphate (S1P)-mediated endothelial cell (EC) barrier enhancement. Binds to NAA10/ARD1 and PTK2B/PYK2.
All isoforms including Telokin bind calmodulin.
All isoforms including Telokin bind calmodulin. Interacts with CTTN; this interaction is reduced during thrombin-induced endothelial cell (EC) contraction but is promoted by the barrier-protective agonist sphingosine 1-phosphate (S1P) within lamellipodia. A complex made of ABL1, CTTN and MYLK regulates cortical actin-based cytoskeletal rearrangement critical to sphingosine 1-phosphate (S1P)-mediated endothelial cell (EC) barrier enhancement. Binds to NAA10/ARD1 (By similarity). Interacts with SVIL and PTK2B/PYK2.
Interacts with myosin (PubMed:22467859). May interact (via protein kinase domain 1) with ball (PubMed:26251439). May interact (via protein kinase domain 1 or 2) with mask (PubMed:26251439). May interact (via protein kinase domain 2) with Tm1/tropomyosin-1 (PubMed:26251439).
May interact (via protein kinase and CRD domains) with mak-1 (via protein kinase domain).
Interacts (via protein kinase domain 2) with CDH2 and (via protein kinase domain 1) with ATP1B1 (By similarity). Isoform 3 interacts with TTN/titin and calmodulin (PubMed:11448995, PubMed:11717165). Isoform 3 interacts with ANK1 isoform Mu17/ank1.5 (PubMed:12527750).
Interacts with MTM1. Isoform 3 is found as a monomer or homodimer.
Interacts (via protein kinase domain 1) with CDH2 and (via protein kinase domain 1) with ATP1B1 (PubMed:23392350). Isoform 2 is found in a complex with DSG2, DESM, GJA1, CDH2 and VCL (PubMed:28826662). Isoform 3 is found in a complex with DSG2, DESM, GJA1, CDH2, ANK3 and VCL (PubMed:28826662).
Interacts with MTM1 (By similarity). Isoform 3 is found as a monomer or homodimer.
Interacts with MTM1 (By similarity).
Interacts with SLIT2.
Component of the 3M complex, composed of core components CUL7, CCDC8 and OBSL1. Interacts with CCDC8. Interacts with CUL7; the interaction is direct. Interacts with FBXW8. Interacts (via N-terminal Ig-like domain) with TTN/titin (via C-terminal Ig-like domain); the interaction is direct (By similarity).
Homodimer; mediates homophilic interactions to promote cell adhesion (By similarity). Interacts with DCC; the interaction is abolished in response to NTN1 (By similarity). Interacts (via extracellular domain) with NTN1 (By similarity). Probably found in a ternary complex composed of DSCAM, PAK1 and RAC1 (By similarity). Interacts (via cytoplasmic domain) with PAK1; the interaction is direct and enhanced in presence of RAC1 (By similarity). Interacts with RAC1; the interaction requires PAK1 (By similarity). Interacts (via extracellular domain) with UNC5C (via Ig-like C2-type domain) (By similarity). Interacts with PTK2 (By similarity). Interacts with FYN (By similarity).
Homodimer; mediates homophilic interactions to promote cell adhesion (By similarity). Interacts with DCC; the interaction is abolished in response to NTN1 (PubMed:18585357). Interacts (via extracellular domain) with NTN1 (PubMed:18585357). Probably found in a ternary complex composed of DSCAM, PAK1 and RAC1 (By similarity). The interaction with PAK1 is direct and enhanced in presence of RAC1 (PubMed:15169762). Interacts with RAC1; the interaction requires PAK1 (By similarity). Interacts (via cytoplasmic domain) with PAK1 (By similarity). Interacts (via extracellular domain) with UNC5C (via Ig-like C2-type domain) (PubMed:22685302). Interacts with PTK2 (PubMed:22685302). Interacts with FYN (PubMed:22685302).
Homodimer; mediates homophilic interactions to promote cell adhesion.
Homodimer; mediates homophilic interactions to promote cell adhesion (By similarity). Interacts with DCC; the interaction is abolished in response to NTN1 (By similarity). Interacts (via extracellular domain) with NTN1 (PubMed:19196994). Probably found in a ternary complex composed of DSCAM, PAK1 and RAC1 (PubMed:15169762). Interacts (via cytoplasmic domain) with PAK1; the interaction is direct and enhanced in presence of RAC1 (PubMed:15169762). Interacts with RAC1; the interaction requires PAK1 (PubMed:15169762). Interacts (via extracellular domain) with UNC5C (via Ig-like C2-type domain) (PubMed:22685302). Interacts with PTK2 (By similarity). Interacts with FYN (By similarity).
Homodimer. Dimerization is mediated by the extracellular domain and is independent of SLIT liganding (PubMed:24673457). Interacts with SLIT1 (By similarity). Interacts with SLIT2 (PubMed:10102268, PubMed:11404413, PubMed:17848514). Interacts with FLRT3 (PubMed:24560577). Interacts with MYO9B (via Rho-GAP domain) (PubMed:26529257).
Purified perlecan has a strong tendency to aggregate in dimers or stellate structures. It interacts with other basement membrane components such as laminin, prolargin and collagen type IV. Interacts with COL13A1, FGFBP1 and VWA1. Interacts (via C-terminus) with ECM1 (via C-terminus) (By similarity).
Homodimer. Dimerization is mediated by the extracellular domain and is independent of SLIT liganding (By similarity). Interacts with SLIT1 (PubMed:10433822) Interacts with SLIT2 (By similarity). Interacts with FLRT3 (PubMed:24560577). Interacts with MYO9B (via Rho-GAP domain) (By similarity).
Interacts with the cytoplasmic part of UNC5A, UNC5B, UNC5C and probably UNC5D. Interacts with MAPK1. Interacts with NTN1 (By similarity). Interacts with DSCAM. Interacts with PTK2/FAK1. Interacts with MYO10. Interacts with CBLN4; this interaction can be competed by NTN1.
Homodimer. Dimerization is mediated by the extracellular domain and is independent of SLIT liganding (By similarity). Interacts with SLIT1 (By similarity). Interacts with SLIT2. Interacts with FLRT3. Interacts with MYO9B (via Rho-GAP domain) (By similarity).
Interacts with the cytoplasmic part of UNC5A, UNC5B, UNC5C and probably UNC5D (By similarity). Interacts with DSCAM. Interacts with PTK2/FAK1. Interacts with MYO10 (By similarity). Interacts with MAPK1. Interacts with NTN1. Interacts with CBLN4; this interaction can be competed by NTN1 (By similarity).
Interacts with the cytoplasmic part of UNC5A, UNC5B, UNC5C and probably UNC5D. Interacts with DSCAM. Interacts with PTK2/FAK1 and MAPK1. Interacts with NTN1 (By similarity). Interacts with MYO10. Interacts with CBLN4; this interaction can be competed by NTN1 (By similarity).
Probably interacts with SLIT2.
Interacts with PTPRG.
Monomer.
Miscellaneous
In some isoforms, after the PEVK repeat region there is a long PEVK duplicated region. On account of this region, it has been very difficult to sequence the whole protein. The length of this region (ranging from 183 to 2174 residues), may be a key elastic element of titin.
The LG3 peptide has been found in the urine of patients with end-stage renal disease and in the amniotic fluid of pregnant women with premature rupture of fetal membranes.
In asthmatic patients, overexpression promotes actin filament propulsion, thus contributing to airway hyperresponsiveness. Some MYLK variants may contribute to acute lung injury (ALI) susceptibility. Potential therapeutic target in the treatment of burn edema.
Determination of the mutation frequency of the unc-22 gene has been used to study the biological effects of short duration spaceflight.
Expression is under the tight control of the locus control region (LCRs).
Maps within a region of overlapping homozygous deletions characterized in both small cell lung cancer cell lines (SCLC) and in a breast cancer cell line. The promoter region of ROBO1 shows complete hypermethylation of CpG sites in the BT-20 breast tumor cell lines, some primary invasive breast carcinomasa and some primary clear cell renal cell carcinomas (CC-RCC).
Inactivation of DCC due to allelic deletion and/or point mutations is related to lymphatic and hematogenous metastatic tumor dissemination.
ROBO3 null deficient mice lack embryonal spinal chord commissural axons crossing the floor plate.
The LG3 peptide has been found in the urine of patients with end-stage renal disease and in the amniotic fluid of pregnant women with premature rupture of fetal membranes.
In asthmatic patients, overexpression promotes actin filament propulsion, thus contributing to airway hyperresponsiveness. Some MYLK variants may contribute to acute lung injury (ALI) susceptibility. Potential therapeutic target in the treatment of burn edema.
Determination of the mutation frequency of the unc-22 gene has been used to study the biological effects of short duration spaceflight.
Expression is under the tight control of the locus control region (LCRs).
Maps within a region of overlapping homozygous deletions characterized in both small cell lung cancer cell lines (SCLC) and in a breast cancer cell line. The promoter region of ROBO1 shows complete hypermethylation of CpG sites in the BT-20 breast tumor cell lines, some primary invasive breast carcinomasa and some primary clear cell renal cell carcinomas (CC-RCC).
Inactivation of DCC due to allelic deletion and/or point mutations is related to lymphatic and hematogenous metastatic tumor dissemination.
ROBO3 null deficient mice lack embryonal spinal chord commissural axons crossing the floor plate.
Similarity
Belongs to the protein kinase superfamily. CAMK Ser/Thr protein kinase family.
Belongs to the myotilin/palladin family.
Belongs to the peroxidase family. XPO subfamily.
Belongs to the immunoglobulin superfamily. ROBO/SAX3 family.
Belongs to the immunoglobulin superfamily. ROBO family.
Belongs to the immunoglobulin superfamily. DCC family.
Belongs to the immunoglobulin superfamily. Contactin family.
Belongs to the myotilin/palladin family.
Belongs to the peroxidase family. XPO subfamily.
Belongs to the immunoglobulin superfamily. ROBO/SAX3 family.
Belongs to the immunoglobulin superfamily. ROBO family.
Belongs to the immunoglobulin superfamily. DCC family.
Belongs to the immunoglobulin superfamily. Contactin family.
Keywords
Alternative splicing
Cell cycle
Cell division
Chromosome
Coiled coil
Complete proteome
Cytoplasm
Developmental protein
Disulfide bond
Immunoglobulin domain
Mitosis
Muscle protein
Nucleus
Reference proteome
Repeat
SH3 domain
TPR repeat
ATP-binding
Calcium
Calmodulin-binding
Direct protein sequencing
Kelch repeat
Kinase
Magnesium
Metal-binding
Methylation
Nucleotide-binding
Phosphoprotein
Transferase
WD repeat
3D-structure
Cardiomyopathy
Disease mutation
Limb-girdle muscular dystrophy
Polymorphism
Alternative promoter usage
Membrane
Actin-binding
Cell junction
Cell projection
Cytoskeleton
EGF-like domain
Extracellular matrix
Glycoprotein
Secreted
Sensory transduction
Signal
Angiogenesis
Basement membrane
Heparan sulfate
Laminin EGF-like domain
Proteoglycan
Acetylation
Aortic aneurysm
Age-related macular degeneration
Vision
Heme
Hydrogen peroxide
Iron
Leucine-rich repeat
Oxidoreductase
Peroxidase
Cell membrane
Chromosomal rearrangement
Differentiation
Lipid-binding
Transmembrane
Transmembrane helix
Chemotaxis
Neurogenesis
Golgi apparatus
Cell adhesion
Synapse
Osteogenesis
Endonuclease
Hydrolase
Nuclease
Receptor
Ubl conjugation
Alternative initiation
Apoptosis
Tumor suppressor
Mental retardation
GPI-anchor
Lipoprotein
Feature
chain Titin
splice variant In isoform B.
sequence variant In CMD1G; affects interaction with TCAP/telethonin; dbSNP:rs139517732.
propeptide Removed in mature form
splice variant In isoform B.
sequence variant In CMD1G; affects interaction with TCAP/telethonin; dbSNP:rs139517732.
propeptide Removed in mature form
Uniprot
Q9I7U4.3
A2ASS6.1
Q8WZ42.4
O01761.3
G4SLH0.2
Q8WX93.3
+ More
Q8NDA2.3 A2AJ76.1 P98160.4 Q15746.4 P11799.2 Q6PDN3.3 A8DYP0.1 D3YXG0.1 Q96RW7.2 Q23551.3 Q92626.2 Q5VST9.3 Q15772.4 A2AAJ9.3 Q3UQ28.2 Q3V1M1.2 A4IGL7.1 Q62407.2 Q63638.2 G5EBF1.1 Q9HCK4.2 D3ZZ80.3 Q7TPD3.2 Q8VHZ8.1 Q9ERC8.1 Q6WRH9.1 Q6WRI0.1 F1NY98.3 A1KZ92.3 O60469.2 Q9Y6N7.1 Q05793.1 O89026.1 P70211.2 Q9NR99.3 O55005.1 Q63155.2 P43146.2 Q96MS0.2 Q9Z2I4.2 Q8IVU1.2 Q69Z26.2 Q8BLI0.2 Q8IWV2.1 Q8BQC3.1 Q9P232.3 Q07409.2 Q589G5.1 Q2VWP7.1
Q8NDA2.3 A2AJ76.1 P98160.4 Q15746.4 P11799.2 Q6PDN3.3 A8DYP0.1 D3YXG0.1 Q96RW7.2 Q23551.3 Q92626.2 Q5VST9.3 Q15772.4 A2AAJ9.3 Q3UQ28.2 Q3V1M1.2 A4IGL7.1 Q62407.2 Q63638.2 G5EBF1.1 Q9HCK4.2 D3ZZ80.3 Q7TPD3.2 Q8VHZ8.1 Q9ERC8.1 Q6WRH9.1 Q6WRI0.1 F1NY98.3 A1KZ92.3 O60469.2 Q9Y6N7.1 Q05793.1 O89026.1 P70211.2 Q9NR99.3 O55005.1 Q63155.2 P43146.2 Q96MS0.2 Q9Z2I4.2 Q8IVU1.2 Q69Z26.2 Q8BLI0.2 Q8IWV2.1 Q8BQC3.1 Q9P232.3 Q07409.2 Q589G5.1 Q2VWP7.1
EC Number
2.7.11.1
2.7.11.18
1.11.1.7
2.7.11.18
1.11.1.7
Pubmed
10629221
10934048
10731132
12537572
9548712
10669599
+ More
9917396 8335002 11062264 12537569 22467859 26251439 19468303 9440711 16702235 17261657 17242355 21183079 24129315 7569978 10850961 11717165 15815621 15489334 8937992 7819249 10051295 12785098 8351016 1582406 8404852 17974005 9645487 12482578 12432079 12444090 14583192 14676215 15967462 16410549 16537787 20634290 7613868 9804419 9782056 11525170 16407954 10462489 12145747 11846417 11788824 12891679 16465475 15802564 17444505 17344846 23033978 25173926 8603916 9851916 15313609 16453163 17326220 18801371 18337465 19244614 21868609 22621901 22768340 23283987 27009202 11080629 12381307 18390597 20346955 10231032 10810093 14702039 12601173 11598191 15147863 16125169 17081983 16367745 16794588 16964243 17322171 17537434 17194196 16175505 17415588 17455999 18669648 19690332 20471940 20068231 21269460 21406692 23186163 24275569 16754980 15164053 16141072 17015624 21215633 1569102 1730768 16710414 8234307 11101850 1685141 1679749 2687294 15591058 12435733 11148217 11279527 11956183 12604605 12754519 16335952 17105986 18024432 19789387 19159218 22171320 21996443 8575746 9160829 10198165 11113114 10536370 15507455 15020676 16641997 12408982 11976941 14741352 15825080 16835238 16723733 16284075 18710790 18088087 18587400 18318008 19413330 19429448 19826488 20453870 20375339 20053363 20861316 20181817 20139351 21918590 19011151 22015949 22814378 18462678 21055718 7589469 2315320 9706877 2202734 3030394 1444462 1373815 9283094 12176732 10194305 10529260 11029314 11121372 11832329 11472067 8764148 12360480 16055522 16184195 17925381 17577141 18586037 21074048 20018858 20404178 15185077 18515368 24951538 14570714 2812002 8397135 7190524 2833427 16765996 25851606 8202162 8969309 10441517 11103812 18929642 9039502 19590037 21907015 11448995 16625316 10997877 11814696 12527750 12618763 16205939 28826662 16959974 8663449 16545539 10718198 16354304 25087613 15289607 23392350 18848646 27137492 15614763 10973969 12693553 16452087 19118250 15057822 22673903 9458046 10993679 16829019 9458045 10102268 11404413 17357069 21572988 14621295 15091338 18585357 11237714 11856873 15169762 18216855 19945391 19196994 22685302 14962803 16641100 15592404 18216854 16421571 12923263 22543864 9426258 10925149 10830953 9608531 9796701 10892742 12082532 24673457 24560577 26529257 17848514 1744087 2972708 7649154 10545953 16407285 18694874 19656770 19349973 11427896 11734623 10433822 12123796 19684588 19706539 8570174 15494734 22220752 28250456 21321230 15609104 15772651 27599751 22696596 23092983 26566883 11754167 28859078 8861902 24090084 21070949 7926722 16177791 2294591 1991322 8188295 9334332 20431009 28250454 21642953 8187090 15105459 10049565 15084255 14678835 16572171 9922388 9221934 15368895 9733924 20133774 12202991 14571131 11013081 15106122 9507132 10819331 8108413 15922677 16881056
9917396 8335002 11062264 12537569 22467859 26251439 19468303 9440711 16702235 17261657 17242355 21183079 24129315 7569978 10850961 11717165 15815621 15489334 8937992 7819249 10051295 12785098 8351016 1582406 8404852 17974005 9645487 12482578 12432079 12444090 14583192 14676215 15967462 16410549 16537787 20634290 7613868 9804419 9782056 11525170 16407954 10462489 12145747 11846417 11788824 12891679 16465475 15802564 17444505 17344846 23033978 25173926 8603916 9851916 15313609 16453163 17326220 18801371 18337465 19244614 21868609 22621901 22768340 23283987 27009202 11080629 12381307 18390597 20346955 10231032 10810093 14702039 12601173 11598191 15147863 16125169 17081983 16367745 16794588 16964243 17322171 17537434 17194196 16175505 17415588 17455999 18669648 19690332 20471940 20068231 21269460 21406692 23186163 24275569 16754980 15164053 16141072 17015624 21215633 1569102 1730768 16710414 8234307 11101850 1685141 1679749 2687294 15591058 12435733 11148217 11279527 11956183 12604605 12754519 16335952 17105986 18024432 19789387 19159218 22171320 21996443 8575746 9160829 10198165 11113114 10536370 15507455 15020676 16641997 12408982 11976941 14741352 15825080 16835238 16723733 16284075 18710790 18088087 18587400 18318008 19413330 19429448 19826488 20453870 20375339 20053363 20861316 20181817 20139351 21918590 19011151 22015949 22814378 18462678 21055718 7589469 2315320 9706877 2202734 3030394 1444462 1373815 9283094 12176732 10194305 10529260 11029314 11121372 11832329 11472067 8764148 12360480 16055522 16184195 17925381 17577141 18586037 21074048 20018858 20404178 15185077 18515368 24951538 14570714 2812002 8397135 7190524 2833427 16765996 25851606 8202162 8969309 10441517 11103812 18929642 9039502 19590037 21907015 11448995 16625316 10997877 11814696 12527750 12618763 16205939 28826662 16959974 8663449 16545539 10718198 16354304 25087613 15289607 23392350 18848646 27137492 15614763 10973969 12693553 16452087 19118250 15057822 22673903 9458046 10993679 16829019 9458045 10102268 11404413 17357069 21572988 14621295 15091338 18585357 11237714 11856873 15169762 18216855 19945391 19196994 22685302 14962803 16641100 15592404 18216854 16421571 12923263 22543864 9426258 10925149 10830953 9608531 9796701 10892742 12082532 24673457 24560577 26529257 17848514 1744087 2972708 7649154 10545953 16407285 18694874 19656770 19349973 11427896 11734623 10433822 12123796 19684588 19706539 8570174 15494734 22220752 28250456 21321230 15609104 15772651 27599751 22696596 23092983 26566883 11754167 28859078 8861902 24090084 21070949 7926722 16177791 2294591 1991322 8188295 9334332 20431009 28250454 21642953 8187090 15105459 10049565 15084255 14678835 16572171 9922388 9221934 15368895 9733924 20133774 12202991 14571131 11013081 15106122 9507132 10819331 8108413 15922677 16881056
EMBL
AB026845
AJ238575
AJ238577
AJ271740
AJ400900
AJ400901
+ More
AJ400902 AE014296 AF045775 AF045776 AF045777 AF045778 AJ245406 AJ012279 AJ012280 AF135062 AF135167 AF241648 AF241649 BK000146 AY094749 AAC23966.1 AAF47604.1 AAG40155.1 AAM11102.1 BAA90301.2 CAA09971.1 CAB76253.1 CAB93524.1 CAB96426.1 DAA00021.1 AL928681 AL928721 AL928789 CAM23449.1 CAM27059.1 X90568 X90569 AJ277892 AC009948 AC010680 FJ695199 AC023270 BC013396 BC058824 BC070170 BC107797 X98114 X98115 X83270 AF058332 AF525413 DQ248309 X64698 X64699 X64697 X69490 AL713647 U33058 FO080458 AY724774 AY714779 AY130758 BX284605 AAN61517.1 AAN61520.1 AAN61521.1 AF077041 AF464873 AB023209 AF151909 AK095512 AK096458 AC079858 AC079926 AC080188 AC084353 AC115538 BC013867 BC144666 AY211921 BX537391 ABBA01012042 ABBA01043973 AL354898 AL360004 AUXG01000072 FP565345 KF458942 CH471090 AK074396 AK093583 AL834139 AK083701 AL732564 AL732572 AL928861 M85289 X62515 AL590556 AL590103 L22078 AL445795 S76436 M64283 X85337 U48959 AF069601 AF069602 AF069603 AF069604 AF096771 AF096766 AF096767 AF096768 AF096769 AF096770 AF096773 AF096774 AF096775 AY424269 AY424270 AY339601 AB037663 AK300610 AK314412 AK314443 AC020634 AC023165 CH471052 BC100761 BC100762 BC100763 BC064420 X90870 X52876 M31048 M14953 AF045285 AF045255 AF045256 AF045257 AF045260 AF045259 AF045258 AF045261 AF045263 AF045265 AF045274 AF045273 AF045272 AF045271 AF045270 AF045269 AF045268 AF045267 AF045266 AF045283 AF045282 AF045281 AF045280 AF045279 AF045278 AF045277 AF045276 AF045275 AF045284 AF045264 AF045262 M96655 M88283 M88284 AY237727 AF314149 AY237726 AK162008 BC034209 BC045197 BC058610 AF335470 AAG34169.1 AAH34209.1 AAH45197.1 AAH58610.2 AAK53241.1 AAO85807.1 BAE36678.1 AE013599 DQ431841 ABD83643.1 AC111145 AC113326 AC115051 AC124120 AF156100 AK056336 AK056557 AL118512 AL121996 AL133515 AL133553 AL135796 AL135797 AL391824 BX928748 AJ306906 X15423 Z73897 Z73899 CAA33463.1 CAA98065.2 AF200348 EF090903 D86983 CH471053 BC098579 AJ002535 AJ314896 AJ314898 AJ314900 AJ314901 AJ314903 AJ314904 AJ314905 AJ314906 AJ314907 AJ314908 AL353593 AL359510 AL670729 AM231061 AB046776 AB046859 U57099 AK126500 AK289531 CR542201 AC053503 CH471063 BC006346 DQ395348 AY603755 AB037718 GL456158 BC044882 BC060226 AY603754 AAT80900.1 AK142872 AC159626 AC165078 BC112913 AC122038 AK143421 AC135238 AK132367 AK081990 BC135155 BK005589 U57098 AF215896 AK035543 AK164360 BC048698 BC062643 AK122488 AABR03067996 U57097 AF041053 FO080516 DQ533874 AB046788 DQ533873 AC016942 AC016952 AC024256 AC026877 AC067717 AC117514 AC117515 AC117516 AC126467 AC130004 AC131005 AC131154 AC133040 AC138974 BC064374 BC146772 AF040991 AC112361 BC055333 AK129396 AF334385 AY005483 AF315558 CH466602 AY273816 AY273815 AK093069 AK098838 BC031063 AADN03000073 AADN03000437 AADN03000849 EU170240 AY877349 AC090186 AC103958 AC107374 AC011128 AC012413 AK058200 AK131524 CH471068 AF023450 AF023449 AF217525 AL163283 AL163282 AL163281 AF040990 Z95705 AC016946 AC055731 AC106718 AC106720 AC108719 AC117461 AC117479 AC119035 AC123565 AC125624 AC125766 AC125815 AC131008 CH471110 BC001969 BC115022 BC157861 BC171855 BX538319 M77174 J04054 J04055 Y17793 X85788 AC105957 AC107230 AC109179 AC109499 AC121523 AC136637 AC161177 AC163492 AC167547 AC167548 AC167549 CH466528 AF245505 AC004616 BC011846 BC064986 BC080586 AL049946 AF041082 U68725 CH473971 X76132 AC011155 AC016383 AC019239 AC021486 AC027248 AC078999 AC090660 AC100777 AC103949 AC110591 AC116002 M32292 M32286 M32288 M32290 M63696 M63700 M63702 M63718 M63698 AY509035 AK056544 AF060570 BQ769335 AC105129 BC042054 BC067107 AF063936 X99043 AK036262 AK043507 BC115766 AK173340 AK045085 AL772130 AL807242 AL824705 BAC32213.1 AF464063 AY090737 AF549455 AK314396 AC018842 AC022002 AC022008 AC024057 AC026882 AC066608 AC087094 AC087427 CH471055 BC026119 AK051027 BC053057 AF026465 AF026466 AC016950 AC024222 AC128653 AC128656 BC150608 AB040929 AL512746 L01991 AC114423 AC153597 AC153600 AC155328 CH466523 AB185923 BAD93619.1 AY630258 AK098622 AAU05741.1 BAC05355.1
AJ400902 AE014296 AF045775 AF045776 AF045777 AF045778 AJ245406 AJ012279 AJ012280 AF135062 AF135167 AF241648 AF241649 BK000146 AY094749 AAC23966.1 AAF47604.1 AAG40155.1 AAM11102.1 BAA90301.2 CAA09971.1 CAB76253.1 CAB93524.1 CAB96426.1 DAA00021.1 AL928681 AL928721 AL928789 CAM23449.1 CAM27059.1 X90568 X90569 AJ277892 AC009948 AC010680 FJ695199 AC023270 BC013396 BC058824 BC070170 BC107797 X98114 X98115 X83270 AF058332 AF525413 DQ248309 X64698 X64699 X64697 X69490 AL713647 U33058 FO080458 AY724774 AY714779 AY130758 BX284605 AAN61517.1 AAN61520.1 AAN61521.1 AF077041 AF464873 AB023209 AF151909 AK095512 AK096458 AC079858 AC079926 AC080188 AC084353 AC115538 BC013867 BC144666 AY211921 BX537391 ABBA01012042 ABBA01043973 AL354898 AL360004 AUXG01000072 FP565345 KF458942 CH471090 AK074396 AK093583 AL834139 AK083701 AL732564 AL732572 AL928861 M85289 X62515 AL590556 AL590103 L22078 AL445795 S76436 M64283 X85337 U48959 AF069601 AF069602 AF069603 AF069604 AF096771 AF096766 AF096767 AF096768 AF096769 AF096770 AF096773 AF096774 AF096775 AY424269 AY424270 AY339601 AB037663 AK300610 AK314412 AK314443 AC020634 AC023165 CH471052 BC100761 BC100762 BC100763 BC064420 X90870 X52876 M31048 M14953 AF045285 AF045255 AF045256 AF045257 AF045260 AF045259 AF045258 AF045261 AF045263 AF045265 AF045274 AF045273 AF045272 AF045271 AF045270 AF045269 AF045268 AF045267 AF045266 AF045283 AF045282 AF045281 AF045280 AF045279 AF045278 AF045277 AF045276 AF045275 AF045284 AF045264 AF045262 M96655 M88283 M88284 AY237727 AF314149 AY237726 AK162008 BC034209 BC045197 BC058610 AF335470 AAG34169.1 AAH34209.1 AAH45197.1 AAH58610.2 AAK53241.1 AAO85807.1 BAE36678.1 AE013599 DQ431841 ABD83643.1 AC111145 AC113326 AC115051 AC124120 AF156100 AK056336 AK056557 AL118512 AL121996 AL133515 AL133553 AL135796 AL135797 AL391824 BX928748 AJ306906 X15423 Z73897 Z73899 CAA33463.1 CAA98065.2 AF200348 EF090903 D86983 CH471053 BC098579 AJ002535 AJ314896 AJ314898 AJ314900 AJ314901 AJ314903 AJ314904 AJ314905 AJ314906 AJ314907 AJ314908 AL353593 AL359510 AL670729 AM231061 AB046776 AB046859 U57099 AK126500 AK289531 CR542201 AC053503 CH471063 BC006346 DQ395348 AY603755 AB037718 GL456158 BC044882 BC060226 AY603754 AAT80900.1 AK142872 AC159626 AC165078 BC112913 AC122038 AK143421 AC135238 AK132367 AK081990 BC135155 BK005589 U57098 AF215896 AK035543 AK164360 BC048698 BC062643 AK122488 AABR03067996 U57097 AF041053 FO080516 DQ533874 AB046788 DQ533873 AC016942 AC016952 AC024256 AC026877 AC067717 AC117514 AC117515 AC117516 AC126467 AC130004 AC131005 AC131154 AC133040 AC138974 BC064374 BC146772 AF040991 AC112361 BC055333 AK129396 AF334385 AY005483 AF315558 CH466602 AY273816 AY273815 AK093069 AK098838 BC031063 AADN03000073 AADN03000437 AADN03000849 EU170240 AY877349 AC090186 AC103958 AC107374 AC011128 AC012413 AK058200 AK131524 CH471068 AF023450 AF023449 AF217525 AL163283 AL163282 AL163281 AF040990 Z95705 AC016946 AC055731 AC106718 AC106720 AC108719 AC117461 AC117479 AC119035 AC123565 AC125624 AC125766 AC125815 AC131008 CH471110 BC001969 BC115022 BC157861 BC171855 BX538319 M77174 J04054 J04055 Y17793 X85788 AC105957 AC107230 AC109179 AC109499 AC121523 AC136637 AC161177 AC163492 AC167547 AC167548 AC167549 CH466528 AF245505 AC004616 BC011846 BC064986 BC080586 AL049946 AF041082 U68725 CH473971 X76132 AC011155 AC016383 AC019239 AC021486 AC027248 AC078999 AC090660 AC100777 AC103949 AC110591 AC116002 M32292 M32286 M32288 M32290 M63696 M63700 M63702 M63718 M63698 AY509035 AK056544 AF060570 BQ769335 AC105129 BC042054 BC067107 AF063936 X99043 AK036262 AK043507 BC115766 AK173340 AK045085 AL772130 AL807242 AL824705 BAC32213.1 AF464063 AY090737 AF549455 AK314396 AC018842 AC022002 AC022008 AC024057 AC026882 AC066608 AC087094 AC087427 CH471055 BC026119 AK051027 BC053057 AF026465 AF026466 AC016950 AC024222 AC128653 AC128656 BC150608 AB040929 AL512746 L01991 AC114423 AC153597 AC153600 AC155328 CH466523 AB185923 BAD93619.1 AY630258 AK098622 AAU05741.1 BAC05355.1
Proteomes
PRIDE
Q9I7U4
A2ASS6
Q8WZ42
O01761
Q8WX93
Q8NDA2
+ More
A2AJ76 P98160 Q15746 P11799 Q6PDN3 A8DYP0 D3YXG0 Q96RW7 Q23551 Q92626 Q5VST9 Q15772 A2AAJ9 Q3UQ28 Q3V1M1 A4IGL7 Q62407 Q63638 G5EBF1 Q9HCK4 D3ZZ80 Q7TPD3 Q8VHZ8 Q9ERC8 Q6WRH9 Q6WRI0 F1NY98 A1KZ92 O60469 Q9Y6N7 Q05793 O89026 P70211 Q9NR99 O55005 Q63155 P43146 Q96MS0 Q9Z2I4 Q8IVU1 Q69Z26 Q8BLI0 Q8IWV2 Q8BQC3 Q9P232 Q07409 Q589G5 Q2VWP7
A2AJ76 P98160 Q15746 P11799 Q6PDN3 A8DYP0 D3YXG0 Q96RW7 Q23551 Q92626 Q5VST9 Q15772 A2AAJ9 Q3UQ28 Q3V1M1 A4IGL7 Q62407 Q63638 G5EBF1 Q9HCK4 D3ZZ80 Q7TPD3 Q8VHZ8 Q9ERC8 Q6WRH9 Q6WRI0 F1NY98 A1KZ92 O60469 Q9Y6N7 Q05793 O89026 P70211 Q9NR99 O55005 Q63155 P43146 Q96MS0 Q9Z2I4 Q8IVU1 Q69Z26 Q8BLI0 Q8IWV2 Q8BQC3 Q9P232 Q07409 Q589G5 Q2VWP7
Pfam
PF00041 fn3
+ More
PF07679 I-set
PF06582 Titin_Ig-rpts
PF00018 SH3_1
PF18362 THB
PF09042 Titin_Z
PF02818 PPAK
PF00069 Pkinase
PF05177 RCSD
PF00621 RhoGEF
PF12662 cEGF
PF07645 EGF_CA
PF07474 G2F
PF13895 Ig_2
PF00053 Laminin_EGF
PF00052 Laminin_B
PF00054 Laminin_G_1
PF00057 Ldl_recept_a
PF00008 EGF
PF00090 TSP_1
PF13855 LRR_8
PF00093 VWC
PF03098 An_peroxidase
PF00612 IQ
PF06583 Neogenin_C
PF08686 PLAC
PF07679 I-set
PF06582 Titin_Ig-rpts
PF00018 SH3_1
PF18362 THB
PF09042 Titin_Z
PF02818 PPAK
PF00069 Pkinase
PF05177 RCSD
PF00621 RhoGEF
PF12662 cEGF
PF07645 EGF_CA
PF07474 G2F
PF13895 Ig_2
PF00053 Laminin_EGF
PF00052 Laminin_B
PF00054 Laminin_G_1
PF00057 Ldl_recept_a
PF00008 EGF
PF00090 TSP_1
PF13855 LRR_8
PF00093 VWC
PF03098 An_peroxidase
PF00612 IQ
PF06583 Neogenin_C
PF08686 PLAC
Interpro
IPR013783
Ig-like_fold
+ More
IPR003961 FN3_dom
IPR003599 Ig_sub
IPR007110 Ig-like_dom
IPR013098 Ig_I-set
IPR036116 FN3_sf
IPR036028 SH3-like_dom_sf
IPR001452 SH3_domain
IPR010939 Titin-rpts
IPR036179 Ig-like_dom_sf
IPR003598 Ig_sub2
IPR015129 Titin_Z_rpt
IPR004168 PPAK_motif
IPR008266 Tyr_kinase_AS
IPR011009 Kinase-like_dom_sf
IPR040849 MyBP-C_THB
IPR013106 Ig_V-set
IPR000719 Prot_kinase_dom
IPR035899 DBL_dom_sf
IPR001849 PH_domain
IPR000219 DH-domain
IPR035526 Obscurin_SH3
IPR011993 PH-like_dom_sf
IPR007850 RCSD
IPR008271 Ser/Thr_kinase_AS
IPR017441 Protein_kinase_ATP_BS
IPR033017 Palladin_C
IPR001881 EGF-like_Ca-bd_dom
IPR032984 Hemicentin-2
IPR036465 vWFA_dom_sf
IPR009030 Growth_fac_rcpt_cys_sf
IPR006605 G2_nidogen/fibulin_G2F
IPR009017 GFP
IPR026823 cEGF
IPR013032 EGF-like_CS
IPR018097 EGF_Ca-bd_CS
IPR000742 EGF-like_dom
IPR000152 EGF-type_Asp/Asn_hydroxyl_site
IPR023415 LDLR_class-A_CS
IPR001791 Laminin_G
IPR000082 SEA_dom
IPR002049 Laminin_EGF
IPR000034 Laminin_IV
IPR013320 ConA-like_dom_sf
IPR036055 LDL_receptor-like_sf
IPR002172 LDrepeatLR_classA_rpt
IPR015725 MLCK1_kinase_dom
IPR036383 TSP1_rpt_sf
IPR000884 TSP1_rpt
IPR032675 LRR_dom_sf
IPR019791 Haem_peroxidase_animal
IPR000483 Cys-rich_flank_reg_C
IPR037120 Haem_peroxidase_sf_animal
IPR034828 Peroxidasin
IPR034824 Peroxidasin_peroxidase
IPR001007 VWF_dom
IPR010255 Haem_peroxidase_sf
IPR001611 Leu-rich_rpt
IPR003591 Leu-rich_rpt_typical-subtyp
IPR000048 IQ_motif_EF-hand-BS
IPR015726 Ser/Thr_kin_striated-sp
IPR000372 LRRNT
IPR033027 DSCAM_chordates
IPR029610 PXDNL
IPR032986 Robo1
IPR010560 Neogenin_C
IPR033012 DCC
IPR032987 Robo3
IPR033007 Contactin-4
IPR013273 ADAMTS/ADAMTS-like
IPR010909 PLAC
IPR033011 Protogenin
IPR003961 FN3_dom
IPR003599 Ig_sub
IPR007110 Ig-like_dom
IPR013098 Ig_I-set
IPR036116 FN3_sf
IPR036028 SH3-like_dom_sf
IPR001452 SH3_domain
IPR010939 Titin-rpts
IPR036179 Ig-like_dom_sf
IPR003598 Ig_sub2
IPR015129 Titin_Z_rpt
IPR004168 PPAK_motif
IPR008266 Tyr_kinase_AS
IPR011009 Kinase-like_dom_sf
IPR040849 MyBP-C_THB
IPR013106 Ig_V-set
IPR000719 Prot_kinase_dom
IPR035899 DBL_dom_sf
IPR001849 PH_domain
IPR000219 DH-domain
IPR035526 Obscurin_SH3
IPR011993 PH-like_dom_sf
IPR007850 RCSD
IPR008271 Ser/Thr_kinase_AS
IPR017441 Protein_kinase_ATP_BS
IPR033017 Palladin_C
IPR001881 EGF-like_Ca-bd_dom
IPR032984 Hemicentin-2
IPR036465 vWFA_dom_sf
IPR009030 Growth_fac_rcpt_cys_sf
IPR006605 G2_nidogen/fibulin_G2F
IPR009017 GFP
IPR026823 cEGF
IPR013032 EGF-like_CS
IPR018097 EGF_Ca-bd_CS
IPR000742 EGF-like_dom
IPR000152 EGF-type_Asp/Asn_hydroxyl_site
IPR023415 LDLR_class-A_CS
IPR001791 Laminin_G
IPR000082 SEA_dom
IPR002049 Laminin_EGF
IPR000034 Laminin_IV
IPR013320 ConA-like_dom_sf
IPR036055 LDL_receptor-like_sf
IPR002172 LDrepeatLR_classA_rpt
IPR015725 MLCK1_kinase_dom
IPR036383 TSP1_rpt_sf
IPR000884 TSP1_rpt
IPR032675 LRR_dom_sf
IPR019791 Haem_peroxidase_animal
IPR000483 Cys-rich_flank_reg_C
IPR037120 Haem_peroxidase_sf_animal
IPR034828 Peroxidasin
IPR034824 Peroxidasin_peroxidase
IPR001007 VWF_dom
IPR010255 Haem_peroxidase_sf
IPR001611 Leu-rich_rpt
IPR003591 Leu-rich_rpt_typical-subtyp
IPR000048 IQ_motif_EF-hand-BS
IPR015726 Ser/Thr_kin_striated-sp
IPR000372 LRRNT
IPR033027 DSCAM_chordates
IPR029610 PXDNL
IPR032986 Robo1
IPR010560 Neogenin_C
IPR033012 DCC
IPR032987 Robo3
IPR033007 Contactin-4
IPR013273 ADAMTS/ADAMTS-like
IPR010909 PLAC
IPR033011 Protogenin
SUPFAM
Gene 3D
CDD
ProteinModelPortal
Q9I7U4.3
A2ASS6.1
Q8WZ42.4
O01761.3
G4SLH0.2
Q8WX93.3
+ More
Q8NDA2.3 A2AJ76.1 P98160.4 Q15746.4 P11799.2 Q6PDN3.3 A8DYP0.1 D3YXG0.1 Q96RW7.2 Q23551.3 Q92626.2 Q5VST9.3 Q15772.4 A2AAJ9.3 Q3UQ28.2 Q3V1M1.2 A4IGL7.1 Q62407.2 Q63638.2 G5EBF1.1 Q9HCK4.2 D3ZZ80.3 Q7TPD3.2 Q8VHZ8.1 Q9ERC8.1 Q6WRH9.1 Q6WRI0.1 F1NY98.3 A1KZ92.3 O60469.2 Q9Y6N7.1 Q05793.1 O89026.1 P70211.2 Q9NR99.3 O55005.1 Q63155.2 P43146.2 Q96MS0.2 Q9Z2I4.2 Q8IVU1.2 Q69Z26.2 Q8BLI0.2 Q8IWV2.1 Q8BQC3.1 Q9P232.3 Q07409.2 Q589G5.1 Q2VWP7.1
Q8NDA2.3 A2AJ76.1 P98160.4 Q15746.4 P11799.2 Q6PDN3.3 A8DYP0.1 D3YXG0.1 Q96RW7.2 Q23551.3 Q92626.2 Q5VST9.3 Q15772.4 A2AAJ9.3 Q3UQ28.2 Q3V1M1.2 A4IGL7.1 Q62407.2 Q63638.2 G5EBF1.1 Q9HCK4.2 D3ZZ80.3 Q7TPD3.2 Q8VHZ8.1 Q9ERC8.1 Q6WRH9.1 Q6WRI0.1 F1NY98.3 A1KZ92.3 O60469.2 Q9Y6N7.1 Q05793.1 O89026.1 P70211.2 Q9NR99.3 O55005.1 Q63155.2 P43146.2 Q96MS0.2 Q9Z2I4.2 Q8IVU1.2 Q69Z26.2 Q8BLI0.2 Q8IWV2.1 Q8BQC3.1 Q9P232.3 Q07409.2 Q589G5.1 Q2VWP7.1
Ontologies
GO
GO:0007517
GO:0007520
GO:0007498
GO:0051301
GO:0000794
GO:0040011
GO:0045214
GO:0007062
GO:0007522
GO:0030018
GO:0005863
GO:0035206
GO:0030017
GO:0007525
GO:0031674
GO:0007076
GO:0003779
GO:0016203
GO:0008307
GO:0007519
GO:0048739
GO:0007512
GO:0055003
GO:0048769
GO:0035995
GO:0031672
GO:0005509
GO:0055002
GO:0042802
GO:0051015
GO:0006936
GO:0050790
GO:0043056
GO:0030016
GO:0007507
GO:0019901
GO:0055008
GO:0060048
GO:0042805
GO:0045859
GO:0060419
GO:0010737
GO:0005865
GO:0005524
GO:0019899
GO:0021591
GO:0051371
GO:0030240
GO:0043621
GO:0051592
GO:0071688
GO:0004674
GO:0002020
GO:0003007
GO:0030506
GO:1901897
GO:0031433
GO:0001701
GO:0005516
GO:0030241
GO:0005859
GO:0003300
GO:0001756
GO:0004713
GO:0010628
GO:0005200
GO:0050714
GO:0031430
GO:0030049
GO:0070062
GO:0006941
GO:0097493
GO:0005576
GO:0002576
GO:0005829
GO:0045989
GO:0004672
GO:1905905
GO:0040017
GO:0019902
GO:0017048
GO:0014722
GO:1905552
GO:0035023
GO:0034613
GO:0031034
GO:0090736
GO:0060298
GO:0005089
GO:0031965
GO:0017022
GO:0046872
GO:0007411
GO:0015629
GO:0030027
GO:0070593
GO:0098632
GO:0007156
GO:0005886
GO:0007010
GO:0030424
GO:0030426
GO:0005884
GO:0016477
GO:0002102
GO:0003382
GO:0003334
GO:0030036
GO:0001726
GO:0005925
GO:0005634
GO:0031012
GO:0032154
GO:0005604
GO:0005938
GO:0030054
GO:0005615
GO:0062023
GO:0050896
GO:0030021
GO:0050750
GO:0009888
GO:0006629
GO:0034446
GO:0043202
GO:0001523
GO:0006954
GO:0006027
GO:0044267
GO:0008022
GO:0030154
GO:0007420
GO:0030198
GO:0006898
GO:0006024
GO:0060548
GO:0005178
GO:0098797
GO:0009887
GO:0001540
GO:0072358
GO:0016525
GO:0001525
GO:1905907
GO:0005796
GO:0090303
GO:0060414
GO:0071476
GO:0032060
GO:0030335
GO:0004687
GO:0051928
GO:0006939
GO:0001725
GO:0006468
GO:0014820
GO:0005737
GO:0016020
GO:0035865
GO:0005911
GO:0071277
GO:0035690
GO:0036309
GO:0007527
GO:0016301
GO:0007275
GO:0005523
GO:0009617
GO:0007049
GO:0007157
GO:0038023
GO:0042803
GO:0005913
GO:0050839
GO:0005201
GO:0007601
GO:0035095
GO:0051782
GO:0018105
GO:0008344
GO:0018107
GO:0006979
GO:0055114
GO:0005783
GO:0042744
GO:0020037
GO:0005152
GO:0004601
GO:0006955
GO:0007186
GO:0043065
GO:0031432
GO:0042383
GO:0010314
GO:0016604
GO:0070273
GO:0032266
GO:0051056
GO:0043325
GO:0005546
GO:0005547
GO:0008285
GO:0042692
GO:1902936
GO:0014067
GO:0046777
GO:0014704
GO:0045296
GO:0042246
GO:0001503
GO:2001222
GO:0055013
GO:0060541
GO:0033563
GO:0005887
GO:1905489
GO:0008046
GO:0035385
GO:0097374
GO:0001764
GO:0007417
GO:0031290
GO:0030673
GO:0050925
GO:0035481
GO:0021891
GO:0060412
GO:0003184
GO:0003148
GO:0009986
GO:0050772
GO:0035904
GO:0001657
GO:0003180
GO:0021510
GO:0032870
GO:0003272
GO:0001656
GO:0016021
GO:0051964
GO:0061364
GO:0016199
GO:0005794
GO:0007088
GO:0007030
GO:0005813
GO:0048471
GO:0050775
GO:0034067
GO:1990393
GO:0000226
GO:0042327
GO:0007162
GO:0048842
GO:0043025
GO:0010842
GO:0030425
GO:0038007
GO:0007416
GO:0060219
GO:0045202
GO:0048813
GO:0007626
GO:1990782
GO:1990890
GO:0060060
GO:0004519
GO:0007155
GO:0007399
GO:1900748
GO:0033600
GO:0030275
GO:0035025
GO:0006919
GO:0002042
GO:0021836
GO:0030336
GO:0033116
GO:0010629
GO:0043406
GO:0070100
GO:0002062
GO:0048738
GO:0001958
GO:0008104
GO:0060351
GO:0048704
GO:0048814
GO:0060976
GO:0060763
GO:0003281
GO:0005042
GO:1901214
GO:0099170
GO:0006915
GO:0003713
GO:0032584
GO:0033564
GO:0098685
GO:0010976
GO:0021965
GO:0070374
GO:0045121
GO:0099061
GO:0071559
GO:0050808
GO:0001975
GO:1902842
GO:2000171
GO:0004888
GO:0097192
GO:0048671
GO:0007409
GO:0010977
GO:0071679
GO:0061642
GO:0050885
GO:0045665
GO:0031225
GO:0031175
GO:0008233
GO:0007158
GO:0048167
GO:0007413
GO:0051260
GO:0050768
GO:0005515
GO:0004177
GO:0008235
GO:0019538
GO:0030145
GO:0005622
GO:0006508
GO:0007169
PANTHER
Topology
Subcellular location
Cytoplasm
Nucleus
Chromosome
Colocalizes with ball and mask in Z-lines of indirect flight muscle (PubMed:26251439). In the embryo, localizes across the muscles in a striped pattern positioned at the sites at which muscles are attached to the epidermis. In the larval body wall muscles, localizes to the Z line and is still present as a doublet at the muscle-epidermal attachment sites. During pupa development, progressively forms broad striations at the Z line which become more defined after the pupa eclosion. With evidence from 12 publications.
Myofibril Localizes throughout the I-band except for dense bodies and in the outer edge of the A-band (PubMed:20346955). In embryo, co-localizes with lamin lmn-1 at the nuclear membrane. The localization to the nuclear envelope is lmn-1-dependent(PubMed:16410549). With evidence from 8 publications.
Sarcomere Localizes throughout the I-band except for dense bodies and in the outer edge of the A-band (PubMed:20346955). In embryo, co-localizes with lamin lmn-1 at the nuclear membrane. The localization to the nuclear envelope is lmn-1-dependent(PubMed:16410549). With evidence from 8 publications.
A band Localizes throughout the I-band except for dense bodies and in the outer edge of the A-band (PubMed:20346955). In embryo, co-localizes with lamin lmn-1 at the nuclear membrane. The localization to the nuclear envelope is lmn-1-dependent(PubMed:16410549). With evidence from 8 publications.
I band Localizes throughout the I-band except for dense bodies and in the outer edge of the A-band (PubMed:20346955). In embryo, co-localizes with lamin lmn-1 at the nuclear membrane. The localization to the nuclear envelope is lmn-1-dependent(PubMed:16410549). With evidence from 8 publications.
Nucleus membrane Localizes throughout the I-band except for dense bodies and in the outer edge of the A-band (PubMed:20346955). In embryo, co-localizes with lamin lmn-1 at the nuclear membrane. The localization to the nuclear envelope is lmn-1-dependent(PubMed:16410549). With evidence from 8 publications.
Cytoskeleton Localizes to stress fibers and Z lines (PubMed:11598191, PubMed:16125169, PubMed:17322171, PubMed:17537434). Preferentially expressed in the excitatory presynaptic terminals (By similarity). With evidence from 12 publications.
Cell junction Localizes to stress fibers and Z lines (PubMed:11598191, PubMed:16125169, PubMed:17322171, PubMed:17537434). Preferentially expressed in the excitatory presynaptic terminals (By similarity). With evidence from 12 publications.
Focal adhesion Localizes to stress fibers and Z lines (PubMed:11598191, PubMed:16125169, PubMed:17322171, PubMed:17537434). Preferentially expressed in the excitatory presynaptic terminals (By similarity). With evidence from 12 publications.
Z line Localizes to stress fibers and Z lines (PubMed:11598191, PubMed:16125169, PubMed:17322171, PubMed:17537434). Preferentially expressed in the excitatory presynaptic terminals (By similarity). With evidence from 12 publications.
Cell projection Localizes to stress fibers and Z lines (PubMed:11598191, PubMed:16125169, PubMed:17322171, PubMed:17537434). Preferentially expressed in the excitatory presynaptic terminals (By similarity). With evidence from 12 publications.
Ruffle Localizes to stress fibers and Z lines (PubMed:11598191, PubMed:16125169, PubMed:17322171, PubMed:17537434). Preferentially expressed in the excitatory presynaptic terminals (By similarity). With evidence from 12 publications.
Podosome Localizes to stress fibers and Z lines (PubMed:11598191, PubMed:16125169, PubMed:17322171, PubMed:17537434). Preferentially expressed in the excitatory presynaptic terminals (By similarity). With evidence from 12 publications.
Lamellipodium Localizes to stress fibers and Z lines (PubMed:11598191, PubMed:16125169, PubMed:17322171, PubMed:17537434). Preferentially expressed in the excitatory presynaptic terminals (By similarity). With evidence from 12 publications.
Axon Localizes to stress fibers and Z lines (PubMed:11598191, PubMed:16125169, PubMed:17322171, PubMed:17537434). Preferentially expressed in the excitatory presynaptic terminals (By similarity). With evidence from 12 publications.
Growth cone Localizes to stress fibers and Z lines (PubMed:11598191, PubMed:16125169, PubMed:17322171, PubMed:17537434). Preferentially expressed in the excitatory presynaptic terminals (By similarity). With evidence from 12 publications.
Secreted The antibody used to determine subcellular location does not distinguish between HMCN1 and HMCN2. With evidence from 1 publications.
Extracellular space The antibody used to determine subcellular location does not distinguish between HMCN1 and HMCN2. With evidence from 1 publications.
Extracellular matrix The antibody used to determine subcellular location does not distinguish between HMCN1 and HMCN2. With evidence from 1 publications.
Cleavage furrow The antibody used to determine subcellular location does not distinguish between HMCN1 and HMCN2. With evidence from 1 publications.
Stress fiber Localized to stress fibers during interphase and to the cleavage furrow during mitosis. With evidence from 20 publications.
Cytosol
Membrane
Basement membrane The antibody used in PubMed:17015624 and PubMed:21215633 to determine subcellular location does not distinguish between HMCN1 and HMCN2. With evidence from 7 publications.
M line
Cell membrane Colocalizes with CDH2 and ATP1B1 to the sarcolemma and to intercalating disks in cardiac muscles. Colocalizes with ATP1B1 to M line and Z line in cardiac muscles. With evidence from 21 publications.
Sarcolemma Colocalizes with CDH2 and ATP1B1 to the sarcolemma and to intercalating disks in cardiac muscles. Colocalizes with ATP1B1 to M line and Z line in cardiac muscles. With evidence from 21 publications.
Perinuclear region Colocalizes with CUL7 at the Golgi apparatus in neurons. With evidence from 2 publications.
Golgi apparatus Colocalizes with CUL7 at the Golgi apparatus in neurons. With evidence from 2 publications.
Dendrite Localized in the soma, cell membrane, axon and growth cone of dissociated commissural axons. With evidence from 4 publications.
Synapse Localized in the soma, cell membrane, axon and growth cone of dissociated commissural axons. With evidence from 4 publications.
Endoplasmic reticulum-Golgi intermediate compartment membrane Detected at growth cones in thalamus neurons. Detected at growth cones in thalamus neurons (By similarity). PRRG4 prevents cell surface location and both colocalize in the Endoplasmic reticulum/Golgi adjacent to the cell nucleus (By similarity). With evidence from 13 publications.
Nucleus
Chromosome
Colocalizes with ball and mask in Z-lines of indirect flight muscle (PubMed:26251439). In the embryo, localizes across the muscles in a striped pattern positioned at the sites at which muscles are attached to the epidermis. In the larval body wall muscles, localizes to the Z line and is still present as a doublet at the muscle-epidermal attachment sites. During pupa development, progressively forms broad striations at the Z line which become more defined after the pupa eclosion. With evidence from 12 publications.
Myofibril Localizes throughout the I-band except for dense bodies and in the outer edge of the A-band (PubMed:20346955). In embryo, co-localizes with lamin lmn-1 at the nuclear membrane. The localization to the nuclear envelope is lmn-1-dependent(PubMed:16410549). With evidence from 8 publications.
Sarcomere Localizes throughout the I-band except for dense bodies and in the outer edge of the A-band (PubMed:20346955). In embryo, co-localizes with lamin lmn-1 at the nuclear membrane. The localization to the nuclear envelope is lmn-1-dependent(PubMed:16410549). With evidence from 8 publications.
A band Localizes throughout the I-band except for dense bodies and in the outer edge of the A-band (PubMed:20346955). In embryo, co-localizes with lamin lmn-1 at the nuclear membrane. The localization to the nuclear envelope is lmn-1-dependent(PubMed:16410549). With evidence from 8 publications.
I band Localizes throughout the I-band except for dense bodies and in the outer edge of the A-band (PubMed:20346955). In embryo, co-localizes with lamin lmn-1 at the nuclear membrane. The localization to the nuclear envelope is lmn-1-dependent(PubMed:16410549). With evidence from 8 publications.
Nucleus membrane Localizes throughout the I-band except for dense bodies and in the outer edge of the A-band (PubMed:20346955). In embryo, co-localizes with lamin lmn-1 at the nuclear membrane. The localization to the nuclear envelope is lmn-1-dependent(PubMed:16410549). With evidence from 8 publications.
Cytoskeleton Localizes to stress fibers and Z lines (PubMed:11598191, PubMed:16125169, PubMed:17322171, PubMed:17537434). Preferentially expressed in the excitatory presynaptic terminals (By similarity). With evidence from 12 publications.
Cell junction Localizes to stress fibers and Z lines (PubMed:11598191, PubMed:16125169, PubMed:17322171, PubMed:17537434). Preferentially expressed in the excitatory presynaptic terminals (By similarity). With evidence from 12 publications.
Focal adhesion Localizes to stress fibers and Z lines (PubMed:11598191, PubMed:16125169, PubMed:17322171, PubMed:17537434). Preferentially expressed in the excitatory presynaptic terminals (By similarity). With evidence from 12 publications.
Z line Localizes to stress fibers and Z lines (PubMed:11598191, PubMed:16125169, PubMed:17322171, PubMed:17537434). Preferentially expressed in the excitatory presynaptic terminals (By similarity). With evidence from 12 publications.
Cell projection Localizes to stress fibers and Z lines (PubMed:11598191, PubMed:16125169, PubMed:17322171, PubMed:17537434). Preferentially expressed in the excitatory presynaptic terminals (By similarity). With evidence from 12 publications.
Ruffle Localizes to stress fibers and Z lines (PubMed:11598191, PubMed:16125169, PubMed:17322171, PubMed:17537434). Preferentially expressed in the excitatory presynaptic terminals (By similarity). With evidence from 12 publications.
Podosome Localizes to stress fibers and Z lines (PubMed:11598191, PubMed:16125169, PubMed:17322171, PubMed:17537434). Preferentially expressed in the excitatory presynaptic terminals (By similarity). With evidence from 12 publications.
Lamellipodium Localizes to stress fibers and Z lines (PubMed:11598191, PubMed:16125169, PubMed:17322171, PubMed:17537434). Preferentially expressed in the excitatory presynaptic terminals (By similarity). With evidence from 12 publications.
Axon Localizes to stress fibers and Z lines (PubMed:11598191, PubMed:16125169, PubMed:17322171, PubMed:17537434). Preferentially expressed in the excitatory presynaptic terminals (By similarity). With evidence from 12 publications.
Growth cone Localizes to stress fibers and Z lines (PubMed:11598191, PubMed:16125169, PubMed:17322171, PubMed:17537434). Preferentially expressed in the excitatory presynaptic terminals (By similarity). With evidence from 12 publications.
Secreted The antibody used to determine subcellular location does not distinguish between HMCN1 and HMCN2. With evidence from 1 publications.
Extracellular space The antibody used to determine subcellular location does not distinguish between HMCN1 and HMCN2. With evidence from 1 publications.
Extracellular matrix The antibody used to determine subcellular location does not distinguish between HMCN1 and HMCN2. With evidence from 1 publications.
Cleavage furrow The antibody used to determine subcellular location does not distinguish between HMCN1 and HMCN2. With evidence from 1 publications.
Stress fiber Localized to stress fibers during interphase and to the cleavage furrow during mitosis. With evidence from 20 publications.
Cytosol
Membrane
Basement membrane The antibody used in PubMed:17015624 and PubMed:21215633 to determine subcellular location does not distinguish between HMCN1 and HMCN2. With evidence from 7 publications.
M line
Cell membrane Colocalizes with CDH2 and ATP1B1 to the sarcolemma and to intercalating disks in cardiac muscles. Colocalizes with ATP1B1 to M line and Z line in cardiac muscles. With evidence from 21 publications.
Sarcolemma Colocalizes with CDH2 and ATP1B1 to the sarcolemma and to intercalating disks in cardiac muscles. Colocalizes with ATP1B1 to M line and Z line in cardiac muscles. With evidence from 21 publications.
Perinuclear region Colocalizes with CUL7 at the Golgi apparatus in neurons. With evidence from 2 publications.
Golgi apparatus Colocalizes with CUL7 at the Golgi apparatus in neurons. With evidence from 2 publications.
Dendrite Localized in the soma, cell membrane, axon and growth cone of dissociated commissural axons. With evidence from 4 publications.
Synapse Localized in the soma, cell membrane, axon and growth cone of dissociated commissural axons. With evidence from 4 publications.
Endoplasmic reticulum-Golgi intermediate compartment membrane Detected at growth cones in thalamus neurons. Detected at growth cones in thalamus neurons (By similarity). PRRG4 prevents cell surface location and both colocalize in the Endoplasmic reticulum/Golgi adjacent to the cell nucleus (By similarity). With evidence from 13 publications.
Length:
20376
Number of predicted TMHs:
0
Exp number of AAs in TMHs:
0.00021
Exp number, first 60 AAs:
0
Total prob of N-in:
0.00001
outside
1 - 20376
Population Genetic Test Statistics
Pi
16.199901
Theta
24.661362
Tajima's D
-2.294231
CLR
0.177331
CSRT
0.00384980750962452
Interpretation
Uncertain
