Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

A5YBL8

- A5YBL8_HORSE

UniProt

A5YBL8 - A5YBL8_HORSE

(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)

Protein

Peptidyl-prolyl cis-trans isomerase

Gene

PPIB

Organism
Equus caballus (Horse)
Status
Unreviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli

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. poly(A) RNA binding Source: Ensembl
  3. protein complex binding Source: UniProt

GO - Biological processi

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

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.
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:
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 ENSGT00760000119072.
HOGENOMi HOG000065981.
HOVERGENi HBG001065.
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

« 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: October 29, 2014
This is version 58 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