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 24-JAN-2024, entry version 202. 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}; 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; 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; 134. DR DIP; DIP-755N; -. DR IntAct; Q00246; 16. DR MINT; Q00246; -. DR STRING; 4932.YKR055W; -. DR iPTMnet; Q00246; -. DR MaxQB; Q00246; -. DR PaxDb; 4932-YKR055W; -. DR PeptideAtlas; Q00246; -. DR EnsemblFungi; YKR055W_mRNA; YKR055W; YKR055W. DR GeneID; 853929; -. DR KEGG; sce:YKR055W; -. DR AGR; SGD:S000001763; -. 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 OrthoDB; 2016743at2759; -. DR BioCyc; YEAST:G3O-32024-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; 853929; 0 hits in 10 CRISPR screens. DR PRO; PR:Q00246; -. DR Proteomes; UP000002311; Chromosome XI. DR RNAct; Q00246; Protein. DR GO; GO:0071944; C:cell periphery; HDA:SGD. DR GO; GO:0005935; C:cellular bud neck; IDA:SGD. DR GO; GO:0005829; C:cytosol; 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: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:0090337; P:regulation of formin-nucleated actin cable assembly; IPI: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; cd04132; Rho4_like; 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:SF181; GTP-BINDING PROTEIN RHO4; 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; 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 //