RHO4_YEAST
ID RHO4_YEAST Reviewed; 291 AA.
AC Q00246; D6VXB6; P30618;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 2.
DT 03-AUG-2022, entry version 195.
DE RecName: Full=GTP-binding protein RHO4;
DE EC=3.6.5.2 {ECO:0000250|UniProtKB:P61586};
DE Flags: Precursor;
GN Name=RHO4; OrderedLocusNames=YKR055W;
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 204508 / S288c;
RX PubMed=8256523; DOI=10.1002/yea.320091015;
RA van Vliet-Reedijk J.C., Planta R.J.;
RT "The RHO4a and NUD1 genes on Saccharomyces cerevisiae chromosome XI.";
RL Yeast 9:1139-1147(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 62-291.
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 [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 38-42.
RX PubMed=1408836; DOI=10.1093/nar/20.19.5215;
RA Chow T.Y.-K., Perkins E.L., Resnick M.A.;
RT "Yeast RNC1 encodes a chimeric protein, RhoNUC, with a human rho motif and
RT deoxyribonuclease activity.";
RL Nucleic Acids Res. 20:5215-5221(1992).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8196765; DOI=10.1038/369371a0;
RA Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V.,
RA Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P.,
RA Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L.,
RA Daignan-Fornier B., del Rey F., Dion C., Domdey H., Duesterhoeft A.,
RA Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H.,
RA Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L.,
RA Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M.,
RA Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H.,
RA Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J.,
RA Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H.,
RA Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J.,
RA Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S.,
RA Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F.,
RA Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R.,
RA Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W.,
RA Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M.,
RA Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C.,
RA Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H.,
RA Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L.,
RA van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S.,
RA von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M.,
RA Becker I., Mewes H.-W.;
RT "Complete DNA sequence of yeast chromosome XI.";
RL Nature 369:371-378(1994).
RN [5]
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 [6]
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 [7]
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 [8]
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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-276, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-264; SER-268 AND SER-276, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
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 -!- 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 -!- SIMILARITY: Belongs to the small GTPase superfamily. Rho family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA78500.1; Type=Frameshift; Note=Leads to a fusion with RNC1.; Evidence={ECO:0000305};
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DR EMBL; Z25734; CAA81020.1; -; Genomic_DNA.
DR EMBL; D10007; BAA00898.1; -; Genomic_DNA.
DR EMBL; Z14126; CAA78500.1; ALT_FRAME; Genomic_DNA.
DR EMBL; Z28280; CAA82133.1; -; Genomic_DNA.
DR EMBL; AY557909; AAS56235.1; -; Genomic_DNA.
DR EMBL; BK006944; DAA09206.1; -; Genomic_DNA.
DR PIR; S37743; S37743.
DR RefSeq; NP_012981.3; NM_001179845.3.
DR AlphaFoldDB; Q00246; -.
DR SMR; Q00246; -.
DR BioGRID; 34186; 129.
DR DIP; DIP-755N; -.
DR IntAct; Q00246; 16.
DR MINT; Q00246; -.
DR STRING; 4932.YKR055W; -.
DR iPTMnet; Q00246; -.
DR MaxQB; Q00246; -.
DR PaxDb; Q00246; -.
DR PRIDE; Q00246; -.
DR EnsemblFungi; YKR055W_mRNA; YKR055W; YKR055W.
DR GeneID; 853929; -.
DR KEGG; sce:YKR055W; -.
DR SGD; S000001763; RHO4.
DR VEuPathDB; FungiDB:YKR055W; -.
DR eggNOG; KOG0393; Eukaryota.
DR GeneTree; ENSGT00940000172016; -.
DR HOGENOM; CLU_041217_21_1_1; -.
DR InParanoid; Q00246; -.
DR OMA; GAFAHIQ; -.
DR BioCyc; YEAST:G3O-32024-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:Q00246; -.
DR Proteomes; UP000002311; Chromosome XI.
DR RNAct; Q00246; 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:0005935; C:cellular bud neck; IDA:SGD.
DR GO; GO:0031410; C:cytoplasmic vesicle; IBA:GO_Central.
DR GO; GO:0005856; C:cytoskeleton; IBA:GO_Central.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD.
DR GO; GO:0000131; C:incipient cellular bud site; IDA:SGD.
DR GO; GO:0005886; C:plasma membrane; IDA:SGD.
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:0007163; P:establishment or maintenance of cell polarity; IBA:GO_Central.
DR GO; GO:0030011; P:maintenance of cell polarity; IGI:SGD.
DR GO; GO:0090338; P:positive regulation of formin-nucleated actin cable assembly; IGI: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:0090337; P:regulation of formin-nucleated actin cable assembly; IPI:SGD.
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; Direct protein sequencing; GTP-binding; Hydrolase;
KW Lipoprotein; Membrane; Methylation; Nucleotide-binding; Phosphoprotein;
KW Prenylation; Reference proteome.
FT CHAIN 1..288
FT /note="GTP-binding protein RHO4"
FT /id="PRO_0000198948"
FT PROPEP 289..291
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000281278"
FT REGION 14..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 250..273
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 101..109
FT /note="Effector region"
FT /evidence="ECO:0000250"
FT COMPBIAS 14..35
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 79..86
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P61586"
FT BINDING 127..131
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 185..188
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P61586"
FT MOD_RES 264
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 268
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 276
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 288
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000250|UniProtKB:P62745"
FT LIPID 288
FT /note="S-farnesyl cysteine"
FT /evidence="ECO:0000250"
FT CONFLICT 43..48
FT /note="PRLPTP -> QIAYS (in Ref. 3; CAA78500)"
FT /evidence="ECO:0000305"
FT CONFLICT 143
FT /note="T -> R (in Ref. 3; CAA78500)"
FT /evidence="ECO:0000305"
FT CONFLICT 201..211
FT /note="PSSAESLAKRL -> QVQQNPWPSVW (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 213..218
FT /note="AFAHIQ -> HLHIFK (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 291 AA; 32186 MW; 4B7BA75EA9BA50FD CRC64;
MNTLLFKRKG GNCGNESNIV SQGSPSSSNL PESPGTLDEK NLPRLPTPFA RSLSTIPSYE
QMKRTNKLPD YHLKIVVVGD GAVGKTCLLI SYVQGTFPTD YIPTIFENYV TNIEGPNGQI
IELALWDTAG QEEYSRLRPL SYTNADVLMV CYSVGSKTSL KNVEDLWFPE VKHFCPSTPI
MLVGLKSDLY EADNLSDLVE PSSAESLAKR LGAFAHIQCS ARLKENIDEV FETAIHTLLS
DSLYAPREPT HTIKNPFKRN TTRSDIDSST GDTSVSISGT KRLRKNKCII M
