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P08539

- GPA1_YEAST

UniProt

P08539 - GPA1_YEAST

Protein

Guanine nucleotide-binding protein alpha-1 subunit

Gene

GPA1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 165 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    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.20 Publications

    Enzyme regulationi

    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).1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi55 – 551MagnesiumBy similarity
    Metal bindingi300 – 3001MagnesiumBy similarity
    Binding sitei444 – 4441GTP; via amide nitrogenBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi48 – 558GTPBy similarity
    Nucleotide bindingi294 – 3007GTPBy similarity
    Nucleotide bindingi319 – 3235GTPBy similarity
    Nucleotide bindingi388 – 3914GTPBy similarity

    GO - Molecular functioni

    1. GTPase activity Source: SGD
    2. GTP binding Source: UniProtKB-KW
    3. metal ion binding Source: UniProtKB-KW
    4. protein binding Source: IntAct
    5. signal transducer activity Source: UniProtKB-KW

    GO - Biological processi

    1. adaptation of signaling pathway by response to pheromone involved in conjugation with cellular fusion Source: SGD
    2. adenylate cyclase-activating G-protein coupled receptor signaling pathway Source: InterPro
    3. heterotrimeric G-protein complex cycle Source: SGD
    4. inositol lipid-mediated signaling Source: SGD
    5. karyogamy involved in conjugation with cellular fusion Source: SGD
    6. nuclear migration involved in conjugation with cellular fusion Source: SGD
    7. pheromone-dependent signal transduction involved in conjugation with cellular fusion Source: SGD
    8. regulation of MAPK export from nucleus Source: SGD

    Keywords - Molecular functioni

    Transducer

    Keywords - Biological processi

    Pheromone response

    Keywords - Ligandi

    GTP-binding, Magnesium, Metal-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciYEAST:G3O-31070-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Guanine nucleotide-binding protein alpha-1 subunit
    Alternative name(s):
    GP1-alpha
    Gene namesi
    Name:GPA1
    Synonyms:CDC70, DAC1, SCG1
    Ordered Locus Names:YHR005C
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome VIII

    Organism-specific databases

    SGDiS000001047. GPA1.

    Subcellular locationi

    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.

    GO - Cellular componenti

    1. endosome Source: SGD
    2. endosome membrane Source: UniProtKB-SubCell
    3. heterotrimeric G-protein complex Source: SGD
    4. plasma membrane Source: SGD

    Keywords - Cellular componenti

    Cell membrane, Endosome, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi2 – 21G → A: Abolishes both palmitoylation and N-myristoylation. 4 Publications
    Mutagenesisi3 – 31C → A: Abolishes palmitoylation but not N-myristoylation. 3 Publications
    Mutagenesisi15 – 151D → V: Slightly reduces ligand-dependent pheromone signaling. 2 Publications
    Mutagenesisi17 – 171F → L: Leads to a hypersensitive signaling phenotype resulting in greatly enhanced signal at low alpha-factor concentrations. 2 Publications
    Mutagenesisi18 – 181L → P or Q: Reduces ligand-dependent pheromone signaling. 2 Publications
    Mutagenesisi21 – 222KR → EE: Impairs interaction with FUS3. 1 Publication
    Mutagenesisi50 – 501G → D: Confers insensitivity to pheromone. 5 Publications
    Mutagenesisi50 – 501G → 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. 5 Publications
    Mutagenesisi54 – 541K → E or I: Prevents GDP to GTP exchange; suppressor of L-323. 3 Publications
    Mutagenesisi165 – 1651K → R: Substantial decrease in ubiquitination. 2 Publications
    Mutagenesisi297 – 2971R → H: Slows hydrolysis of GTP. 1 Publication
    Mutagenesisi302 – 3021G → S in GPA1(SST); weakens interaction to SST2 and blocks its negative regulatory effect. 2 Publications
    Mutagenesisi321 – 3211G → T: Causes a specific mating defect in alpha cells. 2 Publications
    Mutagenesisi322 – 3221G → A, E or R: Confers insensitivity to pheromone. 4 Publications
    Mutagenesisi323 – 3231Q → L: Prevents hydrolysis of GTP; eliminates the interaction with STE4 and constitutively activates the pheromone response pathway. 2 Publications
    Mutagenesisi327 – 3271R → S: Suppressor of L-323; does not prevent GTP binding to GPA1. 2 Publications
    Mutagenesisi345 – 3451A → T: Suppressor of a STE2-L236H mutant. 2 Publications
    Mutagenesisi353 – 3531Missing: Suppressor of L-323. 2 Publications
    Mutagenesisi355 – 3551E → K: Confers insensitivity to pheromone. 2 Publications
    Mutagenesisi364 – 3641E → 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. 4 Publications
    Mutagenesisi388 – 3881N → D: Forms a nondissociable complex with the pheromone receptor in response to receptor activation, resulting in reduced pheromone responsiveness. 5 Publications
    Mutagenesisi388 – 3881N → K: Causes constitutive activation of the pheromone response pathway. 5 Publications
    Mutagenesisi391 – 3911D → A: Causes constitutive activation of the pheromone response pathway. 2 Publications
    Mutagenesisi467 – 4671K → P: Impairs pheromone signaling in a and alpha cells. 2 Publications
    Mutagenesisi468 – 4681K → P: Impairs pheromone signaling specifically in a cells. 2 Publications
    Mutagenesisi470 – 4701G → D: Confers insensitivity to pheromone. 2 Publications

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed
    Chaini2 – 472471Guanine nucleotide-binding protein alpha-1 subunitPRO_0000203616Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Lipidationi2 – 21N-myristoyl glycine3 Publications
    Lipidationi3 – 31S-palmitoyl cysteine2 Publications
    Cross-linki165 – 165Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication

    Post-translational modificationi

    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/APT1.5 Publications
    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.1 Publication

    Keywords - PTMi

    Isopeptide bond, Lipoprotein, Myristate, Palmitate, Ubl conjugation

    Proteomic databases

    MaxQBiP08539.
    PaxDbiP08539.
    PeptideAtlasiP08539.

    Expressioni

    Gene expression databases

    GenevestigatoriP08539.

    Interactioni

    Subunit structurei

    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.7 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    SST2P119723EBI-7376,EBI-18232
    STE4P188518EBI-7376,EBI-7390
    VPS15P222192EBI-7376,EBI-20347
    VPS34P225433EBI-7376,EBI-20405

    Protein-protein interaction databases

    BioGridi36430. 45 interactions.
    DIPiDIP-15N.
    IntActiP08539. 16 interactions.
    MINTiMINT-509090.
    STRINGi4932.YHR005C.

    Structurei

    Secondary structure

    1
    472
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi23 – 3816
    Turni39 – 402
    Beta strandi41 – 477
    Turni50 – 512
    Helixi54 – 6411
    Helixi71 – 755
    Turni76 – 772
    Helixi78 – 9922
    Turni100 – 1001
    Turni216 – 2172
    Helixi218 – 22811
    Beta strandi231 – 2333
    Helixi239 – 24911
    Turni250 – 2512
    Helixi254 – 2607
    Turni261 – 2633
    Turni269 – 2702
    Helixi271 – 2766
    Turni277 – 2771
    Helixi278 – 2825
    Turni284 – 2852
    Helixi290 – 2956
    Beta strandi304 – 3107
    Turni311 – 3122
    Beta strandi313 – 3197
    Turni327 – 3304
    Helixi332 – 3343
    Beta strandi338 – 3469
    Helixi347 – 3504
    Turni354 – 3563
    Helixi361 – 37313
    Turni374 – 3741
    Helixi376 – 3783
    Turni379 – 3802
    Beta strandi383 – 3886
    Helixi390 – 39910
    Helixi402 – 4043
    Turni405 – 4051
    Turni407 – 4082
    Helixi415 – 4195
    Turni420 – 4234
    Helixi424 – 4296
    Turni430 – 4301
    Beta strandi433 – 4353
    Turni444 – 4452
    Helixi447 – 46418

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1SCGmodel-A1-472[»]
    ProteinModelPortaliP08539.
    SMRiP08539. Positions 41-136, 240-462.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni127 – 235109Insert; not present in other G-proteinsAdd
    BLAST

    Domaini

    Contains an 'insertion' sequence of 109 residues which is not present in other G-protein alpha chains.

    Sequence similaritiesi

    Belongs to the G-alpha family. G(q) subfamily.Curated

    Phylogenomic databases

    eggNOGiNOG322962.
    GeneTreeiENSGT00690000102066.
    HOGENOMiHOG000038730.
    KOiK04640.
    OMAiFDGLNAN.
    OrthoDBiEOG7M0P1X.

    Family and domain databases

    Gene3Di1.10.400.10. 2 hits.
    3.40.50.300. 2 hits.
    InterProiIPR002975. Fungi_Gprotein_alpha.
    IPR001019. Gprotein_alpha_su.
    IPR011025. GproteinA_insert.
    IPR027417. P-loop_NTPase.
    [Graphical view]
    PANTHERiPTHR10218. PTHR10218. 1 hit.
    PfamiPF00503. G-alpha. 1 hit.
    [Graphical view]
    PRINTSiPR00318. GPROTEINA.
    PR01241. GPROTEINAFNG.
    SMARTiSM00275. G_alpha. 1 hit.
    [Graphical view]
    SUPFAMiSSF47895. SSF47895. 2 hits.
    SSF52540. SSF52540. 2 hits.

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P08539-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGCTVSTQTI GDESDPFLQN KRANDVIEQS LQLEKQRDKN EIKLLLLGAG    50
    ESGKSTVLKQ LKLLHQGGFS HQERLQYAQV IWADAIQSMK ILIIQARKLG 100
    IQLDCDDPIN NKDLFACKRI LLKAKALDYI NASVAGGSDF LNDYVLKYSE 150
    RYETRRRVQS TGRAKAAFDE DGNISNVKSD TDRDAETVTQ NEDADRNNSS 200
    RINLQDICKD LNQEGDDQMF VRKTSREIQG QNRRNLIHED IAKAIKQLWN 250
    NDKGIKQCFA RSNEFQLEGS AAYYFDNIEK FASPNYVCTD EDILKGRIKT 300
    TGITETEFNI GSSKFKVLDA GGQRSERKKW IHCFEGITAV LFVLAMSEYD 350
    QMLFEDERVN RMHESIMLFD TLLNSKWFKD TPFILFLNKI DLFEEKVKSM 400
    PIRKYFPDYQ GRVGDAEAGL KYFEKIFLSL NKTNKPIYVK RTCATDTQTM 450
    KFVLSAVTDL IIQQNLKKIG II 472
    Length:472
    Mass (Da):54,076
    Last modified:January 23, 2007 - v3
    Checksum:i2E87C546E133D6E5
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti82 – 821W → R in AAA18403. (PubMed:3113738)Curated
    Sequence conflicti194 – 1941A → V in AAA18403. (PubMed:3113738)Curated
    Sequence conflicti226 – 2261R → K in AAA18403. (PubMed:3113738)Curated
    Sequence conflicti246 – 2461K → R in AAA18403. (PubMed:3113738)Curated
    Sequence conflicti469 – 4691I → S in AAA18403. (PubMed:3113738)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M15867 Genomic DNA. Translation: AAA34650.1.
    M17414 Unassigned DNA. Translation: AAA18403.1.
    U10555 Genomic DNA. Translation: AAB68432.1.
    AY692963 Genomic DNA. Translation: AAT92982.1.
    BK006934 Genomic DNA. Translation: DAA06692.1.
    PIRiA25906.
    RefSeqiNP_011868.1. NM_001179135.1.

    Genome annotation databases

    EnsemblFungiiYHR005C; YHR005C; YHR005C.
    GeneIDi856394.
    KEGGisce:YHR005C.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M15867 Genomic DNA. Translation: AAA34650.1 .
    M17414 Unassigned DNA. Translation: AAA18403.1 .
    U10555 Genomic DNA. Translation: AAB68432.1 .
    AY692963 Genomic DNA. Translation: AAT92982.1 .
    BK006934 Genomic DNA. Translation: DAA06692.1 .
    PIRi A25906.
    RefSeqi NP_011868.1. NM_001179135.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1SCG model - A 1-472 [» ]
    ProteinModelPortali P08539.
    SMRi P08539. Positions 41-136, 240-462.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 36430. 45 interactions.
    DIPi DIP-15N.
    IntActi P08539. 16 interactions.
    MINTi MINT-509090.
    STRINGi 4932.YHR005C.

    Proteomic databases

    MaxQBi P08539.
    PaxDbi P08539.
    PeptideAtlasi P08539.

    Protocols and materials databases

    DNASUi 856394.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YHR005C ; YHR005C ; YHR005C .
    GeneIDi 856394.
    KEGGi sce:YHR005C.

    Organism-specific databases

    SGDi S000001047. GPA1.

    Phylogenomic databases

    eggNOGi NOG322962.
    GeneTreei ENSGT00690000102066.
    HOGENOMi HOG000038730.
    KOi K04640.
    OMAi FDGLNAN.
    OrthoDBi EOG7M0P1X.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-31070-MONOMER.

    Miscellaneous databases

    NextBioi 981914.

    Gene expression databases

    Genevestigatori P08539.

    Family and domain databases

    Gene3Di 1.10.400.10. 2 hits.
    3.40.50.300. 2 hits.
    InterProi IPR002975. Fungi_Gprotein_alpha.
    IPR001019. Gprotein_alpha_su.
    IPR011025. GproteinA_insert.
    IPR027417. P-loop_NTPase.
    [Graphical view ]
    PANTHERi PTHR10218. PTHR10218. 1 hit.
    Pfami PF00503. G-alpha. 1 hit.
    [Graphical view ]
    PRINTSi PR00318. GPROTEINA.
    PR01241. GPROTEINAFNG.
    SMARTi SM00275. G_alpha. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47895. SSF47895. 2 hits.
    SSF52540. SSF52540. 2 hits.
    ProtoNeti Search...

    Publicationsi

    1. "Occurrence in Saccharomyces cerevisiae of a gene homologous to the cDNA coding for the alpha subunit of mammalian G proteins."
      Nakafuku M., Itoh H., Nakamura S., Kaziro Y.
      Proc. Natl. Acad. Sci. U.S.A. 84:2140-2144(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "The yeast SCG1 gene: a G alpha-like protein implicated in the a- and alpha-factor response pathway."
      Dietzel C., Kurjan J.
      Cell 50:1001-1010(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    4. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    5. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    6. "Mutations in a gene encoding the alpha subunit of a Saccharomyces cerevisiae G protein indicate a role in mating pheromone signaling."
      Jahng K.-Y., Ferguson J., Reed S.I.
      Mol. Cell. Biol. 8:2484-2493(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    7. "Constitutive mutants in the yeast pheromone response: ordered function of the gene products."
      Blinder D., Bouvier S., Jenness D.D.
      Cell 56:479-486(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    8. "The yeast G-protein homolog is involved in the mating pheromone signal transduction system."
      Fujimura H.A.
      Mol. Cell. Biol. 9:152-158(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    9. "GPA1Val-50 mutation in the mating-factor signaling pathway in Saccharomyces cerevisiae."
      Miyajima I., Arai K., Matsumoto K.
      Mol. Cell. Biol. 9:2289-2297(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF GLY-50.
    10. "Regulation of the yeast pheromone response pathway by G protein subunits."
      Nomoto S., Nakayama N., Arai K., Matsumoto K.
      EMBO J. 9:691-696(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    11. "Stoichiometry of G protein subunits affects the Saccharomyces cerevisiae mating pheromone signal transduction pathway."
      Cole G.M., Stone D.E., Reed S.I.
      Mol. Cell. Biol. 10:510-517(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    12. "G protein mutations that alter the pheromone response in Saccharomyces cerevisiae."
      Stone D.E., Reed S.I.
      Mol. Cell. Biol. 10:4439-4446(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF GLY-50; GLY-322; GLU-355; GLU-364 AND GLY-470.
    13. "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."
      Blumer K.J., Thorner J.
      Proc. Natl. Acad. Sci. U.S.A. 87:4363-4367(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    14. "The carboxyl terminus of Scg1, the G alpha subunit involved in yeast mating, is implicated in interactions with the pheromone receptors."
      Hirsch J.P., Dietzel C., Kurjan J.
      Genes Dev. 5:467-474(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF LYS-467 AND LYS-468.
    15. "Mutations in the guanine nucleotide-binding domains of a yeast G alpha protein confer a constitutive or uninducible state to the pheromone response pathway."
      Kurjan J., Hirsch J.P., Dietzel C.
      Genes Dev. 5:475-483(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF GLY-50; GLY-322; ASN-388 AND ASP-391.
    16. "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."
      Stone D.E., Cole G.M., de Barros Lopes M., Goebl M., Reed S.I.
      Genes Dev. 5:1969-1981(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: MYRISTOYLATION AT GLY-2.
    17. "Interactions among the subunits of the G protein involved in Saccharomyces cerevisiae mating."
      Clark K.L., Dignard D., Thomas D.Y., Whiteway M.
      Mol. Cell. Biol. 13:1-8(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH STE4.
    18. "Suppression of a dominant G-protein beta-subunit mutation in yeast by G alpha protein expression."
      Zhang M., Tipper D.J.
      Mol. Microbiol. 9:813-821(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    19. "Pheromone action regulates G-protein alpha-subunit myristoylation in the yeast Saccharomyces cerevisiae."
      Dohlman H.G., Goldsmith P., Spiegel A.M., Thorner J.
      Proc. Natl. Acad. Sci. U.S.A. 90:9688-9692(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: MYRISTOYLATION AT GLY-2.
    20. "Partial constitutive activation of pheromone responses by a palmitoylation-site mutant of a G protein alpha subunit in yeast."
      Song J., Dohlman H.G.
      Biochemistry 35:14806-14817(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: PALMITOYLATION AT CYS-3, MUTAGENESIS OF GLY-2 AND CYS-3.
    21. "Regulation of membrane and subunit interactions by N-myristoylation of a G protein alpha subunit in yeast."
      Song J., Hirschman J., Gunn K., Dohlman H.G.
      J. Biol. Chem. 271:20273-20283(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: MYRISTOYLATION AT GLY-2, MUTAGENESIS OF GLY-2, SUBCELLULAR LOCATION.
    22. "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)."
      Dohlman H.G., Song J., Ma D., Courchesne W.E., Thorner J.
      Mol. Cell. Biol. 16:5194-5209(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SST2.
    23. "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."
      Stratton H.F., Zhou J., Reed S.I., Stone D.E.
      Mol. Cell. Biol. 16:6325-6337(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF GLY-322; GLU-364 AND ASN-388.
    24. "Sst2 is a GTPase-activating protein for Gpa1: purification and characterization of a cognate RGS-Galpha protein pair in yeast."
      Apanovitch D.M., Slep K.C., Sigler P.B., Dohlman H.G.
      Biochemistry 37:4815-4822(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH SST2.
    25. "Selective uncoupling of RGS action by a single point mutation in the G protein alpha-subunit."
      DiBello P.R., Garrison T.R., Apanovitch D.M., Hoffman G., Shuey D.J., Mason K., Cockett M.I., Dohlman H.G.
      J. Biol. Chem. 273:5780-5784(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF GLY-302.
    26. "Second site suppressor mutations of a GTPase-deficient G-protein alpha-subunit."
      Apanovitch D.M., Iiri T., Karasawa T., Bourne H.R., Dohlman H.G.
      J. Biol. Chem. 273:28597-28602(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF LYS-54; ARG-327 AND LEU-353.
    27. "Switch-domain mutations in the Saccharomyces cerevisiae G protein alpha-subunit Gpa1p identify a receptor subtype-biased mating defect."
      DeSimone S.M., Kurjan J.
      Mol. Gen. Genet. 257:662-671(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF GLY-321 AND GLN-323.
    28. "The yeast pheromone-responsive G alpha protein stimulates recovery from chronic pheromone treatment by two mechanisms that are activated at distinct levels of stimulus."
      Zhou J., Arora M., Stone D.E.
      Cell Biochem. Biophys. 30:193-212(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    29. "Dual lipid modification motifs in G(alpha) and G(gamma) subunits are required for full activity of the pheromone response pathway in Saccharomyces cerevisiae."
      Manahan C.L., Patnana M., Blumer K.J., Linder M.E.
      Mol. Biol. Cell 11:957-968(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: PALMITOYLATION AT CYS-3, MUTAGENESIS OF GLY-2 AND CYS-3.
    30. "The C terminus of the Saccharomyces cerevisiae alpha-factor receptor contributes to the formation of preactivation complexes with its cognate G protein."
      Dosil M., Schandel K.A., Gupta E., Jenness D.D., Konopka J.B.
      Mol. Cell. Biol. 20:5321-5329(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF ALA-345, FORMATION OF PREACTIVATION COMPLEXES.
    31. "The GTP hydrolysis defect of the Saccharomyces cerevisiae mutant G-protein Gpa1(G50V)."
      Kallal L., Fishel R.
      Yeast 16:387-400(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF GLY-50.
    32. "Biochemical analysis of yeast G(alpha) mutants that enhance adaptation to pheromone."
      Cismowski M.J., Metodiev M.V., Draper E., Stone D.E.
      Biochem. Biophys. Res. Commun. 284:247-254(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF GLU-364 AND ASN-388.
    33. "Direct identification of a G protein ubiquitination site by mass spectrometry."
      Marotti L.A. Jr., Newitt R., Wang Y., Aebersold R., Dohlman H.G.
      Biochemistry 41:5067-5074(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: UBIQUITINATION AT LYS-165, MUTAGENESIS OF LYS-165, IDENTIFICATION BY MASS SPECTROMETRY.
    34. "Characterization of Saccharomyces cerevisiae acyl-protein thioesterase 1, the enzyme responsible for G protein alpha subunit deacylation in vivo."
      Duncan J.A., Gilman A.G.
      J. Biol. Chem. 277:31740-31752(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: DEPALMITOYLATION.
    35. "Regulation of MAPK function by direct interaction with the mating-specific G(alpha) in yeast."
      Metodiev M.V., Matheos D., Rose M.D., Stone D.E.
      Science 296:1483-1486(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH FUS3, MUTAGENESIS OF 21-LSY-ARG-22, SUBCELLULAR LOCATION.
    36. "The yeast G protein alpha subunit Gpa1 transmits a signal through an RNA binding effector protein Scp160."
      Guo M., Aston C., Burchett S.A., Dyke C., Fields S., Rajarao S.J.R., Uetz P., Wang Y., Young K., Dohlman H.G.
      Mol. Cell 12:517-524(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH SCP160.
    37. "Effect of the pheromone-responsive G(alpha) and phosphatase proteins of Saccharomyces cerevisiae on the subcellular localization of the Fus3 mitogen-activated protein kinase."
      Blackwell E., Halatek I.M., Kim H.-J.N., Ellicott A.T., Obukhov A.A., Stone D.E.
      Mol. Cell. Biol. 23:1135-1150(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    38. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    39. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    40. "A quantitative characterization of the yeast heterotrimeric G protein cycle."
      Yi T.-M., Kitano H., Simon M.I.
      Proc. Natl. Acad. Sci. U.S.A. 100:10764-10769(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    41. "Dominant-negative inhibition of pheromone receptor signaling by a single point mutation in the G protein alpha subunit."
      Wu Y.-L., Hooks S.B., Harden T.K., Dohlman H.G.
      J. Biol. Chem. 279:35287-35297(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF ASN-388.
    42. Erratum
      Wu Y.-L., Hooks S.B., Harden T.K., Dohlman H.G.
      J. Biol. Chem. 280:29988-29988(2005)
    43. "Effects of mutations in the N terminal region of the yeast G protein alpha-subunit Gpa1p on signaling by pheromone receptors."
      Roginskaya M., Connelly S.M., Kim K.S., Patel D., Dumont M.E.
      Mol. Genet. Genomics 271:237-248(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF ASP-15; PHE-17; LEU-18 AND LYS-54.
    44. "Differential regulation of G protein alpha subunit trafficking by mono-and polyubiquitination."
      Wang Y., Marotti L.A. Jr., Lee M.J., Dohlman H.G.
      J. Biol. Chem. 280:284-291(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION OF UBIQUITINATION.
    45. "Activation of the phosphatidylinositol 3-kinase Vps34 by a G protein alpha subunit at the endosome."
      Slessareva J.E., Routt S.M., Temple B., Bankaitis V.A., Dohlman H.G.
      Cell 126:191-203(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH VPS15 AND VPS34, SUBCELLULAR LOCATION.
    46. "Genome-scale analysis reveals Sst2 as the principal regulator of mating pheromone signaling in the yeast Saccharomyces cerevisiae."
      Chasse S.A., Flanary P., Parnell S.C., Hao N., Cha J.Y., Siderovski D.P., Dohlman H.G.
      Eukaryot. Cell 5:330-346(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MDM1; RAX1; RGS2 AND SST2, ENZYME REGULATION.
    47. "Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
      Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
      J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Strain: ADR376.
    48. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
      Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
      Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    49. Gaitatzes C.G., Neer E.J., Smith T.F.
      Submitted (FEB-1998) to the PDB data bank
      Cited for: 3D-STRUCTURE MODELING.

    Entry informationi

    Entry nameiGPA1_YEAST
    AccessioniPrimary (citable) accession number: P08539
    Secondary accession number(s): D3DKU8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1988
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 165 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Present with 9920 molecules/cell in log phase SD medium.1 Publication

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families
    3. Yeast
      Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
    4. Yeast chromosome VIII
      Yeast (Saccharomyces cerevisiae) chromosome VIII: entries and gene names

    External Data

    Dasty 3