ID   RAS2_PHYPO              Reviewed;         193 AA.
AC   P34726;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=Ras-like protein 2;
DE            EC=3.6.5.2 {ECO:0000250|UniProtKB:P01112};
DE   Flags: Precursor;
GN   Name=RAS-2;
OS   Physarum polycephalum (Slime mold).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Myxogastria;
OC   Myxogastromycetidae; Physariida; Physaraceae; Physarum.
OX   NCBI_TaxID=5791;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=LU352;
RX   PubMed=8373809; DOI=10.1016/0167-4781(93)90203-p;
RA   Kozlowski P., Tymowska Z., Toczko K.;
RT   "Nucleotide and predicted amino acid sequence of a new member of the ras
RT   gene family from the slime mold Physarum polycephalum.";
RL   Biochim. Biophys. Acta 1174:299-302(1993).
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   -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor; Cytoplasmic side.
CC       Note=Inner surface of plasma membrane.
CC   -!- SIMILARITY: Belongs to the small GTPase superfamily. Ras family.
CC       {ECO:0000305}.
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DR   EMBL; L14275; AAC37179.1; -; mRNA.
DR   PIR; S38362; S38362.
DR   AlphaFoldDB; P34726; -.
DR   SMR; P34726; -.
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.
FT   CHAIN           1..190
FT                   /note="Ras-like protein 2"
FT                   /id="PRO_0000082683"
FT   PROPEP          191..193
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000281326"
FT   MOTIF           34..42
FT                   /note="Effector region"
FT   BINDING         12..19
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         59..63
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         118..121
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         190
FT                   /note="Cysteine methyl ester"
FT                   /evidence="ECO:0000250"
FT   LIPID           190
FT                   /note="S-geranylgeranyl cysteine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   193 AA;  21634 MW;  4B0B33CD890EE6CD CRC64;
     MAQLEYKLVI VGGGGVGKSA LTIQLIQNHF IDEYDPTIED SYRKQVVIDE ETCLLDILDT
     AGQEEYSAMR DQYMRTGQGF VMVYSITSRS SFDEINAFRE QILRVKDKDT VPMVLAGNKC
     DLASERQVTT NEGQELARAF GCPFVETSAK ARLNVEECFY GLVREIRKEV IGDKKGGGGK
     KKKLMGIDRC KLL