ID PPIB_ORPSP Reviewed; 203 AA. AC Q01490; DT 17-JAN-2003, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 03-AUG-2022, entry version 93. DE RecName: Full=Peptidyl-prolyl cis-trans isomerase B; DE Short=PPIase B; DE EC=5.2.1.8; DE AltName: Full=Cyclophilin B; DE AltName: Full=Rotamase B; DE Flags: Precursor; GN Name=CYPB; OS Orpinomyces sp. (strain PC-2). OC Eukaryota; Fungi; Fungi incertae sedis; Chytridiomycota; OC Chytridiomycota incertae sedis; Neocallimastigomycetes; Neocallimastigales; OC Neocallimastigaceae; Orpinomyces; unclassified Orpinomyces. OX NCBI_TaxID=50059; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 23-52. RX PubMed=7708690; DOI=10.1073/pnas.92.7.2587; RA Chen H., Li X.-L., Ljungdahl L.G.; RT "A cyclophilin from the polycentric anaerobic rumen fungus Orpinomyces sp. RT strain PC-2 is highly homologous to vertebrate cyclophilin B."; RL Proc. Natl. Acad. Sci. U.S.A. 92:2587-2591(1995). CC -!- FUNCTION: PPIases accelerate the folding of proteins. It catalyzes the CC cis-trans isomerization of proline imidic peptide bonds in CC oligopeptides. 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 -!- ACTIVITY REGULATION: Inhibited by cyclosporin A (CsA). CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000250}. 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; U17900; AAD04195.1; -; mRNA. DR AlphaFoldDB; Q01490; -. DR SMR; Q01490; -. DR GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell. DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW. DR GO; GO:0006457; P:protein folding; IEA:InterPro. DR GO; GO:0000413; P:protein peptidyl-prolyl isomerization; IEA:InterPro. 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 1: Evidence at protein level; KW Direct protein sequencing; Endoplasmic reticulum; Isomerase; Rotamase; KW Signal. FT SIGNAL 1..22 FT /evidence="ECO:0000269|PubMed:7708690" FT CHAIN 23..203 FT /note="Peptidyl-prolyl cis-trans isomerase B" FT /id="PRO_0000025485" FT DOMAIN 33..190 FT /note="PPIase cyclophilin-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00156" FT MOTIF 200..203 FT /note="Prevents secretion from ER" FT /evidence="ECO:0000250" FT BINDING 147 FT /ligand="cyclosporin A" FT /ligand_id="ChEBI:CHEBI:4031" FT /evidence="ECO:0000255" SQ SEQUENCE 203 AA; 21969 MW; A5748C94305B8BE0 CRC64; MNFSIKSVIF LAIVALATLV SASTNPKVTN KVYFDIKQGD KDLGRIVLGL YGEVVPKTVE NFRALATGEK GYGYKNSKFH RVIKDFMIQG GDFTRGDGTG GKSIYGERFA DENFKLRHTG PGILSMANAG RDTNGSQFFI TTVTTSWLDG RHVVFGKVIE GMDVVTAIET TKTLPGDRPA TPVIIADCGE LPVSNNNDAK AEL //