Q9CR16 · PPID_MOUSE

  • Protein
    Peptidyl-prolyl cis-trans isomerase D
  • Gene
    Ppid
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

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.

Caution

This protein should not be confused with mitochondrial peptidyl-prolyl cis-trans isomerase F (PPIF) which is often referred to as cyclophilin D or CypD.

Catalytic activity

Activity regulation

Less sensitive to inhibition by cyclosporin A than is CYP-18.

GO annotations

AspectTerm
Cellular Componentcytoplasm
Cellular Componentcytosol
Cellular Componentnucleolus
Cellular Componentnucleoplasm
Cellular Componentnucleus
Molecular Functioncyclosporin A binding
Molecular Functionenzyme binding
Molecular FunctionFK506 binding
Molecular FunctionHsp70 protein binding
Molecular FunctionHsp90 protein binding
Molecular Functionnuclear estrogen receptor binding
Molecular Functionpeptidyl-prolyl cis-trans isomerase activity
Molecular Functiontranscription factor binding
Biological Processapoptotic process
Biological Processcellular response to UV-A
Biological Processchaperone-mediated protein folding
Biological Processlipid droplet organization
Biological Processnegative regulation of transcription by RNA polymerase II
Biological Processpositive regulation of apoptotic process
Biological Processpositive regulation of protein secretion
Biological Processpositive regulation of viral genome replication
Biological Processprotein folding
Biological Processprotein peptidyl-prolyl isomerization
Biological Processprotein transport
Biological Processprotein-containing complex assembly

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Peptidyl-prolyl cis-trans isomerase D
  • EC number
  • Short names
    PPIase D
  • Alternative names
    • 40 kDa peptidyl-prolyl cis-trans isomerase
    • Cyclophilin-40
      (CYP-40
      )
    • Rotamase D

Gene names

    • Name
      Ppid

Organism names

  • Taxonomic identifier
  • Strains
    • C57BL/6J
    • OF1
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus

Accessions

  • Primary accession
    Q9CR16
  • Secondary accessions
    • Q543G1

Proteomes

Organism-specific databases

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for chain, modified residue.

TypeIDPosition(s)Description
ChainPRO_00000641541-370Peptidyl-prolyl cis-trans isomerase D
Modified residue5Phosphoserine
Modified residue171N6-acetyllysine
Modified residue198Phosphoserine

Keywords

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.

TypeIDPosition(s)Description
Domain19-183PPIase cyclophilin-type
Region185-215Chaperone activity
Region214-370Interaction with HSP90AB1
Repeat223-256TPR 1
Repeat273-306TPR 2
Repeat307-340TPR 3

Sequence similarities

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    370
  • Mass (Da)
    40,743
  • Last updated
    2007-01-23 v3
  • Checksum
    32891716E9113438
MSHASPAAKPSNSKNPRVFFDVDIGGERVGRIVLELFADIVPKTAENFRALCTGEKGTGSTTGKPLHFKGCPFHRIIKKFMIQGGDFSNQNGTGGESIYGEKFEDENFHYKHDREGLLSMANAGPNTNGSQFFITTVPTPHLDGKHVVFGQVIKGLGVARTLENVEVNGEKPAKLCVIAECGELKEGDDWGIFPKDGSGDSHPDFPEDADIDLKDVDKILLISEDLKNIGNTFFKSQNWEMAIKKYAKVLRYVDSSKAVIEKADRSRLQPIALSCVLNIGACKLKMSNWQGAIDSCLEALEMDPSNTKALYRKAQGWQGLKEYDQALADLKKAQEIAPGDKAIQAELLKVKQMIKAQKDKEKAVYAKMFA

Computationally mapped potential isoform sequences

There is 1 potential isoform mapped to this entry

View all
EntryEntry nameGene nameLength
A0A0A6YW70A0A0A6YW70_MOUSEPpid73

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
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

Genome annotation databases

Similar Proteins

Disclaimer

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