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A5YBL8

- A5YBL8_HORSE

UniProt

A5YBL8 - A5YBL8_HORSE

Protein

Peptidyl-prolyl cis-trans isomerase

Gene

PPIB

Organism
Equus caballus (Horse)
Status
Unreviewed - Annotation score: 2 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 57 (01 Oct 2014)
      Sequence version 1 (10 Jul 2007)
      Previous versions | rss
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    Functioni

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

    Catalytic activityi

    Peptidylproline (omega=180) = peptidylproline (omega=0).UniRule annotationSAAS annotation

    GO - Molecular functioni

    1. peptidyl-prolyl cis-trans isomerase activity Source: UniProt
    2. protein complex binding Source: UniProt

    GO - Biological processi

    1. chaperone-mediated protein folding Source: UniProt
    2. protein peptidyl-prolyl isomerization Source: UniProt

    Keywords - Molecular functioni

    Isomerase, RotamaseUniRule annotationSAAS annotation

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Peptidyl-prolyl cis-trans isomeraseUniRule annotation (EC:5.2.1.8UniRule annotation)
    Gene namesi
    Name:PPIBImported
    OrganismiEquus caballus (Horse)Imported
    Taxonomic identifieri9796 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaPerissodactylaEquidaeEquus
    ProteomesiUP000002281: Chromosome 1

    Subcellular locationi

    GO - Cellular componenti

    1. macromolecular complex Source: UniProt

    Interactioni

    Protein-protein interaction databases

    STRINGi9796.ENSECAP00000014710.

    Structurei

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4FRUX-ray1.10A34-216[»]
    4FRVX-ray1.10A34-216[»]
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the cyclophilin-type PPIase family.UniRule annotation
    Contains 1 PPIase cyclophilin-type domain.UniRule annotation
    Contains PPIase cyclophilin-type domain.SAAS annotation

    Phylogenomic databases

    eggNOGiCOG0652.
    GeneTreeiENSGT00750000117331.
    HOGENOMiHOG000065981.
    HOVERGENiHBG001065.
    InParanoidiA5YBL8.
    KOiK03768.
    OMAiPSVANDK.
    OrthoDBiEOG7RFTK4.
    TreeFamiTF354259.

    Family and domain databases

    Gene3Di2.40.100.10. 1 hit.
    InterProiIPR029000. Cyclophilin-like_dom.
    IPR024936. Cyclophilin-type_PPIase.
    IPR020892. Cyclophilin-type_PPIase_CS.
    IPR002130. Cyclophilin-type_PPIase_dom.
    [Graphical view]
    PfamiPF00160. Pro_isomerase. 1 hit.
    [Graphical view]
    PIRSFiPIRSF001467. Peptidylpro_ismrse. 1 hit.
    PRINTSiPR00153. CSAPPISMRASE.
    SUPFAMiSSF50891. SSF50891. 1 hit.
    PROSITEiPS00170. CSA_PPIASE_1. 1 hit.
    PS50072. CSA_PPIASE_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    A5YBL8-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLRFSERNMK VLFAAALIVG SVFFLLLPGP STADEKKKGP KVTVKVYFDL    50
    RIGDEDIGRV VIGLFGKTVP KTVDNFVALA TGEKGFGYKD SKFHRVIKDF 100
    MIQGGDFTRG DGTGGKSIYG ERFPDENFKL KHYGPGWVSM ANAGKDTNGS 150
    QFFITTVKTA WLDGKHVVFG KVLEGMEVVR KVETTKTDGR DKPLKDVTIA 200
    DCGKIEVEKP FAIAKE 216
    Length:216
    Mass (Da):23,808
    Last modified:July 10, 2007 - v1
    Checksum:iEAAEC58447EA20BE
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    EF397503 mRNA. Translation: ABQ82138.1.
    RefSeqiNP_001093231.1. NM_001099761.1.
    UniGeneiEca.5668.

    Genome annotation databases

    EnsembliENSECAT00000018057; ENSECAP00000014710; ENSECAG00000017164.
    GeneIDi100066834.
    KEGGiecb:100066834.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    EF397503 mRNA. Translation: ABQ82138.1 .
    RefSeqi NP_001093231.1. NM_001099761.1.
    UniGenei Eca.5668.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    4FRU X-ray 1.10 A 34-216 [» ]
    4FRV X-ray 1.10 A 34-216 [» ]
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 9796.ENSECAP00000014710.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSECAT00000018057 ; ENSECAP00000014710 ; ENSECAG00000017164 .
    GeneIDi 100066834.
    KEGGi ecb:100066834.

    Organism-specific databases

    CTDi 5479.

    Phylogenomic databases

    eggNOGi COG0652.
    GeneTreei ENSGT00750000117331.
    HOGENOMi HOG000065981.
    HOVERGENi HBG001065.
    InParanoidi A5YBL8.
    KOi K03768.
    OMAi PSVANDK.
    OrthoDBi EOG7RFTK4.
    TreeFami TF354259.

    Family and domain databases

    Gene3Di 2.40.100.10. 1 hit.
    InterProi IPR029000. Cyclophilin-like_dom.
    IPR024936. Cyclophilin-type_PPIase.
    IPR020892. Cyclophilin-type_PPIase_CS.
    IPR002130. Cyclophilin-type_PPIase_dom.
    [Graphical view ]
    Pfami PF00160. Pro_isomerase. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF001467. Peptidylpro_ismrse. 1 hit.
    PRINTSi PR00153. CSAPPISMRASE.
    SUPFAMi SSF50891. SSF50891. 1 hit.
    PROSITEi PS00170. CSA_PPIASE_1. 1 hit.
    PS50072. CSA_PPIASE_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Homozygosity mapping approach identifies a missense mutation in equine cyclophilin B (PPIB) associated with HERDA in the American Quarter Horse."
      Tryon R.C., White S.D., Bannasch D.L.
      Genomics 90:93-102(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE.
    2. "Genome sequence, comparative analysis, and population genetics of the domestic horse."
      Broad Institute Genome Sequencing Platform, Broad Institute Whole Genome Assembly Team
      Wade C.M., Giulotto E., Sigurdsson S., Zoli M., Gnerre S., Imsland F., Lear T.L., Adelson D.L., Bailey E., Bellone R.R., Bloecker H., Distl O., Edgar R.C., Garber M., Leeb T., Mauceli E., MacLeod J.N., Penedo M.C.T.
      , Raison J.M., Sharpe T., Vogel J., Andersson L., Antczak D.F., Biagi T., Binns M.M., Chowdhary B.P., Coleman S.J., Della Valle G., Fryc S., Guerin G., Hasegawa T., Hill E.W., Jurka J., Kiialainen A., Lindgren G., Liu J., Magnani E., Mickelson J.R., Murray J., Nergadze S.G., Onofrio R., Pedroni S., Piras M.F., Raudsepp T., Rocchi M., Roeed K.H., Ryder O.A., Searle S., Skow L., Swinburne J.E., Syvaenen A.C., Tozaki T., Valberg S.J., Vaudin M., White J.R., Zody M.C., Lander E.S., Lindblad-Toh K.
      Science 326:865-867(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ThoroughbredImported.
    3. Ensembl
      Submitted (JUL-2011) to UniProtKB
      Cited for: IDENTIFICATION.
      Strain: ThoroughbredImported.
    4. "Crystal structures of wild-type and mutated cyclophilin B that causes hyperelastosis cutis in the American quarter horse."
      Boudko S.P., Ishikawa Y., Lerch T.F., Nix J., Chapman M.S., Bachinger H.P.
      BMC Res. Notes 5:626-626(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.10 ANGSTROMS) OF 34-216.

    Entry informationi

    Entry nameiA5YBL8_HORSE
    AccessioniPrimary (citable) accession number: A5YBL8
    Entry historyi
    Integrated into UniProtKB/TrEMBL: July 10, 2007
    Last sequence update: July 10, 2007
    Last modified: October 1, 2014
    This is version 57 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiUnreviewed (UniProtKB/TrEMBL)

    Miscellaneousi

    Keywords - Technical termi

    3D-structureImported, Complete proteome, Reference proteomeImported

    External Data

    Dasty 3