GDS1_YEAST
ID GDS1_YEAST Reviewed; 633 AA.
AC P39011; D6W3K7;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=GTPase-GDP dissociation stimulator BEM4 {ECO:0000250|UniProtKB:P52306};
DE AltName: Full=Bud emergence protein 4 {ECO:0000303|PubMed:8754839};
GN Name=BEM4 {ECO:0000303|PubMed:8754839};
GN Synonyms=ROM7 {ECO:0000303|PubMed:8754840}; OrderedLocusNames=YPL161C;
GN ORFNames=P2561;
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], FUNCTION, AND INTERACTION WITH CDC42;
RP RHO1; RHO2 AND RHO4.
RX PubMed=8754839; DOI=10.1128/mcb.16.8.4387;
RA Mack D., Nishimura K., Dennehey B.K., Arbogast T., Parkinson J., Toh-e A.,
RA Pringle J.R., Bender A., Matsui Y.;
RT "Identification of the bud emergence gene BEM4 and its interactions with
RT rho-type GTPases in Saccharomyces cerevisiae.";
RL Mol. Cell. Biol. 16:4387-4395(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204511 / S288c / AB972;
RX PubMed=8948103;
RX DOI=10.1002/(sici)1097-0061(199611)12:14<1483::aid-yea34>3.0.co;2-o;
RA Purnelle B., Coster F., Goffeau A.;
RT "The sequence of 55 kb on the left arm of yeast chromosome XVI identifies a
RT small nuclear RNA, a new putative protein kinase and two new putative
RT regulators.";
RL Yeast 12:1483-1492(1996).
RN [3]
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 [4]
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 [5]
RP FUNCTION, INTERACTION WITH RHO1, AND DISRUPTION PHENOTYPE.
RX PubMed=8754840; DOI=10.1128/mcb.16.8.4396;
RA Hirano H., Tanaka K., Ozaki K., Imamura H., Kohno H., Hihara T.,
RA Kameyama T., Hotta K., Arisawa M., Watanabe T., Qadota H., Ohya Y.,
RA Takai Y.;
RT "ROM7/BEM4 encodes a novel protein that interacts with the Rho1p small GTP-
RT binding protein in Saccharomyces cerevisiae.";
RL Mol. Cell. Biol. 16:4396-4403(1996).
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 INTERACTION WITH CDC11.
RX PubMed=12665577; DOI=10.1128/mcb.23.8.2762-2777.2003;
RA Casamayor A., Snyder M.;
RT "Molecular dissection of a yeast septin: distinct domains are required for
RT septin interaction, localization, and function.";
RL Mol. Cell. Biol. 23:2762-2777(2003).
RN [8]
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).
CC -!- FUNCTION: Probably acts as a GEF (guanine nucleotide exchange factor)
CC for the Rho family of small GTP-binding proteins (G proteins) that
CC stimulates the dissociation of GDP to enable subsequent binding of GTP
CC (By similarity). May also chaperone the processing and/or trafficking
CC of small GTPases independently of GEF activity (By similarity).
CC Involved in the control of polarized cell growth via CDC42-mediated
CC signaling (PubMed:8754839). Involved in the control of cell-wall
CC organization via RHO1-mediated signaling (PubMed:8754839,
CC PubMed:8754840). May also function via RHO2 and RHO4 (PubMed:8754839).
CC {ECO:0000250|UniProtKB:P52306, ECO:0000269|PubMed:8754839,
CC ECO:0000269|PubMed:8754840}.
CC -!- SUBUNIT: Interacts with CDC42; the interaction is direct
CC (PubMed:8754839). Interacts with RHO1; the interaction is direct
CC (PubMed:8754839, PubMed:8754840). Interacts with RHO2 (PubMed:8754839).
CC Interacts with RHO4 (PubMed:8754839). Interacts with CDC11
CC (PubMed:12665577). {ECO:0000269|PubMed:12665577,
CC ECO:0000269|PubMed:8754839, ECO:0000269|PubMed:8754840}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14562095}. Cytoplasm
CC {ECO:0000269|PubMed:14562095}.
CC -!- DISRUPTION PHENOTYPE: Cell polarity defects; delocalized actin patches
CC and abnormal budding (PubMed:8754840). Cell lysis at high temperature
CC (PubMed:8754840). {ECO:0000269|PubMed:8754840}.
CC -!- MISCELLANEOUS: Present with 6330 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; L27816; AAB47774.1; -; Genomic_DNA.
DR EMBL; X96770; CAA65560.1; -; Genomic_DNA.
DR EMBL; Z73517; CAA97866.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11273.1; -; Genomic_DNA.
DR PIR; S45177; S45177.
DR RefSeq; NP_015164.1; NM_001183975.1.
DR AlphaFoldDB; P39011; -.
DR BioGRID; 36022; 399.
DR DIP; DIP-1208N; -.
DR IntAct; P39011; 24.
DR MINT; P39011; -.
DR STRING; 4932.YPL161C; -.
DR iPTMnet; P39011; -.
DR MaxQB; P39011; -.
DR PaxDb; P39011; -.
DR PRIDE; P39011; -.
DR EnsemblFungi; YPL161C_mRNA; YPL161C; YPL161C.
DR GeneID; 855942; -.
DR KEGG; sce:YPL161C; -.
DR SGD; S000006082; BEM4.
DR VEuPathDB; FungiDB:YPL161C; -.
DR eggNOG; ENOG502QQB4; Eukaryota.
DR HOGENOM; CLU_436179_0_0_1; -.
DR InParanoid; P39011; -.
DR OMA; YEEILFG; -.
DR BioCyc; YEAST:G3O-34057-MON; -.
DR PRO; PR:P39011; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; P39011; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; ISS:UniProtKB.
DR GO; GO:0030010; P:establishment of cell polarity; IMP:SGD.
DR GO; GO:0043547; P:positive regulation of GTPase activity; IBA:GO_Central.
DR GO; GO:1903338; P:regulation of cell wall organization or biogenesis; IMP:UniProtKB.
DR GO; GO:0019236; P:response to pheromone; IEA:UniProtKB-KW.
DR GO; GO:0007266; P:Rho protein signal transduction; IMP:SGD.
DR InterPro; IPR040144; RAP1GDS1.
DR PANTHER; PTHR10957; PTHR10957; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Guanine-nucleotide releasing factor; Nucleus;
KW Pheromone response; Reference proteome.
FT CHAIN 1..633
FT /note="GTPase-GDP dissociation stimulator BEM4"
FT /id="PRO_0000064910"
SQ SEQUENCE 633 AA; 70993 MW; 22171643922650AC CRC64;
MDYEEILFGL QPILNASSIK DVPMNDVYLG SYLAVMDQLA VSLREPSNRD IVGKTGLLLN
LVRVLEQALD ICFHDTSISI NDKIAFYEIS SEVIRCIANA IIDNDDNREI LLDSGGKKLL
NYYIGGVLQL DEISSDKSED SLVDKLQMRS VVLLRNFCIG NLKYTENLAP FIRGPLFVLL
KTTQYSYLSS PEKVVLGSDL LNDILKVNYS NVQISDLFFL SQYIKKISSN VQNKELQAME
DGAVEAYSNT ETQKFAGQGN QEYIEKEEED DEEDVNCELL LNLSTCLETI VAKDETINFT
NEEQLVLSMQ KNLILSLVCL ESKTFNNKLI VMRRLISCAG NISANLTNSN KREQSLCIET
IKSSASSYAL AAALMILCNS VASKSDAVAL LKLISLSELI QVGSLLQDPL QYQGFLDLLR
KLLNLENTMW LDIKDLFTLF QIMRRCHEQT KYYNNLRSLL TNLLNKTLTV LPSSKIHNSI
SSDPTIISFI AEHGTLTSCI AMDKLLVSKK ALPKEAITSL WDSIFKFQNL GQAEQLSISD
LFHITKTVGI YLKDSSVTAD VNPIENILFK DYIQKLTLIL ETILSFKENK DKGSESCFNN
GKFIAGIILN IVKNTKCLTP EEQNLEALAK SFF
