RHO5_YEAST
ID RHO5_YEAST Reviewed; 331 AA.
AC P53879; D6W106;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=GTP-binding protein RHO5 {ECO:0000303|PubMed:12118069};
DE Flags: Precursor;
GN Name=RHO5 {ECO:0000303|PubMed:12118069}; OrderedLocusNames=YNL180C;
GN ORFNames=N1644;
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 [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 [2]
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 [3]
RP FUNCTION, AND MUTAGENESIS OF GLN-91.
RX PubMed=12118069; DOI=10.1242/jcs.115.15.3139;
RA Schmitz H.-P., Huppert S., Lorberg A., Heinisch J.J.;
RT "Rho5p downregulates the yeast cell integrity pathway.";
RL J. Cell Sci. 115:3139-3148(2002).
RN [4]
RP INTERACTION WITH RGD2.
RX PubMed=11591390; DOI=10.1016/s0014-5793(01)02906-4;
RA Roumanie O., Weinachter C., Larrieu I., Crouzet M., Doignon F.;
RT "Functional characterization of the Bag7, Lrg1 and Rgd2 RhoGAP proteins
RT from Saccharomyces cerevisiae.";
RL FEBS Lett. 506:149-156(2001).
RN [5]
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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-223, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-223, 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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-223; SER-228; THR-232 AND
RP THR-244, AND 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).
RN [9]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-276, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22106047; DOI=10.1002/pmic.201100166;
RA Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.;
RT "Sites of ubiquitin attachment in Saccharomyces cerevisiae.";
RL Proteomics 12:236-240(2012).
RN [10]
RP FUNCTION, DISRUPTION PHENOTYPE, AND SUBCELLULAR LOCATION.
RX PubMed=25598154; DOI=10.1111/mmi.12937;
RA Schmitz H.P., Jendretzki A., Wittland J., Wiechert J., Heinisch J.J.;
RT "Identification of Dck1 and Lmo1 as upstream regulators of the small GTPase
RT Rho5 in Saccharomyces cerevisiae.";
RL Mol. Microbiol. 96:306-324(2015).
CC -!- FUNCTION: Small GTPase that negatively regulates a MAP kinase branch,
CC downstream of SLT2, of the PKC1-mediated signal transduction pathway
CC (PubMed:12118069). With its specific guanine nucleotide exchange factor
CC (GEF), the heterodimeric complex DCK1/LMO1, relocates to mitochondria
CC upon oxidative stress and triggers cell death (PubMed:25598154). The
CC DCK1/LMO1/RHO5 signaling module that mediates mitochondrial turnover
CC under nitrogen starvation conditions via mitophagy (PubMed:25598154).
CC The DCK1/LMO1/RHO5 signaling module also plays a role in cell wall
CC integrity signaling (PubMed:25598154). {ECO:0000269|PubMed:12118069,
CC ECO:0000269|PubMed:25598154}.
CC -!- SUBUNIT: Interacts with RGD2. {ECO:0000269|PubMed:11591390}.
CC -!- INTERACTION:
CC P53879; P29509: TRR1; NbExp=4; IntAct=EBI-29054, EBI-19497;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Lipid-anchor
CC {ECO:0000305}. Mitochondrion {ECO:0000269|PubMed:25598154}.
CC Note=Localization to mitochondria occurs upon oxidative stress and is
CC dependent of DCK1 and LMO1. {ECO:0000269|PubMed:25598154}.
CC -!- DISRUPTION PHENOTYPE: Leads to resistance to oxidants such as H(2)O(2)
CC (PubMed:25598154). Impairs apoptotic phenotype after H(2)O(2) treatment
CC (PubMed:25598154). Leads to hyper-resistance to cell wall stress agents
CC such as calcofluor white and Congo red (PubMed:25598154).
CC {ECO:0000269|PubMed:25598154}.
CC -!- MISCELLANEOUS: Present with 2180 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; Z71456; CAA96072.1; -; Genomic_DNA.
DR EMBL; BK006947; DAA10372.1; -; Genomic_DNA.
DR RefSeq; NP_014219.1; NM_001183018.1.
DR AlphaFoldDB; P53879; -.
DR SMR; P53879; -.
DR BioGRID; 35652; 138.
DR DIP; DIP-2874N; -.
DR IntAct; P53879; 11.
DR MINT; P53879; -.
DR STRING; 4932.YNL180C; -.
DR iPTMnet; P53879; -.
DR MaxQB; P53879; -.
DR PaxDb; P53879; -.
DR PRIDE; P53879; -.
DR EnsemblFungi; YNL180C_mRNA; YNL180C; YNL180C.
DR GeneID; 855541; -.
DR KEGG; sce:YNL180C; -.
DR SGD; S000005124; RHO5.
DR VEuPathDB; FungiDB:YNL180C; -.
DR eggNOG; KOG0393; Eukaryota.
DR HOGENOM; CLU_041217_21_1_1; -.
DR InParanoid; P53879; -.
DR OMA; EHASFAN; -.
DR BioCyc; YEAST:G3O-33191-MON; -.
DR Reactome; R-SCE-9013423; RAC3 GTPase cycle.
DR PRO; PR:P53879; -.
DR Proteomes; UP000002311; Chromosome XIV.
DR RNAct; P53879; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0012505; C:endomembrane system; IDA:SGD.
DR GO; GO:0000329; C:fungal-type vacuole membrane; IDA:SGD.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; HDA: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:0030036; P:actin cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0032488; P:Cdc42 protein signal transduction; IBA:GO_Central.
DR GO; GO:0006897; P:endocytosis; IBA:GO_Central.
DR GO; GO:0007163; P:establishment or maintenance of cell polarity; IBA:GO_Central.
DR GO; GO:0007266; P:Rho protein signal transduction; ISS: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 GTP-binding; Isopeptide bond; Lipoprotein; Membrane; Methylation;
KW Mitochondrion; Nucleotide-binding; Phosphoprotein; Prenylation;
KW Reference proteome; Ubl conjugation.
FT CHAIN 1..328
FT /note="GTP-binding protein RHO5"
FT /id="PRO_0000198949"
FT PROPEP 329..331
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000281279"
FT REGION 51..76
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 239..331
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 259..273
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 279..298
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 309..331
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 10..17
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q96HU8"
FT BINDING 87..91
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q96HU8"
FT BINDING 156..159
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q96HU8"
FT MOD_RES 223
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 228
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 232
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 244
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 328
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000250|UniProtKB:Q9H0U4"
FT LIPID 328
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:Q9H0U4"
FT CROSSLNK 276
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT MUTAGEN 91
FT /note="Q->H: Cells sensitive to calcofluor, caffeine and
FT Congo red."
FT /evidence="ECO:0000269|PubMed:12118069"
SQ SEQUENCE 331 AA; 36818 MW; EEAFD4E39E7ACF81 CRC64;
MRSIKCVIIG DGAVGKTSLL ISYTTNSFPT DYVPTVFDNY STTIAIPNGT ASSPLELDNG
NDKRGSLSSA SSSPSTDRKL YKINLWDTAG QEDYDRLRPL CYPQTDIFLI CFSVSEHASF
ANVTEKWLPE LKQTSNIEGT SLYTKLGKYP ILLVGTKSDL RDDPATQKKL QEANSDYVSQ
EEIDELVQRC GFMGYTECSA ATQAGVREVF EQAVRYAIYE PESPNQKSAN HTLTDELTTA
TTNTNGDKNI REQKQQPHHN NSTDSTLPKG SLQQEKEALN IKPTKKGQKD KIHEQSKSKG
SKIASNNHHN KQAKPKTRND KKKKKSKCVI L
