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-JUN-1994 (REL. 29, 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. RM 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; RM 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 --------------------------------------------------------------------------- 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; DMCYP1. DR FLYBASE; 04432; CYP1. DR PROSITE; PS00170; CSA_PPIASE. KW CYCLOSPORIN; ISOMERASE; ROTAMASE; MULTIGENE FAMILY. SQ SEQUENCE 165 AA; 17907 MW; 149337 CN; MSTLPRVFFD MTADNEPLGR IVMELRSDVV PKTAENFRAL CTGEKGFGYK GSIFHRVIPN FMCQGGDFTN HNGTGGKSIY GNKFPDENFE LKHTGSGILS MANAGANTNG SQFFICTVKT AWLDNKHVVF GEVVEGLDVV KKIESYGSQS GKTSKKIIVA NSGSL //