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P26882

- PPID_BOVIN

UniProt

P26882 - PPID_BOVIN

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Protein
Peptidyl-prolyl cis-trans isomerase D
Gene
PPID, CYPD
Organism
Bos taurus (Bovine)
Status
Reviewed - 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. Involved in regulation of UV radiation-induced apoptosis.2 Publications

Catalytic activityi

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

Enzyme regulationi

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

GO - Molecular functioni

  1. Hsp70 protein binding Source: UniProtKB
  2. Hsp90 protein binding Source: UniProtKB
  3. estrogen receptor binding Source: UniProtKB
  4. peptide binding Source: UniProtKB-KW
  5. peptidyl-prolyl cis-trans isomerase activity Source: UniProtKB
  6. protein binding Source: IntAct
  7. transcription factor binding Source: UniProtKB

GO - Biological processi

  1. apoptotic process Source: UniProtKB-KW
  2. cellular response to UV-A Source: UniProtKB
  3. chaperone-mediated protein folding Source: UniProtKB
  4. lipid particle organization Source: UniProtKB
  5. negative regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  6. positive regulation of apoptotic process Source: UniProtKB
  7. positive regulation of protein secretion Source: Ensembl
  8. positive regulation of viral genome replication Source: Ensembl
  9. protein complex assembly Source: UniProtKB
  10. protein folding Source: UniProtKB
  11. protein transport Source: UniProtKB-KW
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
Cyclophilin-related protein
Estrogen receptor-binding cyclophilin
Rotamase D
Gene namesi
Name:PPID
Synonyms:CYPD
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
ProteomesiUP000009136: Chromosome 17

Subcellular locationi

Cytoplasm. Nucleusnucleolus By similarity. Nucleusnucleoplasm By similarity

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. intermediate filament cytoskeleton Source: Ensembl
  3. nucleolus Source: UniProtKB
  4. nucleoplasm Source: UniProtKB-SubCell
  5. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed By similarity
Chaini2 – 370369Peptidyl-prolyl cis-trans isomerase D
PRO_0000064152Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei171 – 1711N6-acetyllysine By similarity
Modified residuei198 – 1981Phosphoserine By similarity

Post-translational modificationi

The N-terminus is blocked.

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PRIDEiP26882.

Expressioni

Tissue specificityi

Detected in heart, thymis and brain.1 Publication

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, GNB2L1 and RPS3. Interacts with cytoplasmic dynein 1 intermediate chain (DYNC1I1 or DYNC1I2).6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
HSP90AA1P079004EBI-6477155,EBI-296047From a different organism.
S100A1P026392EBI-6477155,EBI-6477285
S100a1P354677EBI-6477155,EBI-6477109From a different organism.
S100A2P290343EBI-6477155,EBI-752230From a different organism.
S100A6P067033EBI-6477155,EBI-352877From a different organism.

Protein-protein interaction databases

BioGridi158751. 1 interaction.
IntActiP26882. 6 interactions.
MINTiMINT-2832213.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi8 – 114
Beta strandi17 – 248
Beta strandi27 – 3610
Turni38 – 403
Helixi42 – 5312
Turni60 – 623
Beta strandi63 – 664
Beta strandi72 – 776
Turni78 – 803
Beta strandi81 – 844
Turni87 – 893
Beta strandi90 – 934
Beta strandi98 – 1014
Beta strandi117 – 1204
Beta strandi132 – 1376
Helixi140 – 1423
Turni143 – 1453
Beta strandi148 – 1547
Helixi156 – 1638
Beta strandi171 – 1744
Beta strandi176 – 1849
Beta strandi196 – 1983
Helixi206 – 2083
Beta strandi209 – 2113
Helixi216 – 23520
Helixi239 – 25921
Helixi262 – 2654
Helixi266 – 2683
Helixi269 – 28517
Helixi289 – 30012
Helixi307 – 31913
Helixi323 – 33614
Helixi341 – 36222

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1IHGX-ray1.80A1-370[»]
1IIPX-ray2.00A1-370[»]
ProteinModelPortaliP26882.
SMRiP26882. Positions 2-365.

Miscellaneous databases

EvolutionaryTraceiP26882.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini19 – 183165PPIase cyclophilin-type
Add
BLAST
Repeati223 – 25634TPR 1
Add
BLAST
Repeati273 – 30634TPR 2
Add
BLAST
Repeati307 – 34034TPR 3
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni185 – 21531Chaperone activity
Add
BLAST
Regioni214 – 370157Interaction with HSP90AB1
Add
BLAST

Sequence similaritiesi

Contains 3 TPR repeats.

Keywords - Domaini

Repeat, TPR repeat

Phylogenomic databases

eggNOGiCOG0652.
GeneTreeiENSGT00550000074595.
HOGENOMiHOG000065980.
HOVERGENiHBG053654.
InParanoidiP26882.
KOiK05864.
OMAiKGIGHTT.
OrthoDBiEOG79GT7W.
TreeFamiTF324493.

Family and domain databases

Gene3Di1.25.40.10. 1 hit.
2.40.100.10. 1 hit.
InterProiIPR029000. Cyclophilin-like_dom.
IPR020892. Cyclophilin-type_PPIase_CS.
IPR002130. Cyclophilin-type_PPIase_dom.
IPR013026. TPR-contain_dom.
IPR011990. TPR-like_helical.
IPR019734. TPR_repeat.
[Graphical view]
PfamiPF00160. Pro_isomerase. 1 hit.
PF13176. TPR_7. 1 hit.
[Graphical view]
PRINTSiPR00153. CSAPPISMRASE.
SMARTiSM00028. TPR. 3 hits.
[Graphical view]
SUPFAMiSSF50891. 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.

P26882-1 [UniParc]FASTAAdd to Basket

« Hide

MSHPSPQAKP SNPSNPRVFF DVDIGGERVG RIVLELFADI VPKTAENFRA    50
LCTGEKGIGP TTGKPLHFKG CPFHRIIKKF MIQGGDFSNQ NGTGGESIYG 100
EKFEDENFHY KHDKEGLLSM ANAGSNTNGS QFFITTVPTP HLDGKHVVFG 150
QVIKGMGVAK ILENVEVKGE KPAKLCVIAE CGELKEGDDW GIFPKDGSGD 200
SHPDFPEDAD VDLKDVDKIL LISEDLKNIG NTFFKSQNWE MAIKKYTKVL 250
RYVEGSRAAA EDADGAKLQP VALSCVLNIG ACKLKMSDWQ GAVDSCLEAL 300
EIDPSNTKAL YRRAQGWQGL KEYDQALADL KKAQEIAPED KAIQAELLKV 350
KQKIKAQKDK EKAAYAKMFA 370
Length:370
Mass (Da):40,620
Last modified:January 23, 2007 - v6
Checksum:iF278FDE1B9494241
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D14074 mRNA. Translation: BAA03159.1.
BC113318 mRNA. Translation: AAI13319.1.
L11668 mRNA. Translation: AAA30484.1.
PIRiA46579.
RefSeqiNP_776578.1. NM_174153.3.
UniGeneiBt.7221.

Genome annotation databases

EnsembliENSBTAT00000022180; ENSBTAP00000022180; ENSBTAG00000016680.
GeneIDi281420.
KEGGibta:281420.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D14074 mRNA. Translation: BAA03159.1 .
BC113318 mRNA. Translation: AAI13319.1 .
L11668 mRNA. Translation: AAA30484.1 .
PIRi A46579.
RefSeqi NP_776578.1. NM_174153.3.
UniGenei Bt.7221.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1IHG X-ray 1.80 A 1-370 [» ]
1IIP X-ray 2.00 A 1-370 [» ]
ProteinModelPortali P26882.
SMRi P26882. Positions 2-365.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 158751. 1 interaction.
IntActi P26882. 6 interactions.
MINTi MINT-2832213.

Proteomic databases

PRIDEi P26882.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSBTAT00000022180 ; ENSBTAP00000022180 ; ENSBTAG00000016680 .
GeneIDi 281420.
KEGGi bta:281420.

Organism-specific databases

CTDi 5481.

Phylogenomic databases

eggNOGi COG0652.
GeneTreei ENSGT00550000074595.
HOGENOMi HOG000065980.
HOVERGENi HBG053654.
InParanoidi P26882.
KOi K05864.
OMAi KGIGHTT.
OrthoDBi EOG79GT7W.
TreeFami TF324493.

Miscellaneous databases

EvolutionaryTracei P26882.
NextBioi 20805409.

Family and domain databases

Gene3Di 1.25.40.10. 1 hit.
2.40.100.10. 1 hit.
InterProi IPR029000. Cyclophilin-like_dom.
IPR020892. Cyclophilin-type_PPIase_CS.
IPR002130. Cyclophilin-type_PPIase_dom.
IPR013026. TPR-contain_dom.
IPR011990. TPR-like_helical.
IPR019734. TPR_repeat.
[Graphical view ]
Pfami PF00160. Pro_isomerase. 1 hit.
PF13176. TPR_7. 1 hit.
[Graphical view ]
PRINTSi PR00153. CSAPPISMRASE.
SMARTi SM00028. TPR. 3 hits.
[Graphical view ]
SUPFAMi SSF50891. SSF50891. 1 hit.
PROSITEi PS00170. CSA_PPIASE_1. 1 hit.
PS50072. CSA_PPIASE_2. 1 hit.
PS50005. TPR. 3 hits.
PS50293. TPR_REGION. 2 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "The cyclophilin component of the unactivated estrogen receptor contains a tetratricopeptide repeat domain and shares identity with p59 (FKBP59)."
    Ratajczak T., Carrello A., Mark P.J., Warner B.J., Simpson R.J., Moritz R.L., House A.K.
    J. Biol. Chem. 268:13187-13192(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, IDENTIFICATION IN AN ESR1 STEROID RECEPTOR-CHAPERONE COMPLEX, TISSUE SPECIFICITY.
  2. NIH - Mammalian Gene Collection (MGC) project
    Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Hereford.
    Tissue: Uterus.
  3. "Cyclophilin-40, a protein with homology to the P59 component of the steroid receptor complex. Cloning of the cDNA and further characterization."
    Kieffer L.J., Seng T.W., Li W., Osterman D.G., Handschumacher R.E., Bayney R.M.
    J. Biol. Chem. 268:12303-12310(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 37-345.
    Tissue: Brain.
  4. "Isolation and characterization of a 40-kDa cyclophilin-related protein."
    Kieffer L.J., Thalhammer T., Handschumacher R.E.
    J. Biol. Chem. 267:5503-5507(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 18-42; 147-154; 199-219; 228-235 AND 309-312, FUNCTION.
    Tissue: Brain.
  5. "Cyclophilin 40 (CyP-40), mapping of its hsp90 binding domain and evidence that FKBP52 competes with CyP-40 for hsp90 binding."
    Ratajczak T., Carrello A.
    J. Biol. Chem. 271:2961-2965(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HSP90AB1.
  6. "The common tetratricopeptide repeat acceptor site for steroid receptor-associated immunophilins and hop is located in the dimerization domain of Hsp90."
    Carrello A., Ingley E., Minchin R.F., Tsai S., Ratajczak T.
    J. Biol. Chem. 274:2682-2689(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HSP90AA1 AND HSP90AB1.
  7. Cited for: INTERACTION WITH HSPA8.
  8. "The chaperone function of cyclophilin 40 maps to a cleft between the prolyl isomerase and tetratricopeptide repeat domains."
    Mok D., Allan R.K., Carrello A., Wangoo K., Walkinshaw M.D., Ratajczak T.
    FEBS Lett. 580:2761-2768(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH HSP90AB1.
  9. "S100 proteins regulate the interaction of Hsp90 with cyclophilin 40 and FKBP52 through their tetratricopeptide repeats."
    Shimamoto S., Kubota Y., Tokumitsu H., Kobayashi R.
    FEBS Lett. 584:1119-1125(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH S100A1; S100A2 AND S100A6.
  10. "Two structures of cyclophilin 40: folding and fidelity in the TPR domains."
    Taylor P., Dornan J., Carrello A., Minchin R.F., Ratajczak T., Walkinshaw M.D.
    Structure 9:431-438(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).

Entry informationi

Entry nameiPPID_BOVIN
AccessioniPrimary (citable) accession number: P26882
Secondary accession number(s): Q28077, Q2HJ45
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: January 23, 2007
Last modified: June 11, 2014
This is version 121 of the entry and version 6 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.

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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