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 15-DEC-1998 (REL. 37, LAST ANNOTATION UPDATE) DE PEPTIDYL-PROLYL CIS-TRANS ISOMERASE (EC 5.2.1.8) (PPIASE) (ROTAMASE) DE (CYCLOPHILIN) (CYCLOSPORIN A-BINDING PROTEIN). GN CYP1 OR CYP-1. OS DROSOPHILA MELANOGASTER (FRUIT FLY). OC EUKARYOTA; METAZOA; ARTHROPODA; TRACHEATA; HEXAPODA; INSECTA; OC PTERYGOTA; DIPTERA; BRACHYCERA; MUSCOMORPHA; EPHYDROIDEA; OC DROSOPHILIDAE; DROSOPHILA. 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.; RT "The cyclophilin homolog ninaA is a tissue-specific integral membrane RT protein required for the proper synthesis of a subset of Drosophila RT rhodopsins."; RL CELL 65:219-227(1991). RN [2] RP SEQUENCE OF 7-20. RC STRAIN=VALLECAS; TISSUE=WING IMAGINAL DISK; RX MEDLINE; 93272852. RA SANTAREN J.F., VAN DAMME J., PUYPE M., VANDEKERCKHOVE J., RA GARCIA-BELLIDO A.; RT "Identification of Drosophila wing imaginal disc proteins by two- RT dimensional gel analysis and microsequencing."; 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 -!- ENZYME REGULATION: BINDS CYCLOSPORIN A (CSA). CSA MEDIATES SOME CC OF ITS EFFECTS VIA AN INHIBITORY ACTION ON PPIASE. CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC. CC -!- SIMILARITY: BELONGS TO THE CYCLOPHILIN-TYPE PPIASE FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- 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 FLYBASE; FBgn0004432; Cyp1. DR PROSITE; PS00170; CSA_PPIASE_1; 1. DR PROSITE; PS50072; CSA_PPIASE_2; 1. DR PFAM; PF00160; pro_isomerase; 1. DR HSSP; P05092; 3CYS. 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 //