ID   RAS2_HYDVU              Reviewed;         192 AA.
AC   P38976;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=Ras-like protein RAS2;
DE            EC=3.6.5.2 {ECO:0000250|UniProtKB:P01112};
DE   Flags: Precursor;
GN   Name=RAS2;
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;
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   -!- DEVELOPMENTAL STAGE: Ras2 level drops significantly just after the head
CC       is cut. The expression goes up again after 4 to 8 hours.
CC   -!- SIMILARITY: Belongs to the small GTPase superfamily. Ras family.
CC       {ECO:0000305}.
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DR   EMBL; X70839; CAA50187.1; -; mRNA.
DR   PIR; JC4573; S32042.
DR   AlphaFoldDB; P38976; -.
DR   SMR; P38976; -.
DR   PRIDE; P38976; -.
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   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   2: Evidence at transcript level;
KW   Cell membrane; GTP-binding; Hydrolase; Lipoprotein; Membrane; Methylation;
KW   Nucleotide-binding; Prenylation; Reference proteome.
FT   CHAIN           1..189
FT                   /note="Ras-like protein RAS2"
FT                   /id="PRO_0000082671"
FT   PROPEP          190..192
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000281319"
FT   MOTIF           37..45
FT                   /note="Effector region"
FT   BINDING         15..22
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         62..66
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         121..124
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         189
FT                   /note="Cysteine methyl ester"
FT                   /evidence="ECO:0000250"
FT   LIPID           189
FT                   /note="S-geranylgeranyl cysteine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   192 AA;  21787 MW;  2DC2ECC18F10C709 CRC64;
     MSGDLDRQYK LVVVGGGGVG KSALTIQFIQ SHFVQDYDPT IEDSYRKQCV IDDKVAHLDI
     LDTAGQEEFS AMRDEYMRTG EGFLLVFSVT DRSSFDEIPR FHTQILRVKD IEEFPMILVG
     NKSDLENERT VSTAEAQELG RKLKVSYLES SAKQRINVDA AFHDLVRAIR NANKASVEPL
     RKKEKSRRCI VL