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Guanine nucleotide-binding protein alpha-1 subunit (GP1-alpha)

 GPA1_YEAST              Reviewed;         472 AA.
P08539; D3DKU8;
01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
05-JUL-2017, entry version 193.
RecName: Full=Guanine nucleotide-binding protein alpha-1 subunit;
AltName: Full=GP1-alpha;
Name=GPA1; Synonyms=CDC70, DAC1, SCG1; OrderedLocusNames=YHR005C;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=3031665; DOI=10.1073/pnas.84.8.2140;
Nakafuku M., Itoh H., Nakamura S., Kaziro Y.;
"Occurrence in Saccharomyces cerevisiae of a gene homologous to the
cDNA coding for the alpha subunit of mammalian G proteins.";
Proc. Natl. Acad. Sci. U.S.A. 84:2140-2144(1987).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
PubMed=3113738; DOI=10.1016/0092-8674(87)90166-8;
Dietzel C., Kurjan J.;
"The yeast SCG1 gene: a G alpha-like protein implicated in the a- and
alpha-factor response pathway.";
Cell 50:1001-1010(1987).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=8091229; DOI=10.1126/science.8091229;
Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Dover J.,
Du Z., Favello A., Fulton L., Gattung S., Geisel C., Kirsten J.,
Kucaba T., Hillier L.W., Jier M., Johnston L., Langston Y.,
Latreille P., Louis E.J., Macri C., Mardis E., Menezes S., Mouser L.,
Nhan M., Rifkin L., Riles L., St Peter H., Trevaskis E., Vaughan K.,
Vignati D., Wilcox L., Wohldman P., Waterston R., Wilson R.,
Vaudin M.;
"Complete nucleotide sequence of Saccharomyces cerevisiae chromosome
VIII.";
Science 265:2077-2082(1994).
[4]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=17322287; DOI=10.1101/gr.6037607;
Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A.,
Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F.,
Williamson J., Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G.,
Kolodner R.D., LaBaer J.;
"Approaching a complete repository of sequence-verified protein-
encoding clones for Saccharomyces cerevisiae.";
Genome Res. 17:536-543(2007).
[6]
FUNCTION.
PubMed=3136318; DOI=10.1128/MCB.8.6.2484;
Jahng K.-Y., Ferguson J., Reed S.I.;
"Mutations in a gene encoding the alpha subunit of a Saccharomyces
cerevisiae G protein indicate a role in mating pheromone signaling.";
Mol. Cell. Biol. 8:2484-2493(1988).
[7]
FUNCTION.
PubMed=2644047; DOI=10.1016/0092-8674(89)90250-X;
Blinder D., Bouvier S., Jenness D.D.;
"Constitutive mutants in the yeast pheromone response: ordered
function of the gene products.";
Cell 56:479-486(1989).
[8]
FUNCTION.
PubMed=2494429; DOI=10.1128/MCB.9.1.152;
Fujimura H.A.;
"The yeast G-protein homolog is involved in the mating pheromone
signal transduction system.";
Mol. Cell. Biol. 9:152-158(1989).
[9]
FUNCTION, AND MUTAGENESIS OF GLY-50.
PubMed=2548076; DOI=10.1128/MCB.9.6.2289;
Miyajima I., Arai K., Matsumoto K.;
"GPA1Val-50 mutation in the mating-factor signaling pathway in
Saccharomyces cerevisiae.";
Mol. Cell. Biol. 9:2289-2297(1989).
[10]
FUNCTION.
PubMed=2107073;
Nomoto S., Nakayama N., Arai K., Matsumoto K.;
"Regulation of the yeast pheromone response pathway by G protein
subunits.";
EMBO J. 9:691-696(1990).
[11]
FUNCTION.
PubMed=2105453; DOI=10.1128/MCB.10.2.510;
Cole G.M., Stone D.E., Reed S.I.;
"Stoichiometry of G protein subunits affects the Saccharomyces
cerevisiae mating pheromone signal transduction pathway.";
Mol. Cell. Biol. 10:510-517(1990).
[12]
FUNCTION, AND MUTAGENESIS OF GLY-50; GLY-322; GLU-355; GLU-364 AND
GLY-470.
PubMed=2117698; DOI=10.1128/MCB.10.9.4439;
Stone D.E., Reed S.I.;
"G protein mutations that alter the pheromone response in
Saccharomyces cerevisiae.";
Mol. Cell. Biol. 10:4439-4446(1990).
[13]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=2161538; DOI=10.1073/pnas.87.11.4363;
Blumer K.J., Thorner J.;
"Beta and gamma subunits of a yeast guanine nucleotide-binding protein
are not essential for membrane association of the alpha subunit but
are required for receptor coupling.";
Proc. Natl. Acad. Sci. U.S.A. 87:4363-4367(1990).
[14]
MUTAGENESIS OF LYS-467 AND LYS-468.
PubMed=1848203; DOI=10.1101/gad.5.3.467;
Hirsch J.P., Dietzel C., Kurjan J.;
"The carboxyl terminus of Scg1, the G alpha subunit involved in yeast
mating, is implicated in interactions with the pheromone receptors.";
Genes Dev. 5:467-474(1991).
[15]
FUNCTION, AND MUTAGENESIS OF GLY-50; GLY-322; ASN-388 AND ASP-391.
PubMed=1900495; DOI=10.1101/gad.5.3.475;
Kurjan J., Hirsch J.P., Dietzel C.;
"Mutations in the guanine nucleotide-binding domains of a yeast G
alpha protein confer a constitutive or uninducible state to the
pheromone response pathway.";
Genes Dev. 5:475-483(1991).
[16]
MYRISTOYLATION AT GLY-2.
PubMed=1936988; DOI=10.1101/gad.5.11.1969;
Stone D.E., Cole G.M., de Barros Lopes M., Goebl M., Reed S.I.;
"N-myristoylation is required for function of the pheromone-responsive
G alpha protein of yeast: conditional activation of the pheromone
response by a temperature-sensitive N-myristoyl transferase.";
Genes Dev. 5:1969-1981(1991).
[17]
INTERACTION WITH STE4.
PubMed=8417317; DOI=10.1128/MCB.13.1.1;
Clark K.L., Dignard D., Thomas D.Y., Whiteway M.;
"Interactions among the subunits of the G protein involved in
Saccharomyces cerevisiae mating.";
Mol. Cell. Biol. 13:1-8(1993).
[18]
FUNCTION.
PubMed=8231812; DOI=10.1111/j.1365-2958.1993.tb01740.x;
Zhang M., Tipper D.J.;
"Suppression of a dominant G-protein beta-subunit mutation in yeast by
G alpha protein expression.";
Mol. Microbiol. 9:813-821(1993).
[19]
MYRISTOYLATION AT GLY-2.
PubMed=8415763; DOI=10.1073/pnas.90.20.9688;
Dohlman H.G., Goldsmith P., Spiegel A.M., Thorner J.;
"Pheromone action regulates G-protein alpha-subunit myristoylation in
the yeast Saccharomyces cerevisiae.";
Proc. Natl. Acad. Sci. U.S.A. 90:9688-9692(1993).
[20]
PALMITOYLATION AT CYS-3, AND MUTAGENESIS OF GLY-2 AND CYS-3.
PubMed=8942643; DOI=10.1021/bi961846b;
Song J., Dohlman H.G.;
"Partial constitutive activation of pheromone responses by a
palmitoylation-site mutant of a G protein alpha subunit in yeast.";
Biochemistry 35:14806-14817(1996).
[21]
MYRISTOYLATION AT GLY-2, MUTAGENESIS OF GLY-2, AND SUBCELLULAR
LOCATION.
PubMed=8702760; DOI=10.1074/jbc.271.34.20273;
Song J., Hirschman J., Gunn K., Dohlman H.G.;
"Regulation of membrane and subunit interactions by N-myristoylation
of a G protein alpha subunit in yeast.";
J. Biol. Chem. 271:20273-20283(1996).
[22]
INTERACTION WITH SST2.
PubMed=8756677; DOI=10.1128/MCB.16.9.5194;
Dohlman H.G., Song J., Ma D., Courchesne W.E., Thorner J.;
"Sst2, a negative regulator of pheromone signaling in the yeast
Saccharomyces cerevisiae: Expression, localization, and genetic
interaction and physical association with Gpa1 (the G-protein alpha
subunit).";
Mol. Cell. Biol. 16:5194-5209(1996).
[23]
FUNCTION, AND MUTAGENESIS OF GLY-322; GLU-364 AND ASN-388.
PubMed=8887662; DOI=10.1128/MCB.16.11.6325;
Stratton H.F., Zhou J., Reed S.I., Stone D.E.;
"The mating-specific G(alpha) protein of Saccharomyces cerevisiae
downregulates the mating signal by a mechanism that is dependent on
pheromone and independent of G(beta)(gamma) sequestration.";
Mol. Cell. Biol. 16:6325-6337(1996).
[24]
FUNCTION, AND INTERACTION WITH SST2.
PubMed=9537998; DOI=10.1021/bi9729965;
Apanovitch D.M., Slep K.C., Sigler P.B., Dohlman H.G.;
"Sst2 is a GTPase-activating protein for Gpa1: purification and
characterization of a cognate RGS-Galpha protein pair in yeast.";
Biochemistry 37:4815-4822(1998).
[25]
MUTAGENESIS OF GLY-302.
PubMed=9488712; DOI=10.1074/jbc.273.10.5780;
DiBello P.R., Garrison T.R., Apanovitch D.M., Hoffman G., Shuey D.J.,
Mason K., Cockett M.I., Dohlman H.G.;
"Selective uncoupling of RGS action by a single point mutation in the
G protein alpha-subunit.";
J. Biol. Chem. 273:5780-5784(1998).
[26]
MUTAGENESIS OF LYS-54; ARG-327 AND LEU-353.
PubMed=9786851; DOI=10.1074/jbc.273.44.28597;
Apanovitch D.M., Iiri T., Karasawa T., Bourne H.R., Dohlman H.G.;
"Second site suppressor mutations of a GTPase-deficient G-protein
alpha-subunit.";
J. Biol. Chem. 273:28597-28602(1998).
[27]
MUTAGENESIS OF GLY-321 AND GLN-323.
PubMed=9604890; DOI=10.1007/s004380050695;
DeSimone S.M., Kurjan J.;
"Switch-domain mutations in the Saccharomyces cerevisiae G protein
alpha-subunit Gpa1p identify a receptor subtype-biased mating
defect.";
Mol. Gen. Genet. 257:662-671(1998).
[28]
FUNCTION.
PubMed=10356642; DOI=10.1007/BF02738067;
Zhou J., Arora M., Stone D.E.;
"The yeast pheromone-responsive G alpha protein stimulates recovery
from chronic pheromone treatment by two mechanisms that are activated
at distinct levels of stimulus.";
Cell Biochem. Biophys. 30:193-212(1999).
[29]
PALMITOYLATION AT CYS-3, AND MUTAGENESIS OF GLY-2 AND CYS-3.
PubMed=10712512; DOI=10.1091/mbc.11.3.957;
Manahan C.L., Patnana M., Blumer K.J., Linder M.E.;
"Dual lipid modification motifs in G(alpha) and G(gamma) subunits are
required for full activity of the pheromone response pathway in
Saccharomyces cerevisiae.";
Mol. Biol. Cell 11:957-968(2000).
[30]
MUTAGENESIS OF ALA-345, AND FORMATION OF PREACTIVATION COMPLEXES.
PubMed=10866688; DOI=10.1128/MCB.20.14.5321-5329.2000;
Dosil M., Schandel K.A., Gupta E., Jenness D.D., Konopka J.B.;
"The C terminus of the Saccharomyces cerevisiae alpha-factor receptor
contributes to the formation of preactivation complexes with its
cognate G protein.";
Mol. Cell. Biol. 20:5321-5329(2000).
[31]
MUTAGENESIS OF GLY-50.
PubMed=10705368;
DOI=10.1002/(SICI)1097-0061(20000330)16:5<387::AID-YEA525>3.0.CO;2-U;
Kallal L., Fishel R.;
"The GTP hydrolysis defect of the Saccharomyces cerevisiae mutant G-
protein Gpa1(G50V).";
Yeast 16:387-400(2000).
[32]
MUTAGENESIS OF GLU-364 AND ASN-388.
PubMed=11394869; DOI=10.1006/bbrc.2001.4959;
Cismowski M.J., Metodiev M.V., Draper E., Stone D.E.;
"Biochemical analysis of yeast G(alpha) mutants that enhance
adaptation to pheromone.";
Biochem. Biophys. Res. Commun. 284:247-254(2001).
[33]
UBIQUITINATION AT LYS-165, MUTAGENESIS OF LYS-165, AND IDENTIFICATION
BY MASS SPECTROMETRY.
PubMed=11955054; DOI=10.1021/bi015940q;
Marotti L.A. Jr., Newitt R., Wang Y., Aebersold R., Dohlman H.G.;
"Direct identification of a G protein ubiquitination site by mass
spectrometry.";
Biochemistry 41:5067-5074(2002).
[34]
DEPALMITOYLATION.
PubMed=12080046; DOI=10.1074/jbc.M202505200;
Duncan J.A., Gilman A.G.;
"Characterization of Saccharomyces cerevisiae acyl-protein
thioesterase 1, the enzyme responsible for G protein alpha subunit
deacylation in vivo.";
J. Biol. Chem. 277:31740-31752(2002).
[35]
FUNCTION, INTERACTION WITH FUS3, MUTAGENESIS OF 21-LYS-ARG-22, AND
SUBCELLULAR LOCATION.
PubMed=12029138; DOI=10.1126/science.1070540;
Metodiev M.V., Matheos D., Rose M.D., Stone D.E.;
"Regulation of MAPK function by direct interaction with the mating-
specific G(alpha) in yeast.";
Science 296:1483-1486(2002).
[36]
FUNCTION, AND INTERACTION WITH SCP160.
PubMed=14536090; DOI=10.1016/S1097-2765(03)00307-1;
Guo M., Aston C., Burchett S.A., Dyke C., Fields S., Rajarao S.J.R.,
Uetz P., Wang Y., Young K., Dohlman H.G.;
"The yeast G protein alpha subunit Gpa1 transmits a signal through an
RNA binding effector protein Scp160.";
Mol. Cell 12:517-524(2003).
[37]
FUNCTION.
PubMed=12556475; DOI=10.1128/MCB.23.4.1135-1150.2003;
Blackwell E., Halatek I.M., Kim H.-J.N., Ellicott A.T., Obukhov A.A.,
Stone D.E.;
"Effect of the pheromone-responsive G(alpha) and phosphatase proteins
of Saccharomyces cerevisiae on the subcellular localization of the
Fus3 mitogen-activated protein kinase.";
Mol. Cell. Biol. 23:1135-1150(2003).
[38]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
PubMed=14562095; DOI=10.1038/nature02026;
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
Weissman J.S., O'Shea E.K.;
"Global analysis of protein localization in budding yeast.";
Nature 425:686-691(2003).
[39]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
PubMed=14562106; DOI=10.1038/nature02046;
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[40]
FUNCTION.
PubMed=12960402; DOI=10.1073/pnas.1834247100;
Yi T.-M., Kitano H., Simon M.I.;
"A quantitative characterization of the yeast heterotrimeric G protein
cycle.";
Proc. Natl. Acad. Sci. U.S.A. 100:10764-10769(2003).
[41]
MUTAGENESIS OF ASN-388.
PubMed=15197187; DOI=10.1074/jbc.M404896200;
Wu Y.-L., Hooks S.B., Harden T.K., Dohlman H.G.;
"Dominant-negative inhibition of pheromone receptor signaling by a
single point mutation in the G protein alpha subunit.";
J. Biol. Chem. 279:35287-35297(2004).
[42]
ERRATUM.
Wu Y.-L., Hooks S.B., Harden T.K., Dohlman H.G.;
J. Biol. Chem. 280:29988-29988(2005).
[43]
MUTAGENESIS OF ASP-15; PHE-17; LEU-18 AND LYS-54.
PubMed=14767760; DOI=10.1007/s00438-004-0975-y;
Roginskaya M., Connelly S.M., Kim K.S., Patel D., Dumont M.E.;
"Effects of mutations in the N terminal region of the yeast G protein
alpha-subunit Gpa1p on signaling by pheromone receptors.";
Mol. Genet. Genomics 271:237-248(2004).
[44]
FUNCTION OF UBIQUITINATION.
PubMed=15519996; DOI=10.1074/jbc.M411624200;
Wang Y., Marotti L.A. Jr., Lee M.J., Dohlman H.G.;
"Differential regulation of G protein alpha subunit trafficking by
mono-and polyubiquitination.";
J. Biol. Chem. 280:284-291(2005).
[45]
FUNCTION, INTERACTION WITH VPS15 AND VPS34, AND SUBCELLULAR LOCATION.
PubMed=16839886; DOI=10.1016/j.cell.2006.04.045;
Slessareva J.E., Routt S.M., Temple B., Bankaitis V.A., Dohlman H.G.;
"Activation of the phosphatidylinositol 3-kinase Vps34 by a G protein
alpha subunit at the endosome.";
Cell 126:191-203(2006).
[46]
INTERACTION WITH MDM1; RAX1; RGS2 AND SST2, AND ENZYME REGULATION.
PubMed=16467474; DOI=10.1128/EC.5.2.330-346.2006;
Chasse S.A., Flanary P., Parnell S.C., Hao N., Cha J.Y.,
Siderovski D.P., Dohlman H.G.;
"Genome-scale analysis reveals Sst2 as the principal regulator of
mating pheromone signaling in the yeast Saccharomyces cerevisiae.";
Eukaryot. Cell 5:330-346(2006).
[47]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
STRAIN=ADR376;
PubMed=17330950; DOI=10.1021/pr060559j;
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
Elias J.E., Gygi S.P.;
"Large-scale phosphorylation analysis of alpha-factor-arrested
Saccharomyces cerevisiae.";
J. Proteome Res. 6:1190-1197(2007).
[48]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19779198; DOI=10.1126/science.1172867;
Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
"Global analysis of Cdk1 substrate phosphorylation sites provides
insights into evolution.";
Science 325:1682-1686(2009).
[49]
3D-STRUCTURE MODELING.
Gaitatzes C.G., Neer E.J., Smith T.F.;
Submitted (FEB-1998) to the PDB data bank.
-!- FUNCTION: Alpha subunit of the heterotrimeric guanine nucleotide-
binding protein (G protein) that mediates mating pheromone signal
transduction. Binding of alpha-factor or a-factor to its cognate
transmembrane receptor STE2 and STE3, respectively, allows the
receptor to serve as a guanine nucleotide exchange factor (GEF) on
GPA1. The exchange of GDP for GTP on the G protein alpha subunit
alters its interaction with the G protein beta subunit STE4,
leading to dissociation of the G protein beta-gamma dimer STE4-
STE18. The dissociated subunits activate downstream effectors to
activate the mating response pathway and induce changes necessary
to produce mating-competent cells. STE4-STE18 activate the
downstream pheromone signaling MAP kinase cascade leading to
expression of mating-specific genes, inducing cell cycle arrest in
G1, promoting polarized cell growth to form mating projections
(shmoos), and establishing the changes in plasma membrane, cell
wall and nuclear envelope to permit cell-cell fusion (plasmogamy)
and fusion of the two haploid nuclei (karyogamy). GPA1 transmits a
signal that requires direct binding to the effector enzyme PI3K
located at the endosome, promoting increased PI3 production. The
intrinsic GTPase activity of GPA1 determines the duration of
signaling, and is dramatically accelerated by the RGS protein
SST2. In unstimulated cells, GDP-bound GPA1 sequesters the G
protein beta-gamma subunit STE4-STE18, preventing it from
activating the downstream effectors. Also down-regulates the
signal by inhibiting the pheromone-induced accumulation of FUS3 in
the nucleus. {ECO:0000269|PubMed:10356642,
ECO:0000269|PubMed:12029138, ECO:0000269|PubMed:12556475,
ECO:0000269|PubMed:12960402, ECO:0000269|PubMed:14536090,
ECO:0000269|PubMed:15519996, ECO:0000269|PubMed:16839886,
ECO:0000269|PubMed:1900495, ECO:0000269|PubMed:2105453,
ECO:0000269|PubMed:2107073, ECO:0000269|PubMed:2117698,
ECO:0000269|PubMed:2161538, ECO:0000269|PubMed:2494429,
ECO:0000269|PubMed:2548076, ECO:0000269|PubMed:2644047,
ECO:0000269|PubMed:3113738, ECO:0000269|PubMed:3136318,
ECO:0000269|PubMed:8231812, ECO:0000269|PubMed:8887662,
ECO:0000269|PubMed:9537998}.
-!- ENZYME REGULATION: Alternates between an inactive form bound to
GDP and an active form bound to GTP. Activated by the G protein
coupled receptors (GPCRs) STE2 and STE3, which serve as guanine
nucleotide-exchange factors (GEFs), and inactivated by SST2,
probably acting as a GTPase-activating protein (GAP).
{ECO:0000269|PubMed:16467474}.
-!- SUBUNIT: G proteins are composed of 3 units; alpha, beta and
gamma. The alpha chain contains the guanine nucleotide binding
site. In its GDP-bound form, binds to the G protein beta-gamma
dimer STE4-STE18. Directly interacts with the beta subunit STE4.
Probably forms preactivation complexes with unligated receptors
STE2 and STE3. Interacts with FUS3. Pheromone-induced activation
of GPA1 increases its association with FUS3. Interacts with
SCP160. SCP160 binds specifically to the GTP-bound form of GPA1.
Interacts with the phoshpatidylinositol 3-kinase (PI3K) subunits
VPS15 and VPS34 at the endosome. The GTP-bound form of GPA1 binds
directly and selectively to the catalytic subunit VPS34, while the
GDP-bound form binds to VPS15, which appears to function as an
alternative G protein beta subunit for GPA1. Interacts with
regulators of G protein signaling (RGS) proteins MDM1, RAX1, RGS2
and SST2, but SST2 alone binds preferentially to the transition
state conformation of GPA1, indicating that it acts as a GAP for
this G protein. {ECO:0000269|PubMed:12029138,
ECO:0000269|PubMed:14536090, ECO:0000269|PubMed:16467474,
ECO:0000269|PubMed:16839886, ECO:0000269|PubMed:8417317,
ECO:0000269|PubMed:8756677, ECO:0000269|PubMed:9537998}.
-!- INTERACTION:
P11972:SST2; NbExp=3; IntAct=EBI-7376, EBI-18232;
P18851:STE4; NbExp=8; IntAct=EBI-7376, EBI-7390;
P22219:VPS15; NbExp=2; IntAct=EBI-7376, EBI-20347;
P22543:VPS34; NbExp=3; IntAct=EBI-7376, EBI-20405;
-!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor; Cytoplasmic
side. Endosome membrane; Lipid-anchor; Cytoplasmic side.
Note=Localizes predominantly to the plasma membrane in its
inactive, GDP-bound form, and is directed to endosomes once in its
active, GTP-bound form. Concentrates at the tip of the mating
projections.
-!- DOMAIN: Contains an 'insertion' sequence of 109 residues which is
not present in other G-protein alpha chains.
-!- PTM: N-myristoylation by NMT1 is pheromone-stimulated and required
for palmitoylation of Cys-3. This lipid modification anchors the
protein to membranes. Depalmitoylated by YLR118C/APT1.
{ECO:0000269|PubMed:10712512, ECO:0000269|PubMed:1936988,
ECO:0000269|PubMed:8415763, ECO:0000269|PubMed:8702760,
ECO:0000269|PubMed:8942643}.
-!- PTM: Monoubiquitination targets the protein for degradation to the
vacuole, and polyubiquitination tags the protein for degradation
by the proteasome. This may be an additional signaling regulation
mechanism. {ECO:0000269|PubMed:11955054}.
-!- MISCELLANEOUS: Present with 9920 molecules/cell in log phase SD
medium. {ECO:0000269|PubMed:14562106}.
-!- SIMILARITY: Belongs to the G-alpha family. G(q) subfamily.
{ECO:0000305}.
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EMBL; M15867; AAA34650.1; -; Genomic_DNA.
EMBL; M17414; AAA18403.1; -; Unassigned_DNA.
EMBL; U10555; AAB68432.1; -; Genomic_DNA.
EMBL; AY692963; AAT92982.1; -; Genomic_DNA.
EMBL; BK006934; DAA06692.1; -; Genomic_DNA.
PIR; A25906; A25906.
RefSeq; NP_011868.1; NM_001179135.1.
PDB; 1SCG; Model; -; A=1-472.
PDBsum; 1SCG; -.
ProteinModelPortal; P08539; -.
SMR; P08539; -.
BioGrid; 36430; 50.
DIP; DIP-15N; -.
IntAct; P08539; 16.
MINT; MINT-509090; -.
STRING; 4932.YHR005C; -.
iPTMnet; P08539; -.
SwissPalm; P08539; -.
MaxQB; P08539; -.
PRIDE; P08539; -.
DNASU; 856394; -.
EnsemblFungi; YHR005C; YHR005C; YHR005C.
GeneID; 856394; -.
KEGG; sce:YHR005C; -.
EuPathDB; FungiDB:YHR005C; -.
SGD; S000001047; GPA1.
GeneTree; ENSGT00770000120503; -.
HOGENOM; HOG000038730; -.
InParanoid; P08539; -.
KO; K19860; -.
OMA; VARMEDT; -.
OrthoDB; EOG092C25Q3; -.
BioCyc; YEAST:G3O-31070-MONOMER; -.
Reactome; R-SCE-416482; G alpha (12/13) signalling events.
Reactome; R-SCE-418555; G alpha (s) signalling events.
PRO; PR:P08539; -.
Proteomes; UP000002311; Chromosome VIII.
GO; GO:0005768; C:endosome; IDA:SGD.
GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
GO; GO:0005834; C:heterotrimeric G-protein complex; IDA:SGD.
GO; GO:0005886; C:plasma membrane; IDA:SGD.
GO; GO:0031683; F:G-protein beta/gamma-subunit complex binding; IBA:GO_Central.
GO; GO:0001664; F:G-protein coupled receptor binding; IBA:GO_Central.
GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
GO; GO:0003924; F:GTPase activity; IDA:SGD.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004871; F:signal transducer activity; IBA:GO_Central.
GO; GO:0000754; P:adaptation of signaling pathway by response to pheromone involved in conjugation with cellular fusion; IMP:SGD.
GO; GO:0007188; P:adenylate cyclase-modulating G-protein coupled receptor signaling pathway; IBA:GO_Central.
GO; GO:0031684; P:heterotrimeric G-protein complex cycle; IMP:SGD.
GO; GO:0048017; P:inositol lipid-mediated signaling; IMP:SGD.
GO; GO:0000742; P:karyogamy involved in conjugation with cellular fusion; IMP:SGD.
GO; GO:0000743; P:nuclear migration involved in conjugation with cellular fusion; IMP:SGD.
GO; GO:0000750; P:pheromone-dependent signal transduction involved in conjugation with cellular fusion; IMP:SGD.
GO; GO:0071701; P:regulation of MAPK export from nucleus; IMP:SGD.
CDD; cd00066; G-alpha; 1.
InterPro; IPR002975; Fungi_Gprotein_alpha.
InterPro; IPR001019; Gprotein_alpha_su.
InterPro; IPR011025; GproteinA_insert.
InterPro; IPR027417; P-loop_NTPase.
PANTHER; PTHR10218; PTHR10218; 1.
Pfam; PF00503; G-alpha; 1.
PRINTS; PR00318; GPROTEINA.
PRINTS; PR01241; GPROTEINAFNG.
SMART; SM00275; G_alpha; 1.
SUPFAM; SSF47895; SSF47895; 2.
SUPFAM; SSF52540; SSF52540; 2.
1: Evidence at protein level;
3D-structure; Cell membrane; Complete proteome; Endosome; GTP-binding;
Isopeptide bond; Lipoprotein; Magnesium; Membrane; Metal-binding;
Myristate; Nucleotide-binding; Palmitate; Pheromone response;
Reference proteome; Transducer; Ubl conjugation.
INIT_MET 1 1 Removed.
CHAIN 2 472 Guanine nucleotide-binding protein alpha-
1 subunit.
/FTId=PRO_0000203616.
NP_BIND 48 55 GTP. {ECO:0000250}.
NP_BIND 294 300 GTP. {ECO:0000250}.
NP_BIND 319 323 GTP. {ECO:0000250}.
NP_BIND 388 391 GTP. {ECO:0000250}.
REGION 127 235 Insert; not present in other G-proteins.
METAL 55 55 Magnesium. {ECO:0000250}.
METAL 300 300 Magnesium. {ECO:0000250}.
BINDING 444 444 GTP; via amide nitrogen. {ECO:0000250}.
LIPID 2 2 N-myristoyl glycine.
{ECO:0000269|PubMed:1936988,
ECO:0000269|PubMed:8415763,
ECO:0000269|PubMed:8702760}.
LIPID 3 3 S-palmitoyl cysteine.
{ECO:0000269|PubMed:10712512,
ECO:0000269|PubMed:8942643}.
CROSSLNK 165 165 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000269|PubMed:11955054}.
MUTAGEN 2 2 G->A: Abolishes both palmitoylation and
N-myristoylation.
{ECO:0000269|PubMed:10712512,
ECO:0000269|PubMed:8702760,
ECO:0000269|PubMed:8942643}.
MUTAGEN 3 3 C->A: Abolishes palmitoylation but not N-
myristoylation.
{ECO:0000269|PubMed:10712512,
ECO:0000269|PubMed:8942643}.
MUTAGEN 15 15 D->V: Slightly reduces ligand-dependent
pheromone signaling.
{ECO:0000269|PubMed:14767760}.
MUTAGEN 17 17 F->L: Leads to a hypersensitive signaling
phenotype resulting in greatly enhanced
signal at low alpha-factor
concentrations.
{ECO:0000269|PubMed:14767760}.
MUTAGEN 18 18 L->P,Q: Reduces ligand-dependent
pheromone signaling.
{ECO:0000269|PubMed:14767760}.
MUTAGEN 21 22 KR->EE: Impairs interaction with FUS3.
{ECO:0000269|PubMed:12029138}.
MUTAGEN 50 50 G->D: Confers insensitivity to pheromone.
{ECO:0000269|PubMed:10705368,
ECO:0000269|PubMed:1900495,
ECO:0000269|PubMed:2117698,
ECO:0000269|PubMed:2548076}.
MUTAGEN 50 50 G->V: Has increased GTP occupancy and
moderately reduces hydrolysis of GTP,
resulting in a constitutively active form
that down-regulates the pheromone
response and causes hyperadaptation to
pheromone. {ECO:0000269|PubMed:10705368,
ECO:0000269|PubMed:1900495,
ECO:0000269|PubMed:2117698,
ECO:0000269|PubMed:2548076}.
MUTAGEN 54 54 K->E,I: Prevents GDP to GTP exchange;
suppressor of L-323.
{ECO:0000269|PubMed:14767760,
ECO:0000269|PubMed:9786851}.
MUTAGEN 165 165 K->R: Substantial decrease in
ubiquitination.
{ECO:0000269|PubMed:11955054}.
MUTAGEN 297 297 R->H: Slows hydrolysis of GTP.
MUTAGEN 302 302 G->S: In GPA1(SST); weakens interaction
to SST2 and blocks its negative
regulatory effect.
{ECO:0000269|PubMed:9488712}.
MUTAGEN 321 321 G->T: Causes a specific mating defect in
alpha cells.
{ECO:0000269|PubMed:9604890}.
MUTAGEN 322 322 G->A,E,R: Confers insensitivity to
pheromone. {ECO:0000269|PubMed:1900495,
ECO:0000269|PubMed:2117698,
ECO:0000269|PubMed:8887662}.
MUTAGEN 323 323 Q->L: Prevents hydrolysis of GTP;
eliminates the interaction with STE4 and
constitutively activates the pheromone
response pathway.
{ECO:0000269|PubMed:9604890}.
MUTAGEN 327 327 R->S: Suppressor of L-323; does not
prevent GTP binding to GPA1.
{ECO:0000269|PubMed:9786851}.
MUTAGEN 345 345 A->T: Suppressor of a STE2-L236H mutant.
{ECO:0000269|PubMed:10866688}.
MUTAGEN 353 353 Missing: Suppressor of L-323.
{ECO:0000269|PubMed:9786851}.
MUTAGEN 355 355 E->K: Confers insensitivity to pheromone.
{ECO:0000269|PubMed:2117698}.
MUTAGEN 364 364 E->K: Enhances the rate of GDP for GTP
exchange and slows hydrolysis of GTP,
resulting in a constitutively active form
that down-regulates the pheromone
response independently of the pheromone
receptor. {ECO:0000269|PubMed:11394869,
ECO:0000269|PubMed:2117698,
ECO:0000269|PubMed:8887662}.
MUTAGEN 388 388 N->D: Forms a nondissociable complex with
the pheromone receptor in response to
receptor activation, resulting in reduced
pheromone responsiveness.
{ECO:0000269|PubMed:11394869,
ECO:0000269|PubMed:15197187,
ECO:0000269|PubMed:1900495,
ECO:0000269|PubMed:8887662}.
MUTAGEN 388 388 N->K: Causes constitutive activation of
the pheromone response pathway.
{ECO:0000269|PubMed:11394869,
ECO:0000269|PubMed:15197187,
ECO:0000269|PubMed:1900495,
ECO:0000269|PubMed:8887662}.
MUTAGEN 391 391 D->A: Causes constitutive activation of
the pheromone response pathway.
{ECO:0000269|PubMed:1900495}.
MUTAGEN 467 467 K->P: Impairs pheromone signaling in a
and alpha cells.
{ECO:0000269|PubMed:1848203}.
MUTAGEN 468 468 K->P: Impairs pheromone signaling
specifically in a cells.
{ECO:0000269|PubMed:1848203}.
MUTAGEN 470 470 G->D: Confers insensitivity to pheromone.
{ECO:0000269|PubMed:2117698}.
CONFLICT 82 82 W -> R (in Ref. 2; AAA18403).
{ECO:0000305}.
CONFLICT 194 194 A -> V (in Ref. 2; AAA18403).
{ECO:0000305}.
CONFLICT 226 226 R -> K (in Ref. 2; AAA18403).
{ECO:0000305}.
CONFLICT 246 246 K -> R (in Ref. 2; AAA18403).
{ECO:0000305}.
CONFLICT 469 469 I -> S (in Ref. 2; AAA18403).
{ECO:0000305}.
SEQUENCE 472 AA; 54076 MW; 2E87C546E133D6E5 CRC64;
MGCTVSTQTI GDESDPFLQN KRANDVIEQS LQLEKQRDKN EIKLLLLGAG ESGKSTVLKQ
LKLLHQGGFS HQERLQYAQV IWADAIQSMK ILIIQARKLG IQLDCDDPIN NKDLFACKRI
LLKAKALDYI NASVAGGSDF LNDYVLKYSE RYETRRRVQS TGRAKAAFDE DGNISNVKSD
TDRDAETVTQ NEDADRNNSS RINLQDICKD LNQEGDDQMF VRKTSREIQG QNRRNLIHED
IAKAIKQLWN NDKGIKQCFA RSNEFQLEGS AAYYFDNIEK FASPNYVCTD EDILKGRIKT
TGITETEFNI GSSKFKVLDA GGQRSERKKW IHCFEGITAV LFVLAMSEYD QMLFEDERVN
RMHESIMLFD TLLNSKWFKD TPFILFLNKI DLFEEKVKSM PIRKYFPDYQ GRVGDAEAGL
KYFEKIFLSL NKTNKPIYVK RTCATDTQTM KFVLSAVTDL IIQQNLKKIG II


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