Q9CR16 · PPID_MOUSE
- ProteinPeptidyl-prolyl cis-trans isomerase D
- GenePpid
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids370 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
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.
Catalytic activity
- [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
Activity regulation
Less sensitive to inhibition by cyclosporin A than is CYP-18.
GO annotations
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended namePeptidyl-prolyl cis-trans isomerase D
- EC number
- Short namesPPIase D
- Alternative names
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionQ9CR16
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Keywords
- Cellular component
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000064154 | 1-370 | Peptidyl-prolyl cis-trans isomerase D | |||
Sequence: MSHASPAAKPSNSKNPRVFFDVDIGGERVGRIVLELFADIVPKTAENFRALCTGEKGTGSTTGKPLHFKGCPFHRIIKKFMIQGGDFSNQNGTGGESIYGEKFEDENFHYKHDREGLLSMANAGPNTNGSQFFITTVPTPHLDGKHVVFGQVIKGLGVARTLENVEVNGEKPAKLCVIAECGELKEGDDWGIFPKDGSGDSHPDFPEDADIDLKDVDKILLISEDLKNIGNTFFKSQNWEMAIKKYAKVLRYVDSSKAVIEKADRSRLQPIALSCVLNIGACKLKMSNWQGAIDSCLEALEMDPSNTKALYRKAQGWQGLKEYDQALADLKKAQEIAPGDKAIQAELLKVKQMIKAQKDKEKAVYAKMFA | ||||||
Modified residue | 5 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 171 | N6-acetyllysine | ||||
Sequence: K | ||||||
Modified residue | 198 | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
2D gel databases
PTM databases
Expression
Gene expression databases
Interaction
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).
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain, region, repeat.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 19-183 | PPIase cyclophilin-type | ||||
Sequence: FFDVDIGGERVGRIVLELFADIVPKTAENFRALCTGEKGTGSTTGKPLHFKGCPFHRIIKKFMIQGGDFSNQNGTGGESIYGEKFEDENFHYKHDREGLLSMANAGPNTNGSQFFITTVPTPHLDGKHVVFGQVIKGLGVARTLENVEVNGEKPAKLCVIAECGE | ||||||
Region | 185-215 | Chaperone activity | ||||
Sequence: KEGDDWGIFPKDGSGDSHPDFPEDADIDLKD | ||||||
Region | 214-370 | Interaction with HSP90AB1 | ||||
Sequence: KDVDKILLISEDLKNIGNTFFKSQNWEMAIKKYAKVLRYVDSSKAVIEKADRSRLQPIALSCVLNIGACKLKMSNWQGAIDSCLEALEMDPSNTKALYRKAQGWQGLKEYDQALADLKKAQEIAPGDKAIQAELLKVKQMIKAQKDKEKAVYAKMFA | ||||||
Repeat | 223-256 | TPR 1 | ||||
Sequence: SEDLKNIGNTFFKSQNWEMAIKKYAKVLRYVDSS | ||||||
Repeat | 273-306 | TPR 2 | ||||
Sequence: LSCVLNIGACKLKMSNWQGAIDSCLEALEMDPSN | ||||||
Repeat | 307-340 | TPR 3 | ||||
Sequence: TKALYRKAQGWQGLKEYDQALADLKKAQEIAPGD |
Sequence similarities
Belongs to the cyclophilin-type PPIase family. PPIase D subfamily.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length370
- Mass (Da)40,743
- Last updated2007-01-23 v3
- Checksum32891716E9113438
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A0A6YW70 | A0A0A6YW70_MOUSE | Ppid | 73 |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AK003402 EMBL· GenBank· DDBJ | BAB22767.1 EMBL· GenBank· DDBJ | mRNA | ||
AK013919 EMBL· GenBank· DDBJ | BAB29056.1 EMBL· GenBank· DDBJ | mRNA | ||
AK051597 EMBL· GenBank· DDBJ | BAC34686.1 EMBL· GenBank· DDBJ | mRNA | ||
BC011499 EMBL· GenBank· DDBJ | AAH11499.1 EMBL· GenBank· DDBJ | mRNA | ||
BC019778 EMBL· GenBank· DDBJ | AAH19778.1 EMBL· GenBank· DDBJ | mRNA |