GNAS2_MOUSE
ID GNAS2_MOUSE Reviewed; 394 AA.
AC P63094; A2A611; A2A612; A2A613; P04894; P08755; Q3KQM5; Q3TFV3; Q3TWS9;
AC Q3UI70; Q58E62; Q6P7U9; Q80ZK6; Q8K5E1; Q9Z1R7;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 13-AUG-1987, sequence version 1.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=Guanine nucleotide-binding protein G(s) subunit alpha isoforms short;
DE AltName: Full=Adenylate cyclase-stimulating G alpha protein;
GN Name=Gnas; Synonyms=Gnas1; ORFNames=MNCb-5546;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM GNAS-1), AND VARIANT PRO-389.
RC STRAIN=BALB/cJ;
RX PubMed=2826231; DOI=10.1016/0014-5793(87)80486-6;
RA Rall T., Harris B.A.;
RT "Identification of the lesion in the stimulatory GTP-binding protein of the
RT uncoupled S49 lymphoma.";
RL FEBS Lett. 224:365-371(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM GNAS-2).
RX PubMed=3092218; DOI=10.1073/pnas.83.18.6687;
RA Sullivan K.A., Liao Y.-C., Alborzi A., Beiderman B., Chang F.-H.,
RA Masters S.B., Levinson A.D., Bourne H.R.;
RT "Inhibitory and stimulatory G proteins of adenylate cyclase: cDNA and amino
RT acid sequences of the alpha chains.";
RL Proc. Natl. Acad. Sci. U.S.A. 83:6687-6691(1986).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM GNAS-3).
RC STRAIN=C57BL/6J;
RA Wang Y.Z., Kehlenbach R.H., Huttner W.B.;
RT "Molecular characterization of XL2, a neuroendocrine-specific luminal
RT Golgi-resident protein.";
RL Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS GNAS-1 AND GNAS-2).
RC STRAIN=C57BL/6J; TISSUE=Stomach;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS GNAS-1 AND GNAS-2).
RC STRAIN=129, C57BL/6J, Czech II, and FVB/N;
RC TISSUE=Brain, Mammary tumor, and Salivary gland;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 73-394 (ISOFORM GNAS-1).
RC STRAIN=C57BL/6J; TISSUE=Brain;
RA Osada N., Kusuda J., Tanuma R., Ito A., Hirata M., Sugano S., Hashimoto K.;
RT "Isolation of full-length cDNA clones from mouse brain cDNA library made by
RT oligo-capping method.";
RL Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP PROTEIN SEQUENCE OF 266-274 AND 284-293, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RA Lubec G., Kang S.U.;
RL Submitted (APR-2007) to UniProtKB.
RN [9]
RP SUBCELLULAR LOCATION, PALMITOYLATION AT CYS-3, AND MUTAGENESIS OF CYS-3.
RX PubMed=8227063; DOI=10.1016/s0021-9258(19)74563-3;
RA Wedegaertner P.B., Chu D.H., Wilson P.T., Levis M.J., Bourne H.R.;
RT "Palmitoylation is required for signaling functions and membrane attachment
RT of Gq alpha and Gs alpha.";
RL J. Biol. Chem. 268:25001-25008(1993).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [11]
RP INTERACTION WITH GAS2L2.
RX PubMed=23994616; DOI=10.1016/j.bbamcr.2013.08.009;
RA Wu Y.C., Lai H.L., Chang W.C., Lin J.T., Liu Y.J., Chern Y.;
RT "A novel Galphas-binding protein, Gas-2 like 2, facilitates the signaling
RT of the A2A adenosine receptor.";
RL Biochim. Biophys. Acta 1833:3145-3154(2013).
CC -!- FUNCTION: Guanine nucleotide-binding proteins (G proteins) function as
CC transducers in numerous signaling pathways controlled by G protein-
CC coupled receptors (GPCRs). Signaling involves the activation of
CC adenylyl cyclases, resulting in increased levels of the signaling
CC molecule cAMP. GNAS functions downstream of several GPCRs, including
CC beta-adrenergic receptors. Stimulates the Ras signaling pathway via
CC RAPGEF2. {ECO:0000250|UniProtKB:P63092}.
CC -!- SUBUNIT: Heterotrimeric G proteins are composed of 3 units; alpha, beta
CC and gamma. The alpha chain contains the guanine nucleotide binding site
CC (By similarity). Interacts with CRY1; the interaction may block GPCR-
CC mediated regulation of cAMP concentrations. Interacts with ADCY6 and
CC stimulates its adenylyl cyclase activity (By similarity). Interacts
CC with ADCY2 and ADCY5 (By similarity). Stimulates the ADCY5 adenylyl
CC cyclase activity (By similarity). Interaction with SASH1 (By
CC similarity). Interacts with GASL2L2 (PubMed:23994616).
CC {ECO:0000250|UniProtKB:P04896, ECO:0000250|UniProtKB:P63092,
CC ECO:0000269|PubMed:23994616}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:8227063};
CC Lipid-anchor {ECO:0000269|PubMed:8227063}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=9;
CC Name=Gnas-1;
CC IsoId=P63094-1; Sequence=Displayed;
CC Name=Gnas-2;
CC IsoId=P63094-2; Sequence=VSP_011567;
CC Name=Gnas-3; Synonyms=NTas;
CC IsoId=P63094-3; Sequence=VSP_021153;
CC Name=XLas-1; Synonyms=XXL;
CC IsoId=Q6R0H7-1; Sequence=External;
CC Name=XLas-2; Synonyms=XXLb1;
CC IsoId=Q6R0H7-2; Sequence=External;
CC Name=XLas-3; Synonyms=XXLb2;
CC IsoId=Q6R0H7-3; Sequence=External;
CC Name=XLas-4;
CC IsoId=Q6R0H7-4; Sequence=External;
CC Name=Nesp55-1;
CC IsoId=Q9Z0F1-1; Sequence=External;
CC Name=Nesp55-2;
CC IsoId=Q9Z0F1-2; Sequence=External;
CC -!- MISCELLANEOUS: This protein is produced by a bicistronic gene which
CC also produces the ALEX protein from an overlapping reading frame.
CC -!- MISCELLANEOUS: The GNAS locus is imprinted in a complex manner, giving
CC rise to distinct paternally, maternally and biallelically expressed
CC proteins. The XLas isoforms are paternally derived, the Gnas isoforms
CC are biallelically derived and the Nesp55 isoforms are maternally
CC derived.
CC -!- SIMILARITY: Belongs to the G-alpha family. G(s) subfamily.
CC {ECO:0000305}.
CC -!- CAUTION: It was found (PubMed:8227063) that in engineered, C3S-
CC mutagenized sequence expressed in HEK293 cells there was no
CC radiolabeling by either S- or N-palmitoylation. This result is
CC incompatible with a prediction for N-palmitoylation unless N-
CC palmitoylation depends on S-palmitoylation occurring first or N-
CC palmitoylation did not occur in the experimental expression system.
CC {ECO:0000305|PubMed:8227063}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB93551.1; Type=Miscellaneous discrepancy; Evidence={ECO:0000305};
CC Sequence=CAM24410.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; Y00703; CAA68695.1; -; mRNA.
DR EMBL; M13964; AAA37745.1; -; mRNA.
DR EMBL; AF107848; AAD11807.1; -; mRNA.
DR EMBL; AK147051; BAE27636.1; -; mRNA.
DR EMBL; AK159563; BAE35187.1; -; mRNA.
DR EMBL; AK168996; BAE40795.1; -; mRNA.
DR EMBL; AL593857; CAM24410.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL593857; CAM24411.1; -; Genomic_DNA.
DR EMBL; AL593857; CAM24412.1; -; Genomic_DNA.
DR EMBL; BC038067; AAH38067.1; -; mRNA.
DR EMBL; BC048834; AAH48834.1; -; mRNA.
DR EMBL; BC061496; AAH61496.1; -; mRNA.
DR EMBL; BC062654; AAH62654.1; -; mRNA.
DR EMBL; BC080816; AAH80816.1; -; mRNA.
DR EMBL; BC092055; AAH92055.1; -; mRNA.
DR EMBL; BC106133; AAI06134.1; -; mRNA.
DR EMBL; AB041808; BAB93551.1; ALT_SEQ; mRNA.
DR CCDS; CCDS38356.1; -. [P63094-1]
DR CCDS; CCDS38357.1; -. [P63094-2]
DR PIR; A25889; RGMSA1.
DR PIR; S03075; RGMSA2.
DR RefSeq; NP_001070978.1; NM_001077510.4. [P63094-2]
DR RefSeq; NP_001297012.1; NM_001310083.1. [P63094-1]
DR RefSeq; NP_963910.1; NM_201616.2. [P63094-1]
DR AlphaFoldDB; P63094; -.
DR SMR; P63094; -.
DR BioGRID; 199972; 37.
DR CORUM; P63094; -.
DR IntAct; P63094; 3.
DR iPTMnet; P63094; -.
DR PhosphoSitePlus; P63094; -.
DR SwissPalm; P63094; -.
DR EPD; P63094; -.
DR jPOST; P63094; -.
DR PeptideAtlas; P63094; -.
DR PRIDE; P63094; -.
DR ProteomicsDB; 267734; -. [P63094-1]
DR ProteomicsDB; 267735; -. [P63094-2]
DR ProteomicsDB; 267736; -. [P63094-3]
DR Antibodypedia; 4152; 809 antibodies from 44 providers.
DR DNASU; 14683; -.
DR Ensembl; ENSMUST00000087871; ENSMUSP00000085179; ENSMUSG00000027523. [P63094-1]
DR Ensembl; ENSMUST00000109085; ENSMUSP00000104713; ENSMUSG00000027523. [P63094-2]
DR Ensembl; ENSMUST00000109087; ENSMUSP00000104715; ENSMUSG00000027523. [P63094-1]
DR GeneID; 14683; -.
DR KEGG; mmu:14683; -.
DR UCSC; uc008oey.1; mouse. [P63094-1]
DR UCSC; uc033hrs.1; mouse. [P63094-2]
DR CTD; 2778; -.
DR MGI; MGI:95777; Gnas.
DR VEuPathDB; HostDB:ENSMUSG00000027523; -.
DR GeneTree; ENSGT00940000156300; -.
DR HOGENOM; CLU_014184_3_0_1; -.
DR OMA; QENRATC; -.
DR BioGRID-ORCS; 14683; 12 hits in 74 CRISPR screens.
DR ChiTaRS; Gnas; mouse.
DR Proteomes; UP000000589; Chromosome 2.
DR Bgee; ENSMUSG00000027523; Expressed in superior cervical ganglion and 269 other tissues.
DR ExpressionAtlas; P63094; baseline and differential.
DR Genevisible; P63094; MM.
DR GO; GO:0030142; C:COPI-coated Golgi to ER transport vesicle; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0030425; C:dendrite; IDA:MGI.
DR GO; GO:0005768; C:endosome; ISO:MGI.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0005834; C:heterotrimeric G-protein complex; ISO:MGI.
DR GO; GO:0031224; C:intrinsic component of membrane; ISO:MGI.
DR GO; GO:0016020; C:membrane; IDA:MGI.
DR GO; GO:0045121; C:membrane raft; ISO:MGI.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0055037; C:recycling endosome; ISO:MGI.
DR GO; GO:0001726; C:ruffle; ISO:MGI.
DR GO; GO:0042383; C:sarcolemma; ISO:MGI.
DR GO; GO:0032588; C:trans-Golgi network membrane; ISO:MGI.
DR GO; GO:0010856; F:adenylate cyclase activator activity; ISS:UniProtKB.
DR GO; GO:0047391; F:alkylglycerophosphoethanolamine phosphodiesterase activity; ISO:MGI.
DR GO; GO:0043014; F:alpha-tubulin binding; ISO:MGI.
DR GO; GO:0031698; F:beta-2 adrenergic receptor binding; ISO:MGI.
DR GO; GO:0051430; F:corticotropin-releasing hormone receptor 1 binding; ISO:MGI.
DR GO; GO:0031748; F:D1 dopamine receptor binding; ISO:MGI.
DR GO; GO:0001664; F:G protein-coupled receptor binding; IBA:GO_Central.
DR GO; GO:0001965; F:G-protein alpha-subunit binding; ISO:MGI.
DR GO; GO:0031681; F:G-protein beta-subunit binding; ISO:MGI.
DR GO; GO:0031683; F:G-protein beta/gamma-subunit complex binding; IBA:GO_Central.
DR GO; GO:0005525; F:GTP binding; ISO:MGI.
DR GO; GO:0003924; F:GTPase activity; ISO:MGI.
DR GO; GO:0005159; F:insulin-like growth factor receptor binding; ISO:MGI.
DR GO; GO:0035255; F:ionotropic glutamate receptor binding; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0031852; F:mu-type opioid receptor binding; ISO:MGI.
DR GO; GO:0019904; F:protein domain specific binding; ISO:MGI.
DR GO; GO:0071880; P:adenylate cyclase-activating adrenergic receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0007191; P:adenylate cyclase-activating dopamine receptor signaling pathway; IGI:MGI.
DR GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; IDA:MGI.
DR GO; GO:0007188; P:adenylate cyclase-modulating G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0060348; P:bone development; ISO:MGI.
DR GO; GO:0055074; P:calcium ion homeostasis; ISO:MGI.
DR GO; GO:0051216; P:cartilage development; IMP:MGI.
DR GO; GO:0071870; P:cellular response to catecholamine stimulus; ISO:MGI.
DR GO; GO:0071380; P:cellular response to prostaglandin E stimulus; ISO:MGI.
DR GO; GO:0050890; P:cognition; ISO:MGI.
DR GO; GO:0048589; P:developmental growth; ISO:MGI.
DR GO; GO:0006306; P:DNA methylation; IMP:MGI.
DR GO; GO:0048701; P:embryonic cranial skeleton morphogenesis; IMP:MGI.
DR GO; GO:0035116; P:embryonic hindlimb morphogenesis; IMP:MGI.
DR GO; GO:0001958; P:endochondral ossification; IMP:MGI.
DR GO; GO:0006112; P:energy reserve metabolic process; IMP:MGI.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; ISO:MGI.
DR GO; GO:0071514; P:genomic imprinting; IMP:MGI.
DR GO; GO:0060789; P:hair follicle placode formation; ISO:MGI.
DR GO; GO:0035264; P:multicellular organism growth; IMP:MGI.
DR GO; GO:0045776; P:negative regulation of blood pressure; ISO:MGI.
DR GO; GO:0035814; P:negative regulation of renal sodium excretion; ISO:MGI.
DR GO; GO:0070527; P:platelet aggregation; ISO:MGI.
DR GO; GO:0043950; P:positive regulation of cAMP-mediated signaling; ISS:UniProtKB.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISO:MGI.
DR GO; GO:0120162; P:positive regulation of cold-induced thermogenesis; IMP:YuBioLab.
DR GO; GO:0043547; P:positive regulation of GTPase activity; ISS:UniProtKB.
DR GO; GO:0045669; P:positive regulation of osteoblast differentiation; IMP:MGI.
DR GO; GO:0045672; P:positive regulation of osteoclast differentiation; IMP:MGI.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; ISO:MGI.
DR GO; GO:0010765; P:positive regulation of sodium ion transport; ISO:MGI.
DR GO; GO:0040032; P:post-embryonic body morphogenesis; IMP:MGI.
DR GO; GO:0009791; P:post-embryonic development; IMP:MGI.
DR GO; GO:2000828; P:regulation of parathyroid hormone secretion; IMP:MGI.
DR GO; GO:0009966; P:regulation of signal transduction; ISO:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0071107; P:response to parathyroid hormone; ISO:MGI.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IMP:MGI.
DR GO; GO:0007606; P:sensory perception of chemical stimulus; IBA:GO_Central.
DR GO; GO:0001501; P:skeletal system development; IMP:MGI.
DR GO; GO:0043588; P:skin development; IMP:MGI.
DR GO; GO:0001894; P:tissue homeostasis; IMP:MGI.
DR CDD; cd00066; G-alpha; 1.
DR Gene3D; 1.10.400.10; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR000367; Gprotein_alpha_S.
DR InterPro; IPR001019; Gprotein_alpha_su.
DR InterPro; IPR011025; GproteinA_insert.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR10218; PTHR10218; 1.
DR Pfam; PF00503; G-alpha; 1.
DR PRINTS; PR00318; GPROTEINA.
DR PRINTS; PR00443; GPROTEINAS.
DR SMART; SM00275; G_alpha; 1.
DR SUPFAM; SSF47895; SSF47895; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS51882; G_ALPHA; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Direct protein sequencing;
KW GTP-binding; Isopeptide bond; Lipoprotein; Magnesium; Membrane;
KW Metal-binding; Nucleotide-binding; Palmitate; Phosphoprotein;
KW Reference proteome; Transducer; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P04896"
FT CHAIN 2..394
FT /note="Guanine nucleotide-binding protein G(s) subunit
FT alpha isoforms short"
FT /id="PRO_0000203723"
FT DOMAIN 39..394
FT /note="G-alpha"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 42..55
FT /note="G1 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 68..90
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 196..204
FT /note="G2 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 219..228
FT /note="G3 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 288..295
FT /note="G4 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 364..369
FT /note="G5 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT COMPBIAS 9..23
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 47..55
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P04896"
FT BINDING 54
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P04896"
FT BINDING 197..204
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P04896"
FT BINDING 204
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P04896"
FT BINDING 223..227
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P04896"
FT BINDING 292..295
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P04896"
FT BINDING 366
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P04896"
FT MOD_RES 352
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P63092"
FT LIPID 2
FT /note="N-palmitoyl glycine"
FT /evidence="ECO:0000250|UniProtKB:P04896"
FT LIPID 3
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000269|PubMed:8227063"
FT CROSSLNK 300
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P63092"
FT VAR_SEQ 1..46
FT /note="MGCLGNSKTEDQRNEEKAQREANKKIEKQLQKDKQVYRATHRLLLL -> MG
FT DSVQILLVFMDK (in isoform Gnas-3)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_021153"
FT VAR_SEQ 71..86
FT /note="EGGEEDPQAARSNSDG -> DS (in isoform Gnas-2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072, ECO:0000303|PubMed:3092218"
FT /id="VSP_011567"
FT VARIANT 389
FT /note="R -> P (in unc mutant; uncouples receptors from
FT adenylyl cyclases)"
FT /evidence="ECO:0000269|PubMed:2826231"
FT MUTAGEN 3
FT /note="C->S: Abolishes S-palmitoylation."
FT /evidence="ECO:0000269|PubMed:8227063"
FT CONFLICT 1..15
FT /note="MGCLGNSKTEDQRNE -> MAARGAAGLRGGG (in Ref. 2;
FT AAA37745)"
FT /evidence="ECO:0000305"
FT CONFLICT 64
FT /note="H -> L (in Ref. 4; BAE35187)"
FT /evidence="ECO:0000305"
FT CONFLICT 97
FT /note="N -> H (in Ref. 4; BAE35187)"
FT /evidence="ECO:0000305"
FT CONFLICT 130
FT /note="Y -> C (in Ref. 6; AAI06134)"
FT /evidence="ECO:0000305"
FT CONFLICT 137
FT /note="V -> L (in Ref. 2; AAA37745 and 3; AAD11807)"
FT /evidence="ECO:0000305"
FT CONFLICT 139
FT /note="N -> D (in Ref. 1; CAA68695)"
FT /evidence="ECO:0000305"
FT CONFLICT 160
FT /note="R -> P (in Ref. 7; BAB93551)"
FT /evidence="ECO:0000305"
FT CONFLICT 326
FT /note="P -> L (in Ref. 4; BAE40795 and 6; AAI06134)"
FT /evidence="ECO:0000305"
SQ 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
