RHO2_YEAST
ID RHO2_YEAST Reviewed; 192 AA.
AC P06781; D6W190; Q45TZ2;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 2.
DT 03-AUG-2022, entry version 198.
DE RecName: Full=GTP-binding protein RHO2;
DE EC=3.6.5.2 {ECO:0000250|UniProtKB:P61586};
DE Flags: Precursor;
GN Name=RHO2; OrderedLocusNames=YNL090W; ORFNames=N2237;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3543936; DOI=10.1073/pnas.84.3.779;
RA Madaule P., Axel R., Myers A.M.;
RT "Characterization of two members of the rho gene family from the yeast
RT Saccharomyces cerevisiae.";
RL Proc. Natl. Acad. Sci. U.S.A. 84:779-783(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=S96, SK1, YJM 1129, YJM 280, YJM 320, YJM 326, YJM 339, YJM 421, and
RC YJM 627;
RX PubMed=11907579; DOI=10.1038/416326a;
RA Steinmetz L.M., Sinha H., Richards D.R., Spiegelman J.I., Oefner P.J.,
RA McCusker J.H., Davis R.W.;
RT "Dissecting the architecture of a quantitative trait locus in yeast.";
RL Nature 416:326-330(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=SK1;
RX PubMed=16273108; DOI=10.1038/ng1674;
RA Deutschbauer A.M., Davis R.W.;
RT "Quantitative trait loci mapped to single-nucleotide resolution in yeast.";
RL Nat. Genet. 37:1333-1340(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=8740422;
RX DOI=10.1002/(sici)1097-0061(199604)12:5<485::aid-yea928>3.0.co;2-u;
RA Soler-Mira A., Saiz J.E., Ballesta J.P.G., Remacha M.A.;
RT "The sequence of a 17,933 bp segment of Saccharomyces cerevisiae chromosome
RT XIV contains the RHO2, TOP2, MKT1 and END3 genes and five new open reading
RT frames.";
RL Yeast 12:485-491(1996).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169873;
RA Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
RA Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
RA Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
RA Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
RA Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F.,
RA Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C.,
RA Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A.,
RA Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H.,
RA Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L.,
RA Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R.,
RA Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D.,
RA Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A.,
RA Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C.,
RA Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F.,
RA Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G.,
RA Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M.,
RA Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its
RT evolutionary implications.";
RL Nature 387:93-98(1997).
RN [6]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [7]
RP INTERACTION WITH BEM4.
RX PubMed=8754839; DOI=10.1128/mcb.16.8.4387;
RA Mack D., Nishimura K., Dennehey B.K., Arbogast T., Parkinson J., Toh-e A.,
RA Pringle J.R., Bender A., Matsui Y.;
RT "Identification of the bud emergence gene BEM4 and its interactions with
RT rho-type GTPases in Saccharomyces cerevisiae.";
RL Mol. Cell. Biol. 16:4387-4395(1996).
RN [8]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [9]
RP PALMITOYLATION AT CYS-188.
RX PubMed=16751107; DOI=10.1016/j.cell.2006.03.042;
RA Roth A.F., Wan J., Bailey A.O., Sun B., Kuchar J.A., Green W.N.,
RA Phinney B.S., Yates J.R. III, Davis N.G.;
RT "Global analysis of protein palmitoylation in yeast.";
RL Cell 125:1003-1013(2006).
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:P61586};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670;
CC Evidence={ECO:0000250|UniProtKB:P61586};
CC -!- SUBUNIT: Interacts with BEM4. {ECO:0000269|PubMed:8754839}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor
CC {ECO:0000305}; Cytoplasmic side {ECO:0000305}.
CC -!- MISCELLANEOUS: Present with 3870 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rho family.
CC {ECO:0000305}.
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DR EMBL; M15190; AAA34978.1; -; Genomic_DNA.
DR EMBL; AF458969; AAM00517.1; -; Genomic_DNA.
DR EMBL; AF458970; AAM00523.1; -; Genomic_DNA.
DR EMBL; AF458971; AAM00529.1; -; Genomic_DNA.
DR EMBL; AF458972; AAM00535.1; -; Genomic_DNA.
DR EMBL; AF458973; AAM00541.1; -; Genomic_DNA.
DR EMBL; AF458974; AAM00547.1; -; Genomic_DNA.
DR EMBL; AF458976; AAM00559.1; -; Genomic_DNA.
DR EMBL; AF458978; AAM00571.1; -; Genomic_DNA.
DR EMBL; AF458981; AAM00589.1; -; Genomic_DNA.
DR EMBL; DQ115393; AAZ22518.1; -; Genomic_DNA.
DR EMBL; X89016; CAA61421.1; -; Genomic_DNA.
DR EMBL; Z71366; CAA95965.1; -; Genomic_DNA.
DR EMBL; BK006947; DAA10456.1; -; Genomic_DNA.
DR PIR; S57533; TVBYH2.
DR RefSeq; NP_014309.3; NM_001182928.3.
DR AlphaFoldDB; P06781; -.
DR SMR; P06781; -.
DR BioGRID; 35734; 162.
DR DIP; DIP-5750N; -.
DR IntAct; P06781; 14.
DR STRING; 4932.YNL090W; -.
DR iPTMnet; P06781; -.
DR SwissPalm; P06781; -.
DR MaxQB; P06781; -.
DR PaxDb; P06781; -.
DR PRIDE; P06781; -.
DR EnsemblFungi; YNL090W_mRNA; YNL090W; YNL090W.
DR GeneID; 855634; -.
DR KEGG; sce:YNL090W; -.
DR SGD; S000005034; RHO2.
DR VEuPathDB; FungiDB:YNL090W; -.
DR eggNOG; KOG0393; Eukaryota.
DR HOGENOM; CLU_041217_21_2_1; -.
DR InParanoid; P06781; -.
DR OMA; NDNVMRR; -.
DR BioCyc; YEAST:G3O-33118-MON; -.
DR Reactome; R-SCE-416482; G alpha (12/13) signalling events.
DR Reactome; R-SCE-5625740; RHO GTPases activate PKNs.
DR Reactome; R-SCE-6798695; Neutrophil degranulation.
DR Reactome; R-SCE-9013026; RHOB GTPase cycle.
DR Reactome; R-SCE-9013106; RHOC GTPase cycle.
DR Reactome; R-SCE-9013405; RHOD GTPase cycle.
DR Reactome; R-SCE-9035034; RHOF GTPase cycle.
DR Reactome; R-SCE-9696264; RND3 GTPase cycle.
DR Reactome; R-SCE-9696270; RND2 GTPase cycle.
DR Reactome; R-SCE-9696273; RND1 GTPase cycle.
DR PRO; PR:P06781; -.
DR Proteomes; UP000002311; Chromosome XIV.
DR RNAct; P06781; protein.
DR GO; GO:0005938; C:cell cortex; IBA:GO_Central.
DR GO; GO:0071944; C:cell periphery; HDA:SGD.
DR GO; GO:0042995; C:cell projection; IBA:GO_Central.
DR GO; GO:0031410; C:cytoplasmic vesicle; IBA:GO_Central.
DR GO; GO:0005856; C:cytoskeleton; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IDA:SGD.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005525; F:GTP binding; IBA:GO_Central.
DR GO; GO:0003924; F:GTPase activity; IDA:SGD.
DR GO; GO:0019901; F:protein kinase binding; IBA:GO_Central.
DR GO; GO:0007015; P:actin filament organization; IBA:GO_Central.
DR GO; GO:0030865; P:cortical cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0030010; P:establishment of cell polarity; TAS:SGD.
DR GO; GO:0007163; P:establishment or maintenance of cell polarity; IBA:GO_Central.
DR GO; GO:0031505; P:fungal-type cell wall organization; TAS:SGD.
DR GO; GO:0007017; P:microtubule-based process; TAS:SGD.
DR GO; GO:0032956; P:regulation of actin cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0008360; P:regulation of cell shape; IBA:GO_Central.
DR GO; GO:0007264; P:small GTPase mediated signal transduction; TAS:SGD.
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 1: Evidence at protein level;
KW Cell membrane; GTP-binding; Hydrolase; Lipoprotein; Membrane; Methylation;
KW Nucleotide-binding; Palmitate; Prenylation; Reference proteome.
FT CHAIN 1..189
FT /note="GTP-binding protein RHO2"
FT /id="PRO_0000198946"
FT PROPEP 190..192
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000281276"
FT MOTIF 36..44
FT /note="Effector region"
FT /evidence="ECO:0000250"
FT BINDING 14..21
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P61586"
FT BINDING 61..65
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 119..122
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P61586"
FT MOD_RES 189
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000250|UniProtKB:P62745"
FT LIPID 188
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000305|PubMed:16751107"
FT LIPID 189
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:P62745"
FT CONFLICT 48
FT /note="C -> S (in Ref. 1; AAA34978)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 192 AA; 21479 MW; 468AA876DF13F69C CRC64;
MSEKAVRRKL VIIGDGACGK TSLLYVFTLG KFPEQYHPTV FENYVTDCRV DGIKVSLTLW
DTAGQEEYER LRPFSYSKAD IILIGFAVDN FESLINARTK WADEALRYCP DAPIVLVGLK
KDLRQEAHFK ENATDEMVPI EDAKQVARAI GAKKYMECSA LTGEGVDDVF EVATRTSLLM
KKEPGANCCI IL
