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RHO_DIPOM
ID   RHO_DIPOM               Reviewed;         192 AA.
AC   P22122;
DT   01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1991, sequence version 1.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=Ras-like GTP-binding protein O-RHO;
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   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor
CC       {ECO:0000305}; Cytoplasmic side {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the small GTPase superfamily. Rho family.
CC       {ECO:0000305}.
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DR   EMBL; M38396; AAA49225.1; -; mRNA.
DR   PIR; G38625; G38625.
DR   AlphaFoldDB; P22122; -.
DR   SMR; P22122; -.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   GO; GO:0007264; P:small GTPase mediated 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; IPR003578; Small_GTPase_Rho.
DR   PANTHER; PTHR24072; PTHR24072; 1.
DR   Pfam; PF00071; Ras; 1.
DR   SMART; SM00174; RHO; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR00231; small_GTP; 1.
DR   PROSITE; PS51420; RHO; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; GTP-binding; Lipoprotein; Membrane; Methylation;
KW   Nucleotide-binding; Prenylation.
FT   CHAIN           1..189
FT                   /note="Ras-like GTP-binding protein O-RHO"
FT                   /id="PRO_0000198883"
FT   PROPEP          190..192
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000281236"
FT   MOTIF           34..42
FT                   /note="Effector region"
FT                   /evidence="ECO:0000255"
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         117..120
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;  21480 MW;  85FFA493C19AC560 CRC64;
     MAAIRKKLVI VGDGACGKTC LLIVFSKDQF PEVYVPTVFE NYVADIEVDG KQVELALWDT
     AGQEDYDRLR PLSYPDTDVI LMCFSIDSPD SLENIPEKWT PEVKHFCPNI PIILVGNKKT
     AGDEHTRREL AKMKQEPVKP DDAKEMGSRI KAFGYLECSA KTKEGVREVF ELASRAALQA
     KKTKSKSPCL LL
 
 
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