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   27-MAR-2024, entry version 198.
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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; 247.
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; 4932-YIL118W; -.
DR   PeptideAtlas; Q00245; -.
DR   EnsemblFungi; YIL118W_mRNA; YIL118W; YIL118W.
DR   GeneID; 854688; -.
DR   KEGG; sce:YIL118W; -.
DR   AGR; SGD:S000001380; -.
DR   SGD; S000001380; RHO3.
DR   VEuPathDB; FungiDB:YIL118W; -.
DR   eggNOG; KOG0393; Eukaryota.
DR   HOGENOM; CLU_041217_21_2_1; -.
DR   InParanoid; Q00245; -.
DR   OMA; THTIMLC; -.
DR   OrthoDB; 5480056at2759; -.
DR   BioCyc; YEAST:G3O-31371-MONOMER; -.
DR   Reactome; R-SCE-6798695; Neutrophil degranulation.
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   BioGRID-ORCS; 854688; 10 hits in 10 CRISPR screens.
DR   PRO; PR:Q00245; -.
DR   Proteomes; UP000002311; Chromosome IX.
DR   RNAct; Q00245; Protein.
DR   GO; GO:0005933; C:cellular bud; IDA:SGD.
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:0030950; P:establishment or maintenance of actin cytoskeleton polarity; IMP:SGD.
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:0007165; P:signal transduction; IBA:GO_Central.
DR   GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
DR   CDD; cd04134; Rho3; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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   NCBIfam; TIGR00231; small_GTP; 1.
DR   PANTHER; PTHR24072:SF186; GTP-BINDING PROTEIN RHO3; 1.
DR   PANTHER; PTHR24072; RHO FAMILY GTPASE; 1.
DR   Pfam; PF00071; Ras; 1.
DR   PRINTS; PR00449; RASTRNSFRMNG.
DR   SMART; SM00175; RAB; 1.
DR   SMART; SM00176; RAN; 1.
DR   SMART; SM00173; RAS; 1.
DR   SMART; SM00174; RHO; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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
//