ID Q01490 PRELIMINARY; PRT; 203 AA. AC Q01490; DT 01-NOV-1998 (TREMBLREL. 08, CREATED) DT 01-NOV-1998 (TREMBLREL. 08, LAST SEQUENCE UPDATE) DT 01-NOV-1998 (TREMBLREL. 08, LAST ANNOTATION UPDATE) DE PEPTIDYL-PROLYL CIS-TRANS ISOMERASE B PRECURSOR (EC 5.2.1.8) (PPIASE) DE (CYCLOPHILIN B) (ROTAMASE). GN CYPB. OS ORPINOMYCES SP. (STRAIN PC-2). OC EUKARYOTA; FUNGI; CHYTRIDIOMYCOTA; CHYTRIDIOMYCETES; OC NEOCALLIMASTICALES; NEOCALLIMASTICACEAE. RN [1] RP SEQUENCE FROM N.A., AND OF SEQUENCE 23-52. RX MEDLINE; 95223986. RA CHEN H., LI X.-L., LJUNGDAHL L.G.; RT "A cyclophilin from the polycentric anaerobic rumen fungus RT Orpinomyces sp. strain PC-2 is highly homologous to vertebrate RT cyclophilin B."; RL PROC. NATL. ACAD. SCI. U.S.A. 92:2587-2591(1995). CC -!- FUNCTION: PPIASES ACCELERATE THE FOLDING OF PROTEINS. CC -!- CATALYTIC ACTIVITY: CIS-TRANS ISOMERIZATION OF PROLINE IMIDIC CC PEPTIDE BONDS IN OLIGOPEPTIDES. CC -!- ENZYME REGULATION: CYCLOSPORIN A (CSA) INHIBITS CYPB. CC -!- SUBCELLULAR LOCATION: ENDOPLASMIC RETICULUM LUMEN CC (BY SIMILARITY). CC -!- SIMILARITY: BELONGS TO THE CYCLOPHILIN-TYPE PPIASE FAMILY. 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; G849081; -. DR PROSITE; PS00170; CSA_PPIASE_1; 1. DR PROSITE; PS50072; CSA_PPIASE_2; 1. DR PFAM; PF00160; pro_isomerase; 1. KW ISOMERASE; ROTAMASE; SIGNAL; CYCLOSPORIN; ENDOPLASMIC RETICULUM. FT SIGNAL 1 22 FT CHAIN 23 203 PEPTIDYL-PROLYL CIS-TRANS ISOMERASE B. FT BINDING 147 147 CSA (POTENTIAL). FT SITE 200 203 PREVENT SECRETION FROM ER FT (BY SIMILARITY). SQ SEQUENCE 203 AA; 21969 MW; 44241208 CRC32; MNFSIKSVIF LAIVALATLV SASTNPKVTN KVYFDIKQGD KDLGRIVLGL YGEVVPKTVE NFRALATGEK GYGYKNSKFH RVIKDFMIQG GDFTRGDGTG GKSIYGERFA DENFKLRHTG PGILSMANAG RDTNGSQFFI TTVTTSWLDG RHVVFGKVIE GMDVVTAIET TKTLPGDRPA TPVIIADCGE LPVSNNNDAK AEL //