PPIB_CHICK
ID PPIB_CHICK Reviewed; 207 AA.
AC P24367;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-1992, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Peptidyl-prolyl cis-trans isomerase B;
DE Short=PPIase B;
DE EC=5.2.1.8 {ECO:0000250|UniProtKB:P23284};
DE AltName: Full=Cyclophilin B;
DE AltName: Full=Rotamase B;
DE AltName: Full=S-cyclophilin;
DE Short=SCYLP;
DE Flags: Precursor;
GN Name=PPIB;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2040593; DOI=10.1016/s0021-9258(18)99079-4;
RA Caroni P., Rothenfluh A., McGlynn E., Schneider C.;
RT "S-cyclophilin. New member of the cyclophilin family associated with the
RT secretory pathway.";
RL J. Biol. Chem. 266:10739-10742(1991).
CC -!- FUNCTION: PPIase that catalyzes the cis-trans isomerization of proline
CC imidic peptide bonds in oligopeptides and may therefore assist protein
CC folding. {ECO:0000250|UniProtKB:P23284}.
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:0000250|UniProtKB:P23284};
CC -!- ACTIVITY REGULATION: Inhibited by cyclosporin A (CsA).
CC {ECO:0000250|UniProtKB:P23284}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen
CC {ECO:0000250|UniProtKB:P23284}. Melanosome
CC {ECO:0000250|UniProtKB:P23284}. Note=Identified by mass spectrometry in
CC melanosome fractions from stage I to stage IV.
CC {ECO:0000250|UniProtKB:P23284}.
CC -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family. PPIase B
CC subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M63553; AAA49064.1; -; mRNA.
DR PIR; A40516; A40516.
DR RefSeq; NP_990792.1; NM_205461.1.
DR AlphaFoldDB; P24367; -.
DR SMR; P24367; -.
DR BioGRID; 676696; 1.
DR IntAct; P24367; 1.
DR STRING; 9031.ENSGALP00000003455; -.
DR PaxDb; P24367; -.
DR GeneID; 396447; -.
DR KEGG; gga:396447; -.
DR CTD; 5479; -.
DR VEuPathDB; HostDB:geneid_396447; -.
DR eggNOG; KOG0880; Eukaryota.
DR InParanoid; P24367; -.
DR OrthoDB; 1403619at2759; -.
DR PhylomeDB; P24367; -.
DR PRO; PR:P24367; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
DR GO; GO:0016018; F:cyclosporin A binding; ISS:UniProtKB.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IDA:UniProtKB.
DR GO; GO:0061077; P:chaperone-mediated protein folding; IDA:UniProtKB.
DR GO; GO:1904027; P:negative regulation of collagen fibril organization; IDA:UniProtKB.
DR GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR GO; GO:0000413; P:protein peptidyl-prolyl isomerization; IDA:UniProtKB.
DR Gene3D; 2.40.100.10; -; 1.
DR InterPro; IPR029000; Cyclophilin-like_dom_sf.
DR InterPro; IPR024936; Cyclophilin-type_PPIase.
DR InterPro; IPR020892; Cyclophilin-type_PPIase_CS.
DR InterPro; IPR002130; Cyclophilin-type_PPIase_dom.
DR Pfam; PF00160; Pro_isomerase; 1.
DR PIRSF; PIRSF001467; Peptidylpro_ismrse; 1.
DR PRINTS; PR00153; CSAPPISMRASE.
DR SUPFAM; SSF50891; SSF50891; 1.
DR PROSITE; PS00170; CSA_PPIASE_1; 1.
DR PROSITE; PS50072; CSA_PPIASE_2; 1.
PE 2: Evidence at transcript level;
KW Endoplasmic reticulum; Isomerase; Reference proteome; Rotamase; Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000250"
FT CHAIN 25..207
FT /note="Peptidyl-prolyl cis-trans isomerase B"
FT /id="PRO_0000025482"
FT DOMAIN 38..195
FT /note="PPIase cyclophilin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00156"
FT MOTIF 198..207
FT /note="Prevents secretion from ER"
FT /evidence="ECO:0000250"
SQ SEQUENCE 207 AA; 22413 MW; D9C0C2E528E25B59 CRC64;
MKALVAATAL GPALLLLLPA ASRADERKKG PKVTAKVFFD LRVGEEDAGR VVIGLFGKTV
PKTVENFVAL ATGEKGFGFK GSKFHRVIKD FMIQGGDFTR GDGTGGKSIY GDRFPDENFK
LKHYGPGWVS MANAGKDTNG SQFFITTVKT AWLDGKHVVF GKVLEGMDVV RKVENTKTDS
RDKPLKDVTI ADCGTIEVEK PFAIAKE
