ID RAS3_DROME STANDARD; PRT; 184 AA. AC P08645; Q9V3N0; DT 13-AUG-1987 (Rel. 05, Created) DT 01-AUG-1992 (Rel. 23, Last sequence update) DT 20-AUG-2001 (Rel. 40, Last annotation update) DE Ras-like protein 3 (Roughened protein). GN R OR RAS3 OR RAS62B OR RAP OR RAP1 OR CG1956. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Tracheata; Hexapoda; Insecta; OC Pterygota; Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=92034992; PubMed=1934069; 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; PubMed=3926484; 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). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=A1; RX MEDLINE=20020328; PubMed=10552039; RA Gasperini R., Gibson G.; RT "Absence of protein polymorphism in the Ras genes of Drosophila."; RL J. Mol. Evol. 49:583-590(1999). RN [4] RP SEQUENCE FROM N.A. RC STRAIN=BERKELEY; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). 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 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 EMBL; AF186654; AAF15520.1; -. DR EMBL; AE003473; AAF47583.1; -. DR PIR; S07187; TVFFR3. DR PIR; A41217; A41217. DR HSSP; P01112; 1PLL. DR FlyBase; FBgn0004636; R. DR InterPro; IPR003577; Ras. DR InterPro; IPR001806; Ras_trnsfrmng. DR Pfam; PF00071; ras; 1. DR PRINTS; PR00449; RASTRNSFRMNG. DR SMART; SM00173; 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; 9A55889B61FEDE13 CRC64; MREYKIVVLG SGGVGKSALT VQFVQCIFVE KYDPTIEDSY RKQVEVDGQQ CMLEILDTAG TEQFTAMRDL YMKNGQGFVL VYSITAQSTF NDLQDLREQI LRVKDTDDVP MVLVGNKCDL EEERVVGKEL GKNLATQFNC AFMETSAKAK VNVNDIFYDL VRQINKKSPE KKQKKPKKSL CVLL //