ID   LRG1_YEAST              Reviewed;        1017 AA.
AC   P35688; Q07735;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 2.
DT   01-JUL-2008, entry version 83.
DE   Rho-GTPase-activating protein LRG1 (LIM-RhoGAP protein 1).
GN   Name=LRG1; OrderedLocusNames=YDL240W;
OS   Saccharomyces cerevisiae (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=4932;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=DBY874;
RX   MEDLINE=94344779; PubMed=8065929; DOI=10.1093/nar/22.15.3151;
RA   Mueller A., Xu G., Wells R., Hollenberg C.P., Piepersberg W.;
RT   "LRG1 is expressed during sporulation in Saccharomyces cerevisiae and
RT   contains motifs similar to LIM and rho/racGAP domains.";
RL   Nucleic Acids Res. 22:3151-3154(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   MEDLINE=97313263; PubMed=9169867;
RA   Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA   Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA   Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA   Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA   Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA   Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA   Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA   Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N.,
RA   Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M.,
RA   Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L.,
RA   Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M.,
RA   Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S.,
RA   Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M.,
RA   Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S.,
RA   Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K.,
RA   Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D.,
RA   Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C.,
RA   Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T.,
RA   Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E.,
RA   Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W.,
RA   Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K.,
RA   Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S.,
RA   Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A.,
RA   Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA   Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S.,
RA   Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M.,
RA   Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y.,
RA   Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M.,
RA   Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E.,
RA   Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R.,
RA   Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA   Mewes H.-W., Zollner A., Zaccaria P.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL   Nature 387:75-78(1997).
RN   [3]
RP   FUNCTION, AND INTERACTION WITH CDC42; RHO1 AND RHO2.
RX   MEDLINE=21475606; 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
RT   proteins from Saccharomyces cerevisiae.";
RL   FEBS Lett. 506:149-156(2001).
RN   [4]
RP   FUNCTION, INTERACTION WITH RHO1, AND SUBCELLULAR LOCATION.
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   [5]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   MEDLINE=22923965; PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
RA   Dephoure N., 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-562, AND MASS
RP   SPECTROMETRY.
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
RT   phosphoproteome analysis.";
RL   Mol. Cell. Proteomics 0:0-0(2008).
CC   -!- FUNCTION: Acts in signal transduction. Activates CDC42, RHO1 and
CC       RHO2. Negatively regulates 1,3-beta-glucan synthesis. May be
CC       responsible for the down-regulation of CDC42 during mating.
CC   -!- SUBUNIT: Interacts with CDC42, RHO1 and RHO2.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Bud. Bud neck. Note=Localized to
CC       the bud site during bud formation and at the bud neck during
CC       cytokinesis.
CC   -!- DEVELOPMENTAL STAGE: Highly expressed during sporulation.
CC   -!- MISCELLANEOUS: Present with 468 molecules/cell in log phase SD
CC       medium.
CC   -!- SIMILARITY: Contains 3 LIM zinc-binding domains.
CC   -!- SIMILARITY: Contains 1 Rho-GAP domain.
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DR   EMBL; X78453; CAA55210.1; -; Genomic_DNA.
DR   EMBL; Z74288; CAA98820.1; -; Genomic_DNA.
DR   PIR; S67804; S67804.
DR   RefSeq; NP_010041.1; -.
DR   HSSP; Q07960; 1RGP.
DR   DIP; DIP:2588N; -.
DR   Ensembl; YDL240W; Saccharomyces cerevisiae.
DR   GeneID; 851358; -.
DR   GenomeReviews; Z71256_GR; YDL240W.
DR   KEGG; sce:YDL240W; -.
DR   NMPDR; fig|4932.3.peg.774; -.
DR   CYGD; YDL240w; -.
DR   SGD; S000002399; LRG1.
DR   HOGENOM; P35688; -.
DR   LinkHub; P35688; -.
DR   ArrayExpress; P35688; -.
DR   GermOnline; YDL240W; Saccharomyces cerevisiae.
DR   GO; GO:0005935; C:cellular bud neck; IDA:SGD.
DR   GO; GO:0005739; C:mitochondrion; IDA:SGD.
DR   GO; GO:0005100; F:Rho GTPase activator activity; IDA:SGD.
DR   GO; GO:0009272; P:fungal-type cell wall biogenesis; IGI:SGD.
DR   GO; GO:0007264; P:small GTPase mediated signal transduction; IPI:SGD.
DR   InterPro; IPR000198; RhoGAP.
DR   InterPro; IPR001781; Znf_LIM.
DR   Gene3D; G3DSA:1.10.555.10; RhoGAP; 1.
DR   Gene3D; G3DSA:2.10.110.10; Znf_LIM; 2.
DR   Pfam; PF00412; LIM; 3.
DR   Pfam; PF00620; RhoGAP; 1.
DR   ProDom; PD000094; LIM; 3.
DR   SMART; SM00132; LIM; 3.
DR   SMART; SM00324; RhoGAP; 1.
DR   PROSITE; PS00478; LIM_DOMAIN_1; 2.
DR   PROSITE; PS50023; LIM_DOMAIN_2; 3.
DR   PROSITE; PS50238; RHOGAP; 1.
PE   1: Evidence at protein level;
KW   Complete proteome; Cytoplasm; GTPase activation; LIM domain;
KW   Metal-binding; Phosphoprotein; Repeat; Sporulation; Zinc.
FT   CHAIN         1   1017       Rho-GTPase-activating protein LRG1.
FT                                /FTId=PRO_0000075838.
FT   DOMAIN       28     88       LIM zinc-binding 1.
FT   DOMAIN       98    148       LIM zinc-binding 2.
FT   DOMAIN      155    184       LIM zinc-binding 3; truncated.
FT   DOMAIN      419    474       LIM zinc-binding 4.
FT   DOMAIN      730    953       Rho-GAP.
FT   MOD_RES     562    562       Phosphoserine.
FT   CONFLICT    531    531       H -> Q (in Ref. 1; CAA55210).
FT   CONFLICT    766    766       R -> S (in Ref. 1; CAA55210).
FT   CONFLICT    791    791       N -> T (in Ref. 1; CAA55210).
FT   CONFLICT    821    821       L -> Q (in Ref. 1; CAA55210).
FT   CONFLICT    838    838       A -> S (in Ref. 1; CAA55210).
FT   CONFLICT    849    849       V -> L (in Ref. 1; CAA55210).
FT   CONFLICT    895    895       S -> F (in Ref. 1; CAA55210).
FT   CONFLICT    928    928       A -> T (in Ref. 1; CAA55210).
FT   CONFLICT    935    935       Y -> S (in Ref. 1; CAA55210).
FT   CONFLICT    977   1017       INHFISTVMQSKTIDYSECDIKTPVTVKDSTTTVIQGEINK
FT                                -> TILFPPLCKVKQSIIPNVT (in Ref. 1;
FT                                CAA55210).
SQ   SEQUENCE   1017 AA;  116660 MW;  DDEB79B4BBEBBB09 CRC64;
     MIQNSAGYRS LNTASPMTVQ VKNQKKICAR CNKLVIPDSQ RTKTTLKALG KYYHESCFTC
     QDCQKPLKPK YFPYQVDKTS ESILLCQYDY FRRHNLLCHV CDTPLRGLYY TAFGYRYDEE
     HFSCTICATP CGVKKCFMYG NQLYCKYHFL KYFSKRCKGC EFPISDQYIE FPKGEEIHCW
     HPECYGIHKY WHVNLAAETV GLQYLPKLEY NPNSGDKDIN PTAYELDKQM QAFNFILSKT
     WSVLYRFEEE AASCISDMFQ YLTSNDQLKG IESTGLLVLK IDCLFRGLDT LNLSTNKSMP
     VNSDQECIEN NAMAASKYSK FPKNLSTKIM IYLQLLRKLG TENKNETITI SSFMSVITGL
     AHFLKLLTRF GLYTALENNK LTHSVNPLLR FLREVEKNEL FENNPFQYIK TPVNATDSCA
     GCNKYIQEEC IQFYEHRWHI ACFTCSSCHK NINPRSLTDP TFNKEKKKIL CSHCSIDDPA
     SVPGFKFVTK LAQLIFLLKI ALVKSRTVML KSKASNKVGR NSLQSTMLKE HTYIRTLNDI
     KRLRSRRESV RVTHNKQQAR KSVILETAET DLNDPTKQGD SKNLVIQTDD PSSSQQVSTR
     ENVFSNTKTL TLDDISRIVA AEQARELRPN AFAHFKKLKE TDDETSNVVP KKSGVYYSEL
     STMELSMIRA ISLSLLAGKQ LISKTDPNYT SLVSMVFSNE KQVTGSFWNR MKIMMSMEPK
     KPITKTVFGA PLDVLCEKWG VDSDLGVGPV KIRIPIIIDE LISSLRQMDM SVEGIFRKNG
     NIRRLRELTA NIDSNPTEAP DFSKENAIQL SALLKKFIRE LPQPILSTDL YELWIKAAKI
     DLEDEKQRVI LLIYSLLPTY NRNLLEALLS FLHWTSSFSY IENEMGSKMD IHNLSTVITP
     NILYLRHKEI SNDNVPDEPE SGLVDSFAQN KGENYFLAIE IVDYLITHNE EMAMVPKFLM
     NLLKDVQLQK LDNYESINHF ISTVMQSKTI DYSECDIKTP VTVKDSTTTV IQGEINK
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