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P35688 (LRG1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 137. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Rho-GTPase-activating protein LRG1
Alternative name(s):
LIM-RhoGAP protein 1
Gene names
Name:LRG1
Ordered Locus Names:YDL240W
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length1017 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Acts in signal transduction. Activates CDC42, RHO1 and RHO2. Negatively regulates 1,3-beta-glucan synthesis. May be responsible for the down-regulation of CDC42 during mating. Ref.4 Ref.5

Subunit structure

Interacts with CDC42, RHO1 and RHO2. Ref.4 Ref.5

Subcellular location

Cytoplasm. Bud. Bud neck. Note: Localized to the bud site during bud formation and at the bud neck during cytokinesis. Ref.5 Ref.6

Developmental stage

Highly expressed during sporulation.

Miscellaneous

Present with 468 molecules/cell in log phase SD medium.

Sequence similarities

Contains 4 LIM zinc-binding domains.

Contains 1 Rho-GAP domain.

Ontologies

Keywords
   Biological processSporulation
   Cellular componentCytoplasm
   DomainLIM domain
Repeat
   LigandMetal-binding
Zinc
   Molecular functionGTPase activation
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcytogamy

Inferred from mutant phenotype PubMed 15514049. Source: SGD

negative regulation of Rho protein signal transduction

Inferred from mutant phenotype PubMed 11713681. Source: SGD

negative regulation of protein kinase C signaling

Inferred from mutant phenotype PubMed 11713681. Source: SGD

positive regulation of Rho GTPase activity

Inferred from direct assay PubMed 15514049. Source: SGD

regulation of cell wall (1->3)-beta-D-glucan biosynthetic process

Inferred from genetic interaction Ref.5. Source: SGD

regulation of fungal-type cell wall organization

Inferred from mutant phenotype PubMed 11713681. Source: SGD

signal transduction

Inferred from electronic annotation. Source: InterPro

sporulation resulting in formation of a cellular spore

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcellular bud neck

Inferred from direct assay Ref.5PubMed 23613772. Source: SGD

cellular bud tip

Inferred from direct assay Ref.5. Source: SGD

cytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

incipient cellular bud site

Inferred from direct assay Ref.5. Source: SGD

mating projection tip

Inferred from direct assay PubMed 15514049. Source: SGD

site of polarized growth

Inferred from direct assay PubMed 23613772. Source: SGD

   Molecular_functionRho GTPase activator activity

Inferred from direct assay PubMed 15514049. Source: SGD

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 10171017Rho-GTPase-activating protein LRG1
PRO_0000075838

Regions

Domain28 – 8861LIM zinc-binding 1
Domain98 – 14851LIM zinc-binding 2
Domain155 – 18430LIM zinc-binding 3; truncated
Domain419 – 47456LIM zinc-binding 4
Domain730 – 953224Rho-GAP

Amino acid modifications

Modified residue11N-acetylmethionine Ref.9
Modified residue5621Phosphoserine Ref.8

Experimental info

Sequence conflict5311Q → H in CAA98820. Ref.2
Sequence conflict7661R → S in CAA55210. Ref.1
Sequence conflict7911N → T in CAA55210. Ref.1
Sequence conflict8211L → Q in CAA55210. Ref.1
Sequence conflict8381A → S in CAA55210. Ref.1
Sequence conflict8491V → L in CAA55210. Ref.1
Sequence conflict8951S → F in CAA55210. Ref.1
Sequence conflict9281A → T in CAA55210. Ref.1
Sequence conflict9351Y → S in CAA55210. Ref.1
Sequence conflict977 – 101741INHFI…GEINK → TILFPPLCKVKQSIIPNVT in CAA55210. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P35688 [UniParc].

Last modified July 27, 2011. Version 3.
Checksum: 862EC5EF7E57E679

FASTA1,017116,651
        10         20         30         40         50         60 
MIQNSAGYRS LNTASPMTVQ VKNQKKICAR CNKLVIPDSQ RTKTTLKALG KYYHESCFTC 

        70         80         90        100        110        120 
QDCQKPLKPK YFPYQVDKTS ESILLCQYDY FRRHNLLCHV CDTPLRGLYY TAFGYRYDEE 

       130        140        150        160        170        180 
HFSCTICATP CGVKKCFMYG NQLYCKYHFL KYFSKRCKGC EFPISDQYIE FPKGEEIHCW 

       190        200        210        220        230        240 
HPECYGIHKY WHVNLAAETV GLQYLPKLEY NPNSGDKDIN PTAYELDKQM QAFNFILSKT 

       250        260        270        280        290        300 
WSVLYRFEEE AASCISDMFQ YLTSNDQLKG IESTGLLVLK IDCLFRGLDT LNLSTNKSMP 

       310        320        330        340        350        360 
VNSDQECIEN NAMAASKYSK FPKNLSTKIM IYLQLLRKLG TENKNETITI SSFMSVITGL 

       370        380        390        400        410        420 
AHFLKLLTRF GLYTALENNK LTHSVNPLLR FLREVEKNEL FENNPFQYIK TPVNATDSCA 

       430        440        450        460        470        480 
GCNKYIQEEC IQFYEHRWHI ACFTCSSCHK NINPRSLTDP TFNKEKKKIL CSHCSIDDPA 

       490        500        510        520        530        540 
SVPGFKFVTK LAQLIFLLKI ALVKSRTVML KSKASNKVGR NSLQSTMLKE QTYIRTLNDI 

       550        560        570        580        590        600 
KRLRSRRESV RVTHNKQQAR KSVILETAET DLNDPTKQGD SKNLVIQTDD PSSSQQVSTR 

       610        620        630        640        650        660 
ENVFSNTKTL TLDDISRIVA AEQARELRPN AFAHFKKLKE TDDETSNVVP KKSGVYYSEL 

       670        680        690        700        710        720 
STMELSMIRA ISLSLLAGKQ LISKTDPNYT SLVSMVFSNE KQVTGSFWNR MKIMMSMEPK 

       730        740        750        760        770        780 
KPITKTVFGA PLDVLCEKWG VDSDLGVGPV KIRIPIIIDE LISSLRQMDM SVEGIFRKNG 

       790        800        810        820        830        840 
NIRRLRELTA NIDSNPTEAP DFSKENAIQL SALLKKFIRE LPQPILSTDL YELWIKAAKI 

       850        860        870        880        890        900 
DLEDEKQRVI LLIYSLLPTY NRNLLEALLS FLHWTSSFSY IENEMGSKMD IHNLSTVITP 

       910        920        930        940        950        960 
NILYLRHKEI SNDNVPDEPE SGLVDSFAQN KGENYFLAIE IVDYLITHNE EMAMVPKFLM 

       970        980        990       1000       1010 
NLLKDVQLQK LDNYESINHF ISTVMQSKTI DYSECDIKTP VTVKDSTTTV IQGEINK 

« Hide

References

« Hide 'large scale' references
[1]"LRG1 is expressed during sporulation in Saccharomyces cerevisiae and contains motifs similar to LIM and rho/racGAP domains."
Mueller A., Xu G., Wells R., Hollenberg C.P., Piepersberg W.
Nucleic Acids Res. 22:3151-3154(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: DBY874.
[2]"The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."
Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T. expand/collapse author list , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P.
Nature 387:75-78(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[3]Saccharomyces Genome Database
Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION, SEQUENCE REVISION TO 531.
Strain: ATCC 204508 / S288c.
[4]"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] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH CDC42; RHO1 AND RHO2.
[5]"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] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH RHO1, SUBCELLULAR LOCATION.
[6]"Global analysis of protein localization in budding yeast."
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K.
Nature 425:686-691(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[7]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[8]"Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-562, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[9]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X78453 Genomic DNA. Translation: CAA55210.1.
Z74288 Genomic DNA. Translation: CAA98820.1.
BK006938 Genomic DNA. Translation: DAA11626.2.
PIRS67804.
RefSeqNP_010041.2. NM_001180300.2.

3D structure databases

ProteinModelPortalP35688.
SMRP35688. Positions 26-187, 419-452, 719-960.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid31871. 53 interactions.
DIPDIP-2588N.
IntActP35688. 4 interactions.
MINTMINT-422580.
STRING4932.YDL240W.

Proteomic databases

PaxDbP35688.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYDL240W; YDL240W; YDL240W.
GeneID851358.
KEGGsce:YDL240W.

Organism-specific databases

CYGDYDL240w.
SGDS000002399. LRG1.

Phylogenomic databases

eggNOGNOG267887.
GeneTreeENSGT00740000115221.
HOGENOMHOG000165645.
OMAHTNHFTC.
OrthoDBEOG73FQVZ.

Enzyme and pathway databases

BioCycYEAST:G3O-29617-MONOMER.

Gene expression databases

GenevestigatorP35688.

Family and domain databases

Gene3D1.10.555.10. 1 hit.
2.10.110.10. 3 hits.
InterProIPR008936. Rho_GTPase_activation_prot.
IPR000198. RhoGAP_dom.
IPR001781. Znf_LIM.
[Graphical view]
PfamPF00412. LIM. 3 hits.
PF00620. RhoGAP. 1 hit.
[Graphical view]
SMARTSM00132. LIM. 3 hits.
SM00324. RhoGAP. 1 hit.
[Graphical view]
SUPFAMSSF48350. SSF48350. 1 hit.
PROSITEPS00478. LIM_DOMAIN_1. 2 hits.
PS50023. LIM_DOMAIN_2. 3 hits.
PS50238. RHOGAP. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio968456.

Entry information

Entry nameLRG1_YEAST
AccessionPrimary (citable) accession number: P35688
Secondary accession number(s): D6VRB6, Q07735
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: July 27, 2011
Last modified: April 16, 2014
This is version 137 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome IV

Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families