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   27-MAR-2024, entry version 196.
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; 201.
DR   DIP; DIP-2575N; -.
DR   IntAct; P32873; 13.
DR   MINT; P32873; -.
DR   STRING; 4932.YPL115C; -.
DR   GlyGen; P32873; 13 sites, 1 O-linked glycan (13 sites).
DR   iPTMnet; P32873; -.
DR   MaxQB; P32873; -.
DR   PaxDb; 4932-YPL115C; -.
DR   PeptideAtlas; P32873; -.
DR   EnsemblFungi; YPL115C_mRNA; YPL115C; YPL115C.
DR   GeneID; 855988; -.
DR   KEGG; sce:YPL115C; -.
DR   AGR; SGD:S000006036; -.
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; QFISTDT; -.
DR   OrthoDB; 25690at2759; -.
DR   BioCyc; YEAST:G3O-34015-MONOMER; -.
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-9013149; RAC1 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   BioGRID-ORCS; 855988; 0 hits in 10 CRISPR screens.
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:0031106; P:septin ring organization; IGI:SGD.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   CDD; cd13277; PH_Bem3; 1.
DR   CDD; cd06093; PX_domain; 1.
DR   Gene3D; 3.30.1520.10; Phox-like domain; 1.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR   Gene3D; 1.10.555.10; Rho GTPase activation protein; 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   PANTHER; PTHR23176:SF129; RHO GTPASE ACTIVATING PROTEIN AT 16F, ISOFORM E-RELATED; 1.
DR   PANTHER; PTHR23176; RHO/RAC/CDC GTPASE-ACTIVATING PROTEIN; 1.
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; GTPase activation domain, GAP; 1.
DR   SUPFAM; SSF50729; PH domain-like; 1.
DR   SUPFAM; SSF64268; PX domain; 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
//