ID   A5YBL8_HORSE            Unreviewed;       216 AA.
AC   A5YBL8;
DT   10-JUL-2007, integrated into UniProtKB/TrEMBL.
DT   10-JUL-2007, sequence version 1.
DT   27-MAR-2024, entry version 124.
DE   RecName: Full=Peptidyl-prolyl cis-trans isomerase {ECO:0000256|RuleBase:RU363019};
DE            Short=PPIase {ECO:0000256|RuleBase:RU363019};
DE            EC=5.2.1.8 {ECO:0000256|RuleBase:RU363019};
GN   Name=PPIB {ECO:0000313|EMBL:ABQ82138.1};
OS   Equus caballus (Horse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus.
OX   NCBI_TaxID=9796 {ECO:0000313|EMBL:ABQ82138.1};
RN   [1] {ECO:0000313|EMBL:ABQ82138.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=17498917; DOI=10.1016/j.ygeno.2007.03.009;
RA   Tryon R.C., White S.D., Bannasch D.L.;
RT   "Homozygosity mapping approach identifies a missense mutation in equine
RT   cyclophilin B (PPIB) associated with HERDA in the American Quarter Horse.";
RL   Genomics 90:93-102(2007).
RN   [2] {ECO:0007829|PDB:4FRU, ECO:0007829|PDB:4FRV}
RP   X-RAY CRYSTALLOGRAPHY (1.10 ANGSTROMS) OF 34-216 IN COMPLEX WITH ZINC.
RX   PubMed=23137129; DOI=10.1186/1756-0500-5-626;
RA   Boudko S.P., Ishikawa Y., Lerch T.F., Nix J., Chapman M.S., Bachinger H.P.;
RT   "Crystal structures of wild-type and mutated cyclophilin B that causes
RT   hyperelastosis cutis in the American quarter horse.";
RL   BMC Res. Notes 5:626-626(2012).
CC   -!- FUNCTION: PPIases accelerate the folding of proteins. It catalyzes the
CC       cis-trans isomerization of proline imidic peptide bonds in
CC       oligopeptides. {ECO:0000256|RuleBase:RU363019}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[protein]-peptidylproline (omega=180) = [protein]-
CC         peptidylproline (omega=0); Xref=Rhea:RHEA:16237, Rhea:RHEA-
CC         COMP:10747, Rhea:RHEA-COMP:10748, ChEBI:CHEBI:83833,
CC         ChEBI:CHEBI:83834; EC=5.2.1.8;
CC         Evidence={ECO:0000256|ARBA:ARBA00000971,
CC         ECO:0000256|RuleBase:RU363019};
CC   -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family.
CC       {ECO:0000256|RuleBase:RU363019}.
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DR   EMBL; EF397503; ABQ82138.1; -; mRNA.
DR   RefSeq; NP_001093231.1; NM_001099761.1.
DR   PDB; 4FRU; X-ray; 1.10 A; A=34-216.
DR   PDB; 4FRV; X-ray; 1.10 A; A=34-216.
DR   PDBsum; 4FRU; -.
DR   PDBsum; 4FRV; -.
DR   AlphaFoldDB; A5YBL8; -.
DR   SMR; A5YBL8; -.
DR   PeptideAtlas; A5YBL8; -.
DR   GeneID; 100066834; -.
DR   KEGG; ecb:100066834; -.
DR   CTD; 5479; -.
DR   HOGENOM; CLU_012062_4_2_1; -.
DR   OrthoDB; 339082at2759; -.
DR   TreeFam; TF354259; -.
DR   GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR   GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0032991; C:protein-containing complex; ISS:CAFA.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; ISS:CAFA.
DR   GO; GO:0061077; P:chaperone-mediated protein folding; ISS:UniProtKB.
DR   GO; GO:0000413; P:protein peptidyl-prolyl isomerization; ISS:CAFA.
DR   CDD; cd01926; cyclophilin_ABH_like; 1.
DR   Gene3D; 2.40.100.10; Cyclophilin-like; 1.
DR   InterPro; IPR029000; Cyclophilin-like_dom_sf.
DR   InterPro; IPR020892; Cyclophilin-type_PPIase_CS.
DR   InterPro; IPR002130; Cyclophilin-type_PPIase_dom.
DR   PANTHER; PTHR11071; PEPTIDYL-PROLYL CIS-TRANS ISOMERASE; 1.
DR   PANTHER; PTHR11071:SF561; PEPTIDYL-PROLYL CIS-TRANS ISOMERASE H; 1.
DR   Pfam; PF00160; Pro_isomerase; 1.
DR   PRINTS; PR00153; CSAPPISMRASE.
DR   SUPFAM; SSF50891; Cyclophilin-like; 1.
DR   PROSITE; PS00170; CSA_PPIASE_1; 1.
DR   PROSITE; PS50072; CSA_PPIASE_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure {ECO:0007829|PDB:4FRU, ECO:0007829|PDB:4FRV};
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|RuleBase:RU363019};
KW   Metal-binding {ECO:0007829|PDB:4FRU, ECO:0007829|PDB:4FRV};
KW   Rotamase {ECO:0000256|ARBA:ARBA00023110, ECO:0000256|RuleBase:RU363019};
KW   Zinc {ECO:0007829|PDB:4FRU, ECO:0007829|PDB:4FRV}.
FT   DOMAIN          47..204
FT                   /note="PPIase cyclophilin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50072"
FT   BINDING         54
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0007829|PDB:4FRU, ECO:0007829|PDB:4FRV"
FT   BINDING         166
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0007829|PDB:4FRU, ECO:0007829|PDB:4FRV"
SQ   SEQUENCE   216 AA;  23808 MW;  EAAEC58447EA20BE CRC64;
     MLRFSERNMK VLFAAALIVG SVFFLLLPGP STADEKKKGP KVTVKVYFDL RIGDEDIGRV
     VIGLFGKTVP KTVDNFVALA TGEKGFGYKD SKFHRVIKDF MIQGGDFTRG DGTGGKSIYG
     ERFPDENFKL KHYGPGWVSM ANAGKDTNGS QFFITTVKTA WLDGKHVVFG KVLEGMEVVR
     KVETTKTDGR DKPLKDVTIA DCGKIEVEKP FAIAKE
//