RAS_CARAU
ID RAS_CARAU Reviewed; 183 AA.
AC P05774; Q90W85;
DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1988, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Ras-like protein;
DE EC=3.6.5.2 {ECO:0000250|UniProtKB:P01112};
DE Flags: Fragment;
OS Carassius auratus (Goldfish).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Cyprinidae; Cyprininae; Carassius.
OX NCBI_TaxID=7957;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Wakin; TISSUE=Liver;
RX PubMed=3023161; DOI=10.1111/j.1432-0436.1986.tb00551.x;
RA Nemoto N., Kodama K., Tazawa A., Masahito P., Ishikawa T.;
RT "Extensive sequence homology of the goldfish ras gene to mammalian ras
RT genes.";
RL Differentiation 32:17-23(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Liver;
RX PubMed=3029139; DOI=10.1007/bf00389967;
RA Nemoto N., Kodama K., Tazawa A., Matsumoto J., Masahito P., Ishikawa T.;
RT "Nucleotide sequence comparison of the predicted first exonic region of
RT goldfish ras gene between normal and neoplastic tissues.";
RL J. Cancer Res. Clin. Oncol. 113:56-60(1987).
CC -!- FUNCTION: Ras proteins bind GDP/GTP and possess intrinsic GTPase
CC activity.
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:0000305}; Lipid-anchor
CC {ECO:0000305}; Cytoplasmic side {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Ras family.
CC {ECO:0000305}.
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DR EMBL; AH002484; AAA49189.1; -; Genomic_DNA.
DR EMBL; X12878; CAA31371.1; -; Genomic_DNA.
DR EMBL; M38485; AAA49188.1; -; Genomic_DNA.
DR EMBL; M38486; AAA62759.1; -; Genomic_DNA.
DR PIR; S05483; S05483.
DR PIR; S06217; S06217.
DR AlphaFoldDB; P05774; -.
DR BMRB; P05774; -.
DR SMR; P05774; -.
DR Proteomes; UP000515129; Genome assembly.
DR GO; GO:0005737; C:cytoplasm; ISS:AgBase.
DR GO; GO:0005886; C:plasma membrane; ISS:AgBase.
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;
KW Nucleotide-binding; Prenylation; Reference proteome.
FT CHAIN 1..>183
FT /note="Ras-like protein"
FT /id="PRO_0000082658"
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 NON_TER 183
SQ SEQUENCE 183 AA; 21043 MW; BDF1A556C36CDB8F CRC64;
MTEYKLVVVG AGGVGKSALT IQLIQNHFVD EYDPTIEDSY RKQVVIDGET CLLDILDTAG
QEEYSAMRDQ YMRTGEGFLC VFAINNTKSF EDIHHYREQI KRVKDSEDVP MVLVGNKCDL
PSRSVDTKQA QDLARSYGIP FIETSAKTRQ RVEDAFYTLV REIRQYRLRK LSKEEETTQC
IKL