ID RAS3_DROME Reviewed; 184 AA. AC P08645; Q2XYB6; Q540V3; Q9V3N0; DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot. DT 01-AUG-1992, sequence version 2. DT 16-SEP-2015, entry version 165. DE RecName: Full=Ras-like protein 3; DE AltName: Full=Protein roughened; DE Flags: Precursor; GN Name=R; Synonyms=RAP, Rap1, ras3, Ras62B; ORFNames=CG1956; OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; OC Pterygota; Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila; Sophophora. OX NCBI_TaxID=7227; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX 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 [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND DISRUPTION PHENOTYPE. RX PubMed=1934069; DOI=10.1016/0092-8674(91)90066-8; 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 [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=A1; RX PubMed=10552039; DOI=10.1007/PL00006579; RA Gasperini R., Gibson G.; RT "Absence of protein polymorphism in the Ras genes of Drosophila RT melanogaster."; RL J. Mol. Evol. 49:583-590(1999). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley; RX PubMed=10731132; DOI=10.1126/science.287.5461.2185; 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.A., 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.L., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., 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.J., 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.C., Zhu X., RA Smith H.O., 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). RN [5] RP GENOME REANNOTATION. RC STRAIN=Berkeley; RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=Berkeley; TISSUE=Embryo; RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). RN [7] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 8-178. RC STRAIN=Ral1; RX PubMed=16120803; DOI=10.1093/molbev/msi246; RA Comeron J.M., Guthrie T.B.; RT "Intragenic Hill-Robertson interference influences selection intensity RT on synonymous mutations in Drosophila."; RL Mol. Biol. Evol. 22:2519-2530(2005). CC -!- FUNCTION: Ras proteins bind GDP/GTP and possess intrinsic GTPase CC activity. Plays a role in photoreceptor cell determination. CC {ECO:0000269|PubMed:1934069}. CC -!- ENZYME REGULATION: Alternates between an inactive form bound to CC GDP 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 -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor CC {ECO:0000305}; Cytoplasmic side {ECO:0000305}. CC -!- DISRUPTION PHENOTYPE: Flies exhibit disruption of the early stages CC of photoreceptor cell determination, adult eyes lack the R7 cell. CC {ECO:0000269|PubMed:1934069}. CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Ras family. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=CAA26131.1; Type=Frameshift; Positions=76, 96, 160, 180; Evidence={ECO:0000305}; 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; X02200; CAA26131.1; ALT_FRAME; Genomic_DNA. DR EMBL; M80535; AAA28845.1; -; Genomic_DNA. DR EMBL; AF186654; AAF15520.1; -; Genomic_DNA. DR EMBL; AE014296; AAF47583.1; -; Genomic_DNA. DR EMBL; AY121688; AAM52015.1; -; mRNA. DR EMBL; DQ138746; ABA86352.1; -; Genomic_DNA. DR PIR; A41217; A41217. DR PIR; S07187; TVFFR3. DR RefSeq; NP_001189023.1; NM_001202094.2. DR RefSeq; NP_001261295.1; NM_001274366.1. DR RefSeq; NP_476857.1; NM_057509.5. DR UniGene; Dm.822; -. DR ProteinModelPortal; P08645; -. DR SMR; P08645; 1-165. DR BioGrid; 63773; 34. DR IntAct; P08645; 1. DR STRING; 7227.FBpp0072746; -. DR PaxDb; P08645; -. DR PRIDE; P08645; -. DR EnsemblMetazoa; FBtr0072867; FBpp0072746; FBgn0004636. DR EnsemblMetazoa; FBtr0303154; FBpp0292253; FBgn0004636. DR EnsemblMetazoa; FBtr0332671; FBpp0304917; FBgn0004636. DR GeneID; 38244; -. DR KEGG; dme:Dmel_CG1956; -. DR FlyBase; FBgn0004636; R. DR eggNOG; COG1100; -. DR GeneTree; ENSGT00780000121857; -. DR InParanoid; P08645; -. DR KO; K04353; -. DR OMA; TMREYKL; -. DR OrthoDB; EOG7QVM41; -. DR PhylomeDB; P08645; -. DR Reactome; R-DME-170968; Frs2-mediated activation. DR Reactome; R-DME-354192; Integrin alphaIIb beta3 signaling. DR Reactome; R-DME-354194; GRB2:SOS provides linkage to MAPK signaling for Integrins. DR Reactome; R-DME-372708; p130Cas linkage to MAPK signaling for integrins. DR Reactome; R-DME-381676; Glucagon-like Peptide-1 (GLP1) regulates insulin secretion. DR Reactome; R-DME-392517; Rap1 signalling. DR ChiTaRS; R; fly. DR GenomeRNAi; 38244; -. DR NextBio; 807703; -. DR PRO; PR:P08645; -. DR Proteomes; UP000000803; Chromosome 3L. DR Bgee; P08645; -. DR ExpressionAtlas; P08645; differential. DR Genevisible; P08645; DM. DR GO; GO:0031252; C:cell leading edge; IDA:FlyBase. DR GO; GO:0005811; C:lipid particle; IDA:FlyBase. DR GO; GO:0005886; C:plasma membrane; IDA:FlyBase. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW. DR GO; GO:0003924; F:GTPase activity; IDA:FlyBase. DR GO; GO:0034333; P:adherens junction assembly; IGI:FlyBase. DR GO; GO:0007155; P:cell adhesion; IMP:FlyBase. DR GO; GO:0007391; P:dorsal closure; IMP:FlyBase. DR GO; GO:0042067; P:establishment of ommatidial planar polarity; IMP:FlyBase. DR GO; GO:0030718; P:germ-line stem cell maintenance; IGI:FlyBase. DR GO; GO:0035099; P:hemocyte migration; IMP:FlyBase. DR GO; GO:0030713; P:ovarian follicle cell stalk formation; TAS:FlyBase. DR GO; GO:0022409; P:positive regulation of cell-cell adhesion; IMP:FlyBase. DR GO; GO:0032486; P:Rap protein signal transduction; IDA:FlyBase. DR GO; GO:0008360; P:regulation of cell shape; IMP:FlyBase. DR GO; GO:0016476; P:regulation of embryonic cell shape; IMP:FlyBase. DR GO; GO:0006930; P:substrate-dependent cell migration, cell extension; IMP:FlyBase. DR GO; GO:0007601; P:visual perception; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR InterPro; IPR001806; Small_GTPase. DR InterPro; IPR020849; Small_GTPase_Ras. DR PANTHER; PTHR24070; PTHR24070; 1. DR Pfam; PF00071; Ras; 1. DR SMART; SM00173; RAS; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51421; RAS; 1. PE 2: Evidence at transcript level; KW Cell membrane; Complete proteome; GTP-binding; Lipoprotein; Membrane; KW Methylation; Nucleotide-binding; Prenylation; Reference proteome; KW Sensory transduction; Vision. FT CHAIN 1 181 Ras-like protein 3. FT /FTId=PRO_0000030191. FT PROPEP 182 184 Removed in mature form. {ECO:0000250}. FT /FTId=PRO_0000030192. FT NP_BIND 10 17 GTP. {ECO:0000250}. FT NP_BIND 57 61 GTP. {ECO:0000250}. FT NP_BIND 116 119 GTP. {ECO:0000250}. FT MOTIF 32 40 Effector region. FT MOD_RES 181 181 Cysteine methyl ester. {ECO:0000250}. FT LIPID 181 181 S-geranylgeranyl cysteine. {ECO:0000250}. FT VARIANT 157 157 F -> L (in roughened mutants). FT CONFLICT 45 49 EVDGQ -> KVNER (in Ref. 1; CAA26131). FT {ECO:0000305}. FT CONFLICT 56 57 LD -> VN (in Ref. 1; CAA26131). FT {ECO:0000305}. FT CONFLICT 69 69 D -> N (in Ref. 1; CAA26131). FT {ECO:0000305}. 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 //