PPIB_BOVIN
ID PPIB_BOVIN Reviewed; 216 AA.
AC P80311; Q5E9F4;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 4.
DT 03-AUG-2022, entry version 143.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 5-216.
RC TISSUE=Uterus;
RA Carrello A., Mark P.J., House A.K., Ratajczak T.;
RT "The bovine homologue of CyP B.";
RL Submitted (JAN-1993) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP PROTEIN SEQUENCE OF 34-79.
RC TISSUE=Brain;
RX PubMed=8013656; DOI=10.1016/0014-5793(94)00501-x;
RA Galat A., Bouet F.;
RT "Cyclophilin-B is an abundant protein whose conformation is similar to
RT cyclophilin-A.";
RL FEBS Lett. 347:31-36(1994).
RN [5]
RP PROTEIN SEQUENCE OF 34-53.
RX PubMed=8010972; DOI=10.1042/bj3000871;
RA Bose S., Muecke M., Freedman R.B.;
RT "The characterization of a cyclophilin-type peptidyl prolyl cis-trans-
RT isomerase from the endoplasmic-reticulum lumen.";
RL Biochem. J. 300:871-875(1994).
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 -!- SUBUNIT: Interacts with DYM. Interacts with CALR, CLGN and CANX. Part
CC of a large chaperone multiprotein complex comprising DNAJB11, HSP90B1,
CC HSPA5, HYOU, PDIA2, PDIA4, PDIA6, PPIB, SDF2L1, UGGT1 and very small
CC amounts of ERP29, but not, or at very low levels, CALR nor CANX.
CC {ECO:0000250|UniProtKB:P23284}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen
CC {ECO:0000250|UniProtKB:P23284}. Melanosome
CC {ECO:0000250|UniProtKB:P23284}.
CC -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family. PPIase B
CC subfamily. {ECO:0000305}.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-9 is the initiator.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA03158.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; BT020966; AAX08983.1; -; mRNA.
DR EMBL; BC102462; AAI02463.1; -; mRNA.
DR EMBL; D14073; BAA03158.1; ALT_INIT; mRNA.
DR PIR; S45724; S45724.
DR RefSeq; NP_776577.1; NM_174152.2.
DR AlphaFoldDB; P80311; -.
DR SMR; P80311; -.
DR STRING; 9913.ENSBTAP00000022378; -.
DR PaxDb; P80311; -.
DR PeptideAtlas; P80311; -.
DR PRIDE; P80311; -.
DR Ensembl; ENSBTAT00000022378; ENSBTAP00000022378; ENSBTAG00000016822.
DR GeneID; 281419; -.
DR KEGG; bta:281419; -.
DR CTD; 5479; -.
DR VEuPathDB; HostDB:ENSBTAG00000016822; -.
DR VGNC; VGNC:33195; PPIB.
DR eggNOG; KOG0880; Eukaryota.
DR GeneTree; ENSGT00940000158007; -.
DR HOGENOM; CLU_012062_4_2_1; -.
DR InParanoid; P80311; -.
DR OMA; GEGYPGS; -.
DR OrthoDB; 1403619at2759; -.
DR TreeFam; TF354259; -.
DR Proteomes; UP000009136; Chromosome 10.
DR Bgee; ENSBTAG00000016822; Expressed in granulosa cell and 105 other tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0034663; C:endoplasmic reticulum chaperone complex; IEA:Ensembl.
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:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
DR GO; GO:0032991; C:protein-containing complex; ISS:CAFA.
DR GO; GO:0016018; F:cyclosporin A binding; ISS:UniProtKB.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; ISS:UniProtKB.
DR GO; GO:0070063; F:RNA polymerase binding; IEA:Ensembl.
DR GO; GO:0060348; P:bone development; IEA:Ensembl.
DR GO; GO:0061077; P:chaperone-mediated protein folding; ISS:UniProtKB.
DR GO; GO:0030593; P:neutrophil chemotaxis; IEA:Ensembl.
DR GO; GO:0044829; P:positive regulation by host of viral genome replication; IEA:Ensembl.
DR GO; GO:0040018; P:positive regulation of multicellular organism growth; IEA:Ensembl.
DR GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR GO; GO:0000413; P:protein peptidyl-prolyl isomerization; ISS:UniProtKB.
DR GO; GO:0050821; P:protein stabilization; IEA:Ensembl.
DR Gene3D; 2.40.100.10; -; 1.
DR InterPro; IPR029000; Cyclophilin-like_dom_sf.
DR InterPro; IPR020892; Cyclophilin-type_PPIase_CS.
DR InterPro; IPR002130; Cyclophilin-type_PPIase_dom.
DR Pfam; PF00160; Pro_isomerase; 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 1: Evidence at protein level;
KW Acetylation; Direct protein sequencing; Endoplasmic reticulum; Isomerase;
KW Reference proteome; Rotamase; S-nitrosylation; Signal.
FT SIGNAL 1..33
FT /evidence="ECO:0000269|PubMed:8010972,
FT ECO:0000269|PubMed:8013656"
FT CHAIN 34..216
FT /note="Peptidyl-prolyl cis-trans isomerase B"
FT /id="PRO_0000025478"
FT DOMAIN 47..204
FT /note="PPIase cyclophilin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00156"
FT MOTIF 213..216
FT /note="Prevents secretion from ER"
FT /evidence="ECO:0000250"
FT MOD_RES 84
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q99KR7"
FT MOD_RES 165
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q99KR7"
FT MOD_RES 202
FT /note="S-nitrosocysteine"
FT /evidence="ECO:0000250|UniProtKB:Q99KR7"
FT MOD_RES 209
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P24369"
FT MOD_RES 209
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P24369"
FT CONFLICT 38
FT /note="K -> G (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 168
FT /note="V -> G (in Ref. 3; BAA03158)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 216 AA; 23744 MW; 982CFD92FDBBC32F CRC64;
MLRLSERNMK ILFVAALVVG SVFFLLLPGP SAADEKKKGP KVTVKVYFDL RIGDEDIGRV
VIGLFGKTVP KTVDNFVALA TGEKGFGYKD SKFHRVIKDF MIQGGDFTRG DGTGGKSIYG
ERFPDENFKL KHYGPGWVSM ANAGKDTNGS QFFITTVKTA WLDGKHVVFG KVLEGMDVVR
KVESTKTDGR DKPLKDVTIA DCGKIEVEKP FAIAKE
