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 01-FEB-1994 (REL. 28, 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; DIPTERA; BRACHYCERA; MUSCOMORPHA; EPHYDROIDEA; OC 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. CC -!- DISEASE: THE ROUGHENED MUTATION DISRUPTS THE EARLY STAGES OF CC PHOTORECEPTOR CELL DETERMINATION. 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; G158198; -. DR EMBL; X02200; G8408; ALT_FRAME. DR PIR; S07187; TVFFR3. DR PIR; A41217; A41217. DR FLYBASE; FBgn0004636; R. DR PFAM; PF00071; ras; 1. DR HSSP; P01112; 1PLL. 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 //