ID RAS1_DROVI Reviewed; 189 AA.
AC B4LY29;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 27-MAR-2024, entry version 89.
DE RecName: Full=Ras-like protein 1 {ECO:0000250|UniProtKB:P08646};
DE EC=3.6.5.2 {ECO:0000250|UniProtKB:P01112};
DE Flags: Precursor;
GN Name=Ras85D {ECO:0000250|UniProtKB:P08646}; Synonyms=Ras1;
GN ORFNames=GJ23844;
OS Drosophila virilis (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila.
OX NCBI_TaxID=7244;
RN [1] {ECO:0000312|EMBL:EDW66895.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tucson 15010-1051.87 {ECO:0000312|EMBL:EDW66895.1};
RX PubMed=17994087; DOI=10.1038/nature06341;
RG Drosophila 12 genomes consortium;
RT "Evolution of genes and genomes on the Drosophila phylogeny.";
RL Nature 450:203-218(2007).
CC -!- FUNCTION: Ras proteins bind GDP/GTP and possess intrinsic GTPase
CC activity. Plays a role in eye development by regulating cell growth,
CC survival of postmitotic ommatidial cells and differentiation of
CC photoreceptor cells. During larval development, mediates Ptth/tor
CC signaling leading to the production of ecdysone, a hormone required for
CC the initiation of metamorphosis. {ECO:0000250|UniProtKB:P01112,
CC ECO:0000250|UniProtKB:P08646}.
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:0000250|UniProtKB:P08646};
CC Lipid-anchor {ECO:0000250|UniProtKB:P08646}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:P08646}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Ras family.
CC {ECO:0000255}.
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DR EMBL; CH940650; EDW66895.1; -; Genomic_DNA.
DR RefSeq; XP_002053375.1; XM_002053339.2.
DR RefSeq; XP_015027424.1; XM_015171938.1.
DR AlphaFoldDB; B4LY29; -.
DR SMR; B4LY29; -.
DR STRING; 7244.B4LY29; -.
DR EnsemblMetazoa; FBtr0239769; FBpp0238261; FBgn0085906.
DR EnsemblMetazoa; FBtr0435777; FBpp0392722; FBgn0085906.
DR GeneID; 6629799; -.
DR KEGG; dvi:6629799; -.
DR eggNOG; KOG0395; Eukaryota.
DR HOGENOM; CLU_041217_9_8_1; -.
DR InParanoid; B4LY29; -.
DR OMA; CCGGCVI; -.
DR OrthoDB; 8685at2759; -.
DR PhylomeDB; B4LY29; -.
DR ChiTaRS; Ras85D; fly.
DR Proteomes; UP000008792; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0003925; F:G protein activity; IEA:UniProtKB-EC.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR CDD; cd04138; H_N_K_Ras_like; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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 NCBIfam; TIGR00231; small_GTP; 1.
DR PANTHER; PTHR24070; RAS, DI-RAS, AND RHEB FAMILY MEMBERS OF SMALL GTPASE SUPERFAMILY; 1.
DR PANTHER; PTHR24070:SF416; RAS-LIKE PROTEIN 1; 1.
DR Pfam; PF00071; Ras; 1.
DR PRINTS; PR00449; RASTRNSFRMNG.
DR SMART; SM00175; RAB; 1.
DR SMART; SM00176; RAN; 1.
DR SMART; SM00173; RAS; 1.
DR SMART; SM00174; RHO; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS51421; RAS; 1.
PE 3: Inferred from homology;
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 /evidence="ECO:0000250|UniProtKB:P08646"
FT /id="PRO_0000363718"
FT PROPEP 187..189
FT /note="Removed in mature form"
FT /evidence="ECO:0000250|UniProtKB:P08646"
FT /id="PRO_0000363719"
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|UniProtKB:P01112"
FT BINDING 57..61
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P01112"
FT BINDING 116..119
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P01112"
FT MOD_RES 186
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000250|UniProtKB:P08646"
FT LIPID 186
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:P08646"
SQ SEQUENCE 189 AA; 21550 MW; 14048F4FEAD7CCCD CRC64;
MTEYKLVVVG AGGVGKSALT IQLIQNHFVD EYDPTIEDSY RKQVVIDGET CLLDILDTAG
QEEYSAMRDQ YMRTGEGFLL VFAVNSAKSF EDIGTYREQI KRVKDAEEVP MVLVGNKCDL
ASWNVQNEQA REVAKQYGIP YIETSAKTRM GVDDAFYTLV REIRKDKDNK GRKGRKTNKP
NRRFKCKML
//
