RHO1_YEAST
ID RHO1_YEAST Reviewed; 209 AA.
AC P06780; D6W4G6;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 218.
DE RecName: Full=GTP-binding protein RHO1;
DE EC=3.6.5.2 {ECO:0000250|UniProtKB:P61586};
DE AltName: Full=Rho-type GTPase 1;
DE Flags: Precursor;
GN Name=RHO1; OrderedLocusNames=YPR165W; ORFNames=P9325.3;
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], AND MUTAGENESIS OF GLN-68.
RX PubMed=3543936; DOI=10.1073/pnas.84.3.779;
RA Madaule P., Axel R., Myers A.M.;
RT "Characterization of two members of the rho gene family from the yeast
RT Saccharomyces cerevisiae.";
RL Proc. Natl. Acad. Sci. U.S.A. 84:779-783(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169875;
RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA Vo D.H., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL Nature 387:103-105(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 PROTEIN SEQUENCE OF 2-10; 13-73; 104-123; 128-137 AND 168-181, CLEAVAGE OF
RP INITIATOR METHIONINE, ACETYLATION AT SER-2, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RA Bienvenut W.V., Peters C.;
RL Submitted (MAY-2005) to UniProtKB.
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 201-209.
RX PubMed=3029111; DOI=10.1016/s0021-9258(18)61515-7;
RA Myers A.M., Crivellone M.D., Tzagoloff A.;
RT "Assembly of the mitochondrial membrane system. MRP1 and MRP2, two yeast
RT nuclear genes coding for mitochondrial ribosomal proteins.";
RL J. Biol. Chem. 262:3388-3397(1987).
RN [7]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=8195291; DOI=10.1083/jcb.125.5.1077;
RA Yamochi W., Tanaka K., Nonaka H., Maeda A., Musha T., Takai Y.;
RT "Growth site localization of Rho1 small GTP-binding protein and its
RT involvement in bud formation in Saccharomyces cerevisiae.";
RL J. Cell Biol. 125:1077-1093(1994).
RN [8]
RP FUNCTION, INTERACTION WITH PKC1, AND MUTAGENESIS OF VAL-43; PHE-44 AND
RP GLU-45.
RX PubMed=8846785; DOI=10.1002/j.1460-2075.1995.tb00281.x;
RA Nonaka H., Tanaka K., Hirano H., Fujiwara T., Kohno H., Umikawa M.,
RA Mino A., Takai Y.;
RT "A downstream target of RHO1 small GTP-binding protein is PKC1, a homolog
RT of protein kinase C, which leads to activation of the MAP kinase cascade in
RT Saccharomyces cerevisiae.";
RL EMBO J. 14:5931-5938(1995).
RN [9]
RP FUNCTION, AND ACTIVITY REGULATION.
RX PubMed=7579704; DOI=10.1091/mbc.6.8.1011;
RA Wang T., Bretscher A.;
RT "The rho-GAP encoded by BEM2 regulates cytoskeletal structure in budding
RT yeast.";
RL Mol. Biol. Cell 6:1011-1024(1995).
RN [10]
RP ACTIVITY REGULATION.
RX PubMed=8641285; DOI=10.1002/j.1460-2075.1996.tb00573.x;
RA Ozaki K., Tanaka K., Imamura H., Hihara T., Kameyama T., Nonaka H.,
RA Hirano H., Matsuura Y., Takai Y.;
RT "Rom1p and Rom2p are GDP/GTP exchange proteins (GEPs) for the Rho1p small
RT GTP binding protein in Saccharomyces cerevisiae.";
RL EMBO J. 15:2196-2207(1996).
RN [11]
RP FUNCTION, INTERACTION WITH BNI1, AND MUTAGENESIS OF THR-24 AND THR-42.
RX PubMed=8947028; DOI=10.1002/j.1460-2075.1996.tb00994.x;
RA Kohno H., Tanaka K., Mino A., Umikawa M., Imamura H., Fujiwara T.,
RA Fujita Y., Hotta K., Qadota H., Watanabe T., Ohya Y., Takai Y.;
RT "Bni1p implicated in cytoskeletal control is a putative target of Rho1p
RT small GTP binding protein in Saccharomyces cerevisiae.";
RL EMBO J. 15:6060-6068(1996).
RN [12]
RP FUNCTION, AND INTERACTION WITH PKC1.
RX PubMed=8621575; DOI=10.1074/jbc.271.16.9193;
RA Kamada Y., Qadota H., Python C.P., Anraku Y., Ohya Y., Levin D.E.;
RT "Activation of yeast protein kinase C by Rho1 GTPase.";
RL J. Biol. Chem. 271:9193-9196(1996).
RN [13]
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 [14]
RP INTERACTION WITH BEM4.
RX PubMed=8754840; DOI=10.1128/mcb.16.8.4396;
RA Hirano H., Tanaka K., Ozaki K., Imamura H., Kohno H., Hihara T.,
RA Kameyama T., Hotta K., Arisawa M., Watanabe T., Qadota H., Ohya Y.,
RA Takai Y.;
RT "ROM7/BEM4 encodes a novel protein that interacts with the Rho1p small GTP-
RT binding protein in Saccharomyces cerevisiae.";
RL Mol. Cell. Biol. 16:4396-4403(1996).
RN [15]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=8602514; DOI=10.1126/science.272.5259.277;
RA Drgonova J., Drgon T., Tanaka K., Kollar R., Chen G.-C., Ford R.A.,
RA Chan C.S.M., Takai Y., Cabib E.;
RT "Rho1p, a yeast protein at the interface between cell polarization and
RT morphogenesis.";
RL Science 272:277-279(1996).
RN [16]
RP FUNCTION, AND INTERACTION WITH FKS1.
RX PubMed=8602515; DOI=10.1126/science.272.5259.279;
RA Qadota H., Python C.P., Inoue S.B., Arisawa M., Anraku Y., Zheng Y.,
RA Watanabe T., Levin D.E., Ohya Y.;
RT "Identification of yeast Rho1p GTPase as a regulatory subunit of 1,3-beta-
RT glucan synthase.";
RL Science 272:279-281(1996).
RN [17]
RP ACTIVITY REGULATION, AND INTERACTION WITH SAC7.
RX PubMed=9038344; DOI=10.1016/s0092-8674(00)81893-0;
RA Schmidt A., Bickle M., Beck T., Hall M.N.;
RT "The yeast phosphatidylinositol kinase homolog TOR2 activates RHO1 and RHO2
RT via the exchange factor ROM2.";
RL Cell 88:531-542(1997).
RN [18]
RP ACTIVITY REGULATION, AND INTERACTION WITH RDI1.
RX PubMed=9242378; DOI=10.1038/sj.onc.1201194;
RA Koch G., Tanaka K., Masuda T., Yamochi W., Nonaka H., Takai Y.;
RT "Association of the Rho family small GTP-binding proteins with Rho GDP
RT dissociation inhibitor (Rho GDI) in Saccharomyces cerevisiae.";
RL Oncogene 15:417-422(1997).
RN [19]
RP INTERACTION WITH SKN7.
RX PubMed=9535835; DOI=10.1074/jbc.273.15.8616;
RA Alberts A.S., Bouquin N., Johnston L.H., Treisman R.;
RT "Analysis of RhoA-binding proteins reveals an interaction domain conserved
RT in heterotrimeric G protein beta subunits and the yeast response regulator
RT protein Skn7.";
RL J. Biol. Chem. 273:8616-8622(1998).
RN [20]
RP ACTIVITY REGULATION, AND INTERACTION WITH BAG7.
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 [21]
RP MUTAGENESIS OF GLU-45; LEU-60; ASP-70; GLU-102; TRP-104; GLY-121; SER-165
RP AND LYS-167.
RX PubMed=11574532; DOI=10.1074/jbc.m103805200;
RA Saka A., Abe M., Okano H., Minemura M., Qadota H., Utsugi T., Mino A.,
RA Tanaka K., Takai Y., Ohya Y.;
RT "Complementing yeast rho1 mutation groups with distinct functional
RT defects.";
RL J. Biol. Chem. 276:46165-46171(2001).
RN [22]
RP FUNCTION, AND INTERACTION WITH SEC3.
RX PubMed=11283608; DOI=10.1038/35070029;
RA Guo W., Tamanoi F., Novick P.;
RT "Spatial regulation of the exocyst complex by Rho1 GTPase.";
RL Nat. Cell Biol. 3:353-360(2001).
RN [23]
RP FUNCTION, ACTIVITY REGULATION, AND INTERACTION WITH LRG1 AND SAC7.
RX PubMed=11447600; DOI=10.1002/yea.742;
RA Watanabe D., Abe M., Ohya Y.;
RT "Yeast Lrg1p acts as a specialized RhoGAP regulating 1,3-beta-glucan
RT synthesis.";
RL Yeast 18:943-951(2001).
RN [24]
RP FUNCTION.
RX PubMed=12419188; DOI=10.1016/s0960-9822(02)01238-1;
RA Tolliday N., VerPlank L., Li R.;
RT "Rho1 directs formin-mediated actin ring assembly during budding yeast
RT cytokinesis.";
RL Curr. Biol. 12:1864-1870(2002).
RN [25]
RP ACTIVITY REGULATION, AND INTERACTION WITH TUS1.
RX PubMed=11839800; DOI=10.1128/mcb.22.5.1329-1339.2002;
RA Schmelzle T., Helliwell S.B., Hall M.N.;
RT "Yeast protein kinases and the RHO1 exchange factor TUS1 are novel
RT components of the cell integrity pathway in yeast.";
RL Mol. Cell. Biol. 22:1329-1339(2002).
RN [26]
RP FUNCTION, AND INTERACTION WITH BAG7.
RX PubMed=12207708; DOI=10.1046/j.1365-2958.2002.03110.x;
RA Schmidt A., Schmelzle T., Hall M.N.;
RT "The RHO1-GAPs SAC7, BEM2 and BAG7 control distinct RHO1 functions in
RT Saccharomyces cerevisiae.";
RL Mol. Microbiol. 45:1433-1441(2002).
RN [27]
RP FUNCTION.
RX PubMed=12810699; DOI=10.1083/jcb.200212040;
RA Dong Y., Pruyne D., Bretscher A.;
RT "Formin-dependent actin assembly is regulated by distinct modes of Rho
RT signaling in yeast.";
RL J. Cell Biol. 161:1081-1092(2003).
RN [28]
RP INTERACTION WITH STE4, AND SUBCELLULAR LOCATION.
RX PubMed=12660244; DOI=10.1074/jbc.m212636200;
RA Bar E.E., Ellicott A.T., Stone D.E.;
RT "Gbetagamma recruits Rho1 to the site of polarized growth during mating in
RT budding yeast.";
RL J. Biol. Chem. 278:21798-21804(2003).
RN [29]
RP FUNCTION.
RX PubMed=12928491; DOI=10.1073/pnas.1834246100;
RA Valdivia R.H., Schekman R.;
RT "The yeasts Rho1p and Pkc1p regulate the transport of chitin synthase III
RT (Chs3p) from internal stores to the plasma membrane.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:10287-10292(2003).
RN [30]
RP FUNCTION, AND ACTIVITY REGULATION.
RX PubMed=15514049; DOI=10.1534/genetics.104.028027;
RA Fitch P.G., Gammie A.E., Lee D.J., Brizzio de Candal V., Rose M.D.;
RT "Lrg1p Is a Rho1 GTPase-activating protein required for efficient cell
RT fusion in yeast.";
RL Genetics 168:733-746(2004).
RN [31]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=15596542; DOI=10.1083/jcb.200404119;
RA Marelli M., Smith J.J., Jung S., Yi E., Nesvizhskii A.I., Christmas R.H.,
RA Saleem R.A., Tam Y.Y.C., Fagarasanu A., Goodlett D.R., Aebersold R.,
RA Rachubinski R.A., Aitchison J.D.;
RT "Quantitative mass spectrometry reveals a role for the GTPase Rho1p in
RT actin organization on the peroxisome membrane.";
RL J. Cell Biol. 167:1099-1112(2004).
RN [32]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Acts as a central regulator in the cell wall integrity
CC signaling pathway, which is regulated by the cell cycle and in response
CC to various types of cell wall stress. Integrates signals from different
CC cell surface sensors, and activates a set of effectors, regulating
CC processes including beta-glucan synthesis at the site of wall
CC remodeling, gene expression related to cell wall biogenesis,
CC organization of the actin cytoskeleton, and protein- and secretory
CC vesicle-targeting to the growth site. Activates the protein kinase C
CC (PKC1) MAP kinase cascade, the beta-1,3-glucan synthase (FKS1), the
CC formin BNI1, the exocyst component SEC3 and the transcription factor
CC SKN7. {ECO:0000269|PubMed:11283608, ECO:0000269|PubMed:11447600,
CC ECO:0000269|PubMed:12207708, ECO:0000269|PubMed:12419188,
CC ECO:0000269|PubMed:12810699, ECO:0000269|PubMed:12928491,
CC ECO:0000269|PubMed:15514049, ECO:0000269|PubMed:15596542,
CC ECO:0000269|PubMed:7579704, ECO:0000269|PubMed:8195291,
CC ECO:0000269|PubMed:8602514, ECO:0000269|PubMed:8602515,
CC ECO:0000269|PubMed:8621575, ECO:0000269|PubMed:8846785,
CC ECO:0000269|PubMed:8947028}.
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 -!- ACTIVITY REGULATION: Alternates between an inactive form bound to GDP
CC and an active form bound to GTP. Activated by the guanine nucleotide-
CC exchange factors (GEFs) ROM1, ROM2 and TUS1, and inactivated by GTPase-
CC activating proteins (GAPs) BAG7, BEM2, LRG1, and SAC7, and the Rho GDP-
CC dissociation inhibitor RDI1. The different GAPs regulate RHO1 in a
CC target-specific manner. {ECO:0000269|PubMed:11447600,
CC ECO:0000269|PubMed:11591390, ECO:0000269|PubMed:11839800,
CC ECO:0000269|PubMed:15514049, ECO:0000269|PubMed:7579704,
CC ECO:0000269|PubMed:8641285, ECO:0000269|PubMed:9038344,
CC ECO:0000269|PubMed:9242378}.
CC -!- SUBUNIT: Interacts with BEM4; the interaction is direct
CC (PubMed:8754839, PubMed:8754840). Interacts with SEC3; the interaction
CC is direct (PubMed:11283608). Interacts with the GAP BAG7
CC (PubMed:11591390, PubMed:12207708). Interacts with the GAP LRG1
CC (PubMed:11447600). Interacts with the GAP SAC7 (PubMed:11447600,
CC PubMed:9038344). Interacts with the GAP RDI1 (PubMed:9242378).
CC Interacts with the 1,3-beta-glucan synthase component FKS1
CC (PubMed:8602515). Interacts with the protein kinase PKC1
CC (PubMed:8621575, PubMed:8846785). Interacts with the G protein beta
CC subunit STE4 (PubMed:12660244). Interacts with SKN7 (PubMed:9535835).
CC Interacts with TUS1 (PubMed:11839800). Interacts with BNI1
CC (PubMed:8947028). {ECO:0000269|PubMed:11283608,
CC ECO:0000269|PubMed:11447600, ECO:0000269|PubMed:11591390,
CC ECO:0000269|PubMed:11839800, ECO:0000269|PubMed:12207708,
CC ECO:0000269|PubMed:12660244, ECO:0000269|PubMed:8602515,
CC ECO:0000269|PubMed:8621575, ECO:0000269|PubMed:8754839,
CC ECO:0000269|PubMed:8754840, ECO:0000269|PubMed:8846785,
CC ECO:0000269|PubMed:8947028, ECO:0000269|PubMed:9038344,
CC ECO:0000269|PubMed:9242378, ECO:0000269|PubMed:9535835}.
CC -!- INTERACTION:
CC P06780; Q99299: AIM44; NbExp=3; IntAct=EBI-15121, EBI-29423;
CC P06780; P38631: FKS1; NbExp=3; IntAct=EBI-15121, EBI-7708;
CC P06780; P33332: SEC3; NbExp=2; IntAct=EBI-15121, EBI-16850;
CC -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor. Endosome membrane;
CC Lipid-anchor. Peroxisome membrane; Lipid-anchor. Note=Plasma membrane-
CC associated at sites of polarized growth such as incipient bud sites,
CC bud tips, the bud neck during cytokinesis, and the neck and tip of
CC mating projections. Also found on internal membranes of endosomes and
CC peroxisomes.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rho family.
CC {ECO:0000305}.
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DR EMBL; M15189; AAA34977.1; -; Genomic_DNA.
DR EMBL; U25840; AAB68152.1; -; Genomic_DNA.
DR EMBL; M15161; AAA74729.1; -; Genomic_DNA.
DR EMBL; AY558062; AAS56388.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11582.1; -; Genomic_DNA.
DR PIR; A26587; TVBYH1.
DR RefSeq; NP_015491.1; NM_001184262.1.
DR PDB; 3A58; X-ray; 2.60 A; B/D/F=1-188.
DR PDBsum; 3A58; -.
DR AlphaFoldDB; P06780; -.
DR SMR; P06780; -.
DR BioGRID; 36338; 177.
DR ComplexPortal; CPX-1812; 1,3-beta-D-glucan synthase complex, FKS1-RHO1 variant.
DR ComplexPortal; CPX-1813; 1,3-beta-D-glucan synthase complex, FKS2-RHO1 variant.
DR ComplexPortal; CPX-3028; 1,3-beta-D-glucan synthase complex, FKS3-RHO1 variant.
DR DIP; DIP-1040N; -.
DR IntAct; P06780; 12.
DR MINT; P06780; -.
DR STRING; 4932.YPR165W; -.
DR DrugBank; DB12471; Ibrexafungerp.
DR iPTMnet; P06780; -.
DR MaxQB; P06780; -.
DR PaxDb; P06780; -.
DR PRIDE; P06780; -.
DR EnsemblFungi; YPR165W_mRNA; YPR165W; YPR165W.
DR GeneID; 856294; -.
DR KEGG; sce:YPR165W; -.
DR SGD; S000006369; RHO1.
DR VEuPathDB; FungiDB:YPR165W; -.
DR eggNOG; KOG0393; Eukaryota.
DR HOGENOM; CLU_041217_21_2_1; -.
DR InParanoid; P06780; -.
DR OMA; RWIPEIK; -.
DR BioCyc; YEAST:G3O-34294-MON; -.
DR Reactome; R-SCE-198203; PI3K/AKT activation.
DR Reactome; R-SCE-392451; G beta:gamma signalling through PI3Kgamma.
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-8980692; RHOA GTPase cycle.
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 EvolutionaryTrace; P06780; -.
DR PRO; PR:P06780; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; P06780; protein.
DR GO; GO:0000148; C:1,3-beta-D-glucan synthase complex; IDA:SGD.
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:0005933; C:cellular bud; HDA:SGD.
DR GO; GO:0005935; C:cellular bud neck; IDA:SGD.
DR GO; GO:0005934; C:cellular bud tip; 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:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000329; C:fungal-type vacuole membrane; IDA:SGD.
DR GO; GO:0005794; C:Golgi apparatus; IDA:SGD.
DR GO; GO:0000131; C:incipient cellular bud site; IDA:SGD.
DR GO; GO:0043332; C:mating projection tip; IDA:SGD.
DR GO; GO:0016020; C:membrane; IDA:ComplexPortal.
DR GO; GO:0005741; C:mitochondrial outer membrane; HDA:SGD.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0005778; C:peroxisomal membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005777; C:peroxisome; IDA:SGD.
DR GO; GO:0005886; C:plasma membrane; HDA:SGD.
DR GO; GO:0031681; F:G-protein beta-subunit binding; IPI: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:0006075; P:(1->3)-beta-D-glucan biosynthetic process; IDA:ComplexPortal.
DR GO; GO:0030036; P:actin cytoskeleton organization; IMP:SGD.
DR GO; GO:0031532; P:actin cytoskeleton reorganization; IGI:SGD.
DR GO; GO:0007015; P:actin filament organization; IBA:GO_Central.
DR GO; GO:0030476; P:ascospore wall assembly; IC:ComplexPortal.
DR GO; GO:0007117; P:budding cell bud growth; IMP:SGD.
DR GO; GO:0032186; P:cellular bud neck septin ring organization; IMP:SGD.
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:0009272; P:fungal-type cell wall biogenesis; IC:ComplexPortal.
DR GO; GO:0045807; P:positive regulation of endocytosis; IMP:SGD.
DR GO; GO:1903501; P:positive regulation of mitotic actomyosin contractile ring assembly; IMP:SGD.
DR GO; GO:0090037; P:positive regulation of protein kinase C signaling; IDA: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:0008361; P:regulation of cell size; IMP:SGD.
DR GO; GO:0090334; P:regulation of cell wall (1->3)-beta-D-glucan biosynthetic process; IDA:SGD.
DR GO; GO:0060178; P:regulation of exocyst localization; IMP:SGD.
DR GO; GO:0060237; P:regulation of fungal-type cell wall organization; IMP:SGD.
DR GO; GO:0032880; P:regulation of protein localization; IMP:SGD.
DR GO; GO:1903395; P:regulation of secondary cell septum biogenesis; IMP:SGD.
DR GO; GO:0032889; P:regulation of vacuole fusion, non-autophagic; IMP:SGD.
DR GO; GO:0007264; P:small GTPase mediated signal transduction; IDA: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 3D-structure; Acetylation; Cell membrane; Direct protein sequencing;
KW Endosome; GTP-binding; Hydrolase; Lipoprotein; Membrane; Methylation;
KW Nucleotide-binding; Peroxisome; Prenylation; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.5, ECO:0007744|PubMed:22814378"
FT CHAIN 2..206
FT /note="GTP-binding protein RHO1"
FT /id="PRO_0000198945"
FT PROPEP 207..209
FT /note="Removed in mature form"
FT /id="PRO_0000281275"
FT REGION 187..209
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 39..47
FT /note="Effector region"
FT /evidence="ECO:0000250"
FT BINDING 17..24
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P61586"
FT BINDING 64..68
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 122..125
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P61586"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000269|Ref.5, ECO:0007744|PubMed:22814378"
FT MOD_RES 206
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000250|UniProtKB:P62745"
FT LIPID 206
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:P62745"
FT MUTAGEN 22
FT /note="G->A: Abolishes GTP-binding."
FT MUTAGEN 24
FT /note="T->N: Abolishes GTP-binding."
FT /evidence="ECO:0000269|PubMed:8947028"
FT MUTAGEN 42
FT /note="T->A: Impairs interaction with targets."
FT /evidence="ECO:0000269|PubMed:8947028"
FT MUTAGEN 43
FT /note="V->T: Temperature sensitive growth defect."
FT /evidence="ECO:0000269|PubMed:8846785"
FT MUTAGEN 44
FT /note="F->Y: Temperature sensitive growth defect."
FT /evidence="ECO:0000269|PubMed:8846785"
FT MUTAGEN 45
FT /note="E->I: Temperature sensitive growth defect."
FT /evidence="ECO:0000269|PubMed:11574532,
FT ECO:0000269|PubMed:8846785"
FT MUTAGEN 45
FT /note="E->V: In RHO1-2; temperature sensitive, fails to
FT activate PKC1."
FT /evidence="ECO:0000269|PubMed:11574532,
FT ECO:0000269|PubMed:8846785"
FT MUTAGEN 60
FT /note="L->P: In RHO1-3; temperature sensitive, severely
FT decreases beta-1,3-glucan synthase activation."
FT /evidence="ECO:0000269|PubMed:11574532"
FT MUTAGEN 68
FT /note="Q->H: Locks RHO1 in the GTP-bound form by abolishing
FT GTP hydrolysis."
FT /evidence="ECO:0000269|PubMed:3543936"
FT MUTAGEN 70
FT /note="D->G: In RHO1-10; temperature sensitive, severely
FT decreases beta-1,3-glucan synthase activation; when
FT associated with P-165."
FT /evidence="ECO:0000269|PubMed:11574532"
FT MUTAGEN 102
FT /note="E->K: In RHO1-11; temperature sensitive, severely
FT decreases beta-1,3-glucan synthase activation; when
FT associated with E-166."
FT /evidence="ECO:0000269|PubMed:11574532"
FT MUTAGEN 104
FT /note="W->R: In RHO1-4; temperature sensitive, severely
FT decreases beta-1,3-glucan synthase activation."
FT /evidence="ECO:0000269|PubMed:11574532"
FT MUTAGEN 121
FT /note="G->C: In RHO1-5; temperature sensitive, fails to
FT activate PCK1."
FT /evidence="ECO:0000269|PubMed:11574532"
FT MUTAGEN 165
FT /note="S->P: In RHO1-10; temperature sensitive, severely
FT decreases beta-1,3-glucan synthase activation; when
FT associated with G-69."
FT /evidence="ECO:0000269|PubMed:11574532"
FT MUTAGEN 167
FT /note="K->E: In RHO1-11; temperature sensitive, severely
FT decreases beta-1,3-glucan synthase activation; when
FT associated with K-101."
FT /evidence="ECO:0000269|PubMed:11574532"
FT STRAND 9..18
FT /evidence="ECO:0007829|PDB:3A58"
FT HELIX 23..31
FT /evidence="ECO:0007829|PDB:3A58"
FT STRAND 45..53
FT /evidence="ECO:0007829|PDB:3A58"
FT STRAND 56..64
FT /evidence="ECO:0007829|PDB:3A58"
FT HELIX 69..77
FT /evidence="ECO:0007829|PDB:3A58"
FT STRAND 83..90
FT /evidence="ECO:0007829|PDB:3A58"
FT HELIX 94..102
FT /evidence="ECO:0007829|PDB:3A58"
FT HELIX 104..111
FT /evidence="ECO:0007829|PDB:3A58"
FT STRAND 117..122
FT /evidence="ECO:0007829|PDB:3A58"
FT HELIX 124..126
FT /evidence="ECO:0007829|PDB:3A58"
FT HELIX 130..138
FT /evidence="ECO:0007829|PDB:3A58"
FT HELIX 146..155
FT /evidence="ECO:0007829|PDB:3A58"
FT STRAND 161..163
FT /evidence="ECO:0007829|PDB:3A58"
FT TURN 166..168
FT /evidence="ECO:0007829|PDB:3A58"
FT HELIX 172..184
FT /evidence="ECO:0007829|PDB:3A58"
SQ SEQUENCE 209 AA; 23152 MW; 630B17E9E34CFE75 CRC64;
MSQQVGNSIR RKLVIVGDGA CGKTCLLIVF SKGQFPEVYV PTVFENYVAD VEVDGRRVEL
ALWDTAGQED YDRLRPLSYP DSNVVLICFS IDLPDSLENV QEKWIAEVLH FCQGVPIILV
GCKVDLRNDP QTIEQLRQEG QQPVTSQEGQ SVADQIGATG YYECSAKTGY GVREVFEAAT
RASLMGKSKT NGKAKKNTTE KKKKKCVLL
