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Reviewed, UniProtKB/Swiss-Prot P35688 (LRG1_YEAST)

Last modified November 4, 2008. Version 86. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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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 (Baker's yeast) [Complete proteome]
Taxonomic identifier4932 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

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Protein attributes

Sequence length1017 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

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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.

Subunit structure

Interacts with CDC42, RHO1 and RHO2.

Subcellular location

Cytoplasm. Bud. Bud neck. Note= Localized to the bud site during bud formation and at the bud neck during cytokinesis.

Developmental stage

Highly expressed during sporulation.

Miscellaneous

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

Sequence similarities

Contains 3 LIM zinc-binding domains.

Contains 1 Rho-GAP domain.

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Ontologies

Keywords

   Biological processSporulation
   Cellular componentCytoplasm
   DomainLIM domain
Repeat
   LigandMetal-binding
Zinc
   Molecular functionGTPase activation
   PTMPhosphoprotein
   Technical termComplete proteome

Gene Ontology (GO)

   Biological processfungal-type cell wall biogenesis Ref.4

Inferred from genetic interaction. Source: SGD

small GTPase mediated signal transduction Ref.3

Inferred from physical interaction. Source: SGD

   Cellular componentcellular bud neck

Inferred from direct assay. Source: SGD

mitochondrion

Inferred from direct assay. Source: SGD

   Molecular functionRho GTPase activator activity Ref.3

Inferred from direct assay. Source: SGD

Complete GO annotation...

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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 residue5621Phosphoserine

Experimental info

Sequence conflict5311H → Q in CAA55210. Ref.1
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

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Sequences

Sequence LengthMass (Da)Tools
P35688-1 [UniParc].

Last modified November 1, 1997. Version 2.
Checksum: DDEB79B4BBEBBB09

FASTA1,017116,660
        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 HTYIRTLNDI 

       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

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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: 8065929] [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: 9169867] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[3]"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: FUNCTION, INTERACTION WITH CDC42; RHO1 AND RHO2.
[4]"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, INTERACTION WITH RHO1, SUBCELLULAR LOCATION.
[5]"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: 14562106] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[6]"A multidimensional chromatography technology for in-depth phosphoproteome analysis."
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed: 18407956] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-562, MASS SPECTROMETRY.
+Additional computationally mapped references.

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Cross-references

Sequence databases

X78453 Genomic DNA. Translation: CAA55210.1.
Z74288 Genomic DNA. Translation: CAA98820.1.
PIRS67804.
RefSeqNP_010041.1.

3D structure databases

HSSPHSSP built from PDB template 1RGP based on UniProtKB Q07960.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP:2588N.
IntActP35688.

Genome annotation databases

EnsemblYDL240W. Saccharomyces cerevisiae. [Contig view]
GeneID851358.
GenomeReviewsGene locus YDL240W in contig Z71256_GR.
KEGGsce:YDL240W.
NMPDRfig|4932.3.peg.774.

Organism-specific databases

CYGDYDL240w.
SGDS000002399. LRG1.
Yeast-GFPSearch...

Phylogenomic databases

HOGENOMP35688.

Gene expression databases

ArrayExpressP35688.
GermOnlineYDL240W. Saccharomyces cerevisiae.

Family and domain databases

InterProIPR000198. RhoGAP.
IPR001781. Znf_LIM.
[Graphical view]
Gene3DG3DSA:1.10.555.10. RhoGAP. 1 hit.
G3DSA:2.10.110.10. Znf_LIM. 2 hits.
PfamPF00412. LIM. 3 hits.
PF00620. RhoGAP. 1 hit.
[Graphical view]
ProDomPD000094. LIM. 3 hits.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00132. LIM. 3 hits.
SM00324. RhoGAP. 1 hit.
[Graphical view]
PROSITEPS00478. LIM_DOMAIN_1. 2 hits.
PS50023. LIM_DOMAIN_2. 3 hits.
PS50238. RHOGAP. 1 hit.
[Graphical view]
BLOCKSSearch...
ProtoNetSearch...

Other Resources

LinkHubP35688.
NextBio968456.

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Entry information

Entry nameLRG1_YEAST
AccessionPrimary (citable) accession number: P35688
Secondary accession number(s): Q07735
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: November 1, 1997
Last modified: November 4, 2008
This is version 86 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal Proteome Annotation Project)

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Relevant documents

UniProtKB secondary accession numbers

Index of UniProtKB secondary accession numbers

SIMILARITY comments

Index of protein domains and families

Recent format changes

Overview of recent format changes

Yeast

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

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents