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Protein

Peptidyl-prolyl cis-trans isomerase D

Gene

Ppid

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: -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

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

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

Keywordsi

Molecular functionChaperone, Isomerase, Rotamase
Biological processApoptosis, Protein transport, Transport

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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 3

Organism-specific databases

MGIiMGI:1914988 Ppid

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000641541 – 370Peptidyl-prolyl cis-trans isomerase DAdd BLAST370

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-2DPAGEiQ9CR16

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
MINTiQ9CR16
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

Keywords - Domaini

Repeat, TPR repeat

Phylogenomic databases

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

Family and domain databases

Gene3Di1.25.40.10, 1 hit
2.40.100.10, 1 hit
InterProiView protein in InterPro
IPR029000 Cyclophilin-like_dom_sf
IPR024936 Cyclophilin-type_PPIase
IPR020892 Cyclophilin-type_PPIase_CS
IPR002130 Cyclophilin-type_PPIase_dom
IPR013026 TPR-contain_dom
IPR011990 TPR-like_helical_dom_sf
IPR019734 TPR_repeat
PANTHERiPTHR11071 PTHR11071, 1 hit
PfamiView protein in Pfam
PF00160 Pro_isomerase, 1 hit
PF13176 TPR_7, 1 hit
PRINTSiPR00153 CSAPPISMRASE
SMARTiView protein in SMART
SM00028 TPR, 3 hits
SUPFAMiSSF48452 SSF48452, 1 hit
SSF50891 SSF50891, 1 hit
PROSITEiView protein in PROSITE
PS00170 CSA_PPIASE_1, 1 hit
PS50072 CSA_PPIASE_2, 1 hit
PS50005 TPR, 3 hits
PS50293 TPR_REGION, 2 hits

Sequencei

Sequence statusi: Complete.

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

Similar proteinsi

Entry informationi

Entry nameiPPID_MOUSE
AccessioniPrimary (citable) accession number: Q9CR16
Secondary accession number(s): Q543G1
Entry historyiIntegrated into UniProtKB/Swiss-Prot: September 19, 2002
Last sequence update: January 23, 2007
Last modified: April 25, 2018
This is version 149 of the entry and version 3 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome
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Main funding by: National Institutes of Health