ID LRG1_YEAST Reviewed; 1017 AA. AC P35688; D6VRB6; Q07735; DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot. DT 27-JUL-2011, sequence version 3. DT 27-MAR-2024, entry version 203. DE RecName: Full=Rho-GTPase-activating protein LRG1; DE AltName: Full=LIM-RhoGAP protein 1; GN Name=LRG1; OrderedLocusNames=YDL240W; 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]. RC STRAIN=DBY874; RX 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 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., Paulin L., RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., RA Wilson R., 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 GENOME REANNOTATION, AND SEQUENCE REVISION TO 531. 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 FUNCTION, AND INTERACTION WITH CDC42; RHO1 AND RHO2. 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 [5] 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 [6] RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS]. RX PubMed=14562095; DOI=10.1038/nature02026; RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., RA Weissman J.S., O'Shea E.K.; RT "Global analysis of protein localization in budding yeast."; RL Nature 425:686-691(2003). RN [7] RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS]. RX PubMed=14562106; DOI=10.1038/nature02046; RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., RA O'Shea E.K., Weissman J.S.; RT "Global analysis of protein expression in yeast."; RL Nature 425:737-741(2003). RN [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-562, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19779198; DOI=10.1126/science.1172867; RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.; RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights RT into evolution."; RL Science 325:1682-1686(2009). RN [9] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS RP SPECTROMETRY [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 in signal transduction. Activates CDC42, RHO1 and RHO2. CC Negatively regulates 1,3-beta-glucan synthesis. May be responsible for CC the down-regulation of CDC42 during mating. CC {ECO:0000269|PubMed:11447600, ECO:0000269|PubMed:11591390}. CC -!- SUBUNIT: Interacts with CDC42, RHO1 and RHO2. CC {ECO:0000269|PubMed:11447600, ECO:0000269|PubMed:11591390}. CC -!- SUBCELLULAR LOCATION: Cytoplasm. Bud. Bud neck. Note=Localized to the CC bud site during bud formation and at the bud neck during cytokinesis. CC -!- DEVELOPMENTAL STAGE: Highly expressed during sporulation. CC -!- MISCELLANEOUS: Present with 468 molecules/cell in log phase SD medium. CC {ECO:0000269|PubMed:14562106}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X78453; CAA55210.1; -; Genomic_DNA. DR EMBL; Z74288; CAA98820.1; -; Genomic_DNA. DR EMBL; BK006938; DAA11626.2; -; Genomic_DNA. DR PIR; S67804; S67804. DR RefSeq; NP_010041.2; NM_001180300.2. DR AlphaFoldDB; P35688; -. DR SMR; P35688; -. DR BioGRID; 31871; 140. DR DIP; DIP-2588N; -. DR IntAct; P35688; 4. DR MINT; P35688; -. DR STRING; 4932.YDL240W; -. DR iPTMnet; P35688; -. DR MaxQB; P35688; -. DR PaxDb; 4932-YDL240W; -. DR PeptideAtlas; P35688; -. DR EnsemblFungi; YDL240W_mRNA; YDL240W; YDL240W. DR GeneID; 851358; -. DR KEGG; sce:YDL240W; -. DR AGR; SGD:S000002399; -. DR SGD; S000002399; LRG1. DR VEuPathDB; FungiDB:YDL240W; -. DR eggNOG; KOG1703; Eukaryota. DR eggNOG; KOG2710; Eukaryota. DR HOGENOM; CLU_001321_1_0_1; -. DR InParanoid; P35688; -. DR OMA; WQMQSSV; -. DR OrthoDB; 1329523at2759; -. DR BioCyc; YEAST:G3O-29617-MONOMER; -. DR BioGRID-ORCS; 851358; 2 hits in 10 CRISPR screens. DR PRO; PR:P35688; -. DR Proteomes; UP000002311; Chromosome IV. DR RNAct; P35688; Protein. DR GO; GO:0005935; C:cellular bud neck; IDA:SGD. DR GO; GO:0005934; C:cellular bud tip; IDA:SGD. DR GO; GO:0005737; C:cytoplasm; HDA: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:0005739; C:mitochondrion; HDA:SGD. DR GO; GO:0030427; C:site of polarized growth; IDA:SGD. DR GO; GO:0005096; F:GTPase activator activity; IDA:SGD. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0030036; P:actin cytoskeleton organization; IBA:GO_Central. DR GO; GO:0000755; P:cytogamy; IMP:SGD. DR GO; GO:0090038; P:negative regulation of protein kinase C signaling; IMP:SGD. DR GO; GO:0035024; P:negative regulation of Rho protein signal transduction; IMP:SGD. DR GO; GO:0090334; P:regulation of cell wall (1->3)-beta-D-glucan biosynthetic process; IGI:SGD. DR GO; GO:0060237; P:regulation of fungal-type cell wall organization; IMP:SGD. DR GO; GO:0007165; P:signal transduction; IEA:InterPro. DR GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW. DR CDD; cd08368; LIM; 1. DR CDD; cd09391; LIM1_Lrg1p_like; 1. DR CDD; cd09393; LIM3_Lrg1p_like; 1. DR CDD; cd04397; RhoGAP_fLRG1; 1. DR Gene3D; 2.10.110.10; Cysteine Rich Protein; 3. DR Gene3D; 1.10.555.10; Rho GTPase activation protein; 1. DR InterPro; IPR008936; Rho_GTPase_activation_prot. DR InterPro; IPR000198; RhoGAP_dom. DR InterPro; IPR001781; Znf_LIM. DR PANTHER; PTHR14963; RHO GTPASE ACTIVATING PROTEIN 18,19-RELATED; 1. DR PANTHER; PTHR14963:SF1; RHO GTPASE-ACTIVATING PROTEIN CONUNDRUM; 1. DR Pfam; PF00412; LIM; 2. DR Pfam; PF00620; RhoGAP; 1. DR SMART; SM00132; LIM; 3. DR SMART; SM00324; RhoGAP; 1. DR SUPFAM; SSF57716; Glucocorticoid receptor-like (DNA-binding domain); 2. DR SUPFAM; SSF48350; GTPase activation domain, GAP; 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 Acetylation; Cytoplasm; GTPase activation; LIM domain; Metal-binding; KW Phosphoprotein; Reference proteome; Repeat; Sporulation; Zinc. FT CHAIN 1..1017 FT /note="Rho-GTPase-activating protein LRG1" FT /id="PRO_0000075838" FT DOMAIN 28..88 FT /note="LIM zinc-binding 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125" FT DOMAIN 98..148 FT /note="LIM zinc-binding 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125" FT DOMAIN 155..184 FT /note="LIM zinc-binding 3; truncated" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125" FT DOMAIN 419..474 FT /note="LIM zinc-binding 4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125" FT DOMAIN 730..953 FT /note="Rho-GAP" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00172" FT REGION 570..602 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 1 FT /note="N-acetylmethionine" FT /evidence="ECO:0007744|PubMed:22814378" FT MOD_RES 562 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19779198" FT CONFLICT 531 FT /note="Q -> H (in Ref. 2; CAA98820)" FT /evidence="ECO:0000305" FT CONFLICT 766 FT /note="R -> S (in Ref. 1; CAA55210)" FT /evidence="ECO:0000305" FT CONFLICT 791 FT /note="N -> T (in Ref. 1; CAA55210)" FT /evidence="ECO:0000305" FT CONFLICT 821 FT /note="L -> Q (in Ref. 1; CAA55210)" FT /evidence="ECO:0000305" FT CONFLICT 838 FT /note="A -> S (in Ref. 1; CAA55210)" FT /evidence="ECO:0000305" FT CONFLICT 849 FT /note="V -> L (in Ref. 1; CAA55210)" FT /evidence="ECO:0000305" FT CONFLICT 895 FT /note="S -> F (in Ref. 1; CAA55210)" FT /evidence="ECO:0000305" FT CONFLICT 928 FT /note="A -> T (in Ref. 1; CAA55210)" FT /evidence="ECO:0000305" FT CONFLICT 935 FT /note="Y -> S (in Ref. 1; CAA55210)" FT /evidence="ECO:0000305" FT CONFLICT 977..1017 FT /note="INHFISTVMQSKTIDYSECDIKTPVTVKDSTTTVIQGEINK -> TILFPPL FT CKVKQSIIPNVT (in Ref. 1; CAA55210)" FT /evidence="ECO:0000305" SQ SEQUENCE 1017 AA; 116651 MW; 862EC5EF7E57E679 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 QTYIRTLNDI 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 //