ID   RAS1_DROGR              Reviewed;         189 AA.
AC   B4JFU8;
DT   10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   03-AUG-2022, entry version 81.
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}; ORFNames=GH19394;
OS   Drosophila grimshawi (Hawaiian fruit fly) (Idiomyia grimshawi).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Hawaiian Drosophila.
OX   NCBI_TaxID=7222;
RN   [1] {ECO:0000312|EMBL:EDV93579.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tucson 15287-2541.00 {ECO:0000312|EMBL:EDV93579.1};
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; CH916369; EDV93579.1; -; Genomic_DNA.
DR   RefSeq; XP_001990517.1; XM_001990481.1.
DR   AlphaFoldDB; B4JFU8; -.
DR   SMR; B4JFU8; -.
DR   STRING; 7222.FBpp0153300; -.
DR   EnsemblMetazoa; FBtr0154808; FBpp0153300; FBgn0126859.
DR   EnsemblMetazoa; FBtr0452533; FBpp0403220; FBgn0126859.
DR   EnsemblMetazoa; FBtr0455586; FBpp0406167; FBgn0126859.
DR   EnsemblMetazoa; FBtr0467392; FBpp0417556; FBgn0126859.
DR   GeneID; 6563010; -.
DR   KEGG; dgr:6563010; -.
DR   eggNOG; KOG0395; Eukaryota.
DR   HOGENOM; CLU_041217_9_8_1; -.
DR   InParanoid; B4JFU8; -.
DR   OMA; SSRRFKC; -.
DR   OrthoDB; 1259506at2759; -.
DR   PhylomeDB; B4JFU8; -.
DR   ChiTaRS; Ras85D; fly.
DR   Proteomes; UP000001070; 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   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   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_0000363710"
FT   PROPEP          187..189
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000250|UniProtKB:P08646"
FT                   /id="PRO_0000363711"
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;  21576 MW;  F4118F4FF07D7CD7 CRC64;
     MTEYKLVVVG AGGVGKSALT IQLIQNHFVD EYDPTIEDSY RKQVVIDGET CLLDILDTAG
     QEEYSAMRDQ YMRTGEGFLL VFAVNSAKSF EDIGTYREQI KRVKDAEEVP MVLVGNKCDL
     PSWNVQNEQA REVAKQYGIP YIETSAKTRM GVDDAFYTLV REIRKDKDNK GRKGRKTNKP
     NRRFKCKML