ID CYPB_ORPSP STANDARD; PRT; 203 AA. AC Q01490; DT 28-FEB-2003 (Rel. 41, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 10-MAY-2005 (Rel. 47, Last annotation update) DE Peptidyl-prolyl cis-trans isomerase B precursor (EC 5.2.1.8) (PPIase) DE (Rotamase) (Cyclophilin B). GN Name=CYPB; OS Orpinomyces sp. (strain PC-2). OC Eukaryota; Fungi; Chytridiomycota; Neocallimasticales; OC Neocallimasticaceae; Orpinomyces. OX NCBI_TaxID=50059; RN [1] RP NUCLEOTIDE SEQUENCE, AND PROTEIN SEQUENCE OF 23-52. RX MEDLINE=95223986; PubMed=7708690; RA Chen H., Li X.-L., Ljungdahl L.G.; RT "A cyclophilin from the polycentric anaerobic rumen fungus Orpinomyces RT sp. 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 CC the cis-trans isomerization of proline imidic peptide bonds in CC oligopeptides. CC -!- CATALYTIC ACTIVITY: Peptidylproline (omega=180) = peptidylproline CC (omega=0). CC -!- ENZYME REGULATION: Inhibited by cyclosporin A (CsA). CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen (By similarity). CC -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family. CC -!- SIMILARITY: Contains 1 PPIase cyclophilin-type domain. 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 HSSP; P23284; 1CYN. DR SMR; Q01490; 26-193. DR InterPro; IPR002130; CSA_PPIase. DR Pfam; PF00160; Pro_isomerase; 1. DR PRINTS; PR00153; CSAPPISMRASE. DR PROSITE; PS00170; CSA_PPIASE_1; 1. DR PROSITE; PS50072; CSA_PPIASE_2; 1. KW Cyclosporin; Direct protein sequencing; Endoplasmic reticulum; KW Isomerase; Rotamase; Signal. FT SIGNAL 1 22 FT CHAIN 23 203 Peptidyl-prolyl cis-trans isomerase B. FT DOMAIN 33 190 PPIase cyclophilin-type. FT MOTIF 200 203 Prevents secretion from ER (By FT similarity). FT BINDING 147 147 Cyclosporin A (CsA) (Potential). 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 //