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; Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; 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; AAB03701.1; -. DR HSSP; P05092; 3CYS. DR FLYBASE; FBgn0004432; Cyp1. DR INTERPRO; IPR002130; -. 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; Isomerase; Rotamase; Multigene family. SQ SEQUENCE 165 AA; 17907 MW; FEB85148CA2EE7ED CRC64; MSTLPRVFFD MTADNEPLGR IVMELRSDVV PKTAENFRAL CTGEKGFGYK GSIFHRVIPN FMCQGGDFTN HNGTGGKSIY GNKFPDENFE LKHTGSGILS MANAGANTNG SQFFICTVKT AWLDNKHVVF GEVVEGLDVV KKIESYGSQS GKTSKKIIVA NSGSL //