RAS1_DROME
ID RAS1_DROME Reviewed; 189 AA.
AC P08646; Q9V448;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 2.
DT 03-AUG-2022, entry version 211.
DE RecName: Full=Ras-like protein 1;
DE Short=Dras1;
DE EC=3.6.5.2 {ECO:0000250|UniProtKB:P01112};
DE AltName: Full=Dmras85D;
DE Flags: Precursor;
GN Name=Ras85D; Synonyms=Ras1; ORFNames=CG9375;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3110012; DOI=10.1016/0378-1119(87)90301-5;
RA Brock H.W.;
RT "Sequence and genomic structure of ras homologues Dmras85D and Dmras64B of
RT Drosophila melanogaster.";
RL Gene 51:129-137(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=6430564; DOI=10.1016/0092-8674(84)90437-9;
RA Neuman-Silberberg F.S., Schejter E., Hoffmann F.M., Shilo B.-Z.;
RT "The Drosophila ras oncogenes: structure and nucleotide sequence.";
RL Cell 37:1027-1033(1984).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=W13;
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., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., 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., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., 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., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA 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., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT 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., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA 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 1-46, AND TISSUE SPECIFICITY.
RC STRAIN=Canton-S;
RX PubMed=7873789; DOI=10.1002/aja.1002010208;
RA Ezer S.T., Sahar D., Salzberg A., Lev Z.;
RT "Differential expression during embryogenesis of three genes clustered in
RT the Ras1 region of Drosophila melanogaster.";
RL Dev. Dyn. 201:179-190(1994).
RN [8]
RP FUNCTION, AND MUTAGENESIS OF GLY-12; ASP-38 AND TYR-40.
RX PubMed=11290305; DOI=10.1242/dev.128.9.1687;
RA Halfar K., Rommel C., Stocker H., Hafen E.;
RT "Ras controls growth, survival and differentiation in the Drosophila eye by
RT different thresholds of MAP kinase activity.";
RL Development 128:1687-1696(2001).
RN [9]
RP SUBCELLULAR LOCATION, AND ISOPRENYLATION AT CYS-186.
RX PubMed=18503409; DOI=10.1042/bj20080560;
RA Day J.P., Cleghon V., Houslay M.D., Davies S.-A.;
RT "Regulation of a Drosophila melanogaster cGMP-specific phosphodiesterase by
RT prenylation and interaction with a prenyl-binding protein.";
RL Biochem. J. 414:363-374(2008).
RN [10]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=19965758; DOI=10.1126/science.1176450;
RA Rewitz K.F., Yamanaka N., Gilbert L.I., O'Connor M.B.;
RT "The insect neuropeptide PTTH activates receptor tyrosine kinase torso to
RT initiate metamorphosis.";
RL Science 326:1403-1405(2009).
CC -!- FUNCTION: Ras proteins bind GDP/GTP and possess intrinsic GTPase
CC activity (By similarity). Plays a role in eye development by regulating
CC cell growth, survival of postmitotic ommatidial cells and
CC differentiation of photoreceptor cells (PubMed:11290305). During larval
CC development, mediates Ptth/tor signaling leading to the production of
CC ecdysone, a hormone required for the initiation of metamorphosis
CC (PubMed:19965758). {ECO:0000250|UniProtKB:P01112,
CC ECO:0000269|PubMed:11290305, ECO:0000269|PubMed:19965758}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; EC=3.6.5.2;
CC Evidence={ECO:0000250|UniProtKB:P01112};
CC -!- ACTIVITY REGULATION: Alternates between an inactive form bound to GDP
CC and an active form bound to GTP. Activated by a guanine nucleotide-
CC exchange factor (GEF) and inactivated by a GTPase-activating protein
CC (GAP).
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:18503409};
CC Lipid-anchor {ECO:0000269|PubMed:18503409}; Cytoplasmic side
CC {ECO:0000269|PubMed:18503409}. Note=Loss of prenylation causes protein
CC location to the cytoplasm.
CC -!- TISSUE SPECIFICITY: Expressed in the posterior termini of the embryo,
CC restricted mainly to the embryonic central nervous system, and in the
CC eye imaginal disk. {ECO:0000269|PubMed:7873789}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown in the prothoracic gland
CC (PG) delays the onset of pupariation by prolonging the L3 larval stage.
CC {ECO:0000269|PubMed:19965758}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Ras family.
CC {ECO:0000305}.
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DR EMBL; M16429; AAA28847.1; -; Genomic_DNA.
DR EMBL; M16123; AAA28847.1; JOINED; Genomic_DNA.
DR EMBL; M16428; AAA28847.1; JOINED; Genomic_DNA.
DR EMBL; K01960; AAA28846.1; -; mRNA.
DR EMBL; AF186648; AAF15514.1; -; Genomic_DNA.
DR EMBL; AE014297; AAF54388.1; -; Genomic_DNA.
DR EMBL; AY089541; AAL90279.1; -; mRNA.
DR EMBL; AY094888; AAM11241.1; -; mRNA.
DR EMBL; X73219; CAA51689.1; -; Genomic_DNA.
DR PIR; A29048; TVFF85.
DR PIR; S35097; S35097.
DR RefSeq; NP_476699.1; NM_057351.5.
DR AlphaFoldDB; P08646; -.
DR SMR; P08646; -.
DR BioGRID; 66301; 251.
DR DIP; DIP-23541N; -.
DR STRING; 7227.FBpp0081600; -.
DR PaxDb; P08646; -.
DR PRIDE; P08646; -.
DR EnsemblMetazoa; FBtr0082122; FBpp0081600; FBgn0003205.
DR GeneID; 41140; -.
DR KEGG; dme:Dmel_CG9375; -.
DR CTD; 41140; -.
DR FlyBase; FBgn0003205; Ras85D.
DR VEuPathDB; VectorBase:FBgn0003205; -.
DR eggNOG; KOG0395; Eukaryota.
DR GeneTree; ENSGT00940000155653; -.
DR HOGENOM; CLU_041217_9_8_1; -.
DR InParanoid; P08646; -.
DR OMA; SSRRFKC; -.
DR OrthoDB; 1259506at2759; -.
DR PhylomeDB; P08646; -.
DR Reactome; R-DME-1250347; SHC1 events in ERBB4 signaling.
DR Reactome; R-DME-171007; p38MAPK events.
DR Reactome; R-DME-179812; GRB2 events in EGFR signaling.
DR Reactome; R-DME-180336; SHC1 events in EGFR signaling.
DR Reactome; R-DME-186763; Downstream signal transduction.
DR Reactome; R-DME-1963640; GRB2 events in ERBB2 signaling.
DR Reactome; R-DME-210993; Tie2 Signaling.
DR Reactome; R-DME-2179392; EGFR Transactivation by Gastrin.
DR Reactome; R-DME-2424491; DAP12 signaling.
DR Reactome; R-DME-2871796; FCERI mediated MAPK activation.
DR Reactome; R-DME-375165; NCAM signaling for neurite out-growth.
DR Reactome; R-DME-3928662; EPHB-mediated forward signaling.
DR Reactome; R-DME-4086398; Ca2+ pathway.
DR Reactome; R-DME-432553; Phosphorylation of PER and TIM.
DR Reactome; R-DME-5218921; VEGFR2 mediated cell proliferation.
DR Reactome; R-DME-5621575; CD209 (DC-SIGN) signaling.
DR Reactome; R-DME-5654688; SHC-mediated cascade:FGFR1.
DR Reactome; R-DME-5654693; FRS-mediated FGFR1 signaling.
DR Reactome; R-DME-5654699; SHC-mediated cascade:FGFR2.
DR Reactome; R-DME-5654700; FRS-mediated FGFR2 signaling.
DR Reactome; R-DME-5654704; SHC-mediated cascade:FGFR3.
DR Reactome; R-DME-5654706; FRS-mediated FGFR3 signaling.
DR Reactome; R-DME-5654712; FRS-mediated FGFR4 signaling.
DR Reactome; R-DME-5654719; SHC-mediated cascade:FGFR4.
DR Reactome; R-DME-5673000; RAF activation.
DR Reactome; R-DME-5673001; RAF/MAP kinase cascade.
DR Reactome; R-DME-5674135; MAP2K and MAPK activation.
DR Reactome; R-DME-5675221; Negative regulation of MAPK pathway.
DR Reactome; R-DME-6798695; Neutrophil degranulation.
DR Reactome; R-DME-8849471; PTK6 Regulates RHO GTPases, RAS GTPase and MAP kinases.
DR Reactome; R-DME-8951936; RUNX3 regulates p14-ARF.
DR Reactome; R-DME-9607240; FLT3 Signaling.
DR Reactome; R-DME-9634635; Estrogen-stimulated signaling through PRKCZ.
DR Reactome; R-DME-9648002; RAS processing.
DR SignaLink; P08646; -.
DR BioGRID-ORCS; 41140; 1 hit in 3 CRISPR screens.
DR ChiTaRS; Ras85D; fly.
DR GenomeRNAi; 41140; -.
DR PRO; PR:P08646; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0003205; Expressed in embryonic/larval hemocyte (Drosophila) and 25 other tissues.
DR Genevisible; P08646; DM.
DR GO; GO:0016020; C:membrane; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:FlyBase.
DR GO; GO:0003925; F:G protein activity; IDA:FlyBase.
DR GO; GO:0019003; F:GDP binding; IBA:GO_Central.
DR GO; GO:0005525; F:GTP binding; IBA:GO_Central.
DR GO; GO:0003924; F:GTPase activity; IDA:FlyBase.
DR GO; GO:0007298; P:border follicle cell migration; IMP:FlyBase.
DR GO; GO:0001709; P:cell fate determination; IMP:FlyBase.
DR GO; GO:0009267; P:cellular response to starvation; IMP:FlyBase.
DR GO; GO:0030381; P:chorion-containing eggshell pattern formation; IMP:FlyBase.
DR GO; GO:0048749; P:compound eye development; IMP:FlyBase.
DR GO; GO:0051607; P:defense response to virus; IMP:FlyBase.
DR GO; GO:0008340; P:determination of adult lifespan; IMP:FlyBase.
DR GO; GO:0007391; P:dorsal closure; IMP:UniProtKB.
DR GO; GO:0007395; P:dorsal closure, spreading of leading edge cells; IMP:UniProtKB.
DR GO; GO:0007173; P:epidermal growth factor receptor signaling pathway; IMP:FlyBase.
DR GO; GO:0007427; P:epithelial cell migration, open tracheal system; IMP:FlyBase.
DR GO; GO:0035088; P:establishment or maintenance of apical/basal cell polarity; IMP:FlyBase.
DR GO; GO:0007455; P:eye-antennal disc morphogenesis; IMP:FlyBase.
DR GO; GO:0008543; P:fibroblast growth factor receptor signaling pathway; IDA:FlyBase.
DR GO; GO:0007369; P:gastrulation; IMP:FlyBase.
DR GO; GO:0035099; P:hemocyte migration; IMP:FlyBase.
DR GO; GO:0007476; P:imaginal disc-derived wing morphogenesis; IMP:FlyBase.
DR GO; GO:0008586; P:imaginal disc-derived wing vein morphogenesis; IMP:FlyBase.
DR GO; GO:0007474; P:imaginal disc-derived wing vein specification; IMP:FlyBase.
DR GO; GO:0002168; P:instar larval development; IMP:FlyBase.
DR GO; GO:0036335; P:intestinal stem cell homeostasis; IMP:FlyBase.
DR GO; GO:0007479; P:leg disc proximal/distal pattern formation; IEP:FlyBase.
DR GO; GO:0035170; P:lymph gland crystal cell differentiation; IMP:FlyBase.
DR GO; GO:0035169; P:lymph gland plasmatocyte differentiation; IMP:FlyBase.
DR GO; GO:0072002; P:Malpighian tubule development; IMP:FlyBase.
DR GO; GO:0000165; P:MAPK cascade; IMP:UniProtKB.
DR GO; GO:0001710; P:mesodermal cell fate commitment; IMP:FlyBase.
DR GO; GO:0007552; P:metamorphosis; IMP:FlyBase.
DR GO; GO:0048626; P:myoblast fate specification; IGI:FlyBase.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:FlyBase.
DR GO; GO:2001234; P:negative regulation of apoptotic signaling pathway; IGI:FlyBase.
DR GO; GO:0010507; P:negative regulation of autophagy; IMP:FlyBase.
DR GO; GO:0046673; P:negative regulation of compound eye retinal cell programmed cell death; IMP:FlyBase.
DR GO; GO:0010629; P:negative regulation of gene expression; IMP:UniProtKB.
DR GO; GO:0016242; P:negative regulation of macroautophagy; IMP:FlyBase.
DR GO; GO:0016318; P:ommatidial rotation; IMP:FlyBase.
DR GO; GO:0007309; P:oocyte axis specification; IMP:FlyBase.
DR GO; GO:0007422; P:peripheral nervous system development; IMP:FlyBase.
DR GO; GO:0042461; P:photoreceptor cell development; IGI:UniProtKB.
DR GO; GO:0046530; P:photoreceptor cell differentiation; IMP:FlyBase.
DR GO; GO:0043703; P:photoreceptor cell fate determination; IGI:FlyBase.
DR GO; GO:0008594; P:photoreceptor cell morphogenesis; IMP:FlyBase.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IMP:FlyBase.
DR GO; GO:0045793; P:positive regulation of cell size; IMP:FlyBase.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IDA:FlyBase.
DR GO; GO:0035208; P:positive regulation of hemocyte proliferation; IMP:FlyBase.
DR GO; GO:0046534; P:positive regulation of photoreceptor cell differentiation; IMP:FlyBase.
DR GO; GO:0071902; P:positive regulation of protein serine/threonine kinase activity; IEA:GOC.
DR GO; GO:1904263; P:positive regulation of TORC1 signaling; IMP:FlyBase.
DR GO; GO:0007465; P:R7 cell fate commitment; IMP:FlyBase.
DR GO; GO:0007265; P:Ras protein signal transduction; IMP:FlyBase.
DR GO; GO:0042981; P:regulation of apoptotic process; IMP:FlyBase.
DR GO; GO:0008361; P:regulation of cell size; IMP:FlyBase.
DR GO; GO:0040008; P:regulation of growth; IMP:FlyBase.
DR GO; GO:0040014; P:regulation of multicellular organism growth; IMP:FlyBase.
DR GO; GO:0045500; P:sevenless signaling pathway; IMP:FlyBase.
DR GO; GO:0048863; P:stem cell differentiation; IMP:FlyBase.
DR GO; GO:0048865; P:stem cell fate commitment; IMP:FlyBase.
DR GO; GO:0072089; P:stem cell proliferation; IMP:FlyBase.
DR GO; GO:0007430; P:terminal branching, open tracheal system; IMP:FlyBase.
DR GO; GO:0007362; P:terminal region determination; IGI:FlyBase.
DR GO; GO:0008293; P:torso signaling pathway; IMP:FlyBase.
DR GO; GO:0060438; P:trachea development; IMP:FlyBase.
DR GO; GO:0007426; P:tracheal outgrowth, open tracheal system; IMP:FlyBase.
DR GO; GO:0048010; P:vascular endothelial growth factor receptor signaling pathway; IMP:FlyBase.
DR GO; GO:0007472; P:wing disc morphogenesis; IMP:FlyBase.
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-type.
DR PANTHER; PTHR24070; PTHR24070; 1.
DR Pfam; PF00071; Ras; 1.
DR SMART; SM00174; RHO; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS51421; RAS; 1.
PE 1: Evidence at protein level;
KW Cell membrane; GTP-binding; Hydrolase; Lipoprotein; Membrane; Methylation;
KW Nucleotide-binding; Prenylation; Reference proteome.
FT CHAIN 1..186
FT /note="Ras-like protein 1"
FT /id="PRO_0000082665"
FT PROPEP 187..189
FT /note="Removed in mature form"
FT /evidence="ECO:0000305"
FT /id="PRO_0000281313"
FT MOTIF 32..40
FT /note="Effector region"
FT BINDING 10..17
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 57..61
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 116..119
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT MOD_RES 186
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000305"
FT LIPID 186
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000305|PubMed:18503409"
FT MUTAGEN 12
FT /note="G->V: Rough eyes characterized by the presence of
FT additional R7 photoreceptor cells. Normal survival of
FT postmitotic ommatidial cells but differentiation into
FT photoreceptor cells is limited to R8 cells. Less severe
FT Rough eye phenotype; when associated with E-38. Normal
FT eyes; when associated with C-40."
FT /evidence="ECO:0000269|PubMed:11290305"
FT MUTAGEN 38
FT /note="D->E: Mild rough eye phenotype; when associated with
FT V-12."
FT /evidence="ECO:0000269|PubMed:11290305"
FT MUTAGEN 40
FT /note="Y->C: Impaired cell growth, survival of postmitotic
FT ommatidial cells and differentiation into R8
FT photoreceptors. Normal eye morphology; when associated with
FT V-12."
FT /evidence="ECO:0000269|PubMed:11290305"
FT CONFLICT 11
FT /note="A -> P (in Ref. 2; AAA28846)"
FT /evidence="ECO:0000305"
FT CONFLICT 44..45
FT /note="VV -> RF (in Ref. 2; AAA28846)"
FT /evidence="ECO:0000305"
FT CONFLICT 84
FT /note="V -> I (in Ref. 2; AAA28846)"
FT /evidence="ECO:0000305"
FT CONFLICT 102
FT /note="R -> H (in Ref. 2; AAA28846)"
FT /evidence="ECO:0000305"
FT CONFLICT 114
FT /note="V -> A (in Ref. 2; AAA28846)"
FT /evidence="ECO:0000305"
FT CONFLICT 182
FT /note="R -> C (in Ref. 2; AAA28846)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 189 AA; 21594 MW; 14236DCD65EACCD2 CRC64;
MTEYKLVVVG AGGVGKSALT IQLIQNHFVD EYDPTIEDSY RKQVVIDGET CLLDILDTAG
QEEYSAMRDQ YMRTGEGFLL VFAVNSAKSF EDIGTYREQI KRVKDAEEVP MVLVGNKCDL
ASWNVNNEQA REVAKQYGIP YIETSAKTRM GVDDAFYTLV REIRKDKDNK GRRGRKMNKP
NRRFKCKML
