Pre Gene Modal
BGIBMGA000620
Annotation
heparanase-like_protein_[Bombyx_mori]
Location in the cell
PlasmaMembrane   Reliability : 2.273
Sequence
CDS
ATGATGTCGAATAAACGATTAGTAGCTACATGTGCGATAGCATTTTGCTGCAACGTGGCTATGCTCGTATTATTTGTAAAATACAACGGCGGTGTAAGGTACTTTGTTACGATTAATGAAAATCAAGAAGATATCAAGCTAATCTCGGAAGACTTTCTCAGCTTTGGGATTGACACCATTGAAATTGAGAACTACAACAGAATTAACTATTCGGACACTAGGTTGAGGGAGTTAGCAGCAGCACTATCCCCAGCGCGGCTTCGTCTTGGCGGCACCATGTCTGAACGTCTCATATTTAGTAAAGAAAATATCCCAATTTCATGCCACAATTGTAGTTATAAATCTTATCCAAAATCTTTATGCCAACTTATTGAAAAACCATGTAAACACAAACACAAGTTTTTACCCTTCTTTATAATGACTGGAAATGAATGGAACCAAATTAACGATTTTTGCAGAAAGACTAATCTAAAATTGTTATTCTCGTTGAATGCAATGCTTCGTGATAATCATGGTTGGAATGAAAAGAATGCTAGAGAACTTATTGAATTTTCAAAACACAAACAGTATGCTATTGATTGGCAGTTAGGAAACGAGCCAAACTCTTTTCAACATGTTTTTAATGAAAGTGTAACTCCTCAAATATTAGCCAAGGACTTTGAAAAGCTACGTAAACTTTTGAATCATAATGGTTACAGACATTCTCTGATTGTCGGCCCAGACACAACAAGACCACAACCACACCGTCCTGAATGCCTTAAATATATGATAGAATTTTTAGGTAATGGATCTCATTATATAAATGTAAGATCATGGCATCAGTATTATTTAAACAGTAAAACTGCCAAATTGGAGGATTTTTGGAATCCAGAAACATTTGATTTGCTCAGACAGCAAATAGAAACAATGCAAAATCAAACCAAGAAGTACAAAAATATCCCAATGTGGCTAAGTGAAACTAGTAGCTCATATGGAGGTGGTGCACCAGGATTATCAAATACTTATGCAGGTAGCCCGCTTTGGATTGATAAACTAGGTCTATCGGCAAAATACAATATATCCACCGTCATTCGACAAAGCTTTATTGGTGGATATTACAGCCTAGTGGATGAAAATCTGAAACCCTTACCAGATTGGTGGATCAGTGTCTTGTATAAAAAATTGGTTGGAAATAAAGTTTTACAGGTGCAATGCAATTGCTCAAGGTTTCAAAGACTGTATATTCATTGCACCAACAGAAAATACACTAATGACACATCAGCTGTAACACTGTATGGTGTTAATTTGGAAATGGCAAAAGCTCGATTCTTCCTTAATGGCACTGCTTTACATGGAGACGATTTAATAATTCATGAATATATCATAAGTGCACCTTCAAATAACCGAAAATCAAAAACAATATTGTTAAATGGCTGGCCACTTTATTATGAATCTAATTTACACAATTTGCGGCCTAATATTCATAGGTATGGACGCTATGTTTCACTACCTCCATATTCTATTGGATTTTGGGTAATTAAGAAAACATCAATTACTGTATGCGAATAA
Protein
MMSNKRLVATCAIAFCCNVAMLVLFVKYNGGVRYFVTINENQEDIKLISEDFLSFGIDTIEIENYNRINYSDTRLRELAAALSPARLRLGGTMSERLIFSKENIPISCHNCSYKSYPKSLCQLIEKPCKHKHKFLPFFIMTGNEWNQINDFCRKTNLKLLFSLNAMLRDNHGWNEKNARELIEFSKHKQYAIDWQLGNEPNSFQHVFNESVTPQILAKDFEKLRKLLNHNGYRHSLIVGPDTTRPQPHRPECLKYMIEFLGNGSHYINVRSWHQYYLNSKTAKLEDFWNPETFDLLRQQIETMQNQTKKYKNIPMWLSETSSSYGGGAPGLSNTYAGSPLWIDKLGLSAKYNISTVIRQSFIGGYYSLVDENLKPLPDWWISVLYKKLVGNKVLQVQCNCSRFQRLYIHCTNRKYTNDTSAVTLYGVNLEMAKARFFLNGTALHGDDLIIHEYIISAPSNNRKSKTILLNGWPLYYESNLHNLRPNIHRYGRYVSLPPYSIGFWVIKKTSITVCE
Summary
Description
Endoglycosidase that cleaves heparan sulfate proteoglycans (HSPGs) into heparan sulfate side chains and core proteoglycans. Participates in extracellular matrix (ECM) degradation and remodeling. Selectively cleaves the linkage between a glucuronic acid unit and an N-sulfo glucosamine unit carrying either a 3-O-sulfo or a 6-O-sulfo group. Can also cleave the linkage between a glucuronic acid unit and an N-sulfo glucosamine unit carrying a 2-O-sulfo group, but not linkages between a glucuronic acid unit and a 2-O-sulfated iduronic acid moiety. Essentially inactive at neutral pH but becomes active under acidic conditions such as during tumor invasion and in inflammatory processes. Facilitates cell migration associated with metastasis, wound healing and inflammation. Enhances shedding of syndecans. Acts as procoagulant by enhancing the generation of activated factor X/F10 in the presence of tissue factor/TF and activated factor VII/F7. Independent of its enzymatic activity, increases cell adhesion to the extracellular matrix (ECM). Enhances AKT1/PKB phosphorylation, possibly via interaction with a lipid raft-resident receptor. Plays a role in the regulation of osteogenesis. Enhances angiogenesis through up-regulation of SRC-mediated activation of VEGF. Implicated in hair follicle inner root sheath differentiation and hair homeostasis (By similarity).
Catalytic Activity
Endohydrolysis of (1->4)-beta-D-glycosidic bonds of heparan sulfate chains in heparan sulfate proteoglycan.
Subunit
Heterodimer; heterodimer formation between the 8 kDa and the 50 kDa subunits is required for enzyme activity (By similarity). Interacts with TF; the interaction, inhibited by heparin, enhances the generation of activated factor X and activates coagulation. Interacts with HRG; the interaction is enhanced at acidic pH, partially inhibits binding of HPSE to cell surface receptors and modulates its enzymatic activity. Interacts with SDC1; the interaction enhances the shedding of SDC1. Interacts with HPSE2 (By similarity).
Similarity
Belongs to the glycosyl hydrolase 79 family.
Keywords
Calcium
Cell adhesion
Complete proteome
Disulfide bond
Glycoprotein
Hydrolase
Lysosome
Magnesium
Membrane
Nucleus
Reference proteome
Secreted
Signal
Feature
chain Heparanase 8 kDa subunit
propeptide Linker peptide
PDB
5LA7
E-value=5.07643e-62,
Score=604
Ontologies
Topology
Subcellular location
Lysosome membrane
Proheparanase is secreted via vesicles of the Golgi. Interacts with cell membrane heparan sulfate proteoglycans (HSPGs). Endocytosed and accumulates in endosomes. Transferred to lysosomes where it is proteolytically cleaved to produce the active enzyme. Under certain stimuli, transferred to the cell surface. Associates with lipid rafts. Colocalizes with SDC1 in endosomal/lysosomal vesicles. Accumulates in perinuclear lysosomal vesicles. Heparin retains proheparanase in the extracellular medium (By similarity). With evidence from 1 publications.
Secreted
Proheparanase is secreted via vesicles of the Golgi. Interacts with cell membrane heparan sulfate proteoglycans (HSPGs). Endocytosed and accumulates in endosomes. Transferred to lysosomes where it is proteolytically cleaved to produce the active enzyme. Under certain stimuli, transferred to the cell surface. Associates with lipid rafts. Colocalizes with SDC1 in endosomal/lysosomal vesicles. Accumulates in perinuclear lysosomal vesicles. Heparin retains proheparanase in the extracellular medium (By similarity). With evidence from 1 publications.
Nucleus
Proheparanase is secreted via vesicles of the Golgi. Interacts with cell membrane heparan sulfate proteoglycans (HSPGs). Endocytosed and accumulates in endosomes. Transferred to lysosomes where it is proteolytically cleaved to produce the active enzyme. Under certain stimuli, transferred to the cell surface. Associates with lipid rafts. Colocalizes with SDC1 in endosomal/lysosomal vesicles. Accumulates in perinuclear lysosomal vesicles. Heparin retains proheparanase in the extracellular medium (By similarity). With evidence from 1 publications.
Number of predicted TMHs:
1
Exp number of AAs in TMHs:
20.09637
Exp number, first 60 AAs:
20.07637
Total prob of N-in:
0.99543
POSSIBLE N-term signal
sequence
Population Genetic Test Statistics