ID RAS1_HYDVU Reviewed; 194 AA.
AC P51539;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1999, sequence version 2.
DT 13-SEP-2023, entry version 102.
DE RecName: Full=Ras-like protein RAS1;
DE EC=3.6.5.2 {ECO:0000250|UniProtKB:P01112};
DE Flags: Precursor;
GN Name=RAS1;
OS Hydra vulgaris (Hydra) (Hydra attenuata).
OC Eukaryota; Metazoa; Cnidaria; Hydrozoa; Hydroidolina; Anthoathecata;
OC Aplanulata; Hydridae; Hydra.
OX NCBI_TaxID=6087;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=105;
RA Guaderrama M., Bosch T.C.G., Salgado L.M.;
RL Submitted (DEC-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PRELIMINARY NUCLEOTIDE SEQUENCE OF 25-167.
RC STRAIN=105;
RX PubMed=8566776; DOI=10.1016/0378-1119(95)00703-2;
RA Bosch T.C.G., Benitez E., Gellner K., Praetzel G., Salgado L.M.;
RT "Cloning of a ras-related gene from Hydra which responds to head-specific
RT signals.";
RL Gene 167:191-195(1995).
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; X78597; CAA55332.1; -; mRNA.
DR RefSeq; NP_001296618.1; NM_001309689.1.
DR AlphaFoldDB; P51539; -.
DR SMR; P51539; -.
DR EnsemblMetazoa; NM_001309689.1; NP_001296618.1; LOC100209445.
DR GeneID; 100209445; -.
DR KEGG; hmg:100209445; -.
DR OrthoDB; 8685at2759; -.
DR Proteomes; UP000694840; Unplaced.
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 CDD; cd04138; H_N_K_Ras_like; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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 NCBIfam; TIGR00231; small_GTP; 1.
DR PANTHER; PTHR24070; RAS, DI-RAS, AND RHEB FAMILY MEMBERS OF SMALL GTPASE SUPERFAMILY; 1.
DR PANTHER; PTHR24070:SF416; RAS-LIKE PROTEIN 1; 1.
DR Pfam; PF00071; Ras; 1.
DR PRINTS; PR00449; RASTRNSFRMNG.
DR SMART; SM00175; RAB; 1.
DR SMART; SM00176; RAN; 1.
DR SMART; SM00173; RAS; 1.
DR SMART; SM00174; RHO; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS51421; RAS; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; GTP-binding; Hydrolase; Lipoprotein; Membrane; Methylation;
KW Nucleotide-binding; Prenylation; Reference proteome.
FT CHAIN 1..191
FT /note="Ras-like protein RAS1"
FT /id="PRO_0000082670"
FT PROPEP 192..194
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000281318"
FT MOTIF 38..46
FT /note="Effector region"
FT BINDING 16..23
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 63..67
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 122..125
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT MOD_RES 191
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000250"
FT LIPID 191
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 194 AA; 21584 MW; F08083B1DABBD201 CRC64;
MSSSSEPTKF KMVVVGAGGV GKSALTIQLI QNHFVEDYDP TIEDSYIKQV VVDGAICILD
ILDTAGQEEY SAMREHYMRT GEGFLCIFAV TSLKSFQEID NFRTQALRVK DADKVPMVLV
GNKVDLPKRD VSTKDGNDKA LSFGIPYVET SAKTKQGVEE AFFTLVREIL ADRRNQEGQK
KSDSKRAKFK CTLL
//
