ID   RAS_GEOCY               Reviewed;         209 AA.
AC   P24498;
DT   01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-1992, sequence version 1.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=Ras-like protein;
DE            EC=3.6.5.2 {ECO:0000250|UniProtKB:P01112};
DE   Flags: Precursor;
OS   Geodia cydonium (Sponge).
OC   Eukaryota; Metazoa; Porifera; Demospongiae; Heteroscleromorpha;
OC   Tetractinellida; Astrophorina; Geodiidae; Geodia.
OX   NCBI_TaxID=6047;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=2209606; DOI=10.1111/j.1432-1033.1990.tb19253.x;
RA   Robitzki A., Schroeder H.C., Ugarkovic D., Kuchino Y., Kurelec B.,
RA   Gamulin V., Mueller W.E.G.;
RT   "Regulated expression and phosphorylation of the 23-26-kDa ras protein in
RT   the sponge Geodia cydonium.";
RL   Eur. J. Biochem. 192:499-506(1990).
CC   -!- FUNCTION: This protein is activated by the insulin/insulin (insulin-
CC       like)-receptor system. This transition enables the ras protein to
CC       interact with the lectin-receptor/lectin complex, a process which
CC       ultimately lead to an initiation of an intra-cellular signal-
CC       transduction chain.
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   -!- PTM: Phosphorylated in the presence of insulin.
CC   -!- SIMILARITY: Belongs to the small GTPase superfamily. Ras family.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; M30929; -; NOT_ANNOTATED_CDS; mRNA.
DR   PIR; S13179; S13179.
DR   AlphaFoldDB; P24498; -.
DR   SMR; P24498; -.
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; IPR001806; Small_GTPase.
DR   InterPro; IPR020849; Small_GTPase_Ras-type.
DR   PANTHER; PTHR24070; PTHR24070; 2.
DR   Pfam; PF00071; Ras; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS51421; RAS; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; GTP-binding; Hydrolase; Lipoprotein; Membrane; Methylation;
KW   Nucleotide-binding; Phosphoprotein; Prenylation.
FT   CHAIN           1..206
FT                   /note="Ras-like protein"
FT                   /id="PRO_0000082669"
FT   PROPEP          207..209
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000281317"
FT   MOTIF           55..63
FT                   /note="Effector region"
FT   BINDING         10..17
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         79..83
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         140..143
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         58
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         206
FT                   /note="Cysteine methyl ester"
FT                   /evidence="ECO:0000250"
FT   LIPID           206
FT                   /note="S-geranylgeranyl cysteine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   209 AA;  23854 MW;  C544C43102C8323D CRC64;
     MTEYKIVIVG GGLVGKSALT LQLVQVCIKD QYYLIEFQNN QFQFENLQNH YIDEYDPTVE
     DSRREVSIDD QTCLLNILDT AGQQHSNAQS MDAHWSTVFV CLFNYFNITS MYDEIASFRE
     QILRVKDGAK DLVPLILIIN KADLDHESQG SGNEGQLAKD SLSFHQSSAK SRINLEEIPY
     SLVRELRKEL KLDQSSGKAQ KKKKQCLII