BEM3_YEAST
ID BEM3_YEAST Reviewed; 1128 AA.
AC P32873; D6W3Q3;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 3.
DT 03-AUG-2022, entry version 187.
DE RecName: Full=GTPase-activating protein BEM3;
DE AltName: Full=Bud emergence protein 3;
GN Name=BEM3; OrderedLocusNames=YPL115C; ORFNames=LPH12C;
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], AND FUNCTION.
RX PubMed=8300560; DOI=10.1016/s0021-9258(17)41953-3;
RA Zheng Y., Cerione R., Bender A.;
RT "Control of the yeast bud-site assembly GTPase Cdc42. Catalysis of guanine
RT nucleotide exchange by Cdc24 and stimulation of GTPase activity by Bem3.";
RL J. Biol. Chem. 269:2369-2372(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169875;
RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA Vo D.H., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL Nature 387:103-105(1997).
RN [3]
RP GENOME REANNOTATION.
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.
RX PubMed=8227021; DOI=10.1016/s0021-9258(19)74512-8;
RA Zheng Y., Hart M.J., Shinjo K., Evans T., Bender A., Cerione R.A.;
RT "Biochemical comparisons of the Saccharomyces cerevisiae Bem2 and Bem3
RT proteins. Delineation of a limit Cdc42 GTPase-activating protein domain.";
RL J. Biol. Chem. 268:24629-24634(1993).
RN [5]
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 [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT "Analysis of phosphorylation sites on proteins from Saccharomyces
RT cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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 phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-254, 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).
CC -!- FUNCTION: GTPase-activating protein (GAP) for CDC42 and less
CC efficiently for RHO1. Negative regulator of the pheromone-response
CC pathway through the STE20 protein kinase. {ECO:0000269|PubMed:8227021,
CC ECO:0000269|PubMed:8300560}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- MISCELLANEOUS: Present with 752 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; L14558; AAA34453.1; -; Genomic_DNA.
DR EMBL; U43503; AAB68247.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11319.1; -; Genomic_DNA.
DR PIR; A49960; A49960.
DR RefSeq; NP_015210.1; NM_001183929.1.
DR PDB; 6FSF; X-ray; 2.20 A; A=500-765.
DR PDB; 6LP3; X-ray; 3.55 A; C/F=1-99.
DR PDBsum; 6FSF; -.
DR PDBsum; 6LP3; -.
DR AlphaFoldDB; P32873; -.
DR SMR; P32873; -.
DR BioGRID; 36066; 193.
DR DIP; DIP-2575N; -.
DR IntAct; P32873; 13.
DR MINT; P32873; -.
DR STRING; 4932.YPL115C; -.
DR iPTMnet; P32873; -.
DR MaxQB; P32873; -.
DR PaxDb; P32873; -.
DR PRIDE; P32873; -.
DR EnsemblFungi; YPL115C_mRNA; YPL115C; YPL115C.
DR GeneID; 855988; -.
DR KEGG; sce:YPL115C; -.
DR SGD; S000006036; BEM3.
DR VEuPathDB; FungiDB:YPL115C; -.
DR eggNOG; KOG4269; Eukaryota.
DR GeneTree; ENSGT00940000165908; -.
DR HOGENOM; CLU_010436_0_0_1; -.
DR InParanoid; P32873; -.
DR OMA; NNHIHSP; -.
DR BioCyc; YEAST:G3O-34015-MON; -.
DR Reactome; R-SCE-6798695; Neutrophil degranulation.
DR Reactome; R-SCE-8980692; RHOA GTPase cycle.
DR Reactome; R-SCE-9013148; CDC42 GTPase cycle.
DR Reactome; R-SCE-9013405; RHOD GTPase cycle.
DR Reactome; R-SCE-9013423; RAC3 GTPase cycle.
DR Reactome; R-SCE-9013424; RHOV GTPase cycle.
DR Reactome; R-SCE-9035034; RHOF GTPase cycle.
DR PRO; PR:P32873; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; P32873; protein.
DR GO; GO:0005938; C:cell cortex; IDA:SGD.
DR GO; GO:0005934; C:cellular bud tip; IDA:SGD.
DR GO; GO:0005737; C:cytoplasm; IDA: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:0005096; F:GTPase activator activity; IDA:SGD.
DR GO; GO:0032266; F:phosphatidylinositol-3-phosphate binding; IDA:SGD.
DR GO; GO:0030010; P:establishment of cell polarity; 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:0043087; P:regulation of GTPase activity; IBA:GO_Central.
DR GO; GO:0031106; P:septin ring organization; IGI:SGD.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR Gene3D; 1.10.555.10; -; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR Gene3D; 3.30.1520.10; -; 1.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR001683; PX_dom.
DR InterPro; IPR036871; PX_dom_sf.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR000198; RhoGAP_dom.
DR Pfam; PF00169; PH; 1.
DR Pfam; PF00787; PX; 1.
DR Pfam; PF00620; RhoGAP; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00312; PX; 1.
DR SMART; SM00324; RhoGAP; 1.
DR SUPFAM; SSF48350; SSF48350; 1.
DR SUPFAM; SSF64268; SSF64268; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS50238; RHOGAP; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; GTPase activation; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..1128
FT /note="GTPase-activating protein BEM3"
FT /id="PRO_0000056728"
FT DOMAIN 634..741
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 913..1128
FT /note="Rho-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00172"
FT REGION 194..241
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 345..391
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 418..486
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 746..777
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 796..838
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 377..391
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 796..829
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 254
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT HELIX 509..514
FT /evidence="ECO:0007829|PDB:6FSF"
FT STRAND 515..525
FT /evidence="ECO:0007829|PDB:6FSF"
FT STRAND 531..539
FT /evidence="ECO:0007829|PDB:6FSF"
FT TURN 540..542
FT /evidence="ECO:0007829|PDB:6FSF"
FT STRAND 545..551
FT /evidence="ECO:0007829|PDB:6FSF"
FT HELIX 553..566
FT /evidence="ECO:0007829|PDB:6FSF"
FT HELIX 578..581
FT /evidence="ECO:0007829|PDB:6FSF"
FT HELIX 586..603
FT /evidence="ECO:0007829|PDB:6FSF"
FT HELIX 611..621
FT /evidence="ECO:0007829|PDB:6FSF"
FT STRAND 623..626
FT /evidence="ECO:0007829|PDB:6FSF"
FT STRAND 638..644
FT /evidence="ECO:0007829|PDB:6FSF"
FT STRAND 656..663
FT /evidence="ECO:0007829|PDB:6FSF"
FT STRAND 666..689
FT /evidence="ECO:0007829|PDB:6FSF"
FT STRAND 691..693
FT /evidence="ECO:0007829|PDB:6FSF"
FT STRAND 701..707
FT /evidence="ECO:0007829|PDB:6FSF"
FT STRAND 717..722
FT /evidence="ECO:0007829|PDB:6FSF"
FT HELIX 726..736
FT /evidence="ECO:0007829|PDB:6FSF"
SQ SEQUENCE 1128 AA; 124913 MW; 4BF03EAD6EF10283 CRC64;
MTDNLTTTHG GSTTLELLAQ YNDHRSKKDK SIEHIEKGTC SGKERNPSYD EIFTENIKLK
LQVQEYETEI ESLEKVIDML QKNREASLEV VLEQVQNDSR DSYVNDQSFV LPPRSAERKA
HIKSLNLPIP TLSPPLQQGS DVALETSVTP TVPQIGVTSN TSISRKHLQN MILNDEIEAN
SSFSSPKIIN RSVSSPTKIH SEQLASPAAS VTYTTSRITI KSPNKGSKSP LQERLRSPQN
PNRMTAVINN HLHSPLKAST SNNLDELTES KSQQLTNDAI QKNDRVYSSI TSSAYTTGTP
TSAAKSPSSL LEVKEGENKA LGFSPASKEK LDDFTQLLDS SFGEEDLVNT DSKDPLSIKS
TINESLPPPP APPTFFSPTS SGNIKNSTPL SSHLASPVIL NKKDDNFGAQ SAKNLKKPVL
TSSLPNLSTK LSTTSQNASL PPNPPVESSS KQKQLGETAS IHSTNTLNTF SSTPQGSLKT
LRRPHASSVS TVKSVAQSLK SDIPLFVQPE DFGTIQIEVL STLYRDNEDD LSILIAIIDR
KSGKEMFKFS KSIHKVRELD VYMKSHVPDL PLPTLPDRQL FQTLSPTKVD TRKNILNQYY
TSIFSVPEFP KNVGLKIAQF ISTDTVMTPP MMDDNVKDGS LLLRRPKTLT GNSTWRVRYG
ILRDDVLQLF DKNQLTETIK LRQSSIELIP NLPEDRFGTR NGFLITEHKK SGLSTSTKYY
ICTETSKERE LWLSAFSDYI DPSQSLSLSS SRNANDTDSA SHLSAGTHHS KFGNATISAT
DTPSYVTDLT QEYNNNNNIS NSSNNIANSD GIDSNPSSHS NFLASSSGNA EEEKDSRRAK
MRSLFPFKKL TGPASAMNHI GITISNDSDS PTSPDSIIKS PSKKLMEVSS SSNSSTGPHV
STAIFGSSLE TCLRLSSHKY QNVYDLPSVV YRCLEYLYKN RGIQEEGIFR LSGSSTVIKT
LQERFDKEYD VDLCRYNESI EAKDDEASPS LYIGVNTVSG LLKLYLRKLP HLLFGDEQFL
SFKRVVDENH NNPVQISLGF KELIESGLVP HANLSLMYAL FELLVRINEN SKFNKMNLRN
LCIVFSPTLN IPISMLQPFI TDFACIFQGG EPVKEEEREK VDIHIPQV
