P06780 (RHO1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
GTP-binding protein RHO1

Alternative name(s):
Rho-type GTPase 1

Gene names

Name:	RHO1
Ordered Locus Names:	YPR165W
ORF Names:	P9325.3

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	209 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Acts as a central regulator in the cell wall integrity signaling pathway, which is regulated by the cell cycle and in response to various types of cell wall stress. Integrates signals from different cell surface sensors, and activates a set of effectors, regulating processes including beta-glucan synthesis at the site of wall remodeling, gene expression related to cell wall biogenesis, organization of the actin cytoskeleton, and protein- and secretory vesicle-targeting to the growth site. Activates the protein kinase C (PKC1) MAP kinase cascade, the beta-1,3-glucan synthase (FKS1), the formin BNI1, the exocyst component SEC3 and the transcription factor SKN7. Ref.7 Ref.8 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.20 Ref.21 Ref.22 Ref.24 Ref.25 Ref.27 Ref.28 Ref.29
Enzyme regulation	Alternates between an inactive form bound to GDP and an active form bound to GTP. Activated by the guanine nucleotide-exchange factors (GEFs) ROM1, ROM2 and TUS1, and inactivated by GTPase-activating proteins (GAPs) BAG7, BEM2, LRG1, and SAC7, and the Rho GDP-dissociation inhibitor RDI1. The different GAPs regulate RHO1 in a target-specific manner. Ref.8 Ref.9 Ref.15 Ref.16 Ref.18 Ref.21 Ref.23 Ref.28
Subunit structure	Interacts with the GAPs BAG7, LRG1, SAC7, and with RDI1. Interacts with the 1,3-beta-glucan synthase component FKS1, with protein kinase PKC1, with the G protein beta subunit STE4 and with SKN7. Ref.10 Ref.11 Ref.12 Ref.14 Ref.15 Ref.16 Ref.17 Ref.18 Ref.20 Ref.21 Ref.23 Ref.24 Ref.26
Subcellular location	Cell membrane; Lipid-anchor. Endosome membrane; Lipid-anchor. Peroxisome membrane; Lipid-anchor. Note: Plasma membrane-associated at sites of polarized growth such as incipient bud sites, bud tips, the bud neck during cytokinesis, and the neck and tip of mating projections. Also found on internal membranes of endosomes and peroxisomes. Ref.7 Ref.13 Ref.26 Ref.29
Sequence similarities	Belongs to the small GTPase superfamily. Rho family.

Ontologies

Keywords
Cellular component	Cell membrane Endosome Membrane Peroxisome
Ligand	GTP-binding Nucleotide-binding
PTM	Acetylation Lipoprotein Methylation Prenylation
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	actin cytoskeleton reorganization Inferred from physical interaction Ref.11. Source: SGD budding cell bud growth Inferred from mutant phenotype Ref.7. Source: SGD positive regulation of endocytosis Inferred from mutant phenotype. Source: SGD positive regulation of protein kinase C signaling cascade Inferred from direct assay Ref.12. Source: SGD regulation of cell size Inferred from mutant phenotype. Source: SGD regulation of exocyst localization Inferred from mutant phenotype Ref.20. Source: SGD regulation of fungal-type cell wall (1->3)-alpha-glucan biosynthetic process Inferred from direct assay. Source: SGD regulation of fungal-type cell wall organization Inferred from mutant phenotype Ref.12. Source: SGD regulation of vacuole fusion, non-autophagic Inferred from mutant phenotype. Source: SGD small GTPase mediated signal transduction Inferred from direct assay Ref.12. Source: SGD
Cellular component	1,3-beta-D-glucan synthase complex Inferred from direct assay Ref.14. Source: SGD Golgi apparatus Inferred from direct assay. Source: SGD cellular bud neck Inferred from direct assay Ref.7. Source: SGD cellular bud tip Inferred from direct assay Ref.7. Source: SGD endosome membrane Inferred from electronic annotation. Source: UniProtKB-SubCell incipient cellular bud site Inferred from direct assay Ref.7. Source: SGD mating projection tip Inferred from direct assay Ref.26. Source: SGD mitochondrial outer membrane Inferred from direct assay. Source: SGD peroxisomal membrane Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membrane enriched fraction Inferred from direct assay. Source: SGD
Molecular function	GTP binding Inferred from electronic annotation. Source: UniProtKB-KW GTPase activity Inferred from direct assay Ref.18. Source: SGD protein binding Inferred from physical interaction Ref.14. Source: IntAct signal transducer activity Traceable author statement. Source: SGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
FKS1	P38631	3	EBI-15121,EBI-7708

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.5

Chain

2 – 206

205

GTP-binding protein RHO1

PRO_0000198945

Propeptide

207 – 209

3

Removed in mature form

PRO_0000281275

Regions

Nucleotide binding

17 – 24

8

GTP By similarity

Nucleotide binding

64 – 68

5

GTP By similarity

Nucleotide binding

122 – 125

4

GTP By similarity

Motif

39 – 47

9

Effector region By similarity

Amino acid modifications

Modified residue

2

1

N-acetylserine Ref.5

Modified residue

206

1

Cysteine methyl ester

Lipidation

206

1

S-geranylgeranyl cysteine

Experimental info

Mutagenesis

22

1

G → A: Abolishes GTP-binding.

Mutagenesis

24

1

T → N: Abolishes GTP-binding. Ref.11

Mutagenesis

42

1

T → A: Impairs interaction with targets. Ref.11

Mutagenesis

43

1

V → T: Temperature sensitive growth defect. Ref.10

Mutagenesis

44

1

F → Y: Temperature sensitive growth defect. Ref.10

Mutagenesis

45

1

E → I: Temperature sensitive growth defect. Ref.10 Ref.19

Mutagenesis

45

1

E → V in RHO1-2; temperature sensitive, fails to activate PKC1. Ref.10 Ref.19

Mutagenesis

60

1

L → P in RHO1-3; temperature sensitive, severely decreases beta-1,3-glucan synthase activation. Ref.19

Mutagenesis

68

1

Q → H: Locks RHO1 in the GTP-bound form by abolishing GTP hydrolysis. Ref.1

Mutagenesis

70

1

D → G in RHO1-10; temperature sensitive, severely decreases beta-1,3-glucan synthase activation; when associated with P-165. Ref.19

Mutagenesis

102

1

E → K in RHO1-11; temperature sensitive, severely decreases beta-1,3-glucan synthase activation; when associated with E-166. Ref.19

Mutagenesis

104

1

W → R in RHO1-4; temperature sensitive, severely decreases beta-1,3-glucan synthase activation. Ref.19

Mutagenesis

121

1

G → C in RHO1-5; temperature sensitive, fails to activate PCK1. Ref.19

Mutagenesis

165

1

S → P in RHO1-10; temperature sensitive, severely decreases beta-1,3-glucan synthase activation; when associated with G-69. Ref.19

Mutagenesis

167

1

K → E in RHO1-11; temperature sensitive, severely decreases beta-1,3-glucan synthase activation; when associated with K-101. Ref.19

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

209

Helix Strand Turn

Details...

Beta strand

9 – 16

8

Helix

24 – 31

8

Beta strand

45 – 52

8

Beta strand

57 – 64

8

Helix

69 – 78

10

Beta strand

83 – 88

6

Helix

94 – 102

9

Helix

104 – 111

8

Beta strand

117 – 120

4

Helix

124 – 126

3

Helix

130 – 138

9

Helix

151 – 155

5

Helix

173 – 184

12

Sequences

	Sequence		Length	Mass (Da)
	P06780 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 630B17E9E34CFE75	FASTA	209	23,152
	10 20 30 40 50 60 MSQQVGNSIR RKLVIVGDGA CGKTCLLIVF SKGQFPEVYV PTVFENYVAD VEVDGRRVEL 70 80 90 100 110 120 ALWDTAGQED YDRLRPLSYP DSNVVLICFS IDLPDSLENV QEKWIAEVLH FCQGVPIILV 130 140 150 160 170 180 GCKVDLRNDP QTIEQLRQEG QQPVTSQEGQ SVADQIGATG YYECSAKTGY GVREVFEAAT 190 200 RASLMGKSKT NGKAKKNTTE KKKKKCVLL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Characterization of two members of the rho gene family from the yeast Saccharomyces cerevisiae." Madaule P., Axel R., Myers A.M. Proc. Natl. Acad. Sci. U.S.A. 84:779-783(1987) [PubMed: 3543936] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], MUTAGENESIS OF GLN-68.
[2]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI." Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W., Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D., Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E., Churcher C.M. , Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H., DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N., Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K., Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M., Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A., Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S., Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D., Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S., Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B., Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A., Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R., Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A., Vo D.H., Hani J. Nature 387:103-105(1997) [PubMed: 9169875] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[3]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[4]	"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae." Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J. , Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., LaBaer J. Genome Res. 17:536-543(2007) [PubMed: 17322287] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[5]	Bienvenut W.V., Peters C. Submitted (MAY-2005) to UniProtKB Cited for: PROTEIN SEQUENCE OF 2-10; 13-73; 104-123; 128-137 AND 168-181, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2, MASS SPECTROMETRY.
[6]	"Assembly of the mitochondrial membrane system. MRP1 and MRP2, two yeast nuclear genes coding for mitochondrial ribosomal proteins." Myers A.M., Crivellone M.D., Tzagoloff A. J. Biol. Chem. 262:3388-3397(1987) [PubMed: 3029111] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 201-209.
[7]	"Growth site localization of Rho1 small GTP-binding protein and its involvement in bud formation in Saccharomyces cerevisiae." Yamochi W., Tanaka K., Nonaka H., Maeda A., Musha T., Takai Y. J. Cell Biol. 125:1077-1093(1994) [PubMed: 8195291] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION.
[8]	"The rho-GAP encoded by BEM2 regulates cytoskeletal structure in budding yeast." Wang T., Bretscher A. Mol. Biol. Cell 6:1011-1024(1995) [PubMed: 7579704] [Abstract] Cited for: FUNCTION, ENZYME REGULATION.
[9]	"Rom1p and Rom2p are GDP/GTP exchange proteins (GEPs) for the Rho1p small GTP binding protein in Saccharomyces cerevisiae." Ozaki K., Tanaka K., Imamura H., Hihara T., Kameyama T., Nonaka H., Hirano H., Matsuura Y., Takai Y. EMBO J. 15:2196-2207(1996) [PubMed: 8641285] [Abstract] Cited for: ENZYME REGULATION.
[10]	"A downstream target of RHO1 small GTP-binding protein is PKC1, a homolog of protein kinase C, which leads to activation of the MAP kinase cascade in Saccharomyces cerevisiae." Nonaka H., Tanaka K., Hirano H., Fujiwara T., Kohno H., Umikawa M., Mino A., Takai Y. EMBO J. 14:5931-5938(1995) [PubMed: 8846785] [Abstract] Cited for: FUNCTION, INTERACTION WITH PKC1, MUTAGENESIS OF VAL-43; PHE-44 AND GLU-45.
[11]	"Bni1p implicated in cytoskeletal control is a putative target of Rho1p small GTP binding protein in Saccharomyces cerevisiae." Kohno H., Tanaka K., Mino A., Umikawa M., Imamura H., Fujiwara T., Fujita Y., Hotta K., Qadota H., Watanabe T., Ohya Y., Takai Y. EMBO J. 15:6060-6068(1996) [PubMed: 8947028] [Abstract] Cited for: FUNCTION, INTERACTION WITH BNI1, MUTAGENESIS OF THR-24 AND THR-42.
[12]	"Activation of yeast protein kinase C by Rho1 GTPase." Kamada Y., Qadota H., Python C.P., Anraku Y., Ohya Y., Levin D.E. J. Biol. Chem. 271:9193-9196(1996) [PubMed: 8621575] [Abstract] Cited for: FUNCTION, INTERACTION WITH PKC1.
[13]	"Rho1p, a yeast protein at the interface between cell polarization and morphogenesis." Drgonova J., Drgon T., Tanaka K., Kollar R., Chen G.-C., Ford R.A., Chan C.S.M., Takai Y., Cabib E. Science 272:277-279(1996) [PubMed: 8602514] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION.
[14]	"Identification of yeast Rho1p GTPase as a regulatory subunit of 1,3-beta-glucan synthase." Qadota H., Python C.P., Inoue S.B., Arisawa M., Anraku Y., Zheng Y., Watanabe T., Levin D.E., Ohya Y. Science 272:279-281(1996) [PubMed: 8602515] [Abstract] Cited for: FUNCTION, INTERACTION WITH FKS1.
[15]	"The yeast phosphatidylinositol kinase homolog TOR2 activates RHO1 and RHO2 via the exchange factor ROM2." Schmidt A., Bickle M., Beck T., Hall M.N. Cell 88:531-542(1997) [PubMed: 9038344] [Abstract] Cited for: ENZYME REGULATION, INTERACTION WITH SAC7.
[16]	"Association of the Rho family small GTP-binding proteins with Rho GDP dissociation inhibitor (Rho GDI) in Saccharomyces cerevisiae." Koch G., Tanaka K., Masuda T., Yamochi W., Nonaka H., Takai Y. Oncogene 15:417-422(1997) [PubMed: 9242378] [Abstract] Cited for: ENZYME REGULATION, INTERACTION WITH RDI1.
[17]	"Analysis of RhoA-binding proteins reveals an interaction domain conserved in heterotrimeric G protein beta subunits and the yeast response regulator protein Skn7." Alberts A.S., Bouquin N., Johnston L.H., Treisman R. J. Biol. Chem. 273:8616-8622(1998) [PubMed: 9535835] [Abstract] Cited for: INTERACTION WITH SKN7.
[18]	"Functional characterization of the Bag7, Lrg1 and Rgd2 RhoGAP proteins from Saccharomyces cerevisiae." Roumanie O., Weinachter C., Larrieu I., Crouzet M., Doignon F. FEBS Lett. 506:149-156(2001) [PubMed: 11591390] [Abstract] Cited for: ENZYME REGULATION, INTERACTION WITH BAG7.
[19]	"Complementing yeast rho1 mutation groups with distinct functional defects." Saka A., Abe M., Okano H., Minemura M., Qadota H., Utsugi T., Mino A., Tanaka K., Takai Y., Ohya Y. J. Biol. Chem. 276:46165-46171(2001) [PubMed: 11574532] [Abstract] Cited for: MUTAGENESIS OF GLU-45; LEU-60; ASP-70; GLU-102; TRP-104; GLY-121; SER-165 AND LYS-167.
[20]	"Spatial regulation of the exocyst complex by Rho1 GTPase." Guo W., Tamanoi F., Novick P. Nat. Cell Biol. 3:353-360(2001) [PubMed: 11283608] [Abstract] Cited for: FUNCTION, INTERACTION WITH SEC3.
[21]	"Yeast Lrg1p acts as a specialized RhoGAP regulating 1,3-beta-glucan synthesis." Watanabe D., Abe M., Ohya Y. Yeast 18:943-951(2001) [PubMed: 11447600] [Abstract] Cited for: FUNCTION, ENZYME REGULATION, INTERACTION WITH LRG1 AND SAC7.
[22]	"Rho1 directs formin-mediated actin ring assembly during budding yeast cytokinesis." Tolliday N., VerPlank L., Li R. Curr. Biol. 12:1864-1870(2002) [PubMed: 12419188] [Abstract] Cited for: FUNCTION.
[23]	"Yeast protein kinases and the RHO1 exchange factor TUS1 are novel components of the cell integrity pathway in yeast." Schmelzle T., Helliwell S.B., Hall M.N. Mol. Cell. Biol. 22:1329-1339(2002) [PubMed: 11839800] [Abstract] Cited for: ENZYME REGULATION, INTERACTION WITH TUS1.
[24]	"The RHO1-GAPs SAC7, BEM2 and BAG7 control distinct RHO1 functions in Saccharomyces cerevisiae." Schmidt A., Schmelzle T., Hall M.N. Mol. Microbiol. 45:1433-1441(2002) [PubMed: 12207708] [Abstract] Cited for: FUNCTION, INTERACTION WITH BAG7.
[25]	"Formin-dependent actin assembly is regulated by distinct modes of Rho signaling in yeast." Dong Y., Pruyne D., Bretscher A. J. Cell Biol. 161:1081-1092(2003) [PubMed: 12810699] [Abstract] Cited for: FUNCTION.
[26]	"Gbetagamma recruits Rho1 to the site of polarized growth during mating in budding yeast." Bar E.E., Ellicott A.T., Stone D.E. J. Biol. Chem. 278:21798-21804(2003) [PubMed: 12660244] [Abstract] Cited for: INTERACTION WITH STE4, SUBCELLULAR LOCATION.
[27]	"The yeasts Rho1p and Pkc1p regulate the transport of chitin synthase III (Chs3p) from internal stores to the plasma membrane." Valdivia R.H., Schekman R. Proc. Natl. Acad. Sci. U.S.A. 100:10287-10292(2003) [PubMed: 12928491] [Abstract] Cited for: FUNCTION.
[28]	"Lrg1p Is a Rho1 GTPase-activating protein required for efficient cell fusion in yeast." Fitch P.G., Gammie A.E., Lee D.J., Brizzio de Candal V., Rose M.D. Genetics 168:733-746(2004) [PubMed: 15514049] [Abstract] Cited for: FUNCTION, ENZYME REGULATION.
[29]	"Quantitative mass spectrometry reveals a role for the GTPase Rho1p in actin organization on the peroxisome membrane." Marelli M., Smith J.J., Jung S., Yi E., Nesvizhskii A.I., Christmas R.H., Saleem R.A., Tam Y.Y.C., Fagarasanu A., Goodlett D.R., Aebersold R., Rachubinski R.A., Aitchison J.D. J. Cell Biol. 167:1099-1112(2004) [PubMed: 15596542] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M15189 Genomic DNA. Translation: AAA34977.1.
U25840 Genomic DNA. Translation: AAB68152.1.
M15161 Genomic DNA. Translation: AAA74729.1.
AY558062 Genomic DNA. Translation: AAS56388.1.
BK006949 Genomic DNA. Translation: DAA11582.1.

PIR

TVBYH1. A26587.

RefSeq

NP_015491.1. NM_001184262.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3A58	X-ray	2.60	B/D/F	1-188	[»]

ProteinModelPortal

P06780.

SMR

P06780. Positions 7-187.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-1040N.

IntAct

P06780. 13 interactions.

MINT

MINT-399819.

STRING

P06780.

Proteomic databases

PeptideAtlas

P06780.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblFungi

YPR165W; YPR165W; YPR165W.

GeneID

856294.

KEGG

sce:YPR165W.

NMPDR

fig|4932.3.peg.6637.

Organism-specific databases

SGD

S000006369. RHO1.

Phylogenomic databases

eggNOG

fuNOG04623.

GeneTree

EFGT00070000008719.

HOGENOM

HBG745225.

OMA

KWIAEVL.

OrthoDB

EOG48KVMG.

Gene expression databases

ArrayExpress

P06780.

Genevestigator

P06780.

GermOnline

YPR165W. Saccharomyces cerevisiae.

Family and domain databases

InterPro

IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
IPR003578. Small_GTPase_Rho.
[Graphical view]

KO

K07975.

Pfam

PF00071. Ras. 1 hit.
[Graphical view]

PRINTS

PR00449. RASTRNSFRMNG.

SMART

SM00174. RHO. 1 hit.
[Graphical view]

TIGRFAMs

TIGR00231. Small_GTP. 1 hit.

PROSITE

PS51420. RHO. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

981641.

Entry information

Entry name

RHO1_YEAST

Accession

Primary (citable) accession number: P06780
Secondary accession number(s): D6W4G6

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 1, 1988
Last sequence update:	January 23, 2007
Last modified:	January 25, 2012
This is version 129 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program