LRG1_YEAST
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 03-AUG-2022, entry version 195.
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}.
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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; 133.
DR DIP; DIP-2588N; -.
DR IntAct; P35688; 4.
DR MINT; P35688; -.
DR STRING; 4932.YDL240W; -.
DR iPTMnet; P35688; -.
DR MaxQB; P35688; -.
DR PaxDb; P35688; -.
DR PRIDE; P35688; -.
DR EnsemblFungi; YDL240W_mRNA; YDL240W; YDL240W.
DR GeneID; 851358; -.
DR KEGG; sce:YDL240W; -.
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 BioCyc; YEAST:G3O-29617-MON; -.
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:0043547; P:positive regulation of GTPase activity; IDA: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 Gene3D; 1.10.555.10; -; 1.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR000198; RhoGAP_dom.
DR InterPro; IPR001781; Znf_LIM.
DR Pfam; PF00412; LIM; 2.
DR Pfam; PF00620; RhoGAP; 1.
DR SMART; SM00132; LIM; 3.
DR SMART; SM00324; RhoGAP; 1.
DR SUPFAM; SSF48350; SSF48350; 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
