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P10823

- GPA2_YEAST

UniProt

P10823 - GPA2_YEAST

Protein

Guanine nucleotide-binding protein alpha-2 subunit

Gene

GPA2

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 150 (01 Oct 2014)
      Sequence version 2 (01 Feb 1995)
      Previous versions | rss
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    Functioni

    Alpha subunit of the heterotrimeric guanine nucleotide-binding protein (G protein) involved in glucose-induced cAMP signaling. Binds to its cognate transmembrane receptor GPR1, which senses extracellular carbon sources, and activates cAMP-PKA signaling and governs diploid pseudohyphal differentiation and haploid invasive growth. The G protein beta-mimic proteins GPB1 and GPB2 inhibit GPA2-GPR1 coupling, probably to reduce signaling in the absence of glucose.2 Publications

    Enzyme regulationi

    Alternates between an inactive form bound to GDP and an active form bound to GTP. Activated by the G protein coupled receptor (GPCR) GPR1, which serves as a guanine nucleotide-exchange factor (GEF), and inactivated by RGS2, acting as a GTPase-activating protein (GAP) for GPA2.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi137 – 1371MagnesiumBy similarity
    Metal bindingi276 – 2761MagnesiumBy similarity
    Binding sitei420 – 4201GTP; via amide nitrogenBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi130 – 1378GTPBy similarity
    Nucleotide bindingi270 – 2767GTPBy similarity
    Nucleotide bindingi296 – 3005GTPBy similarity
    Nucleotide bindingi365 – 3684GTPBy similarity

    GO - Molecular functioni

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

    GO - Biological processi

    1. adenylate cyclase-activating G-protein coupled receptor signaling pathway Source: SGD
    2. ascospore formation Source: SGD
    3. glucose mediated signaling pathway Source: SGD
    4. hexose mediated signaling Source: SGD
    5. pseudohyphal growth Source: SGD
    6. replicative cell aging Source: SGD
    7. signal transduction Source: SGD

    Keywords - Molecular functioni

    Transducer

    Keywords - Ligandi

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

    Enzyme and pathway databases

    BioCyciYEAST:G3O-30204-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Guanine nucleotide-binding protein alpha-2 subunit
    Alternative name(s):
    GP2-alpha
    Gene namesi
    Name:GPA2
    Synonyms:SSP101
    Ordered Locus Names:YER020W
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome V

    Organism-specific databases

    CYGDiYER020w.
    SGDiS000000822. GPA2.

    Subcellular locationi

    Cell membrane 2 Publications; Lipid-anchor 2 Publications; Cytoplasmic side 2 Publications

    GO - Cellular componenti

    1. plasma membrane Source: SGD

    Keywords - Cellular componenti

    Cell membrane, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi2 – 21G → A: Abolishes both palmitoylation and N-myristoylation. 1 Publication
    Mutagenesisi4 – 41C → A: Abolishes palmitoylation but not N-myristoylation. 1 Publication
    Mutagenesisi6 – 61S → A: Abolishes both palmitoylation and N-myristoylation. 1 Publication
    Mutagenesisi132 – 1321G → V: Locks GPA2 in its activated GTP-bound form and abrogates the negative control by RGS2. 2 Publications
    Mutagenesisi299 – 2991G → A: Dominant negativ allele unable to undergo the GTP-induced conformational change. 2 Publications
    Mutagenesisi300 – 3001Q → L: Dominant active allele that abolishes intrinsic GTPase activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed
    Chaini2 – 449448Guanine nucleotide-binding protein alpha-2 subunitPRO_0000203617Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Lipidationi2 – 21N-myristoyl glycine1 Publication
    Lipidationi4 – 41S-palmitoyl cysteine1 Publication

    Post-translational modificationi

    Myristoylation at Gly-2 and palmitoylation at Cys-4 are required for membrane localization and function of the protein.1 Publication

    Keywords - PTMi

    Lipoprotein, Myristate, Palmitate

    Proteomic databases

    MaxQBiP10823.
    PaxDbiP10823.
    PeptideAtlasiP10823.

    Expressioni

    Gene expression databases

    GenevestigatoriP10823.

    Interactioni

    Subunit structurei

    G proteins are composed of 3 units; alpha, beta and gamma. The alpha chain contains the guanine nucleotide binding site. GPA2 interacts with the kelch repeat beta-mimic proteins GPB1 and GPB2 and with the gamma subunit GPG1. Interacts with the G protein coupled receptor GPR1. Interacts also with regulators of G protein signaling (RGS) protein RGS2.3 Publications

    Protein-protein interaction databases

    BioGridi36754. 79 interactions.
    DIPiDIP-4346N.
    IntActiP10823. 38 interactions.
    MINTiMINT-548605.
    STRINGi4932.YER020W.

    Structurei

    3D structure databases

    ProteinModelPortaliP10823.
    SMRiP10823. Positions 122-444.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiNOG322962.
    GeneTreeiENSGT00690000101672.
    HOGENOMiHOG000038730.
    KOiK04640.
    OMAiLEPECEL.
    OrthoDBiEOG7M0P1X.

    Family and domain databases

    Gene3Di1.10.400.10. 1 hit.
    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. 1 hit.
    SSF52540. SSF52540. 2 hits.

    Sequencei

    Sequence statusi: Complete.

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

    P10823-1 [UniParc]FASTAAdd to Basket

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    MGLCASSEKN GSTPDTQTAS AGSDNVGKAK VPPKQEPQKT VRTVNTANQQ    50
    EKQQQRQQQP SPHNVKDRKE QNGSINNAIS PTATANTSGS QQINIDSALR 100
    DRSSNVAAQP SLSDASSGSN DKELKVLLLG AGESGKSTVL QQLKILHQNG 150
    FSEQEIKEYI PLIYQNLLEI GRNLIQARTR FNVNLEPECE LTQQDLSRTM 200
    SYEMPNNYTG QFPEDIAGVI STLWALPSTQ DLVNGPNASK FYLMDSTPYF 250
    MENFTRITSP NYRPTQQDIL RSRQMTSGIF DTVIDMGSDI KMHIYDVGGQ 300
    RSERKKWIHC FDNVTLVIFC VSLSEYDQTL MEDKNQNRFQ ESLVLFDNIV 350
    NSRWFARTSV VLFLNKIDLF AEKLSKVPME NYFPDYTGGS DINKAAKYIL 400
    WRFVQLNRAN LSIYPHVTQA TDTSNIRLVF AAIKETILEN TLKDSGVLQ 449
    Length:449
    Mass (Da):50,448
    Last modified:February 1, 1995 - v2
    Checksum:i881B91792AE91748
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti375 – 3751S → R in AAA34651. (PubMed:2830616)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J03609 Genomic DNA. Translation: AAA34651.1.
    U18778 Genomic DNA. Translation: AAB64553.1.
    BK006939 Genomic DNA. Translation: DAA07673.1.
    PIRiS50478.
    RefSeqiNP_010937.3. NM_001178911.3.

    Genome annotation databases

    EnsemblFungiiYER020W; YER020W; YER020W.
    GeneIDi856741.
    KEGGisce:YER020W.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J03609 Genomic DNA. Translation: AAA34651.1 .
    U18778 Genomic DNA. Translation: AAB64553.1 .
    BK006939 Genomic DNA. Translation: DAA07673.1 .
    PIRi S50478.
    RefSeqi NP_010937.3. NM_001178911.3.

    3D structure databases

    ProteinModelPortali P10823.
    SMRi P10823. Positions 122-444.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 36754. 79 interactions.
    DIPi DIP-4346N.
    IntActi P10823. 38 interactions.
    MINTi MINT-548605.
    STRINGi 4932.YER020W.

    Proteomic databases

    MaxQBi P10823.
    PaxDbi P10823.
    PeptideAtlasi P10823.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YER020W ; YER020W ; YER020W .
    GeneIDi 856741.
    KEGGi sce:YER020W.

    Organism-specific databases

    CYGDi YER020w.
    SGDi S000000822. GPA2.

    Phylogenomic databases

    eggNOGi NOG322962.
    GeneTreei ENSGT00690000101672.
    HOGENOMi HOG000038730.
    KOi K04640.
    OMAi LEPECEL.
    OrthoDBi EOG7M0P1X.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-30204-MONOMER.

    Miscellaneous databases

    NextBioi 982873.

    Gene expression databases

    Genevestigatori P10823.

    Family and domain databases

    Gene3Di 1.10.400.10. 1 hit.
    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. 1 hit.
    SSF52540. SSF52540. 2 hits.
    ProtoNeti Search...

    Publicationsi

    1. "Isolation of a second yeast Saccharomyces cerevisiae gene (GPA2) coding for guanine nucleotide-binding regulatory protein: studies on its structure and possible functions."
      Nakafuku M., Obara T., Kaibuchi K., Miyajima I., Miyajima A., Itoh H., Nakamura S., Arai K., Matsumoto K., Kaziro Y.
      Proc. Natl. Acad. Sci. U.S.A. 85:1374-1378(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    3. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    4. "A novel regulator of G protein signalling in yeast, Rgs2, downregulates glucose-activation of the cAMP pathway through direct inhibition of Gpa2."
      Versele M., de Winde J.H., Thevelein J.M.
      EMBO J. 18:5577-5591(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH RGS2, MUTAGENESIS OF GLY-132.
    5. "The Galpha protein Gpa2 controls yeast differentiation by interacting with kelch repeat proteins that mimic Gbeta subunits."
      Harashima T., Heitman J.
      Mol. Cell 10:163-173(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH GPG1; GPB1 AND GPB2, MUTAGENESIS OF GLY-132; GLY-299 AND GLN-300.
    6. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    7. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    8. "Galpha subunit Gpa2 recruits kelch repeat subunits that inhibit receptor-G protein coupling during cAMP-induced dimorphic transitions in Saccharomyces cerevisiae."
      Harashima T., Heitman J.
      Mol. Biol. Cell 16:4557-4571(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MYRISTOYLATION AT GLY-2, PALMITOYLATION AT CYS-4, MUTAGENESIS OF GLY-2; CYS-4; SER-6 AND GLY-299, SUBCELLULAR LOCATION, INTERACTION WITH GPB2 AND GPR1.
    9. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
      Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
      Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    10. "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].

    Entry informationi

    Entry nameiGPA2_YEAST
    AccessioniPrimary (citable) accession number: P10823
    Secondary accession number(s): D3DLR9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1989
    Last sequence update: February 1, 1995
    Last modified: October 1, 2014
    This is version 150 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Present with 4570 molecules/cell in log phase SD medium.1 Publication

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

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

    External Data

    Dasty 3