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Protein

Guanine nucleotide-binding protein alpha-2 subunit

Gene

GPA2

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: -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

Miscellaneous

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

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)DescriptionActionsGraphical viewLength
Metal bindingi137MagnesiumBy similarity1
Metal bindingi276MagnesiumBy similarity1
Binding sitei420GTP; via amide nitrogenBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi130 – 137GTPBy similarity8
Nucleotide bindingi270 – 276GTPBy similarity7
Nucleotide bindingi296 – 300GTPBy similarity5
Nucleotide bindingi365 – 368GTPBy similarity4

GO - Molecular functioni

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
  • invasive growth in response to glucose limitation Source: SGD
  • pseudohyphal growth Source: SGD
  • replicative cell aging Source: SGD
  • signal transduction Source: SGD

Keywordsi

Molecular functionTransducer
LigandGTP-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-30204-MONOMER
ReactomeiR-SCE-193648 NRAGE signals death through JNK
R-SCE-194840 Rho GTPase cycle
R-SCE-202040 G-protein activation
R-SCE-2514859 Inactivation, recovery and regulation of the phototransduction cascade
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 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
Proteomesi
  • UP000002311 Componenti: Chromosome V

Organism-specific databases

EuPathDBiFungiDB:YER020W
SGDiS000000822 GPA2

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi2G → A: Abolishes both palmitoylation and N-myristoylation. 1 Publication1
Mutagenesisi4C → A: Abolishes palmitoylation but not N-myristoylation. 1 Publication1
Mutagenesisi6S → A: Abolishes both palmitoylation and N-myristoylation. 1 Publication1
Mutagenesisi132G → V: Locks GPA2 in its activated GTP-bound form and abrogates the negative control by RGS2. 2 Publications1
Mutagenesisi299G → A: Dominant negativ allele unable to undergo the GTP-induced conformational change. 2 Publications1
Mutagenesisi300Q → L: Dominant active allele that abolishes intrinsic GTPase activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved
ChainiPRO_00002036172 – 449Guanine nucleotide-binding protein alpha-2 subunitAdd BLAST448

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Lipidationi2N-myristoyl glycine1 Publication1
Lipidationi4S-palmitoyl cysteine1 Publication1

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
PRIDEiP10823

PTM databases

iPTMnetiP10823
SwissPalmiP10823

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

Binary interactionsi

Show more details

GO - Molecular functioni

Protein-protein interaction databases

BioGridi36754, 85 interactors
DIPiDIP-4346N
IntActiP10823, 51 interactors
MINTiP10823
STRINGi4932.YER020W

Structurei

3D structure databases

ProteinModelPortaliP10823
SMRiP10823
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

GeneTreeiENSGT00760000118851
HOGENOMiHOG000038730
InParanoidiP10823
KOiK04630
OMAiWRFTQTN
OrthoDBiEOG092C25Q3

Family and domain databases

CDDicd00066 G-alpha, 1 hit
Gene3Di1.10.400.10, 1 hit
InterProiView protein in InterPro
IPR002975 Fungi_Gprotein_alpha
IPR001019 Gprotein_alpha_su
IPR011025 GproteinA_insert
IPR027417 P-loop_NTPase
PANTHERiPTHR10218 PTHR10218, 1 hit
PfamiView protein in Pfam
PF00503 G-alpha, 1 hit
PRINTSiPR00318 GPROTEINA
PR01241 GPROTEINAFNG
SMARTiView protein in SMART
SM00275 G_alpha, 1 hit
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)DescriptionActionsGraphical viewLength
Sequence conflicti375S → R in AAA34651 (PubMed:2830616).Curated1

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

Similar proteinsi

Entry informationi

Entry nameiGPA2_YEAST
AccessioniPrimary (citable) accession number: P10823
Secondary accession number(s): D3DLR9
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: February 1, 1995
Last modified: June 20, 2018
This is version 187 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

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

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