UniProtKB - P10823 (GPA2_YEAST)
Protein
Guanine nucleotide-binding protein alpha-2 subunit
Gene
GPA2
Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
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
Miscellaneous
Present with 4570 molecules/cell in log phase SD medium.1 Publication
Activity 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 key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Metal bindingi | 137 | MagnesiumBy similarity | 1 | |
Metal bindingi | 276 | MagnesiumBy similarity | 1 | |
Binding sitei | 420 | GTP; via amide nitrogenBy similarity | 1 |
Regions
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Nucleotide bindingi | 130 – 137 | GTPBy similarity | 8 | |
Nucleotide bindingi | 270 – 276 | GTPBy similarity | 7 | |
Nucleotide bindingi | 296 – 300 | GTPBy similarity | 5 | |
Nucleotide bindingi | 365 – 368 | GTPBy similarity | 4 |
GO - Molecular functioni
- G-protein beta/gamma-subunit complex binding Source: GO_Central
- G protein-coupled receptor binding Source: GO_Central
- GTPase activity Source: SGD
- GTP binding Source: UniProtKB-KW
- metal ion binding Source: UniProtKB-KW
GO - Biological processi
- adenylate cyclase-activating G protein-coupled receptor signaling pathway Source: SGD
- adenylate cyclase-modulating G protein-coupled receptor signaling pathway Source: GO_Central
- ascospore formation Source: SGD
- glucose mediated signaling pathway Source: SGD
- hexose mediated signaling Source: SGD
- invasive growth in response to glucose limitation Source: SGD
- protein kinase A signaling Source: SGD
- pseudohyphal growth Source: SGD
- regulation of cell size Source: SGD
- signal transduction Source: SGD
Keywordsi
Molecular function | Transducer |
Ligand | GTP-binding, Magnesium, Metal-binding, Nucleotide-binding |
Enzyme and pathway databases
Reactomei | R-SCE-399997, Acetylcholine regulates insulin secretion R-SCE-416476, G alpha (q) signalling events R-SCE-416482, G alpha (12/13) signalling events R-SCE-418592, ADP signalling through P2Y purinoceptor 1 R-SCE-434316, Fatty Acids bound to GPR40 (FFAR1) regulate insulin secretion |
Names & Taxonomyi
Protein namesi | Recommended name: Guanine nucleotide-binding protein alpha-2 subunitAlternative name(s): GP2-alpha |
Gene namesi | Name:GPA2 Synonyms:SSP101 Ordered Locus Names:YER020W |
Organismi | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
Taxonomic identifieri | 559292 [NCBI] |
Taxonomic lineagei | Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › |
Proteomesi |
|
Organism-specific databases
SGDi | S000000822, GPA2 |
VEuPathDBi | FungiDB:YER020W |
Subcellular locationi
Plasma membrane
- Cell membrane 2 Publications; Lipid-anchor 2 Publications; Cytoplasmic side 2 Publications
Cytosol
- cytosol Source: SGD
Mitochondrion
- mitochondrion Source: SGD
Plasma Membrane
- heterotrimeric G-protein complex Source: GO_Central
- plasma membrane Source: SGD
Keywords - Cellular componenti
Cell membrane, MembranePathology & Biotechi
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 2 | G → A: Abolishes both palmitoylation and N-myristoylation. 1 Publication | 1 | |
Mutagenesisi | 4 | C → A: Abolishes palmitoylation but not N-myristoylation. 1 Publication | 1 | |
Mutagenesisi | 6 | S → A: Abolishes both palmitoylation and N-myristoylation. 1 Publication | 1 | |
Mutagenesisi | 132 | G → V: Locks GPA2 in its activated GTP-bound form and abrogates the negative control by RGS2. 2 Publications | 1 | |
Mutagenesisi | 299 | G → A: Dominant negative allele unable to undergo the GTP-induced conformational change. 2 Publications | 1 | |
Mutagenesisi | 300 | Q → L: Dominant active allele that abolishes intrinsic GTPase activity. 1 Publication | 1 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Initiator methioninei | Removed | |||
ChainiPRO_0000203617 | 2 – 449 | Guanine nucleotide-binding protein alpha-2 subunitAdd BLAST | 448 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Lipidationi | 2 | N-myristoyl glycine1 Publication | 1 | |
Lipidationi | 4 | S-palmitoyl cysteine1 Publication | 1 |
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, PalmitateProteomic databases
MaxQBi | P10823 |
PaxDbi | P10823 |
PRIDEi | P10823 |
PTM databases
iPTMneti | P10823 |
SwissPalmi | P10823 |
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 PublicationsBinary interactionsi
Hide detailsP10823
With | #Exp. | IntAct |
---|---|---|
CYR1 [P08678] | 3 | EBI-7382,EBI-5364 |
GPB2 [P39717] | 4 | EBI-7382,EBI-20711 |
GO - Molecular functioni
- G protein-coupled receptor binding Source: GO_Central
Protein-protein interaction databases
BioGRIDi | 36754, 88 interactors |
DIPi | DIP-4346N |
IntActi | P10823, 51 interactors |
MINTi | P10823 |
STRINGi | 4932.YER020W |
Miscellaneous databases
RNActi | P10823, protein |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 122 – 448 | G-alphaPROSITE-ProRule annotationAdd BLAST | 327 |
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 125 – 138 | G1 motifPROSITE-ProRule annotationAdd BLAST | 14 | |
Regioni | 268 – 276 | G2 motifPROSITE-ProRule annotation | 9 | |
Regioni | 292 – 301 | G3 motifPROSITE-ProRule annotation | 10 | |
Regioni | 361 – 368 | G4 motifPROSITE-ProRule annotation | 8 | |
Regioni | 418 – 423 | G5 motifPROSITE-ProRule annotation | 6 |
Sequence similaritiesi
Phylogenomic databases
eggNOGi | KOG0082, Eukaryota |
HOGENOMi | CLU_014184_0_2_1 |
InParanoidi | P10823 |
OMAi | YFSEEMA |
Family and domain databases
CDDi | cd00066, G-alpha, 1 hit |
Gene3Di | 1.10.400.10, 1 hit |
InterProi | View protein in InterPro IPR002975, Fungi_Gprotein_alpha IPR001019, Gprotein_alpha_su IPR011025, GproteinA_insert IPR027417, P-loop_NTPase |
PANTHERi | PTHR10218, PTHR10218, 1 hit |
Pfami | View protein in Pfam PF00503, G-alpha, 1 hit |
PRINTSi | PR00318, GPROTEINA PR01241, GPROTEINAFNG |
SMARTi | View protein in SMART SM00275, G_alpha, 1 hit |
SUPFAMi | SSF47895, SSF47895, 1 hit SSF52540, SSF52540, 1 hit |
PROSITEi | View protein in PROSITE PS51882, G_ALPHA, 1 hit |
i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
P10823-1 [UniParc]FASTAAdd to basket
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
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 375 | S → R in AAA34651 (PubMed:2830616).Curated | 1 |
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 |
PIRi | S50478 |
RefSeqi | NP_010937.3, NM_001178911.3 |
Genome annotation databases
EnsemblFungii | YER020W_mRNA; YER020W; YER020W |
GeneIDi | 856741 |
KEGGi | sce:YER020W |
Similar proteinsi
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 |
PIRi | S50478 |
RefSeqi | NP_010937.3, NM_001178911.3 |
3D structure databases
SMRi | P10823 |
ModBasei | Search... |
Protein-protein interaction databases
BioGRIDi | 36754, 88 interactors |
DIPi | DIP-4346N |
IntActi | P10823, 51 interactors |
MINTi | P10823 |
STRINGi | 4932.YER020W |
PTM databases
iPTMneti | P10823 |
SwissPalmi | P10823 |
Proteomic databases
MaxQBi | P10823 |
PaxDbi | P10823 |
PRIDEi | P10823 |
Genome annotation databases
EnsemblFungii | YER020W_mRNA; YER020W; YER020W |
GeneIDi | 856741 |
KEGGi | sce:YER020W |
Organism-specific databases
SGDi | S000000822, GPA2 |
VEuPathDBi | FungiDB:YER020W |
Phylogenomic databases
eggNOGi | KOG0082, Eukaryota |
HOGENOMi | CLU_014184_0_2_1 |
InParanoidi | P10823 |
OMAi | YFSEEMA |
Enzyme and pathway databases
Reactomei | R-SCE-399997, Acetylcholine regulates insulin secretion R-SCE-416476, G alpha (q) signalling events R-SCE-416482, G alpha (12/13) signalling events R-SCE-418592, ADP signalling through P2Y purinoceptor 1 R-SCE-434316, Fatty Acids bound to GPR40 (FFAR1) regulate insulin secretion |
Miscellaneous databases
PROi | PR:P10823 |
RNActi | P10823, protein |
Family and domain databases
CDDi | cd00066, G-alpha, 1 hit |
Gene3Di | 1.10.400.10, 1 hit |
InterProi | View protein in InterPro IPR002975, Fungi_Gprotein_alpha IPR001019, Gprotein_alpha_su IPR011025, GproteinA_insert IPR027417, P-loop_NTPase |
PANTHERi | PTHR10218, PTHR10218, 1 hit |
Pfami | View protein in Pfam PF00503, G-alpha, 1 hit |
PRINTSi | PR00318, GPROTEINA PR01241, GPROTEINAFNG |
SMARTi | View protein in SMART SM00275, G_alpha, 1 hit |
SUPFAMi | SSF47895, SSF47895, 1 hit SSF52540, SSF52540, 1 hit |
PROSITEi | View protein in PROSITE PS51882, G_ALPHA, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | GPA2_YEAST | |
Accessioni | P10823Primary (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: | February 10, 2021 | |
This is version 207 of the entry and version 2 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Fungal Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
Reference proteomeDocuments
- Yeast
Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD - Yeast chromosome V
Yeast (Saccharomyces cerevisiae) chromosome V: entries and gene names - SIMILARITY comments
Index of protein domains and families