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   24-JAN-2024, entry version 207.
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; 90.
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; 4932-YOR212W; -.
DR   PeptideAtlas; P18851; -.
DR   DNASU; 854387; -.
DR   EnsemblFungi; YOR212W_mRNA; YOR212W; YOR212W.
DR   GeneID; 854387; -.
DR   KEGG; sce:YOR212W; -.
DR   AGR; SGD:S000005738; -.
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   OrthoDB; 102097at2759; -.
DR   BioCyc; YEAST:G3O-33714-MONOMER; -.
DR   Reactome; R-SCE-6814122; Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding.
DR   BioGRID-ORCS; 854387; 0 hits in 10 CRISPR screens.
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; NAS: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; NAS:ComplexPortal.
DR   CDD; cd00200; WD40; 1.
DR   Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 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; IPR019775; WD40_repeat_CS.
DR   InterPro; IPR036322; WD40_repeat_dom_sf.
DR   InterPro; IPR001680; WD40_rpt.
DR   PANTHER; PTHR19850; GUANINE NUCLEOTIDE-BINDING PROTEIN BETA G PROTEIN BETA; 1.
DR   PANTHER; PTHR19850:SF25; GUANINE NUCLEOTIDE-BINDING PROTEIN SUBUNIT BETA-1; 1.
DR   Pfam; PF00400; WD40; 6.
DR   PIRSF; PIRSF002394; GN-bd_beta; 1.
DR   PRINTS; PR00319; GPROTEINB.
DR   PRINTS; PR00320; GPROTEINBRPT.
DR   SMART; SM00320; WD40; 7.
DR   SUPFAM; SSF50978; WD40 repeat-like; 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
//