RHO3_YEAST
ID RHO3_YEAST Reviewed; 231 AA.
AC Q00245; D6VVG9;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 2.
DT 03-AUG-2022, entry version 191.
DE RecName: Full=GTP-binding protein RHO3;
DE Flags: Precursor;
GN Name=RHO3; OrderedLocusNames=YIL118W;
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].
RC STRAIN=ATCC 38626 / AH22 / NRRL Y-12843;
RX PubMed=1587484; DOI=10.1016/0378-1119(92)90705-t;
RA Matsui Y., Toh-E A.;
RT "Isolation and characterization of two novel ras superfamily genes in
RT Saccharomyces cerevisiae.";
RL Gene 114:43-49(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169870;
RA Churcher C.M., Bowman S., Badcock K., Bankier A.T., Brown D.,
RA Chillingworth T., Connor R., Devlin K., Gentles S., Hamlin N., Harris D.E.,
RA Horsnell T., Hunt S., Jagels K., Jones M., Lye G., Moule S., Odell C.,
RA Pearson D., Rajandream M.A., Rice P., Rowley N., Skelton J., Smith V.,
RA Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IX.";
RL Nature 387:84-87(1997).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [5]
RP FUNCTION.
RX PubMed=1448099; DOI=10.1128/mcb.12.12.5690-5699.1992;
RA Matsui Y., Toh-E A.;
RT "Yeast RHO3 and RHO4 ras superfamily genes are necessary for bud growth,
RT and their defect is suppressed by a high dose of bud formation genes CDC42
RT and BEM1.";
RL Mol. Cell. Biol. 12:5690-5699(1992).
RN [6]
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).
CC -!- FUNCTION: Plays an important role in cell growth. Required to keep the
CC uninucleated state. May be involved in the organization of the
CC cytoskeleton which affects microtubule functions. Most likely RHO3 and
CC RHO4 of S.cerevisiae regulate partially overlapping but different
CC pathways. {ECO:0000269|PubMed:1448099}.
CC -!- INTERACTION:
CC Q00245; P19658: EXO70; NbExp=4; IntAct=EBI-15138, EBI-6717;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor
CC {ECO:0000305}; Cytoplasmic side {ECO:0000305}.
CC -!- MISCELLANEOUS: Present with 5910 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; D10006; BAA00897.1; -; Genomic_DNA.
DR EMBL; Z46833; CAA86874.1; -; Genomic_DNA.
DR EMBL; AY557857; AAS56183.1; -; Genomic_DNA.
DR EMBL; BK006942; DAA08435.1; -; Genomic_DNA.
DR PIR; S49891; S49891.
DR RefSeq; NP_012148.1; NM_001179466.1.
DR AlphaFoldDB; Q00245; -.
DR SMR; Q00245; -.
DR BioGRID; 34873; 244.
DR DIP; DIP-4820N; -.
DR IntAct; Q00245; 3.
DR MINT; Q00245; -.
DR STRING; 4932.YIL118W; -.
DR iPTMnet; Q00245; -.
DR SwissPalm; Q00245; -.
DR MaxQB; Q00245; -.
DR PaxDb; Q00245; -.
DR PRIDE; Q00245; -.
DR EnsemblFungi; YIL118W_mRNA; YIL118W; YIL118W.
DR GeneID; 854688; -.
DR KEGG; sce:YIL118W; -.
DR SGD; S000001380; RHO3.
DR VEuPathDB; FungiDB:YIL118W; -.
DR eggNOG; KOG0393; Eukaryota.
DR HOGENOM; CLU_041217_21_2_1; -.
DR InParanoid; Q00245; -.
DR OMA; MPLCGGS; -.
DR BioCyc; YEAST:G3O-31371-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:Q00245; -.
DR Proteomes; UP000002311; Chromosome IX.
DR RNAct; Q00245; protein.
DR GO; GO:0005938; C:cell cortex; IBA:GO_Central.
DR GO; GO:0042995; C:cell projection; IBA:GO_Central.
DR GO; GO:0005933; C:cellular bud; IDA:SGD.
DR GO; GO:0031410; C:cytoplasmic vesicle; IBA:GO_Central.
DR GO; GO:0005856; C:cytoskeleton; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:SGD.
DR GO; GO:0005886; C:plasma membrane; HDA:SGD.
DR GO; GO:0005525; F:GTP binding; IDA:SGD.
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:0030950; P:establishment or maintenance of actin cytoskeleton polarity; IMP:SGD.
DR GO; GO:0007163; P:establishment or maintenance of cell polarity; IBA:GO_Central.
DR GO; GO:0045921; P:positive regulation of exocytosis; IMP:SGD.
DR GO; GO:0090338; P:positive regulation of formin-nucleated actin cable assembly; IMP: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; 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 1: Evidence at protein level;
KW Cell membrane; GTP-binding; Lipoprotein; Membrane; Methylation;
KW Nucleotide-binding; Prenylation; Reference proteome.
FT CHAIN 1..228
FT /note="GTP-binding protein RHO3"
FT /id="PRO_0000198947"
FT PROPEP 229..231
FT /note="Removed in mature form"
FT /evidence="ECO:0000250|UniProtKB:P62745"
FT /id="PRO_0000281277"
FT REGION 139..165
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 45..53
FT /note="Effector region"
FT BINDING 23..30
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P61586"
FT BINDING 70..74
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P20171"
FT BINDING 128..131
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P61586"
FT MOD_RES 228
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000250|UniProtKB:P62745"
FT LIPID 228
FT /note="S-farnesyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:P62745"
FT CONFLICT 129
FT /note="K -> E (in Ref. 1; BAA00897)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 231 AA; 25312 MW; 7C8BEB15502AD024 CRC64;
MSFLCGSAST SNKPIERKIV ILGDGACGKT SLLNVFTRGY FPEVYEPTVF ENYIHDIFVD
SKHITLSLWD TAGQEEFDRL RSLSYSDTQC IMLCFSIDSR DSLENVQNKW VGEITDHCEG
VKLVLVALKC DLRNNENESN AITPNNIQQD NSVSNDNGNN INSTSNGKNL ISYEEGLAMA
KKIGALRYLE CSAKLNKGVN EAFTEAARVA LTAGPVATEV KSDSGSSCTI M
