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Protein

Peptidyl-prolyl cis-trans isomerase

Gene

PPIB

Organism
Equus caballus (Horse)
Status
Unreviewed-Annotation score: Annotation score: 3 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.UniRule annotation

Catalytic activityi

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

GO - Molecular functioni

  1. peptidyl-prolyl cis-trans isomerase activity Source: UniProtKB
  2. poly(A) RNA binding Source: Ensembl
  3. protein complex binding Source: UniProtKB

GO - Biological processi

  1. bone development Source: Ensembl
  2. chaperone-mediated protein folding Source: UniProtKB
  3. positive regulation of multicellular organism growth Source: Ensembl
  4. protein peptidyl-prolyl isomerization Source: UniProtKB
  5. protein stabilization Source: Ensembl
Complete GO annotation...

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)
Taxonomic identifieri9796 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaPerissodactylaEquidaeEquus
ProteomesiUP000002281: Chromosome 1

Subcellular locationi

GO - Cellular componenti

  1. endoplasmic reticulum Source: Ensembl
  2. extracellular vesicular exosome Source: Ensembl
  3. macromolecular complex Source: UniProtKB
  4. membrane Source: Ensembl
  5. nucleus Source: Ensembl
Complete GO annotation...

Interactioni

Protein-protein interaction databases

STRINGi9796.ENSECAP00000014710.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4FRVX-ray1.10A34-216[»]
ProteinModelPortaliA5YBL8.
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.
GeneTreeiENSGT00760000119072.
HOGENOMiHOG000065981.
HOVERGENiHBG001065.
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

        10         20         30         40         50
MLRFSERNMK VLFAAALIVG SVFFLLLPGP STADEKKKGP KVTVKVYFDL
60 70 80 90 100
RIGDEDIGRV VIGLFGKTVP KTVDNFVALA TGEKGFGYKD SKFHRVIKDF
110 120 130 140 150
MIQGGDFTRG DGTGGKSIYG ERFPDENFKL KHYGPGWVSM ANAGKDTNGS
160 170 180 190 200
QFFITTVKTA WLDGKHVVFG KVLEGMEVVR KVETTKTDGR DKPLKDVTIA
210
DCGKIEVEKP FAIAKE
Length:216
Mass (Da):23,808
Last modified:July 10, 2007 - v1
Checksum:iEAAEC58447EA20BE
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
Links Updated
EF397503 mRNA. Translation: ABQ82138.1.
RefSeqiNP_001093231.1. NM_001099761.1.
UniGeneiEca.5668.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4FRVX-ray1.10A34-216[»]
ProteinModelPortaliA5YBL8.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9796.ENSECAP00000014710.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi5479.

Phylogenomic databases

eggNOGiCOG0652.
GeneTreeiENSGT00760000119072.
HOGENOMiHOG000065981.
HOVERGENiHBG001065.
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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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: February 4, 2015
This is version 61 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureCombined sources, Complete proteome, Reference proteomeImported

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.