Pre Gene Modal
BGIBMGA009341
Annotation
PREDICTED:_peptidyl-prolyl_cis-trans_isomerase_D_isoform_X1_[Bombyx_mori]
Full name
Peptidyl-prolyl cis-trans isomerase D
Alternative Name
40 kDa peptidyl-prolyl cis-trans isomerase
Cyclophilin-40
Rotamase D
Cyclophilin-related protein
Estrogen receptor-binding cyclophilin
Location in the cell
Cytoplasmic   Reliability : 1.645 Nuclear   Reliability : 1.865
Sequence
CDS
ATGAGTTCCGACAGGCGATCACAAACGAATCCTTTTGTTTATTTGGACATCTCTATTGATGGAGTATCAGCTGGACGAATCGTGATCGAACTGAGGAGTGACGTAGTCCCGAAAACCGCAGAGAACTTCCGGGCGCTTTGTACGGGCGAGAAGGGCATTGGAGTTTACGGGAAACCCTTACACTACAAAGGAGTCAGATTCCATAAAGCGGTTAATCAGTTCATGGTGCAGGGCGGAGACATAGTCAACGGCGACGGCAGCGGCGGCGAGAGCATATACGGCCCGAAATTCGAAGACGAGAATTTTACTCTTACGGCAAAGTCTGGGGTACTGGCGATGGCGAACGAAGGTCGACCGGACACAAACAGTTCGCAGTTCTGTATAACGACGATACCGTGCCCGCACATAAACGGCACTAATGTTATATTCGGGGAGGTGGTCGCCGGATTCGAACTGGTCGACGAGATGCAGAGATACGGCGAAGGGGACGACGGGAGGCCCGGGGCGGAATGCGTGATCGAAGACTGCGGCGAAATAACAGAGCAGAACTGGGACGTGTGCTGCAGGGATGGCACCTCCGACAAAATACCCGAATTCCCGACGGACTGGAGGAATATTGGAGCCGTTTCGTTAGACGATTTAATATCGTGCATAAGGGACGTCAAGGCAGCCGGCAATGGAATGTTCAGCGAGCGTCGGTACAAAGCCGCGATCAGAAAGTACCGCAAGTGCCTCAGATACGTCGACTACGCTTTGAGTATAGTACAAGGAATGCACGAGAAAGAGACAGAACATATAATAGATTTAACATCAACGTTTATACTGCAGTGTAATTTGAATCTGGCCGCGTGTTACTCGAGAACCGAAGACTACAGAGCGTGTATCGAGTGCTGTACGCAGGTGCTGGACAGAAGCCCTCGCAACGAGAAGGCCCTGTACCGGCGGGGCCAAGCGAACTTCGCCCTTAAGAACTACGAGGCCGCGCTGTCCGATCTGAGGCGGGCCGAGCGCGCGTCGCCGCACAATCGCGCCGTGCTCGCGCTGCTGGACGAGGTGCGCCGCTGCAGCCGCCGCTACAACGAGCTGCAGAAACAGAGGCTCTCAAAGTTTTTTCGTGAGCAAAAAGAGCGCGCCGCCGCCGCCAACAACTGA
Protein
MSSDRRSQTNPFVYLDISIDGVSAGRIVIELRSDVVPKTAENFRALCTGEKGIGVYGKPLHYKGVRFHKAVNQFMVQGGDIVNGDGSGGESIYGPKFEDENFTLTAKSGVLAMANEGRPDTNSSQFCITTIPCPHINGTNVIFGEVVAGFELVDEMQRYGEGDDGRPGAECVIEDCGEITEQNWDVCCRDGTSDKIPEFPTDWRNIGAVSLDDLISCIRDVKAAGNGMFSERRYKAAIRKYRKCLRYVDYALSIVQGMHEKETEHIIDLTSTFILQCNLNLAACYSRTEDYRACIECCTQVLDRSPRNEKALYRRGQANFALKNYEAALSDLRRAERASPHNRAVLALLDEVRRCSRRYNELQKQRLSKFFREQKERAAAANN
Summary
Description
PPIase that catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and may therefore assist protein folding. Proposed to act as a co-chaperone in HSP90 complexes such as in unligated steroid receptors heterocomplexes. Different co-chaperones seem to compete for association with HSP90 thus establishing distinct HSP90-co-chaperone-receptor complexes with the potential to exert tissue-specific receptor activity control. May have a preference for estrogen receptor complexes and is not found in glucocorticoid receptor complexes. May be involved in cytoplasmic dynein-dependent movement of the receptor from the cytoplasm to the nucleus. May regulate MYB by inhibiting its DNA-binding activity. Involved in regulation of AHR signaling by promoting the formation of the AHR:ARNT dimer; the function is independent of HSP90 but requires the chaperone activity region. Involved in regulation of UV radiation-induced apoptosis.
PPIase that catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and may therefore assist protein folding. Proposed to act as a co-chaperone in HSP90 complexes such as in unligated steroid receptors heterocomplexes. Different co-chaperones seem to compete for association with HSP90 thus establishing distinct HSP90-co-chaperone-receptor complexes with the potential to exert tissue-specific receptor activity control. May have a preference for estrogen receptor complexes and is not found in glucocorticoid receptor complexes. May be involved in cytoplasmic dynein-dependent movement of the receptor from the cytoplasm to the nucleus. May regulate MYB by inhibiting its DNA-binding activity. Involved in regulation of AHR signaling by promoting the formation of the AHR:ARNT dimer; the function is independent of HSP90 but requires the chaperone activity. Involved in regulation of UV radiation-induced apoptosis.
PPIase that catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and may therefore assist protein folding (PubMed:11350175, PubMed:20676357). Proposed to act as a co-chaperone in HSP90 complexes such as in unligated steroid receptors heterocomplexes. Different co-chaperones seem to compete for association with HSP90 thus establishing distinct HSP90-co-chaperone-receptor complexes with the potential to exert tissue-specific receptor activity control. May have a preference for estrogen receptor complexes and is not found in glucocorticoid receptor complexes. May be involved in cytoplasmic dynein-dependent movement of the receptor from the cytoplasm to the nucleus. May regulate MYB by inhibiting its DNA-binding activity. Involved in regulation of AHR signaling by promoting the formation of the AHR:ARNT dimer; the function is independent of HSP90 but requires the chaperone activity. Involved in regulation of UV radiation-induced apoptosis. Promotes cell viability in anaplastic lymphoma kinase-positive anaplastic large-cell lymphoma (ALK+ ALCL) cell lines.
(Microbial infection) May be involved in hepatitis C virus (HCV) replication and release.
Catalytic Activity
[protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
Subunit
Identified in ESR1 or NR3C1/GCR steroid receptor-chaperone complexes. Found in HSP90 chaperone complexes with kinase clients LCK or EIF2AK1. Two monomers associate with one HSP90 homodimer. Interacts with HSP90AA1. Interacts with HSP90AB1; PPID and FKBP4 compete for binding to HSP90AB1 and the interaction is mutually exclusive with the PPID:HSPA8 interaction. Interacts with HSPA8; PPID and STIP1 but not FKBP4 compete for binding to HSPA8 and the interaction is mutually exclusive with the PPID:HSP90AB1 interaction. Interacts with S100A1 and S100A2; the interactions dissociate the PPID:HSP90AA1 interaction. Interacts with S100A6. Interacts with MYB, ILF2, XRCC6, RACK1 and RPS3. Interacts with cytoplasmic dynein 1 intermediate chain (DYNC1I1 or DYNC1I2).
Identified in ESR1 or NR3C1/GCR steroid receptor-chaperone complexes. Found in HSP90 chaperone complexes with kinase clients LCK or EIF2AK1. Two monomers associate with one HSP90 homodimer. Interacts with HSP90AA1. Interacts with HSP90AB1; PPID and FKBP4 compete for binding to HSP90AB1 and the interaction is mutually exclusive with the PPID:HSPA8 interaction. Interacts with HSPA8; PPID and STIP1 but not FKBP4 compete for binding to HSPA8 and the interaction is mutually exclusive with the PPID:HSP90AB1 interaction. Interacts with S100A1 and S100A2; the interactions dissociate the PPID:HSP90AA1 interaction. Interacts with S100A6. Interacts with MYB, ILF2, XRCC6, RACK1 and RPS3. Interacts with cytoplasmic dynein 1 intermediate chain (DYNC1I1 or DYNC1I2) (By similarity).
Similarity
Belongs to the cyclophilin-type PPIase family. PPIase D subfamily.
Keywords
Acetylation
Apoptosis
Chaperone
Complete proteome
Cytoplasm
Direct protein sequencing
Isomerase
Nucleus
Phosphoprotein
Protein transport
Reference proteome
Repeat
Rotamase
TPR repeat
Transport
3D-structure
Polymorphism
Feature
chain Peptidyl-prolyl cis-trans isomerase D
sequence variant In dbSNP:rs2070631.
PDB
1IIP
E-value=3.88417e-70,
Score=673
Ontologies
Topology
Subcellular location
Cytoplasm
Nucleus
Nucleolus
Nucleoplasm
Number of predicted TMHs:
0
Exp number of AAs in TMHs:
0.09648
Exp number, first 60 AAs:
0.0792999999999999
Total prob of N-in:
0.06601
Population Genetic Test Statistics