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Guanine nucleotide-binding protein G(s) subunit alpha isoforms short (Adenylate cyclase-stimulating G alpha protein)

 GNAS2_MOUSE             Reviewed;         394 AA.
P63094; A2A611; A2A612; A2A613; P04894; P08755; Q3KQM5; Q3TFV3;
Q3TWS9; Q3UI70; Q58E62; Q6P7U9; Q80ZK6; Q8K5E1; Q9Z1R7;
13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
13-AUG-1987, sequence version 1.
12-SEP-2018, entry version 154.
RecName: Full=Guanine nucleotide-binding protein G(s) subunit alpha isoforms short;
AltName: Full=Adenylate cyclase-stimulating G alpha protein;
Name=Gnas; Synonyms=Gnas1; ORFNames=MNCb-5546;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM GNAS-1), AND VARIANT PRO-389.
STRAIN=BALB/cJ;
PubMed=2826231; DOI=10.1016/0014-5793(87)80486-6;
Rall T., Harris B.A.;
"Identification of the lesion in the stimulatory GTP-binding protein
of the uncoupled S49 lymphoma.";
FEBS Lett. 224:365-371(1987).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM GNAS-2).
PubMed=3092218; DOI=10.1073/pnas.83.18.6687;
Sullivan K.A., Liao Y.-C., Alborzi A., Beiderman B., Chang F.-H.,
Masters S.B., Levinson A.D., Bourne H.R.;
"Inhibitory and stimulatory G proteins of adenylate cyclase: cDNA and
amino acid sequences of the alpha chains.";
Proc. Natl. Acad. Sci. U.S.A. 83:6687-6691(1986).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM GNAS-3).
STRAIN=C57BL/6J;
Wang Y.Z., Kehlenbach R.H., Huttner W.B.;
"Molecular characterization of XL2, a neuroendocrine-specific luminal
Golgi-resident protein.";
Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS GNAS-1 AND GNAS-2).
STRAIN=C57BL/6J; TISSUE=Stomach;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS GNAS-1 AND GNAS-2).
STRAIN=129, C57BL/6J, Czech II, and FVB/N;
TISSUE=Brain, Mammary tumor, and Salivary gland;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 73-394 (ISOFORM GNAS-1).
STRAIN=C57BL/6J; TISSUE=Brain;
Osada N., Kusuda J., Tanuma R., Ito A., Hirata M., Sugano S.,
Hashimoto K.;
"Isolation of full-length cDNA clones from mouse brain cDNA library
made by oligo-capping method.";
Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases.
[8]
PROTEIN SEQUENCE OF 266-274 AND 284-293, AND IDENTIFICATION BY MASS
SPECTROMETRY.
STRAIN=C57BL/6J; TISSUE=Brain;
Lubec G., Kang S.U.;
Submitted (APR-2007) to UniProtKB.
[9]
SUBCELLULAR LOCATION, PALMITOYLATION AT CYS-3, AND MUTAGENESIS OF
CYS-3.
PubMed=8227063;
Wedegaertner P.B., Chu D.H., Wilson P.T., Levis M.J., Bourne H.R.;
"Palmitoylation is required for signaling functions and membrane
attachment of Gq alpha and Gs alpha.";
J. Biol. Chem. 268:25001-25008(1993).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
Pancreas, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- FUNCTION: Guanine nucleotide-binding proteins (G proteins)
function as transducers in numerous signaling pathways controlled
by G protein-coupled receptors (GPCRs). Signaling involves the
activation of adenylyl cyclases, resulting in increased levels of
the signaling molecule cAMP. GNAS functions downstream of several
GPCRs, including beta-adrenergic receptors. Stimulates the Ras
signaling pathway via RAPGEF2. {ECO:0000250|UniProtKB:P63092}.
-!- SUBUNIT: Heterotrimeric G proteins are composed of 3 units; alpha,
beta and gamma. The alpha chain contains the guanine nucleotide
binding site (By similarity). Interacts with CRY1; the interaction
may block GPCR-mediated regulation of cAMP concentrations.
Interacts with ADCY6 and stimulates its adenylyl cyclase activity
(By similarity). Interacts with ADCY2 and ADCY5 (By similarity).
Stimulates the ADCY5 adenylyl cyclase activity (By similarity).
{ECO:0000250|UniProtKB:P04896, ECO:0000250|UniProtKB:P63092}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:8227063};
Lipid-anchor {ECO:0000269|PubMed:8227063}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=9;
Name=Gnas-1;
IsoId=P63094-1; Sequence=Displayed;
Name=Gnas-2;
IsoId=P63094-2; Sequence=VSP_011567;
Name=Gnas-3; Synonyms=NTas;
IsoId=P63094-3; Sequence=VSP_021153;
Name=XLas-1; Synonyms=XXL;
IsoId=Q6R0H7-1; Sequence=External;
Name=XLas-2; Synonyms=XXLb1;
IsoId=Q6R0H7-2; Sequence=External;
Name=XLas-3; Synonyms=XXLb2;
IsoId=Q6R0H7-3; Sequence=External;
Name=XLas-4;
IsoId=Q6R0H7-4; Sequence=External;
Name=Nesp55-1;
IsoId=Q9Z0F1-1; Sequence=External;
Note=Shares no sequence similarity with other isoforms (except
isoform Nesp55-2) due to a novel first exon containing the
entire reading frame spliced to shared exon 2 so that exons 2-13
make up the 3'-UTR.;
Name=Nesp55-2;
IsoId=Q9Z0F1-2; Sequence=External;
Note=Shares no sequence similarity with other isoforms (except
isoform Nesp55-1) due to a novel first exon containing the
entire reading frame spliced to shared exon 2 so that exons 2-13
make up the 3'-UTR.;
-!- MISCELLANEOUS: This protein is produced by a bicistronic gene
which also produces the ALEX protein from an overlapping reading
frame.
-!- MISCELLANEOUS: The GNAS locus is imprinted in a complex manner,
giving rise to distinct paternally, maternally and biallelically
expressed proteins. The XLas isoforms are paternally derived, the
Gnas isoforms are biallelically derived and the Nesp55 isoforms
are maternally derived.
-!- SIMILARITY: Belongs to the G-alpha family. G(s) subfamily.
{ECO:0000305}.
-!- CAUTION: It was found (PubMed:8227063) that in engineered, C3S-
mutagenized sequence expressed in HEK293 cells there was no
radiolabeling by either S- or N-palmitoylation. This result is
incompatible with a prediction for N-palmitoylation unless N-
palmitoylation depends on S-palmitoylation occurring first or N-
palmitoylation did not occur in the experimental expression
system. {ECO:0000305|PubMed:8227063}.
-!- SEQUENCE CAUTION:
Sequence=BAB93551.1; Type=Miscellaneous discrepancy; Evidence={ECO:0000305};
Sequence=CAM24410.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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EMBL; Y00703; CAA68695.1; -; mRNA.
EMBL; M13964; AAA37745.1; -; mRNA.
EMBL; AF107848; AAD11807.1; -; mRNA.
EMBL; AK147051; BAE27636.1; -; mRNA.
EMBL; AK159563; BAE35187.1; -; mRNA.
EMBL; AK168996; BAE40795.1; -; mRNA.
EMBL; AL593857; CAM24410.1; ALT_SEQ; Genomic_DNA.
EMBL; AL593857; CAM24411.1; -; Genomic_DNA.
EMBL; AL593857; CAM24412.1; -; Genomic_DNA.
EMBL; BC038067; AAH38067.1; -; mRNA.
EMBL; BC048834; AAH48834.1; -; mRNA.
EMBL; BC061496; AAH61496.1; -; mRNA.
EMBL; BC062654; AAH62654.1; -; mRNA.
EMBL; BC080816; AAH80816.1; -; mRNA.
EMBL; BC092055; AAH92055.1; -; mRNA.
EMBL; BC106133; AAI06134.1; -; mRNA.
EMBL; AB041808; BAB93551.1; ALT_SEQ; mRNA.
CCDS; CCDS38356.1; -. [P63094-1]
CCDS; CCDS38357.1; -. [P63094-2]
PIR; A25889; RGMSA1.
PIR; S03075; RGMSA2.
RefSeq; NP_001070978.1; NM_001077510.4. [P63094-2]
RefSeq; NP_001297012.1; NM_001310083.1. [P63094-1]
RefSeq; NP_963910.1; NM_201616.2. [P63094-1]
UniGene; Mm.125770; -.
UniGene; Mm.394046; -.
ProteinModelPortal; P63094; -.
SMR; P63094; -.
BioGrid; 199972; 6.
CORUM; P63094; -.
IntAct; P63094; 6.
MINT; P63094; -.
iPTMnet; P63094; -.
PhosphoSitePlus; P63094; -.
SwissPalm; P63094; -.
EPD; P63094; -.
PeptideAtlas; P63094; -.
PRIDE; P63094; -.
Ensembl; ENSMUST00000087871; ENSMUSP00000085179; ENSMUSG00000027523. [P63094-1]
Ensembl; ENSMUST00000109085; ENSMUSP00000104713; ENSMUSG00000027523. [P63094-2]
Ensembl; ENSMUST00000109087; ENSMUSP00000104715; ENSMUSG00000027523. [P63094-1]
GeneID; 14683; -.
KEGG; mmu:14683; -.
UCSC; uc008oey.1; mouse. [P63094-1]
UCSC; uc033hrs.1; mouse. [P63094-2]
CTD; 2778; -.
MGI; MGI:95777; Gnas.
GeneTree; ENSGT00910000144108; -.
HOVERGEN; HBG063184; -.
KO; K04632; -.
Reactome; R-MMU-163359; Glucagon signaling in metabolic regulation.
Reactome; R-MMU-164378; PKA activation in glucagon signalling.
Reactome; R-MMU-381676; Glucagon-like Peptide-1 (GLP1) regulates insulin secretion.
Reactome; R-MMU-392851; Prostacyclin signalling through prostacyclin receptor.
Reactome; R-MMU-418555; G alpha (s) signalling events.
Reactome; R-MMU-420092; Glucagon-type ligand receptors.
Reactome; R-MMU-432040; Vasopressin regulates renal water homeostasis via Aquaporins.
Reactome; R-MMU-5610787; Hedgehog 'off' state.
ChiTaRS; Gnas; mouse.
Proteomes; UP000000589; Chromosome 2.
Bgee; ENSMUSG00000027523; Expressed in 324 organ(s), highest expression level in brain.
ExpressionAtlas; P63094; baseline and differential.
Genevisible; P63094; MM.
GO; GO:0005737; C:cytoplasm; ISO:MGI.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0030425; C:dendrite; IDA:MGI.
GO; GO:0005768; C:endosome; ISO:MGI.
GO; GO:0005834; C:heterotrimeric G-protein complex; ISO:MGI.
GO; GO:0031224; C:intrinsic component of membrane; ISO:MGI.
GO; GO:0016020; C:membrane; IDA:MGI.
GO; GO:0045121; C:membrane raft; ISO:MGI.
GO; GO:0043025; C:neuronal cell body; ISO:MGI.
GO; GO:0005634; C:nucleus; ISO:MGI.
GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
GO; GO:0005886; C:plasma membrane; ISO:MGI.
GO; GO:0055037; C:recycling endosome; ISO:MGI.
GO; GO:0001726; C:ruffle; ISO:MGI.
GO; GO:0032588; C:trans-Golgi network membrane; ISO:MGI.
GO; GO:0047391; F:alkylglycerophosphoethanolamine phosphodiesterase activity; ISO:MGI.
GO; GO:0043014; F:alpha-tubulin binding; ISO:MGI.
GO; GO:0031698; F:beta-2 adrenergic receptor binding; ISO:MGI.
GO; GO:0051430; F:corticotropin-releasing hormone receptor 1 binding; ISO:MGI.
GO; GO:0031748; F:D1 dopamine receptor binding; ISO:MGI.
GO; GO:0001965; F:G-protein alpha-subunit binding; ISO:MGI.
GO; GO:0031681; F:G-protein beta-subunit binding; ISO:MGI.
GO; GO:0031683; F:G-protein beta/gamma-subunit complex binding; IEA:InterPro.
GO; GO:0005525; F:GTP binding; ISO:MGI.
GO; GO:0003924; F:GTPase activity; ISO:MGI.
GO; GO:0005159; F:insulin-like growth factor receptor binding; ISO:MGI.
GO; GO:0035255; F:ionotropic glutamate receptor binding; ISO:MGI.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0031852; F:mu-type opioid receptor binding; ISO:MGI.
GO; GO:0019904; F:protein domain specific binding; ISO:MGI.
GO; GO:0071880; P:adenylate cyclase-activating adrenergic receptor signaling pathway; ISS:UniProtKB.
GO; GO:0007191; P:adenylate cyclase-activating dopamine receptor signaling pathway; IGI:MGI.
GO; GO:0007189; P:adenylate cyclase-activating G-protein coupled receptor signaling pathway; IDA:MGI.
GO; GO:0060348; P:bone development; ISO:MGI.
GO; GO:0055074; P:calcium ion homeostasis; ISO:MGI.
GO; GO:0051216; P:cartilage development; IMP:MGI.
GO; GO:0071870; P:cellular response to catecholamine stimulus; ISO:MGI.
GO; GO:0071380; P:cellular response to prostaglandin E stimulus; ISO:MGI.
GO; GO:0050890; P:cognition; ISO:MGI.
GO; GO:0048589; P:developmental growth; ISO:MGI.
GO; GO:0006306; P:DNA methylation; IMP:MGI.
GO; GO:0048701; P:embryonic cranial skeleton morphogenesis; IMP:MGI.
GO; GO:0035116; P:embryonic hindlimb morphogenesis; IMP:MGI.
GO; GO:0001958; P:endochondral ossification; IMP:MGI.
GO; GO:0006112; P:energy reserve metabolic process; IMP:MGI.
GO; GO:0007186; P:G-protein coupled receptor signaling pathway; ISO:MGI.
GO; GO:0071514; P:genetic imprinting; IMP:MGI.
GO; GO:0060789; P:hair follicle placode formation; ISO:MGI.
GO; GO:0035264; P:multicellular organism growth; IMP:MGI.
GO; GO:0045776; P:negative regulation of blood pressure; ISO:MGI.
GO; GO:0035814; P:negative regulation of renal sodium excretion; ISO:MGI.
GO; GO:0070527; P:platelet aggregation; ISO:MGI.
GO; GO:0043950; P:positive regulation of cAMP-mediated signaling; ISS:UniProtKB.
GO; GO:0008284; P:positive regulation of cell proliferation; ISO:MGI.
GO; GO:0120162; P:positive regulation of cold-induced thermogenesis; IMP:YuBioLab.
GO; GO:0043547; P:positive regulation of GTPase activity; ISS:UniProtKB.
GO; GO:0045669; P:positive regulation of osteoblast differentiation; IMP:MGI.
GO; GO:0045672; P:positive regulation of osteoclast differentiation; IMP:MGI.
GO; GO:0001934; P:positive regulation of protein phosphorylation; ISO:MGI.
GO; GO:0010765; P:positive regulation of sodium ion transport; ISO:MGI.
GO; GO:0040032; P:post-embryonic body morphogenesis; IMP:MGI.
GO; GO:0009791; P:post-embryonic development; IMP:MGI.
GO; GO:2000828; P:regulation of parathyroid hormone secretion; IMP:MGI.
GO; GO:0009966; P:regulation of signal transduction; ISO:MGI.
GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISO:MGI.
GO; GO:0042493; P:response to drug; IMP:MGI.
GO; GO:0071107; P:response to parathyroid hormone; ISO:MGI.
GO; GO:0001501; P:skeletal system development; IMP:MGI.
GO; GO:0043588; P:skin development; IMP:MGI.
GO; GO:0001894; P:tissue homeostasis; IMP:MGI.
CDD; cd00066; G-alpha; 1.
Gene3D; 1.10.400.10; -; 1.
InterPro; IPR000367; Gprotein_alpha_S.
InterPro; IPR001019; Gprotein_alpha_su.
InterPro; IPR011025; GproteinA_insert.
InterPro; IPR027417; P-loop_NTPase.
PANTHER; PTHR10218; PTHR10218; 1.
Pfam; PF00503; G-alpha; 1.
PRINTS; PR00318; GPROTEINA.
PRINTS; PR00443; GPROTEINAS.
SMART; SM00275; G_alpha; 1.
SUPFAM; SSF47895; SSF47895; 1.
SUPFAM; SSF52540; SSF52540; 2.
1: Evidence at protein level;
Alternative splicing; Cell membrane; Complete proteome;
Direct protein sequencing; GTP-binding; Isopeptide bond; Lipoprotein;
Magnesium; Membrane; Metal-binding; Nucleotide-binding; Palmitate;
Phosphoprotein; Polymorphism; Reference proteome; Transducer;
Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:P04896}.
CHAIN 2 394 Guanine nucleotide-binding protein G(s)
subunit alpha isoforms short.
/FTId=PRO_0000203723.
NP_BIND 47 55 GTP. {ECO:0000250|UniProtKB:P04896}.
NP_BIND 197 204 GTP. {ECO:0000250|UniProtKB:P04896}.
NP_BIND 223 227 GTP. {ECO:0000250|UniProtKB:P04896}.
NP_BIND 292 295 GTP. {ECO:0000250|UniProtKB:P04896}.
METAL 54 54 Magnesium.
{ECO:0000250|UniProtKB:P04896}.
METAL 204 204 Magnesium.
{ECO:0000250|UniProtKB:P04896}.
BINDING 366 366 GTP; via amide nitrogen.
{ECO:0000250|UniProtKB:P04896}.
MOD_RES 352 352 Phosphoserine.
{ECO:0000250|UniProtKB:P63092}.
LIPID 2 2 N-palmitoyl glycine.
{ECO:0000250|UniProtKB:P04896}.
LIPID 3 3 S-palmitoyl cysteine.
{ECO:0000269|PubMed:8227063}.
CROSSLNK 300 300 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000250|UniProtKB:P63092}.
VAR_SEQ 1 46 MGCLGNSKTEDQRNEEKAQREANKKIEKQLQKDKQVYRATH
RLLLL -> MGDSVQILLVFMDK (in isoform Gnas-
3). {ECO:0000303|Ref.3}.
/FTId=VSP_021153.
VAR_SEQ 71 86 EGGEEDPQAARSNSDG -> DS (in isoform Gnas-
2). {ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:16141072,
ECO:0000303|PubMed:3092218}.
/FTId=VSP_011567.
VARIANT 389 389 R -> P (in unc mutant; uncouples
receptors from adenylyl cyclases).
{ECO:0000269|PubMed:2826231}.
MUTAGEN 3 3 C->S: Abolishes S-palmitoylation.
{ECO:0000269|PubMed:8227063}.
CONFLICT 1 15 MGCLGNSKTEDQRNE -> MAARGAAGLRGGG (in Ref.
2; AAA37745). {ECO:0000305}.
CONFLICT 64 64 H -> L (in Ref. 4; BAE35187).
{ECO:0000305}.
CONFLICT 97 97 N -> H (in Ref. 4; BAE35187).
{ECO:0000305}.
CONFLICT 130 130 Y -> C (in Ref. 6; AAI06134).
{ECO:0000305}.
CONFLICT 137 137 V -> L (in Ref. 2; AAA37745 and 3;
AAD11807). {ECO:0000305}.
CONFLICT 139 139 N -> D (in Ref. 1; CAA68695).
{ECO:0000305}.
CONFLICT 160 160 R -> P (in Ref. 7; BAB93551).
{ECO:0000305}.
CONFLICT 326 326 P -> L (in Ref. 4; BAE40795 and 6;
AAI06134). {ECO:0000305}.
SEQUENCE 394 AA; 45664 MW; 20341187BE4412ED CRC64;
MGCLGNSKTE DQRNEEKAQR EANKKIEKQL QKDKQVYRAT HRLLLLGAGE SGKSTIVKQM
RILHVNGFNG EGGEEDPQAA RSNSDGEKAT KVQDIKNNLK EAIETIVAAM SNLVPPVELA
NPENQFRVDY ILSVMNVPNF DFPPEFYEHA KALWEDEGVR ACYERSNEYQ LIDCAQYFLD
KIDVIKQADY VPSDQDLLRC RVLTSGIFET KFQVDKVNFH MFDVGGQRDE RRKWIQCFND
VTAIIFVVAS SSYNMVIRED NQTNRLQEAL NLFKSIWNNR WLRTISVILF LNKQDLLAEK
VLAGKSKIED YFPEFARYTT PEDATPEPGE DPRVTRAKYF IRDEFLRIST ASGDGRHYCY
PHFTCAVDTE NIRRVFNDCR DIIQRMHLRQ YELL


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