ID RAS3_DROME STANDARD; PRT; 184 AA. AC P08645; DT 13-AUG-1987 (Rel. 05, Created) DT 01-AUG-1992 (Rel. 23, Last sequence update) DT 15-JUL-1999 (Rel. 38, Last annotation update) DE RAS-LIKE PROTEIN 3 (ROUGHENED PROTEIN). GN R OR RAS3 OR RAS62B OR RAP OR RAP1. 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; 92034992. RA HARIHARAN I.K., CARTHEW R.W., RUBIN G.M.; RT "The Drosophila roughened mutation: activation of a rap homolog RT disrupts eye development and interferes with cell determination."; RL Cell 67:717-722(1991). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE; 85257468. RA SCHEJTER E.D., SHILO B.-Z.; RT "Characterization of functional domains of p21 ras by use of chimeric RT genes."; RL EMBO J. 4:407-412(1985). CC -!- FUNCTION: RAS PROTEINS BIND GDP/GTP AND POSSESS INTRINSIC GTPASE CC ACTIVITY. THE ROUGHENED MUTATION DISRUPTS THE EARLY STAGES OF CC PHOTORECEPTOR CELL DETERMINATION. CC -!- ENZYME REGULATION: ALTERNATE BETWEEN AN INACTIVE FORM BOUND TO GDP CC AND AN ACTIVE FORM BOUND TO GTP. ACTIVATED BY A GUANINE CC NUCLEOTIDE-EXCHANGE FACTOR (GEF) AND INACTIVATED BY A GTPASE- CC ACTIVATING PROTEIN (GAP). CC -!- SIMILARITY: TO RAS PROTEINS. BELONGS TO THE RAP SUB-FAMILY. CC -!- CAUTION: REF.2 SEQUENCE DIFFERS FROM THAT SHOWN IN POSITIONS 76 CC TO 96 AND 160 TO 180 DUE TO FRAMESHIFTS. 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; M80535; AAA28845.1; -. DR EMBL; X02200; CAA26131.1; ALT_FRAME. DR PIR; S07187; TVFFR3. DR PIR; A41217; A41217. DR HSSP; P01112; 1PLL. DR FLYBASE; FBgn0004636; R. DR PFAM; PF00071; ras; 1. KW GTP-binding; Prenylation; Lipoprotein; Vision. FT CHAIN 1 181 RAS-LIKE PROTEIN 3. FT PROPEP 182 184 REMOVED IN MATURE FORM (BY SIMILARITY). FT NP_BIND 10 17 GTP (BY SIMILARITY). FT NP_BIND 57 61 GTP (BY SIMILARITY). FT NP_BIND 116 119 GTP (BY SIMILARITY). FT DOMAIN 32 40 EFFECTOR REGION (BY SIMILARITY). FT LIPID 181 181 GERANYL-GERANYL (BY SIMILARITY). FT VARIANT 157 157 F -> L (IN ROUGHENED MUTANTS). FT CONFLICT 45 49 EVDGQ -> KVNER (IN REF. 2). FT CONFLICT 56 57 LD -> VN (IN REF. 2). FT CONFLICT 69 69 D -> N (IN REF. 2). SQ SEQUENCE 184 AA; 20863 MW; 0522CE83 CRC32; MREYKIVVLG SGGVGKSALT VQFVQCIFVE KYDPTIEDSY RKQVEVDGQQ CMLEILDTAG TEQFTAMRDL YMKNGQGFVL VYSITAQSTF NDLQDLREQI LRVKDTDDVP MVLVGNKCDL EEERVVGKEL GKNLATQFNC AFMETSAKAK VNVNDIFYDL VRQINKKSPE KKQKKPKKSL CVLL //