ID   RAS1_DROMA              Reviewed;         189 AA.
AC   P83832;
DT   29-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2004, sequence version 1.
DT   03-AUG-2022, entry version 81.
DE   RecName: Full=Ras-like protein 1;
DE            EC=3.6.5.2 {ECO:0000250|UniProtKB:P01112};
DE   Flags: Precursor;
GN   Name=Ras85D; Synonyms=Ras1;
OS   Drosophila mauritiana (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7226 {ECO:0000312|EMBL:AAF15516.1};
RN   [1] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
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).
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}; Lipid-anchor
CC       {ECO:0000250}; Cytoplasmic side {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the small GTPase superfamily. Ras family.
CC       {ECO:0000305}.
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DR   EMBL; AF186650; AAF15516.1; -; Genomic_DNA.
DR   AlphaFoldDB; P83832; -.
DR   SMR; P83832; -.
DR   FlyBase; FBgn0029365; Dmau\Ras85D.
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.
FT   CHAIN           1..186
FT                   /note="Ras-like protein 1"
FT                   /id="PRO_0000082666"
FT   PROPEP          187..189
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000281314"
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:P08646"
FT   BINDING         57..61
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P08646"
FT   BINDING         116..119
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P08646"
FT   MOD_RES         186
FT                   /note="Cysteine methyl ester"
FT                   /evidence="ECO:0000250"
FT   LIPID           186
FT                   /note="S-geranylgeranyl cysteine"
FT                   /evidence="ECO:0000250|UniProtKB:P08646"
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