Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-559292-00164
Entry Name
UniProt Accession
Theoretical PI
6.06
Molecular Weight
50447.65
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
Guanine nucleotide-binding protein alpha-2 subunit
Protein Synonyms/Alias
GP2-alpha;
Gene Name
GPA2
Gene Synonyms/Alias
SSP101; YER020W;
Created Date
01-JUL-1989
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
2
Canonical
******MGLCASSEK
[1]
N-Myristoylation
4
Canonical
****MGLCASSEKNG
[1]
S-Palmitoylation
Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
NCBI Taxa ID
559292
Reference
[1] Harashima T, Heitman J. Galpha subunit Gpa2 recruits kelch repeat subunitsthat inhibit receptor-G protein coupling during cAMP-induced dimorphictransitions in Saccharomyces cerevisiae. Mol Biol Cell. 2005 Oct;16(10):4557-71. Epub 2005 Jul 19.[PMID:16030250]
Functional Description
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.
Sequence Annotation
Nucleotide-binding: 130 137 GTP.
Nucleotide-binding: 270 276 GTP.
Nucleotide-binding: 296 300 GTP.
Nucleotide-binding: 365 368 GTP.
Metal binding site: 137 137 Magnesium.
Metal binding site: 276 276 Magnesium.
Binding site: 420 420 GTP; via amide nitrogen.
Protein Length
449 AA.
Protein Sequence
(Canonical)
MGLCASSEKN GSTPDTQTAS AGSDNVGKAK VPPKQEPQKT VRTVNTANQQ EKQQQRQQQP  60
SPHNVKDRKE QNGSINNAIS PTATANTSGS QQINIDSALR DRSSNVAAQP SLSDASSGSN  120
DKELKVLLLG AGESGKSTVL QQLKILHQNG FSEQEIKEYI PLIYQNLLEI GRNLIQARTR  180
FNVNLEPECE LTQQDLSRTM SYEMPNNYTG QFPEDIAGVI STLWALPSTQ DLVNGPNASK  240
FYLMDSTPYF MENFTRITSP NYRPTQQDIL RSRQMTSGIF DTVIDMGSDI KMHIYDVGGQ  300
RSERKKWIHC FDNVTLVIFC VSLSEYDQTL MEDKNQNRFQ ESLVLFDNIV NSRWFARTSV  360
VLFLNKIDLF AEKLSKVPME NYFPDYTGGS DINKAAKYIL WRFVQLNRAN LSIYPHVTQA  420
TDTSNIRLVF AAIKETILEN TLKDSGVLQ                                    449
MGLCASSEKN GSTPDTQTAS AGSDNVGKAK VPPKQEPQKT VRTVNTANQQ EKQQQRQQQP  60
SPHNVKDRKE QNGSINNAIS PTATANTSGS QQINIDSALR DRSSNVAAQP SLSDASSGSN  120
DKELKVLLLG AGESGKSTVL QQLKILHQNG FSEQEIKEYI PLIYQNLLEI GRNLIQARTR  180
FNVNLEPECE LTQQDLSRTM SYEMPNNYTG QFPEDIAGVI STLWALPSTQ DLVNGPNASK  240
FYLMDSTPYF MENFTRITSP NYRPTQQDIL RSRQMTSGIF DTVIDMGSDI KMHIYDVGGQ  300
RSERKKWIHC FDNVTLVIFC VSLSEYDQTL MEDKNQNRFQ ESLVLFDNIV NSRWFARTSV  360
VLFLNKIDLF AEKLSKVPME NYFPDYTGGS DINKAAKYIL WRFVQLNRAN LSIYPHVTQA  420
TDTSNIRLVF AAIKETILEN TLKDSGVLQ                                    449
FASTA
(Canonical)
>LipidDB-559292-00164|P10823
MGLCASSEKNGSTPDTQTASAGSDNVGKAKVPPKQEPQKTVRTVNTANQQEKQQQRQQQP
SPHNVKDRKEQNGSINNAISPTATANTSGSQQINIDSALRDRSSNVAAQPSLSDASSGSN
DKELKVLLLGAGESGKSTVLQQLKILHQNGFSEQEIKEYIPLIYQNLLEIGRNLIQARTR
FNVNLEPECELTQQDLSRTMSYEMPNNYTGQFPEDIAGVISTLWALPSTQDLVNGPNASK
FYLMDSTPYFMENFTRITSPNYRPTQQDILRSRQMTSGIFDTVIDMGSDIKMHIYDVGGQ
RSERKKWIHCFDNVTLVIFCVSLSEYDQTLMEDKNQNRFQESLVLFDNIVNSRWFARTSV
VLFLNKIDLFAEKLSKVPMENYFPDYTGGSDINKAAKYILWRFVQLNRANLSIYPHVTQA
TDTSNIRLVFAAIKETILENTLKDSGVLQ
MGLCASSEKNGSTPDTQTASAGSDNVGKAKVPPKQEPQKTVRTVNTANQQEKQQQRQQQP
SPHNVKDRKEQNGSINNAISPTATANTSGSQQINIDSALRDRSSNVAAQPSLSDASSGSN
DKELKVLLLGAGESGKSTVLQQLKILHQNGFSEQEIKEYIPLIYQNLLEIGRNLIQARTR
FNVNLEPECELTQQDLSRTMSYEMPNNYTGQFPEDIAGVISTLWALPSTQDLVNGPNASK
FYLMDSTPYFMENFTRITSPNYRPTQQDILRSRQMTSGIFDTVIDMGSDIKMHIYDVGGQ
RSERKKWIHCFDNVTLVIFCVSLSEYDQTLMEDKNQNRFQESLVLFDNIVNSRWFARTSV
VLFLNKIDLFAEKLSKVPMENYFPDYTGGSDINKAAKYILWRFVQLNRANLSIYPHVTQA
TDTSNIRLVFAAIKETILENTLKDSGVLQ
Gene Ontology
GO:0005886; C:plasma membrane; IDA:SGD
GO:0005525; F:GTP binding; IEA:UniProtKB-KW
GO:0003924; F:GTPase activity; IDA:SGD
GO:0046872; F:metal ion binding; IEA:UniProtKB-KW
GO:0004871; F:signal transducer activity; IEA:UniProtKB-KW
GO:0007189; P:adenylate cyclase-activating G-protein coupled receptor signaling pathway; IMP:SGD
GO:0030437; P:ascospore formation; IMP:SGD
GO:0010255; P:glucose mediated signaling pathway; IMP:SGD
GO:0009757; P:hexose mediated signaling; IMP:SGD
GO:0007124; P:pseudohyphal growth; IMP:SGD
GO:0001302; P:replicative cell aging; IMP:SGD
GO:0007165; P:signal transduction; IMP:SGD
Interpro
InterPro; IPR002975; Fungi_Gprotein_alpha
InterPro; IPR001019; Gprotein_alpha_su
InterPro; IPR011025; GproteinA_insert
InterPro; IPR027417; P-loop_NTPase
Pfam
Pfam; PF00503; G-alpha;
SMART
SMART; SM00275; G_alpha;
PROSITE
PRINTS
PRINTS; PR00318; GPROTEINA;
PRINTS; PR01241; GPROTEINAFNG;