RAS1_DROMO
ID RAS1_DROMO Reviewed; 181 AA.
AC B4KB60;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 80.
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=GI22599;
OS Drosophila mojavensis (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila.
OX NCBI_TaxID=7230;
RN [1] {ECO:0000312|EMBL:EDW15764.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tucson 15081-1352.22 {ECO:0000312|EMBL:EDW15764.1};
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; CH933806; EDW15764.1; -; Genomic_DNA.
DR RefSeq; XP_002000303.2; XM_002000267.2.
DR AlphaFoldDB; B4KB60; -.
DR SMR; B4KB60; -.
DR STRING; 7230.FBpp0171816; -.
DR GeneID; 6574247; -.
DR KEGG; dmo:Dmoj_GI22599; -.
DR eggNOG; KOG0395; Eukaryota.
DR HOGENOM; CLU_041217_9_8_1; -.
DR InParanoid; B4KB60; -.
DR OMA; CCSGCVV; -.
DR PhylomeDB; B4KB60; -.
DR ChiTaRS; Ras85D; fly.
DR Proteomes; UP000009192; 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..178
FT /note="Ras-like protein 1"
FT /evidence="ECO:0000250|UniProtKB:P08646"
FT /id="PRO_0000363712"
FT PROPEP 179..181
FT /note="Removed in mature form"
FT /evidence="ECO:0000250|UniProtKB:P08646"
FT /id="PRO_0000363713"
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 178
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000250|UniProtKB:P08646"
FT LIPID 178
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:P08646"
SQ SEQUENCE 181 AA; 20621 MW; 74C7779E1DEECFA4 CRC64;
MTEYKLVVVG AGGVGKSALT IQLIQNHFVD EYDPTIEDSY RKQVVIDGET CLLDILDTAG
QEEYSAMRDQ YMRTGEGFLL VFAVNSAKSF EDIGTYREQI KRVKDAEEVP MVLVGNKCDL
PSWNVAKQYG IPYIETSAKT RMGVDDAFYT LVREIRKDKD NKGRKGRKTN KPNRRFKCKM
L
