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P10823 (GPA2_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 147. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Guanine nucleotide-binding protein alpha-2 subunit
Alternative name(s):
GP2-alpha
Gene names
Name:GPA2
Synonyms:SSP101
Ordered Locus Names:YER020W
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length449 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.4 Ref.8

Enzyme regulation

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.

Subunit structure

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. Ref.4 Ref.5 Ref.8

Subcellular location

Cell membrane; Lipid-anchor; Cytoplasmic side Ref.6 Ref.8.

Post-translational modification

Myristoylation at Gly-2 and palmitoylation at Cys-4 are required for membrane localization and function of the protein. Ref.8

Miscellaneous

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

Sequence similarities

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed
Chain2 – 449448Guanine nucleotide-binding protein alpha-2 subunit
PRO_0000203617

Regions

Nucleotide binding130 – 1378GTP By similarity
Nucleotide binding270 – 2767GTP By similarity
Nucleotide binding296 – 3005GTP By similarity
Nucleotide binding365 – 3684GTP By similarity

Sites

Metal binding1371Magnesium By similarity
Metal binding2761Magnesium By similarity
Binding site4201GTP; via amide nitrogen By similarity

Amino acid modifications

Lipidation21N-myristoyl glycine Ref.8
Lipidation41S-palmitoyl cysteine Ref.8

Experimental info

Mutagenesis21G → A: Abolishes both palmitoylation and N-myristoylation. Ref.8
Mutagenesis41C → A: Abolishes palmitoylation but not N-myristoylation. Ref.8
Mutagenesis61S → A: Abolishes both palmitoylation and N-myristoylation. Ref.8
Mutagenesis1321G → V: Locks GPA2 in its activated GTP-bound form and abrogates the negative control by RGS2. Ref.4 Ref.5
Mutagenesis2991G → A: Dominant negativ allele unable to undergo the GTP-induced conformational change. Ref.5 Ref.8
Mutagenesis3001Q → L: Dominant active allele that abolishes intrinsic GTPase activity. Ref.5
Sequence conflict3751S → R in AAA34651. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P10823 [UniParc].

Last modified February 1, 1995. Version 2.
Checksum: 881B91792AE91748

FASTA44950,448
        10         20         30         40         50         60 
MGLCASSEKN GSTPDTQTAS AGSDNVGKAK VPPKQEPQKT VRTVNTANQQ EKQQQRQQQP 

        70         80         90        100        110        120 
SPHNVKDRKE QNGSINNAIS PTATANTSGS QQINIDSALR DRSSNVAAQP SLSDASSGSN 

       130        140        150        160        170        180 
DKELKVLLLG AGESGKSTVL QQLKILHQNG FSEQEIKEYI PLIYQNLLEI GRNLIQARTR 

       190        200        210        220        230        240 
FNVNLEPECE LTQQDLSRTM SYEMPNNYTG QFPEDIAGVI STLWALPSTQ DLVNGPNASK 

       250        260        270        280        290        300 
FYLMDSTPYF MENFTRITSP NYRPTQQDIL RSRQMTSGIF DTVIDMGSDI KMHIYDVGGQ 

       310        320        330        340        350        360 
RSERKKWIHC FDNVTLVIFC VSLSEYDQTL MEDKNQNRFQ ESLVLFDNIV NSRWFARTSV 

       370        380        390        400        410        420 
VLFLNKIDLF AEKLSKVPME NYFPDYTGGS DINKAAKYIL WRFVQLNRAN LSIYPHVTQA 

       430        440 
TDTSNIRLVF AAIKETILEN TLKDSGVLQ 

« Hide

References

« Hide 'large scale' references
[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]"The nucleotide sequence of Saccharomyces cerevisiae chromosome V."
Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E., Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G., Hunicke-Smith S., Hyman R.W. expand/collapse author list , Kayser A., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Norgren R., Oefner P., Oh C., Petel F.X., Roberts D., Sehl P., Schramm S., Shogren T., Smith V., Taylor P., Wei Y., Botstein D., Davis R.W.
Nature 387:78-81(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[3]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
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]"Global analysis of protein localization in budding yeast."
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K.
Nature 425:686-691(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[7]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract]
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].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
J03609 Genomic DNA. Translation: AAA34651.1.
U18778 Genomic DNA. Translation: AAB64553.1.
BK006939 Genomic DNA. Translation: DAA07673.1.
PIRS50478.
RefSeqNP_010937.3. NM_001178911.3.

3D structure databases

ProteinModelPortalP10823.
SMRP10823. Positions 123-443.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid36754. 79 interactions.
DIPDIP-4346N.
IntActP10823. 38 interactions.
MINTMINT-548605.
STRING4932.YER020W.

Proteomic databases

PaxDbP10823.
PeptideAtlasP10823.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYER020W; YER020W; YER020W.
GeneID856741.
KEGGsce:YER020W.

Organism-specific databases

CYGDYER020w.
SGDS000000822. GPA2.

Phylogenomic databases

eggNOGNOG322962.
GeneTreeENSGT00690000101672.
HOGENOMHOG000038730.
KOK04640.
OMAENEANRA.
OrthoDBEOG7M0P1X.

Enzyme and pathway databases

BioCycYEAST:G3O-30204-MONOMER.

Gene expression databases

GenevestigatorP10823.

Family and domain databases

Gene3D1.10.400.10. 1 hit.
3.40.50.300. 2 hits.
InterProIPR002975. Fungi_Gprotein_alpha.
IPR001019. Gprotein_alpha_su.
IPR011025. GproteinA_insert.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERPTHR10218. PTHR10218. 1 hit.
PfamPF00503. G-alpha. 1 hit.
[Graphical view]
PRINTSPR00318. GPROTEINA.
PR01241. GPROTEINAFNG.
SMARTSM00275. G_alpha. 1 hit.
[Graphical view]
SUPFAMSSF47895. SSF47895. 1 hit.
SSF52540. SSF52540. 2 hits.
ProtoNetSearch...

Other

NextBio982873.

Entry information

Entry nameGPA2_YEAST
AccessionPrimary (citable) accession number: P10823
Secondary accession number(s): D3DLR9
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: February 1, 1995
Last modified: April 16, 2014
This is version 147 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome V

Yeast (Saccharomyces cerevisiae) chromosome V: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families