Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P26882

- PPID_BOVIN

UniProt

P26882 - PPID_BOVIN

Protein

Peptidyl-prolyl cis-trans isomerase D

Gene

PPID

Organism
Bos taurus (Bovine)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 122 (01 Oct 2014)
      Sequence version 6 (23 Jan 2007)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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. estrogen receptor binding Source: UniProtKB
    2. Hsp70 protein binding Source: UniProtKB
    3. Hsp90 protein 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

    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

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 370369Peptidyl-prolyl cis-trans isomerase DPRO_0000064152Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei171 – 1711N6-acetyllysineBy similarity
    Modified residuei198 – 1981PhosphoserineBy 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

    1
    370
    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.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP26882.

    Family & Domainsi

    Domains and Repeats

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

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni185 – 21531Chaperone activityAdd
    BLAST
    Regioni214 – 370157Interaction with HSP90AB1Add
    BLAST

    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

    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

    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: October 1, 2014
    This is version 122 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.Curated

    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