GBB_YEAST
ID GBB_YEAST Reviewed; 423 AA.
AC P18851; D6W2R8;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 2.
DT 03-AUG-2022, entry version 200.
DE RecName: Full=Guanine nucleotide-binding protein subunit beta;
GN Name=STE4; OrderedLocusNames=YOR212W; ORFNames=YOR50-2;
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].
RX PubMed=2536595; DOI=10.1016/0092-8674(89)90249-3;
RA Whiteway M., Hougan L., Dignard D., Thomas D.Y., Bell L., Saari G.C.,
RA Grant F.J., O'Hara P., Mackay V.L.;
RT "The STE4 and STE18 genes of yeast encode potential beta and gamma subunits
RT of the mating factor receptor-coupled G protein.";
RL Cell 56:467-477(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=8840505;
RX DOI=10.1002/(sici)1097-0061(199607)12:9<877::aid-yea969>3.0.co;2-s;
RA Galisson F., Dujon B.;
RT "Sequence and analysis of a 33 kb fragment from the right arm of chromosome
RT XV of the yeast Saccharomyces cerevisiae.";
RL Yeast 12:877-885(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(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 INTERACTION WITH SYG1.
RX PubMed=7592711; DOI=10.1074/jbc.270.43.25435;
RA Spain B.H., Koo D., Ramakrishnan M., Dzudzor B., Colicelli J.;
RT "Truncated forms of a novel yeast protein suppress the lethality of a G
RT protein alpha subunit deficiency by interacting with the beta subunit.";
RL J. Biol. Chem. 270:25435-25444(1995).
RN [6]
RP INTERACTION WITH PLP1 AND PLP2.
RX PubMed=10749875; DOI=10.1074/jbc.m002163200;
RA Flanary P.L., DiBello P.R., Estrada P., Dohlman H.G.;
RT "Functional analysis of Plp1 and Plp2, two homologues of phosducin in
RT yeast.";
RL J. Biol. Chem. 275:18462-18469(2000).
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 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 IDENTIFICATION BY 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: Implicated in the a- and alpha-factor response pathway. The
CC beta and gamma chains of the putative yeast mating response pathway G
CC protein play a positive role in initiation of the mating response. The
CC beta and gamma chains are required for the GTPase activity, for
CC replacement of GDP by GTP, and for G protein-effector interaction.
CC -!- SUBUNIT: G proteins are composed of 3 units, alpha, beta and gamma. The
CC beta-gamma subunit complex (STE4-STE18 complex) interacts with PLP1 and
CC PLP2. Interacts with SYG1. {ECO:0000269|PubMed:10749875,
CC ECO:0000269|PubMed:7592711}.
CC -!- INTERACTION:
CC P18851; P39010: AKR1; NbExp=3; IntAct=EBI-7390, EBI-2421;
CC P18851; P11433: CDC24; NbExp=6; IntAct=EBI-7390, EBI-4220;
CC P18851; P21268: FAR1; NbExp=2; IntAct=EBI-7390, EBI-6780;
CC P18851; P08539: GPA1; NbExp=8; IntAct=EBI-7390, EBI-7376;
CC P18851; P18852: STE18; NbExp=3; IntAct=EBI-7390, EBI-7397;
CC P18851; Q03497: STE20; NbExp=3; IntAct=EBI-7390, EBI-18285;
CC P18851; P32917: STE5; NbExp=3; IntAct=EBI-7390, EBI-18373;
CC -!- MISCELLANEOUS: Present with 2050 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the WD repeat G protein beta family.
CC {ECO:0000305}.
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DR EMBL; M23982; AAA35114.1; -; Genomic_DNA.
DR EMBL; X92441; CAA63175.1; -; Genomic_DNA.
DR EMBL; Z75120; CAA99427.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA10984.1; -; Genomic_DNA.
DR PIR; S60939; S60939.
DR RefSeq; NP_014855.3; NM_001183631.3.
DR PDB; 7AD3; EM; 3.50 A; F=1-423.
DR PDBsum; 7AD3; -.
DR AlphaFoldDB; P18851; -.
DR SMR; P18851; -.
DR BioGRID; 34607; 89.
DR ComplexPortal; CPX-1645; Ste4-Ste18 heterodimer.
DR ComplexPortal; CPX-1646; G protein heterotrimer.
DR ComplexPortal; CPX-977; CDC24-FAR1-Gbetagamma complex.
DR DIP; DIP-954N; -.
DR IntAct; P18851; 65.
DR MINT; P18851; -.
DR STRING; 4932.YOR212W; -.
DR iPTMnet; P18851; -.
DR MaxQB; P18851; -.
DR PaxDb; P18851; -.
DR PRIDE; P18851; -.
DR DNASU; 854387; -.
DR EnsemblFungi; YOR212W_mRNA; YOR212W; YOR212W.
DR GeneID; 854387; -.
DR KEGG; sce:YOR212W; -.
DR SGD; S000005738; STE4.
DR VEuPathDB; FungiDB:YOR212W; -.
DR eggNOG; KOG0286; Eukaryota.
DR GeneTree; ENSGT01000000214413; -.
DR HOGENOM; CLU_000288_57_34_1; -.
DR InParanoid; P18851; -.
DR OMA; PLDSQWV; -.
DR BioCyc; YEAST:G3O-33714-MON; -.
DR Reactome; R-SCE-6814122; Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding.
DR PRO; PR:P18851; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; P18851; protein.
DR GO; GO:0120171; C:Cdc24p-Far1p-Gbetagamma complex; IDA:SGD.
DR GO; GO:0005938; C:cell cortex; IC:ComplexPortal.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0031680; C:G-protein beta/gamma-subunit complex; IDA:SGD.
DR GO; GO:0005834; C:heterotrimeric G-protein complex; IDA:SGD.
DR GO; GO:0005937; C:mating projection; IDA:SGD.
DR GO; GO:0005886; C:plasma membrane; IDA:SGD.
DR GO; GO:0001965; F:G-protein alpha-subunit binding; IPI:SGD.
DR GO; GO:0031682; F:G-protein gamma-subunit binding; IPI:SGD.
DR GO; GO:0019901; F:protein kinase binding; IDA:SGD.
DR GO; GO:0097110; F:scaffold protein binding; IPI:SGD.
DR GO; GO:0030159; F:signaling receptor complex adaptor activity; IBA:GO_Central.
DR GO; GO:0031267; F:small GTPase binding; IMP:SGD.
DR GO; GO:0043577; P:chemotropism; IMP:SGD.
DR GO; GO:0061951; P:establishment of protein localization to plasma membrane; IMP:SGD.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0001403; P:invasive growth in response to glucose limitation; IMP:SGD.
DR GO; GO:0000750; P:pheromone-dependent signal transduction involved in conjugation with cellular fusion; IDA:ComplexPortal.
DR GO; GO:1903260; P:protein localization to mating projection tip; IMP:SGD.
DR GO; GO:0010969; P:regulation of pheromone-dependent signal transduction involved in conjugation with cellular fusion; IC:ComplexPortal.
DR GO; GO:0010525; P:regulation of transposition, RNA-mediated; IMP:SGD.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR InterPro; IPR001632; Gprotein_B.
DR InterPro; IPR016346; Guanine_nucleotide-bd_bsu.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR19850; PTHR19850; 1.
DR Pfam; PF00400; WD40; 4.
DR PRINTS; PR00319; GPROTEINB.
DR PRINTS; PR00320; GPROTEINBRPT.
DR SMART; SM00320; WD40; 7.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 3.
DR PROSITE; PS50082; WD_REPEATS_2; 4.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Pheromone response; Reference proteome; Repeat; Transducer;
KW WD repeat.
FT CHAIN 1..423
FT /note="Guanine nucleotide-binding protein subunit beta"
FT /id="PRO_0000127720"
FT REPEAT 90..120
FT /note="WD 1"
FT REPEAT 132..162
FT /note="WD 2"
FT REPEAT 179..208
FT /note="WD 3"
FT REPEAT 220..256
FT /note="WD 4"
FT REPEAT 268..298
FT /note="WD 5"
FT REPEAT 348..377
FT /note="WD 6"
FT REPEAT 389..419
FT /note="WD 7"
FT CONFLICT 33
FT /note="D -> E (in Ref. 1; AAA35114)"
FT /evidence="ECO:0000305"
FT CONFLICT 236
FT /note="S -> L (in Ref. 1; AAA35114)"
FT /evidence="ECO:0000305"
FT HELIX 65..68
FT /evidence="ECO:0007829|PDB:7AD3"
FT HELIX 69..71
FT /evidence="ECO:0007829|PDB:7AD3"
FT STRAND 97..100
FT /evidence="ECO:0007829|PDB:7AD3"
FT STRAND 106..110
FT /evidence="ECO:0007829|PDB:7AD3"
FT STRAND 112..131
FT /evidence="ECO:0007829|PDB:7AD3"
FT STRAND 139..142
FT /evidence="ECO:0007829|PDB:7AD3"
FT STRAND 146..156
FT /evidence="ECO:0007829|PDB:7AD3"
FT STRAND 158..162
FT /evidence="ECO:0007829|PDB:7AD3"
FT STRAND 173..177
FT /evidence="ECO:0007829|PDB:7AD3"
FT STRAND 184..202
FT /evidence="ECO:0007829|PDB:7AD3"
FT STRAND 204..208
FT /evidence="ECO:0007829|PDB:7AD3"
FT TURN 209..211
FT /evidence="ECO:0007829|PDB:7AD3"
FT STRAND 243..245
FT /evidence="ECO:0007829|PDB:7AD3"
FT STRAND 257..261
FT /evidence="ECO:0007829|PDB:7AD3"
FT STRAND 273..278
FT /evidence="ECO:0007829|PDB:7AD3"
FT STRAND 282..289
FT /evidence="ECO:0007829|PDB:7AD3"
FT STRAND 294..300
FT /evidence="ECO:0007829|PDB:7AD3"
FT STRAND 352..357
FT /evidence="ECO:0007829|PDB:7AD3"
FT STRAND 359..371
FT /evidence="ECO:0007829|PDB:7AD3"
FT STRAND 373..377
FT /evidence="ECO:0007829|PDB:7AD3"
FT TURN 378..381
FT /evidence="ECO:0007829|PDB:7AD3"
FT STRAND 396..399
FT /evidence="ECO:0007829|PDB:7AD3"
FT STRAND 401..404
FT /evidence="ECO:0007829|PDB:7AD3"
FT STRAND 406..409
FT /evidence="ECO:0007829|PDB:7AD3"
FT STRAND 415..418
FT /evidence="ECO:0007829|PDB:7AD3"
SQ SEQUENCE 423 AA; 46581 MW; 4B0E26040AAA83E5 CRC64;
MAAHQMDSIT YSNNVTQQYI QPQSLQDISA VEDEIQNKIE AARQESKQLH AQINKAKHKI
QDASLFQMAN KVTSLTKNKI NLKPNIVLKG HNNKISDFRW SRDSKRILSA SQDGFMLIWD
SASGLKQNAI PLDSQWVLSC AISPSSTLVA SAGLNNNCTI YRVSKENRVA QNVASIFKGH
TCYISDIEFT DNAHILTASG DMTCALWDIP KAKRVREYSD HLGDVLALAI PEEPNSENSS
NTFASCGSDG YTYIWDSRSP SAVQSFYVND SDINALRFFK DGMSIVAGSD NGAINMYDLR
SDCSIATFSL FRGYEERTPT PTYMAANMEY NTAQSPQTLK STSSSYLDNQ GVVSLDFSAS
GRLMYSCYTD IGCVVWDVLK GEIVGKLEGH GGRVTGVRSS PDGLAVCTGS WDSTMKIWSP
GYQ
