ID CYPH_DROME STANDARD; PRT; 165 AA. AC P25007; DT 01-MAR-1992 (REL. 21, CREATED) DT 01-MAR-1992 (REL. 21, LAST SEQUENCE UPDATE) DT 01-NOV-1995 (REL. 32, LAST ANNOTATION UPDATE) DE PEPTIDYL-PROLYL CIS-TRANS ISOMERASE (EC 5.2.1.8) (PPIASE) (ROTAMASE) DE (CYCLOPHILIN) (CYCLOSPORIN A-BINDING PROTEIN). GN CYP1. OS DROSOPHILA MELANOGASTER (FRUIT FLY). OC EUKARYOTA; METAZOA; ARTHROPODA; INSECTA; DIPTERA. RN [1] RP SEQUENCE FROM N.A. RX MEDLINE; 91199192. RA STAMNES M.A., SHEIH B.-H., CHUMAN L., HARRIS G.L., ZUKER C.S.; RL CELL 65:219-227(1991). RN [2] RP SEQUENCE OF 7-20. RC STRAIN=VALLECAS; TISSUE=WING IMAGINAL DISCS; RX MEDLINE; 93272852. RA SANTAREN J.F., VAN DAMME J., PUYPE M., VANDEKERCKHOVE J., RA GARCIA-BELLIDO A.; RL EXP. CELL RES. 206:220-226(1993). CC -!- FUNCTION: PPIASES ACCELERATE THE FOLDING OF PROTEINS. CC -!- CATALYTIC ACTIVITY: CIS-TRANS ISOMERIZATION OF PROLINE IMIDIC CC PEPTIDE BONDS IN OLIGOPEPTIDES. CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC. CC -!- ENZYME REGULATION: BINDS CYCLOSPORIN A (CSA). CSA MEDIATES SOME CC OF ITS EFFECTS VIA AN INHIBITORY ACTION ON PPIASE. 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; M62398; G157164; -. DR HSSP; P05092; 1CYH. DR FLYBASE; FBGN0004432; CYP1. DR PROSITE; PS00170; CSA_PPIASE. KW CYCLOSPORIN; ISOMERASE; ROTAMASE; MULTIGENE FAMILY. SQ SEQUENCE 165 AA; 17907 MW; 5DAE9590 CRC32; MSTLPRVFFD MTADNEPLGR IVMELRSDVV PKTAENFRAL CTGEKGFGYK GSIFHRVIPN FMCQGGDFTN HNGTGGKSIY GNKFPDENFE LKHTGSGILS MANAGANTNG SQFFICTVKT AWLDNKHVVF GEVVEGLDVV KKIESYGSQS GKTSKKIIVA NSGSL //