ID   GBG_YEAST               Reviewed;         110 AA.
AC   P18852; D6VWQ5;
DT   01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1990, sequence version 1.
DT   27-MAR-2024, entry version 183.
DE   RecName: Full=Guanine nucleotide-binding protein subunit gamma;
DE   Flags: Precursor;
GN   Name=STE18; OrderedLocusNames=YJR086W; ORFNames=J1866;
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 204508 / S288c;
RX   PubMed=8840504;
RX   DOI=10.1002/(sici)1097-0061(199607)12:9<869::aid-yea964>3.0.co;2-1;
RA   Huang M.-E., Manus V., Chuat J.-C., Galibert F.;
RT   "Analysis of a 62 kb DNA sequence of chromosome X reveals 36 open reading
RT   frames and a gene cluster with a counterpart on chromosome XI.";
RL   Yeast 12:869-875(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=8641269; DOI=10.1002/j.1460-2075.1996.tb00557.x;
RA   Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C.,
RA   Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D.,
RA   Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J.,
RA   Heumann K., Hilger F., Hollenberg C.P., Huang M.-E., Jacq C.,
RA   Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E.,
RA   Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T.,
RA   Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B.,
RA   Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R.,
RA   Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N.,
RA   To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H.,
RA   von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.;
RT   "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X.";
RL   EMBO J. 15:2031-2049(1996).
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   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=17322287; DOI=10.1101/gr.6037607;
RA   Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA   Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA   Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA   Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA   LaBaer J.;
RT   "Approaching a complete repository of sequence-verified protein-encoding
RT   clones for Saccharomyces cerevisiae.";
RL   Genome Res. 17:536-543(2007).
RN   [6]
RP   MUTAGENESIS OF CYS-107.
RX   PubMed=7982577; DOI=10.1093/genetics/137.4.967;
RA   Whiteway M.S., Thomas D.Y.;
RT   "Site-directed mutations altering the CAAX box of Ste18, the yeast
RT   pheromone-response pathway G gamma subunit.";
RL   Genetics 137:967-976(1994).
RN   [7]
RP   ISOPRENYLATION AT CYS-107, METHYLATION AT CYS-107, PALMITOYLATION AT
RP   CYS-106, AND MUTAGENESIS OF CYS-106.
RX   PubMed=10523659; DOI=10.1128/mcb.19.11.7705;
RA   Hirschman J.E., Jenness D.D.;
RT   "Dual lipid modification of the yeast gamma subunit Ste18p determines
RT   membrane localization of Gbetagamma.";
RL   Mol. Cell. Biol. 19:7705-7711(1999).
RN   [8]
RP   ISOPRENYLATION AT CYS-107, AND PALMITOYLATION AT CYS-106.
RX   PubMed=10712512; DOI=10.1091/mbc.11.3.957;
RA   Manahan C.L., Patnana M., Blumer K.J., Linder M.E.;
RT   "Dual lipid modification motifs in G(alpha) and G(gamma) subunits are
RT   required for full activity of the pheromone response pathway in
RT   Saccharomyces cerevisiae.";
RL   Mol. Biol. Cell 11:957-968(2000).
RN   [9]
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   [10]
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   [11]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA   Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA   Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA   Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT   "N-terminal acetylome analyses and functional insights of the N-terminal
RT   acetyltransferase NatB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC   -!- FUNCTION: Implicated in the pheromone A- and alpha-factor response
CC       pathway. The beta and gamma chains of the putative yeast mating
CC       response pathway G protein play a positive role in initiation of the
CC       mating response.
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. {ECO:0000269|PubMed:10749875}.
CC   -!- INTERACTION:
CC       P18852; P18851: STE4; NbExp=3; IntAct=EBI-7397, EBI-7390;
CC   -!- SUBCELLULAR LOCATION: Membrane; Lipid-anchor.
CC   -!- MISCELLANEOUS: Present with 5550 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the G protein gamma family. {ECO:0000305}.
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DR   EMBL; M23983; AAA35110.1; -; Genomic_DNA.
DR   EMBL; L47993; AAB39309.1; -; Genomic_DNA.
DR   EMBL; Z49586; CAA89613.1; -; Genomic_DNA.
DR   EMBL; AY557888; AAS56214.1; -; Genomic_DNA.
DR   EMBL; BK006943; DAA08871.1; -; Genomic_DNA.
DR   PIR; B30102; B30102.
DR   RefSeq; NP_012619.1; NM_001181743.1.
DR   PDB; 7AD3; EM; 3.50 A; G=2-110.
DR   PDBsum; 7AD3; -.
DR   AlphaFoldDB; P18852; -.
DR   EMDB; EMD-11720; -.
DR   SMR; P18852; -.
DR   BioGRID; 33841; 18.
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-314N; -.
DR   IntAct; P18852; 3.
DR   MINT; P18852; -.
DR   STRING; 4932.YJR086W; -.
DR   iPTMnet; P18852; -.
DR   SwissPalm; P18852; -.
DR   MaxQB; P18852; -.
DR   PaxDb; 4932-YJR086W; -.
DR   PeptideAtlas; P18852; -.
DR   DNASU; 853548; -.
DR   EnsemblFungi; YJR086W_mRNA; YJR086W; YJR086W.
DR   GeneID; 853548; -.
DR   KEGG; sce:YJR086W; -.
DR   AGR; SGD:S000003846; -.
DR   SGD; S000003846; STE18.
DR   VEuPathDB; FungiDB:YJR086W; -.
DR   eggNOG; ENOG502S5Z5; Eukaryota.
DR   HOGENOM; CLU_163540_0_0_1; -.
DR   InParanoid; P18852; -.
DR   OMA; CLTIINY; -.
DR   OrthoDB; 1977980at2759; -.
DR   BioCyc; YEAST:G3O-31714-MONOMER; -.
DR   BioGRID-ORCS; 853548; 0 hits in 10 CRISPR screens.
DR   ChiTaRS; STE18; yeast.
DR   PRO; PR:P18852; -.
DR   Proteomes; UP000002311; Chromosome X.
DR   RNAct; P18852; Protein.
DR   GO; GO:0120171; C:Cdc24p-Far1p-Gbetagamma complex; IDA:SGD.
DR   GO; GO:0005938; C:cell cortex; NAS:ComplexPortal.
DR   GO; GO:0071944; C:cell periphery; HDA:SGD.
DR   GO; GO:0005737; C:cytoplasm; IDA:SGD.
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:0005886; C:plasma membrane; IDA:SGD.
DR   GO; GO:0031681; F:G-protein beta-subunit binding; IPI:SGD.
DR   GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR   GO; GO:0000750; P:pheromone-dependent signal transduction involved in conjugation with cellular fusion; IDA:ComplexPortal.
DR   GO; GO:0010969; P:regulation of pheromone-dependent signal transduction involved in conjugation with cellular fusion; NAS:ComplexPortal.
DR   CDD; cd00068; GGL; 1.
DR   Gene3D; 4.10.260.10; Transducin (heterotrimeric G protein), gamma chain; 1.
DR   InterPro; IPR015898; G-protein_gamma-like_dom.
DR   InterPro; IPR036284; GGL_sf.
DR   InterPro; IPR041848; Ste18_fungal.
DR   PANTHER; PTHR28189; GUANINE NUCLEOTIDE-BINDING PROTEIN SUBUNIT GAMMA; 1.
DR   PANTHER; PTHR28189:SF1; GUANINE NUCLEOTIDE-BINDING PROTEIN SUBUNIT GAMMA; 1.
DR   Pfam; PF00631; G-gamma; 1.
DR   SMART; SM01224; G_gamma; 1.
DR   SMART; SM00224; GGL; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Lipoprotein; Membrane; Methylation; Palmitate;
KW   Pheromone response; Prenylation; Reference proteome; Transducer.
FT   CHAIN           1..107
FT                   /note="Guanine nucleotide-binding protein subunit gamma"
FT                   /id="PRO_0000194812"
FT   PROPEP          108..110
FT                   /note="Removed in mature form"
FT                   /id="PRO_0000396775"
FT   MOD_RES         107
FT                   /note="Cysteine methyl ester"
FT                   /evidence="ECO:0000269|PubMed:10523659"
FT   LIPID           106
FT                   /note="S-palmitoyl cysteine"
FT                   /evidence="ECO:0000269|PubMed:10523659,
FT                   ECO:0000269|PubMed:10712512"
FT   LIPID           107
FT                   /note="S-farnesyl cysteine"
FT                   /evidence="ECO:0000269|PubMed:10523659,
FT                   ECO:0000269|PubMed:10712512"
FT   MUTAGEN         106
FT                   /note="C->S: Partial loss of function."
FT                   /evidence="ECO:0000269|PubMed:10523659"
FT   MUTAGEN         107
FT                   /note="C->X: Loss of function."
FT                   /evidence="ECO:0000269|PubMed:7982577"
FT   HELIX           53..65
FT                   /evidence="ECO:0007829|PDB:7AD3"
SQ   SEQUENCE   110 AA;  12625 MW;  6A78E946DA5059FA CRC64;
     MTSVQNSPRL QQPQEQQQQQ QQLSLKIKQL KLKRINELNN KLRKELSRER ITASNACLTI
     INYTSNTKDY TLPELWGYPV AGSNHFIEGL KNAQKNSQMS NSNSVCCTLM
//