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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
 
 
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