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Protein

Peptidyl-prolyl cis-trans isomerase D

Gene

Ppid

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. 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.1 Publication

Catalytic activityi

Peptidylproline (omega=180) = peptidylproline (omega=0).

Enzyme regulationi

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

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Chaperone, Isomerase, Rotamase

Keywords - Biological processi

Apoptosis, Protein transport, Transport

Keywords - Ligandi

Cyclosporin

Names & Taxonomyi

Protein namesi
Recommended name:
Peptidyl-prolyl cis-trans isomerase D (EC:5.2.1.8)
Short name:
PPIase D
Alternative name(s):
40 kDa peptidyl-prolyl cis-trans isomerase
Cyclophilin-40
Short name:
CYP-40
Rotamase D
Gene namesi
Name:Ppid
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 3

Organism-specific databases

MGIiMGI:1914988. Ppid.

Subcellular locationi

  • Cytoplasm By similarity
  • Nucleusnucleolus By similarity
  • Nucleusnucleoplasm By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00000641542 – 370Peptidyl-prolyl cis-trans isomerase DAdd BLAST369

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei5PhosphoserineBy similarity1
Modified residuei171N6-acetyllysineCombined sources1
Modified residuei198PhosphoserineBy similarity1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ9CR16.
MaxQBiQ9CR16.
PaxDbiQ9CR16.
PeptideAtlasiQ9CR16.
PRIDEiQ9CR16.

2D gel databases

REPRODUCTION-2DPAGEQ9CR16.

PTM databases

iPTMnetiQ9CR16.
PhosphoSitePlusiQ9CR16.
SwissPalmiQ9CR16.

Expressioni

Gene expression databases

BgeeiENSMUSG00000027804.
CleanExiMM_PPID.
ExpressionAtlasiQ9CR16. baseline and differential.
GenevisibleiQ9CR16. MM.

Interactioni

Subunit structurei

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).1 Publication

GO - Molecular functioni

Protein-protein interaction databases

BioGridi212408. 3 interactors.
IntActiQ9CR16. 2 interactors.
MINTiMINT-1856717.
STRINGi10090.ENSMUSP00000029382.

Structurei

3D structure databases

ProteinModelPortaliQ9CR16.
SMRiQ9CR16.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini19 – 183PPIase cyclophilin-typePROSITE-ProRule annotationAdd BLAST165
Repeati223 – 256TPR 1Add BLAST34
Repeati273 – 306TPR 2Add BLAST34
Repeati307 – 340TPR 3Add BLAST34

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni185 – 215Chaperone activityBy similarityAdd BLAST31
Regioni214 – 370Interaction with HSP90AB1By similarityAdd BLAST157

Sequence similaritiesi

Contains 1 PPIase cyclophilin-type domain.PROSITE-ProRule annotation
Contains 3 TPR repeats.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, TPR repeat

Phylogenomic databases

eggNOGiKOG0546. Eukaryota.
COG0652. LUCA.
GeneTreeiENSGT00550000074595.
HOGENOMiHOG000065980.
HOVERGENiHBG053654.
InParanoidiQ9CR16.
KOiK05864.
OMAiKGIGHTT.
OrthoDBiEOG091G0BGL.
PhylomeDBiQ9CR16.
TreeFamiTF324493.

Family and domain databases

Gene3Di1.10.150.160. 1 hit.
1.25.40.10. 1 hit.
2.40.100.10. 1 hit.
InterProiIPR029000. Cyclophilin-like_dom.
IPR024936. Cyclophilin-type_PPIase.
IPR020892. Cyclophilin-type_PPIase_CS.
IPR002130. Cyclophilin-type_PPIase_dom.
IPR023114. Elongated_TPR_rpt_dom.
IPR013026. TPR-contain_dom.
IPR011990. TPR-like_helical_dom.
IPR019734. TPR_repeat.
[Graphical view]
PANTHERiPTHR11071. PTHR11071. 1 hit.
PfamiPF00160. Pro_isomerase. 1 hit.
PF13176. TPR_7. 1 hit.
[Graphical view]
PRINTSiPR00153. CSAPPISMRASE.
SMARTiSM00028. TPR. 3 hits.
[Graphical view]
SUPFAMiSSF48452. SSF48452. 1 hit.
SSF50891. SSF50891. 1 hit.
PROSITEiPS00170. CSA_PPIASE_1. 1 hit.
PS50072. CSA_PPIASE_2. 1 hit.
PS50005. TPR. 3 hits.
PS50293. TPR_REGION. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9CR16-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSHASPAAKP SNSKNPRVFF DVDIGGERVG RIVLELFADI VPKTAENFRA
60 70 80 90 100
LCTGEKGTGS TTGKPLHFKG CPFHRIIKKF MIQGGDFSNQ NGTGGESIYG
110 120 130 140 150
EKFEDENFHY KHDREGLLSM ANAGPNTNGS QFFITTVPTP HLDGKHVVFG
160 170 180 190 200
QVIKGLGVAR TLENVEVNGE KPAKLCVIAE CGELKEGDDW GIFPKDGSGD
210 220 230 240 250
SHPDFPEDAD IDLKDVDKIL LISEDLKNIG NTFFKSQNWE MAIKKYAKVL
260 270 280 290 300
RYVDSSKAVI EKADRSRLQP IALSCVLNIG ACKLKMSNWQ GAIDSCLEAL
310 320 330 340 350
EMDPSNTKAL YRKAQGWQGL KEYDQALADL KKAQEIAPGD KAIQAELLKV
360 370
KQMIKAQKDK EKAVYAKMFA
Length:370
Mass (Da):40,743
Last modified:January 23, 2007 - v3
Checksum:i32891716E9113438
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK003402 mRNA. Translation: BAB22767.1.
AK013919 mRNA. Translation: BAB29056.1.
AK051597 mRNA. Translation: BAC34686.1.
BC011499 mRNA. Translation: AAH11499.1.
BC019778 mRNA. Translation: AAH19778.1.
CCDSiCCDS17417.1.
RefSeqiNP_080628.1. NM_026352.3.
UniGeneiMm.295252.

Genome annotation databases

EnsembliENSMUST00000029382; ENSMUSP00000029382; ENSMUSG00000027804.
GeneIDi67738.
KEGGimmu:67738.
UCSCiuc008pnp.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK003402 mRNA. Translation: BAB22767.1.
AK013919 mRNA. Translation: BAB29056.1.
AK051597 mRNA. Translation: BAC34686.1.
BC011499 mRNA. Translation: AAH11499.1.
BC019778 mRNA. Translation: AAH19778.1.
CCDSiCCDS17417.1.
RefSeqiNP_080628.1. NM_026352.3.
UniGeneiMm.295252.

3D structure databases

ProteinModelPortaliQ9CR16.
SMRiQ9CR16.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi212408. 3 interactors.
IntActiQ9CR16. 2 interactors.
MINTiMINT-1856717.
STRINGi10090.ENSMUSP00000029382.

PTM databases

iPTMnetiQ9CR16.
PhosphoSitePlusiQ9CR16.
SwissPalmiQ9CR16.

2D gel databases

REPRODUCTION-2DPAGEQ9CR16.

Proteomic databases

EPDiQ9CR16.
MaxQBiQ9CR16.
PaxDbiQ9CR16.
PeptideAtlasiQ9CR16.
PRIDEiQ9CR16.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000029382; ENSMUSP00000029382; ENSMUSG00000027804.
GeneIDi67738.
KEGGimmu:67738.
UCSCiuc008pnp.1. mouse.

Organism-specific databases

CTDi5481.
MGIiMGI:1914988. Ppid.

Phylogenomic databases

eggNOGiKOG0546. Eukaryota.
COG0652. LUCA.
GeneTreeiENSGT00550000074595.
HOGENOMiHOG000065980.
HOVERGENiHBG053654.
InParanoidiQ9CR16.
KOiK05864.
OMAiKGIGHTT.
OrthoDBiEOG091G0BGL.
PhylomeDBiQ9CR16.
TreeFamiTF324493.

Miscellaneous databases

PROiQ9CR16.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000027804.
CleanExiMM_PPID.
ExpressionAtlasiQ9CR16. baseline and differential.
GenevisibleiQ9CR16. MM.

Family and domain databases

Gene3Di1.10.150.160. 1 hit.
1.25.40.10. 1 hit.
2.40.100.10. 1 hit.
InterProiIPR029000. Cyclophilin-like_dom.
IPR024936. Cyclophilin-type_PPIase.
IPR020892. Cyclophilin-type_PPIase_CS.
IPR002130. Cyclophilin-type_PPIase_dom.
IPR023114. Elongated_TPR_rpt_dom.
IPR013026. TPR-contain_dom.
IPR011990. TPR-like_helical_dom.
IPR019734. TPR_repeat.
[Graphical view]
PANTHERiPTHR11071. PTHR11071. 1 hit.
PfamiPF00160. Pro_isomerase. 1 hit.
PF13176. TPR_7. 1 hit.
[Graphical view]
PRINTSiPR00153. CSAPPISMRASE.
SMARTiSM00028. TPR. 3 hits.
[Graphical view]
SUPFAMiSSF48452. SSF48452. 1 hit.
SSF50891. SSF50891. 1 hit.
PROSITEiPS00170. CSA_PPIASE_1. 1 hit.
PS50072. CSA_PPIASE_2. 1 hit.
PS50005. TPR. 3 hits.
PS50293. TPR_REGION. 2 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPPID_MOUSE
AccessioniPrimary (citable) accession number: Q9CR16
Secondary accession number(s): Q543G1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 19, 2002
Last sequence update: January 23, 2007
Last modified: November 2, 2016
This is version 137 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

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.Curated

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.