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P26882 (PPID_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 119. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Peptidyl-prolyl cis-trans isomerase D

Short name=PPIase D
EC=5.2.1.8
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 names
Name:PPID
Synonyms:CYPD
OrganismBos taurus (Bovine) [Reference proteome]
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos

Protein attributes

Sequence length370 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.4 Ref.8

Catalytic activity

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

Enzyme regulation

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

Subunit structure

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). Ref.1 Ref.5 Ref.6 Ref.7 Ref.8 Ref.9

Subcellular location

Cytoplasm. Nucleusnucleolus By similarity. Nucleusnucleoplasm By similarity.

Tissue specificity

Detected in heart, thymis and brain. Ref.1

Post-translational modification

The N-terminus is blocked.

Sequence similarities

Belongs to the cyclophilin-type PPIase family. PPIase D subfamily.

Contains 1 PPIase cyclophilin-type domain.

Contains 3 TPR repeats.

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.

Ontologies

Keywords
   Biological processApoptosis
Protein transport
Transport
   Cellular componentCytoplasm
Nucleus
   DomainRepeat
TPR repeat
   LigandCyclosporin
   Molecular functionChaperone
Isomerase
Rotamase
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processapoptotic process

Inferred from electronic annotation. Source: UniProtKB-KW

cellular response to UV-A

Inferred from sequence or structural similarity. Source: UniProtKB

chaperone-mediated protein folding

Inferred from sequence or structural similarity. Source: UniProtKB

lipid particle organization

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of transcription from RNA polymerase II promoter

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of apoptotic process

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of protein secretion

Inferred from electronic annotation. Source: Ensembl

positive regulation of viral genome replication

Inferred from electronic annotation. Source: Ensembl

protein complex assembly

Inferred from sequence or structural similarity. Source: UniProtKB

protein folding

Inferred from direct assay Ref.8. Source: UniProtKB

protein transport

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytoplasm

Inferred from sequence or structural similarity. Source: UniProtKB

intermediate filament cytoskeleton

Inferred from electronic annotation. Source: Ensembl

nucleolus

Inferred from sequence or structural similarity. Source: UniProtKB

nucleoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionHsp70 protein binding

Inferred from direct assay Ref.7. Source: UniProtKB

Hsp90 protein binding

Inferred from sequence or structural similarity. Source: UniProtKB

estrogen receptor binding

Inferred from direct assay Ref.1. Source: UniProtKB

peptide binding

Inferred from electronic annotation. Source: UniProtKB-KW

peptidyl-prolyl cis-trans isomerase activity

Inferred from sequence or structural similarity. Source: UniProtKB

transcription factor binding

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 370369Peptidyl-prolyl cis-trans isomerase D
PRO_0000064152

Regions

Domain19 – 183165PPIase cyclophilin-type
Repeat223 – 25634TPR 1
Repeat273 – 30634TPR 2
Repeat307 – 34034TPR 3
Region185 – 21531Chaperone activity
Region214 – 370157Interaction with HSP90AB1

Amino acid modifications

Modified residue1711N6-acetyllysine By similarity
Modified residue1981Phosphoserine By similarity

Secondary structure

........................................................... 370
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P26882 [UniParc].

Last modified January 23, 2007. Version 6.
Checksum: F278FDE1B9494241

FASTA37040,620
        10         20         30         40         50         60 
MSHPSPQAKP SNPSNPRVFF DVDIGGERVG RIVLELFADI VPKTAENFRA LCTGEKGIGP 

        70         80         90        100        110        120 
TTGKPLHFKG CPFHRIIKKF MIQGGDFSNQ NGTGGESIYG EKFEDENFHY KHDKEGLLSM 

       130        140        150        160        170        180 
ANAGSNTNGS QFFITTVPTP HLDGKHVVFG QVIKGMGVAK ILENVEVKGE KPAKLCVIAE 

       190        200        210        220        230        240 
CGELKEGDDW GIFPKDGSGD SHPDFPEDAD VDLKDVDKIL LISEDLKNIG NTFFKSQNWE 

       250        260        270        280        290        300 
MAIKKYTKVL RYVEGSRAAA EDADGAKLQP VALSCVLNIG ACKLKMSDWQ GAVDSCLEAL 

       310        320        330        340        350        360 
EIDPSNTKAL YRRAQGWQGL KEYDQALADL KKAQEIAPED KAIQAELLKV KQKIKAQKDK 

       370 
EKAAYAKMFA 

« Hide

References

« Hide 'large scale' references
[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]"Interaction of the Hsp90 cochaperone cyclophilin 40 with Hsc70."
Carrello A., Allan R.K., Morgan S.L., Owen B.A., Mok D., Ward B.K., Minchin R.F., Toft D.O., Ratajczak T.
Cell Stress Chaperones 9:167-181(2004) [PubMed] [Europe PMC] [Abstract]
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).

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D14074 mRNA. Translation: BAA03159.1.
BC113318 mRNA. Translation: AAI13319.1.
L11668 mRNA. Translation: AAA30484.1.
PIRA46579.
RefSeqNP_776578.1. NM_174153.3.
UniGeneBt.7221.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1IHGX-ray1.80A1-370[»]
1IIPX-ray2.00A1-370[»]
ProteinModelPortalP26882.
SMRP26882. Positions 2-365.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid158751. 1 interaction.
IntActP26882. 6 interactions.
MINTMINT-2832213.

Proteomic databases

PRIDEP26882.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSBTAT00000022180; ENSBTAP00000022180; ENSBTAG00000016680.
GeneID281420.
KEGGbta:281420.

Organism-specific databases

CTD5481.

Phylogenomic databases

eggNOGCOG0652.
GeneTreeENSGT00550000074595.
HOGENOMHOG000065980.
HOVERGENHBG053654.
InParanoidP26882.
KOK05864.
OMAKFEDEAF.
OrthoDBEOG79GT7W.
TreeFamTF324493.

Family and domain databases

Gene3D1.25.40.10. 1 hit.
InterProIPR020892. Cyclophilin-type_PPIase_CS.
IPR002130. Cyclophilin-type_PPIase_dom.
IPR013026. TPR-contain_dom.
IPR011990. TPR-like_helical.
IPR019734. TPR_repeat.
[Graphical view]
PfamPF00160. Pro_isomerase. 1 hit.
PF13176. TPR_7. 1 hit.
[Graphical view]
PRINTSPR00153. CSAPPISMRASE.
SMARTSM00028. TPR. 3 hits.
[Graphical view]
PROSITEPS00170. CSA_PPIASE_1. 1 hit.
PS50072. CSA_PPIASE_2. 1 hit.
PS50005. TPR. 3 hits.
PS50293. TPR_REGION. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP26882.
NextBio20805409.

Entry information

Entry namePPID_BOVIN
AccessionPrimary (citable) accession number: P26882
Secondary accession number(s): Q28077, Q2HJ45
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 119 of the entry and version 6 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references