ID GNAS2_BOVIN Reviewed; 394 AA. AC P04896; Q0II85; Q3SZE7; DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot. DT 13-AUG-1987, sequence version 1. DT 29-OCT-2014, entry version 152. 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; OS Bos taurus (Bovine). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia; OC Pecora; Bovidae; Bovinae; Bos. OX NCBI_TaxID=9913; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=3080331; DOI=10.1016/0014-5793(86)80164-8; RA Nukada T., Tanabe T., Takahashi H., Noda M., Hirose T., Inayama S., RA Numa S.; RT "Primary structure of the alpha-subunit of bovine adenylate cyclase- RT stimulating G-protein deduced from the cDNA sequence."; RL FEBS Lett. 195:220-224(1986). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=3081893; DOI=10.1073/pnas.83.5.1251; RA Robishaw J.D., Russell D.W., Harris B.A., Smigel M.D., Gilman A.G.; RT "Deduced primary structure of the alpha subunit of the GTP-binding RT stimulatory protein of adenylate cyclase."; RL Proc. Natl. Acad. Sci. U.S.A. 83:1251-1255(1986). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=Hereford; TISSUE=Hypothalamus, and Kidney; RG NIH - Mammalian Gene Collection (MGC) project; RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] OF 69-90. RX PubMed=3015900; RA Robishaw J.D., Smigel M.D., Gilman A.G.; RT "Molecular basis for two forms of the G protein that stimulates RT adenylate cyclase."; RL J. Biol. Chem. 261:9587-9590(1986). RN [5] RP PALMITOYLATION AT GLY-2 AND CYS-3, AND IDENTIFICATION BY MASS RP SPECTROMETRY. RX PubMed=12574119; DOI=10.1093/emboj/cdg095; RA Kleuss C., Krause E.; RT "Galpha(s) is palmitoylated at the N-terminal glycine."; RL EMBO J. 22:826-832(2003). RN [6] RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 1-394 OF GNAS-2 FORM. RX PubMed=9395396; DOI=10.1126/science.278.5345.1943; RA Sunahara R.K., Tesmer J.J.G., Gilman A.G., Sprang S.R.; RT "Crystal structure of the adenylyl cyclase activator Gsalpha."; RL Science 278:1943-1947(1997). RN [7] RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF COMPLEX WITH CATALYTIC RP DOMAINS OF ADENYLATE CYCLASE. RX PubMed=9417641; DOI=10.1126/science.278.5345.1907; RA Tesmer J.J.G., Sunahara R.K., Gilman A.G., Sprang S.R.; RT "Crystal structure of the catalytic domains of adenylyl cyclase in a RT complex with Gsalpha.GTPgammaS."; RL Science 278:1907-1916(1997). RN [8] RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF COMPLEX WITH CATALYTIC RP DOMAINS OF ADENYLATE CYCLASE. RX PubMed=10427002; DOI=10.1126/science.285.5428.756; RA Tesmer J.J.G., Sunahara R.K., Johnson R.A., Gosselin G., Gilman A.G., RA Sprang S.R.; RT "Two-metal-ion catalysis in adenylyl cyclase."; RL Science 285:756-760(1999). CC -!- FUNCTION: Guanine nucleotide-binding proteins (G proteins) are CC involved as modulators or transducers in various transmembrane CC signaling systems. The G(s) protein is involved in hormonal CC regulation of adenylate cyclase: it activates the cyclase in CC response to beta-adrenergic stimuli. Stimulates the Ras signaling CC pathway via RAPGEF2 (By similarity). {ECO:0000250}. CC -!- SUBUNIT: G proteins are composed of 3 units; alpha, beta and CC gamma. The alpha chain contains the guanine nucleotide binding CC site. Interacts with CRY1; the interaction may block GPCR-mediated CC regulation of cAMP concentrations. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Lipid-anchor CC {ECO:0000250}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=Gnas-1; Synonyms=Alpha-S2; CC IsoId=P04896-1; Sequence=Displayed; CC Name=Gnas-2; Synonyms=Alpha-S1; CC IsoId=P04896-2; Sequence=VSP_001832; CC Name=Nesp55; CC IsoId=O18979-1; Sequence=External; CC Note=Shares no sequence similarity with other isoforms due to a CC novel first exon containing the entire reading frame spliced to CC shared exon 2 so that exons 2-13 make up the 3'-UTR.; CC -!- MISCELLANEOUS: The GNAS locus is imprinted in a complex manner, CC giving rise to distinct paternally, maternally and biallelically CC expressed proteins. CC -!- SIMILARITY: Belongs to the G-alpha family. G(s) subfamily. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X03404; CAA27137.1; -; mRNA. DR EMBL; M13006; AAA30560.1; -; mRNA. DR EMBL; BC102905; AAI02906.1; -; mRNA. DR EMBL; BC122757; AAI22758.1; -; mRNA. DR EMBL; M14014; AAA30557.1; -; mRNA. DR PIR; A23818; RGBOGA. DR PIR; I45904; I45904. DR RefSeq; NP_001258700.1; NM_001271771.1. DR RefSeq; NP_851364.1; NM_181021.3. [P04896-1] DR UniGene; Bt.64619; -. DR UniGene; Bt.91987; -. DR PDB; 1AZS; X-ray; 2.30 A; C=1-394. DR PDB; 1AZT; X-ray; 2.30 A; A/B=1-394. DR PDB; 1CJK; X-ray; 3.00 A; C=1-394. DR PDB; 1CJT; X-ray; 2.80 A; C=1-394. DR PDB; 1CJU; X-ray; 2.80 A; C=1-394. DR PDB; 1CJV; X-ray; 3.00 A; C=1-394. DR PDB; 1CS4; X-ray; 2.50 A; C=1-394. DR PDB; 1CUL; X-ray; 2.40 A; C=1-394. DR PDB; 1TL7; X-ray; 2.80 A; C=1-394. DR PDB; 1U0H; X-ray; 2.90 A; C=1-394. DR PDB; 2GVD; X-ray; 2.90 A; C=1-394. DR PDB; 2GVZ; X-ray; 3.27 A; C=1-394. DR PDB; 3C14; X-ray; 2.68 A; C=1-394. DR PDB; 3C15; X-ray; 2.78 A; C=1-394. DR PDB; 3C16; X-ray; 2.87 A; C=1-394. DR PDB; 3G82; X-ray; 3.11 A; C=1-394. DR PDB; 3MAA; X-ray; 3.00 A; C=1-394. DR PDB; 3SN6; X-ray; 3.20 A; A=1-394. DR PDBsum; 1AZS; -. DR PDBsum; 1AZT; -. DR PDBsum; 1CJK; -. DR PDBsum; 1CJT; -. DR PDBsum; 1CJU; -. DR PDBsum; 1CJV; -. DR PDBsum; 1CS4; -. DR PDBsum; 1CUL; -. DR PDBsum; 1TL7; -. DR PDBsum; 1U0H; -. DR PDBsum; 2GVD; -. DR PDBsum; 2GVZ; -. DR PDBsum; 3C14; -. DR PDBsum; 3C15; -. DR PDBsum; 3C16; -. DR PDBsum; 3G82; -. DR PDBsum; 3MAA; -. DR PDBsum; 3SN6; -. DR ProteinModelPortal; P04896; -. DR SMR; P04896; 35-391. DR DIP; DIP-588N; -. DR IntAct; P04896; 1. DR STRING; 9913.ENSBTAP00000023234; -. DR PRIDE; P04896; -. DR GeneID; 281793; -. DR KEGG; bta:281793; -. DR CTD; 2778; -. DR eggNOG; NOG325092; -. DR HOGENOM; HOG000038729; -. DR HOVERGEN; HBG063184; -. DR InParanoid; P04896; -. DR KO; K04632; -. DR Reactome; REACT_202137; Regulation of water balance by renal Aquaporins. DR Reactome; REACT_206547; G alpha (s) signalling events. DR Reactome; REACT_209033; G alpha (z) signalling events. DR Reactome; REACT_210568; G alpha (i) signalling events. DR Reactome; REACT_217846; Glucagon-like Peptide-1 (GLP1) regulates insulin secretion. DR Reactome; REACT_219718; PKA activation in glucagon signalling. DR Reactome; REACT_220607; Glucagon-type ligand receptors. DR Reactome; REACT_221707; Glucagon signaling in metabolic regulation. DR Reactome; REACT_227415; Prostacyclin signalling through prostacyclin receptor. DR EvolutionaryTrace; P04896; -. DR NextBio; 20805706; -. DR ExpressionAtlas; P04896; baseline. DR GO; GO:0030425; C:dendrite; IEA:Ensembl. DR GO; GO:0070062; C:extracellular vesicular exosome; IEA:Ensembl. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW. DR GO; GO:0003924; F:GTPase activity; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004871; F:signal transducer activity; ISS:UniProtKB. 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; IEA:Ensembl. DR GO; GO:0051216; P:cartilage development; IEA:Ensembl. DR GO; GO:0050890; P:cognition; IEA:Ensembl. DR GO; GO:0048589; P:developmental growth; IEA:Ensembl. DR GO; GO:0006306; P:DNA methylation; IEA:Ensembl. DR GO; GO:0048701; P:embryonic cranial skeleton morphogenesis; IEA:Ensembl. DR GO; GO:0035116; P:embryonic hindlimb morphogenesis; IEA:Ensembl. DR GO; GO:0001958; P:endochondral ossification; IEA:Ensembl. DR GO; GO:0006112; P:energy reserve metabolic process; IEA:Ensembl. DR GO; GO:0071514; P:genetic imprinting; IEA:Ensembl. DR GO; GO:0060789; P:hair follicle placode formation; IEA:Ensembl. DR GO; GO:0035264; P:multicellular organism growth; IEA:Ensembl. DR GO; GO:0070527; P:platelet aggregation; IEA:Ensembl. DR GO; GO:0030819; P:positive regulation of cAMP biosynthetic process; ISS:UniProtKB. DR GO; GO:0043950; P:positive regulation of cAMP-mediated signaling; ISS:UniProtKB. DR GO; GO:0045669; P:positive regulation of osteoblast differentiation; IEA:Ensembl. DR GO; GO:0045672; P:positive regulation of osteoclast differentiation; IEA:Ensembl. DR GO; GO:0032320; P:positive regulation of Ras GTPase activity; ISS:UniProtKB. DR GO; GO:0040032; P:post-embryonic body morphogenesis; IEA:Ensembl. DR GO; GO:0042493; P:response to drug; IEA:Ensembl. DR GO; GO:0001894; P:tissue homeostasis; IEA:Ensembl. DR Gene3D; 1.10.400.10; -; 1. DR Gene3D; 3.40.50.300; -; 2. 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; 2. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Cell membrane; Complete proteome; KW GTP-binding; Isopeptide bond; Lipoprotein; Magnesium; Membrane; KW Metal-binding; Nucleotide-binding; Palmitate; Phosphoprotein; KW Reference proteome; Transducer; Ubl conjugation. FT CHAIN 1 394 Guanine nucleotide-binding protein G(s) FT subunit alpha isoforms short. FT /FTId=PRO_0000203717. FT NP_BIND 47 54 GTP. {ECO:0000250}. FT NP_BIND 198 204 GTP. {ECO:0000250}. FT NP_BIND 223 227 GTP. {ECO:0000250}. FT NP_BIND 292 295 GTP. {ECO:0000250}. FT METAL 54 54 Magnesium. {ECO:0000250}. FT METAL 204 204 Magnesium. {ECO:0000250}. FT BINDING 366 366 GTP; via amide nitrogen. {ECO:0000250}. FT MOD_RES 352 352 Phosphoserine. {ECO:0000250}. FT LIPID 2 2 N-palmitoyl glycine. FT {ECO:0000269|PubMed:12574119}. FT LIPID 3 3 S-palmitoyl cysteine. FT {ECO:0000269|PubMed:12574119}. FT CROSSLNK 300 300 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in ubiquitin). FT {ECO:0000250}. FT VAR_SEQ 71 84 Missing (in isoform Gnas-2). FT {ECO:0000305}. FT /FTId=VSP_001832. FT CONFLICT 18 18 A -> G (in Ref. 2; AAA30560). FT {ECO:0000305}. FT CONFLICT 85 85 D -> S (in Ref. 2; AAA30560). FT {ECO:0000305}. FT CONFLICT 363 363 F -> S (in Ref. 2; AAA30560). FT {ECO:0000305}. FT HELIX 36 39 FT STRAND 40 48 FT HELIX 53 64 FT HELIX 87 89 FT HELIX 90 112 FT STRAND 113 115 FT HELIX 122 124 FT HELIX 125 133 FT TURN 134 136 FT HELIX 144 155 FT HELIX 157 163 FT HELIX 164 168 FT HELIX 175 179 FT HELIX 182 185 FT STRAND 187 189 FT HELIX 194 199 FT STRAND 206 214 FT STRAND 217 224 FT HELIX 228 237 FT TURN 238 240 FT STRAND 243 249 FT HELIX 252 254 FT TURN 258 260 FT STRAND 261 264 FT HELIX 265 277 FT HELIX 280 282 FT STRAND 283 285 FT STRAND 287 292 FT HELIX 294 303 FT HELIX 308 310 FT HELIX 313 316 FT HELIX 332 350 FT TURN 354 356 FT STRAND 359 363 FT STRAND 365 367 FT HELIX 369 392 SQ SEQUENCE 394 AA; 45709 MW; 4D07A734AFF2A6BC CRC64; MGCLGNSKTE DQRNEEKAQR EANKKIEKQL QKDKQVYRAT HRLLLLGAGE SGKSTIVKQM RILHVNGFNG EGGEEDPQAA RSNSDGEKAT KVQDIKNNLK EAIETIVAAM SNLVPPVELA NPENQFRVDY ILSVMNVPDF DFPPEFYEHA KALWEDEGVR ACYERSNEYQ LIDCAQYFLD KIDVIKQDDY VPSDQDLLRC RVLTSGIFET KFQVDKVNFH MFDVGGQRDE RRKWIQCFND VTAIIFVVAS SSYNMVIRED NQTNRLQEAL NLFKSIWNNR WLRTISVILF LNKQDLLAEK VLAGKSKIED YFPEFARYTT PEDATPEPGE DPRVTRAKYF IRDEFLRIST ASGDGRHYCY PHFTCAVDTE NIRRVFNDCR DIIQRMHLRQ YELL //