ID   RAPA_DIPOM              Reviewed;         184 AA.
AC   P22123;
DT   01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1991, sequence version 1.
DT   03-AUG-2022, entry version 107.
DE   RecName: Full=Ras-related protein O-Krev;
DE            EC=3.6.5.2 {ECO:0000250|UniProtKB:P10114};
DE   Flags: Precursor;
OS   Diplobatis ommata (Ocellated electric ray) (Discopyge ommata).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes;
OC   Elasmobranchii; Batoidea; Torpediniformes; Narcinidae; Diplobatis.
OX   NCBI_TaxID=1870830;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Electric lobe;
RX   PubMed=1899244; DOI=10.1016/s0021-9258(18)52297-3;
RA   Ngsee J.K., Elferink L.A., Scheller R.H.;
RT   "A family of ras-like GTP-binding proteins expressed in electromotor
RT   neurons.";
RL   J. Biol. Chem. 266:2675-2680(1991).
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:P10114};
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; M38395; AAA49226.1; -; mRNA.
DR   PIR; F38625; F38625.
DR   AlphaFoldDB; P22123; -.
DR   SMR; P22123; -.
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:0032486; P:Rap protein signal transduction; IEA:InterPro.
DR   CDD; cd04175; Rap1; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR038851; Rap1.
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..181
FT                   /note="Ras-related protein O-Krev"
FT                   /id="PRO_0000030205"
FT   PROPEP          182..184
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000030206"
FT   MOTIF           32..40
FT                   /note="Effector region"
FT                   /evidence="ECO:0000305"
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   MOD_RES         181
FT                   /note="Cysteine methyl ester"
FT                   /evidence="ECO:0000250"
FT   LIPID           181
FT                   /note="S-geranylgeranyl cysteine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   184 AA;  20931 MW;  D1B18E38CBB3140E CRC64;
     MREYKLVVLG SGGVGKSALT VQFVQGIFVE KYDPTIEDSY RKQVEVDCQP CMLEILDTAG
     TEQFTAMRDL YMKNGQGFAL VYSITAQSTF NDLQDLREQI LRVKDTEDVP MILVGNKCDL
     EDERVVGKEQ GQNLARQWNN CAFLESSAKS KINVNEIFYD LVRQINRKAP VEKCKKKKSQ
     CTLL