Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Guanine nucleotide-binding protein alpha-2 subunit

Gene

GPA2

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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

  • GTPase activity Source: SGD
  • GTP binding Source: UniProtKB-KW
  • metal ion binding Source: UniProtKB-KW
  • signal transducer activity Source: UniProtKB-KW

GO - Biological processi

  • adenylate cyclase-activating G-protein coupled receptor signaling pathway Source: SGD
  • ascospore formation Source: SGD
  • glucose mediated signaling pathway Source: SGD
  • hexose mediated signaling Source: SGD
  • metabolic process Source: GOC
  • pseudohyphal growth Source: SGD
  • replicative cell aging Source: SGD
  • signal transduction Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Transducer

Keywords - Ligandi

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

Enzyme and pathway databases

BioCyciYEAST:G3O-30204-MONOMER.
ReactomeiREACT_288501. Inactivation, recovery and regulation of the phototransduction cascade.
REACT_291144. G alpha (i) signalling events.
REACT_306630. G alpha (z) signalling events.
REACT_336917. PLC beta mediated events.
REACT_338076. G-protein activation.

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 Componenti: Chromosome V

Organism-specific databases

CYGDiYER020w.
EuPathDBiFungiDB:YER020W.
SGDiS000000822. GPA2.

Subcellular locationi

GO - Cellular componenti

  • plasma membrane Source: SGD
Complete GO annotation...

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.

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. 80 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.
GeneTreeiENSGT00770000120503.
HOGENOMiHOG000038730.
InParanoidiP10823.
KOiK04640.
OMAiVNSRWFS.
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

« Hide

        10         20         30         40         50
MGLCASSEKN GSTPDTQTAS AGSDNVGKAK VPPKQEPQKT VRTVNTANQQ
60 70 80 90 100
EKQQQRQQQP SPHNVKDRKE QNGSINNAIS PTATANTSGS QQINIDSALR
110 120 130 140 150
DRSSNVAAQP SLSDASSGSN DKELKVLLLG AGESGKSTVL QQLKILHQNG
160 170 180 190 200
FSEQEIKEYI PLIYQNLLEI GRNLIQARTR FNVNLEPECE LTQQDLSRTM
210 220 230 240 250
SYEMPNNYTG QFPEDIAGVI STLWALPSTQ DLVNGPNASK FYLMDSTPYF
260 270 280 290 300
MENFTRITSP NYRPTQQDIL RSRQMTSGIF DTVIDMGSDI KMHIYDVGGQ
310 320 330 340 350
RSERKKWIHC FDNVTLVIFC VSLSEYDQTL MEDKNQNRFQ ESLVLFDNIV
360 370 380 390 400
NSRWFARTSV VLFLNKIDLF AEKLSKVPME NYFPDYTGGS DINKAAKYIL
410 420 430 440
WRFVQLNRAN LSIYPHVTQA TDTSNIRLVF AAIKETILEN TLKDSGVLQ
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

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

Protein-protein interaction databases

BioGridi36754. 80 interactions.
DIPiDIP-4346N.
IntActiP10823. 38 interactions.
MINTiMINT-548605.
STRINGi4932.YER020W.

Proteomic databases

MaxQBiP10823.
PaxDbiP10823.
PeptideAtlasiP10823.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CYGDiYER020w.
EuPathDBiFungiDB:YER020W.
SGDiS000000822. GPA2.

Phylogenomic databases

eggNOGiNOG322962.
GeneTreeiENSGT00770000120503.
HOGENOMiHOG000038730.
InParanoidiP10823.
KOiK04640.
OMAiVNSRWFS.
OrthoDBiEOG7M0P1X.

Enzyme and pathway databases

BioCyciYEAST:G3O-30204-MONOMER.
ReactomeiREACT_288501. Inactivation, recovery and regulation of the phototransduction cascade.
REACT_291144. G alpha (i) signalling events.
REACT_306630. G alpha (z) signalling events.
REACT_336917. PLC beta mediated events.
REACT_338076. G-protein activation.

Miscellaneous databases

NextBioi982873.
PROiP10823.

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.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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: June 24, 2015
This is version 158 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.