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Guanine nucleotide-binding protein G(s) subunit alpha isoforms short (Adenylate cyclase-stimulating G alpha protein) (G-alpha-8)

 GNAS2_RAT               Reviewed;         394 AA.
P63095; P04894; P08755; Q05087; Q45QM7; Q9Z1R8;
13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
13-AUG-1987, sequence version 1.
20-DEC-2017, entry version 123.
RecName: Full=Guanine nucleotide-binding protein G(s) subunit alpha isoforms short;
AltName: Full=Adenylate cyclase-stimulating G alpha protein;
AltName: Full=G-alpha-8;
Name=Gnas; Synonyms=Gnas1;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM GNAS-1).
PubMed=3086867; DOI=10.1073/pnas.83.11.3776;
Itoh H., Kozasa T., Nagata S., Nakamura S., Katada T., Ui M., Iwai S.,
Ohtsuka E., Kawasaki H., Suzuki K., Kaziro Y.;
"Molecular cloning and sequence determination of cDNAs for alpha
subunits of the guanine nucleotide-binding proteins Gs, Gi, and Go
from rat brain.";
Proc. Natl. Acad. Sci. U.S.A. 83:3776-3780(1986).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM GNAS-1).
PubMed=2820999;
Jones D.T., Reed R.R.;
"Molecular cloning of five GTP-binding protein cDNA species from rat
olfactory neuroepithelium.";
J. Biol. Chem. 262:14241-14249(1987).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM GNAS-3), AND TISSUE SPECIFICITY.
TISSUE=Thyroid;
PubMed=8486667;
Crawford J.A., Mutchler K.J., Sullivan B.E., Lanigan T.M., Clark M.S.,
Russo A.F.;
"Neural expression of a novel alternatively spliced and polyadenylated
Gsa alpha transcript.";
J. Biol. Chem. 268:9879-9885(1993).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM GNAS-2).
STRAIN=New England Deaconess Hospital;
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.
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM GNAS-1).
STRAIN=SHR, and Wistar Kyoto;
Jackson E.K., Zhu C.;
"Genetic similarity between spontaneously hypertensive rats and
Wistar-Kyoto rats in the coding regions of signal transduction
proteins.";
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM GNAS-1).
TISSUE=Prostate;
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]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-352, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
[8]
STRUCTURE BY NMR OF 81-209.
PubMed=7500342; DOI=10.1006/jmbi.1995.0647;
Benjamin D.R., Markby D.W., Bourne H.R., Kuntz I.D.;
"Solution structure of the GTPase activating domain of alpha s.";
J. Mol. Biol. 254:681-691(1995).
[9]
PALMITOYLATION AT CYS-3, AND MUTAGENESIS OF CYS-3.
PubMed=8347607; DOI=10.1021/bi00083a001;
Degtyarev M.Y., Spiegel A.M., Jones T.L.Z.;
"The G protein alpha s subunit incorporates [3H]palmitic acid and
mutation of cysteine-3 prevents this modification.";
Biochemistry 32:8057-8061(1993).
-!- 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:0000250|UniProtKB:P63094}; Lipid-anchor
{ECO:0000250|UniProtKB:P63094}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=5;
Name=Gnas-1;
IsoId=P63095-1; Sequence=Displayed;
Name=Gnas-2;
IsoId=P63095-2; Sequence=VSP_021154;
Name=Gnas-3; Synonyms=GsaN1;
IsoId=P63095-3; Sequence=VSP_021155, VSP_021156;
Name=XLas-1;
IsoId=Q63803-1; Sequence=External;
Name=Nesp55;
IsoId=Q792G6-1; Sequence=External;
Note=Shares no sequence similarity with other isoforms 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.;
-!- TISSUE SPECIFICITY: Isoform Gnas-3 is abundant in brain with
intermediate levels in skeletal muscle and very low levels in
other tissues. {ECO:0000269|PubMed:8486667}.
-!- 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}.
-----------------------------------------------------------------------
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EMBL; M12673; AAA41261.1; -; mRNA.
EMBL; M17525; AAA40827.1; -; mRNA.
EMBL; L10326; AAA41664.1; -; mRNA.
EMBL; AF107844; AAD11802.1; -; mRNA.
EMBL; DQ120475; AAZ23814.1; -; mRNA.
EMBL; DQ120476; AAZ23815.1; -; mRNA.
EMBL; BC061967; AAH61967.1; -; mRNA.
PIR; A27423; RGRTA2.
PIR; A46685; A46685.
RefSeq; NP_062005.1; NM_019132.1. [P63095-1]
UniGene; Rn.127731; -.
UniGene; Rn.31; -.
ProteinModelPortal; P63095; -.
SMR; P63095; -.
BioGrid; 247005; 1.
IntAct; P63095; 1.
iPTMnet; P63095; -.
PhosphoSitePlus; P63095; -.
SwissPalm; P63095; -.
PRIDE; P63095; -.
GeneID; 24896; -.
CTD; 2778; -.
RGD; 2716; Gnas.
HOVERGEN; HBG063184; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0005737; C:cytoplasm; IDA:RGD.
GO; GO:0005829; C:cytosol; IDA:BHF-UCL.
GO; GO:0030425; C:dendrite; ISO:RGD.
GO; GO:0005768; C:endosome; IDA:RGD.
GO; GO:0070062; C:extracellular exosome; ISO:RGD.
GO; GO:0005834; C:heterotrimeric G-protein complex; IDA:BHF-UCL.
GO; GO:0031224; C:intrinsic component of membrane; ISO:RGD.
GO; GO:0016020; C:membrane; IDA:BHF-UCL.
GO; GO:0045121; C:membrane raft; IDA:RGD.
GO; GO:0043025; C:neuronal cell body; IDA:RGD.
GO; GO:0005634; C:nucleus; ISO:RGD.
GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:RGD.
GO; GO:0005886; C:plasma membrane; IDA:RGD.
GO; GO:0001726; C:ruffle; IDA:RGD.
GO; GO:0032588; C:trans-Golgi network membrane; ISO:RGD.
GO; GO:0031982; C:vesicle; IDA:RGD.
GO; GO:0047391; F:alkylglycerophosphoethanolamine phosphodiesterase activity; IDA:MGI.
GO; GO:0043014; F:alpha-tubulin binding; IDA:RGD.
GO; GO:0031698; F:beta-2 adrenergic receptor binding; IPI:RGD.
GO; GO:0051430; F:corticotropin-releasing hormone receptor 1 binding; IPI:RGD.
GO; GO:0031748; F:D1 dopamine receptor binding; IPI:RGD.
GO; GO:0001965; F:G-protein alpha-subunit binding; IPI:RGD.
GO; GO:0031681; F:G-protein beta-subunit binding; IDA:RGD.
GO; GO:0031683; F:G-protein beta/gamma-subunit complex binding; IEA:InterPro.
GO; GO:0005525; F:GTP binding; IDA:RGD.
GO; GO:0003924; F:GTPase activity; IEA:InterPro.
GO; GO:0005159; F:insulin-like growth factor receptor binding; IPI:RGD.
GO; GO:0035255; F:ionotropic glutamate receptor binding; IPI:RGD.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0031852; F:mu-type opioid receptor binding; IDA:RGD.
GO; GO:0019904; F:protein domain specific binding; IPI:RGD.
GO; GO:0004871; F:signal transducer activity; IDA:RGD.
GO; GO:0071880; P:adenylate cyclase-activating adrenergic receptor signaling pathway; ISS:UniProtKB.
GO; GO:0007191; P:adenylate cyclase-activating dopamine receptor signaling pathway; IDA:BHF-UCL.
GO; GO:0007189; P:adenylate cyclase-activating G-protein coupled receptor signaling pathway; IDA:RGD.
GO; GO:0060348; P:bone development; ISO:RGD.
GO; GO:0055074; P:calcium ion homeostasis; IMP:RGD.
GO; GO:0051216; P:cartilage development; ISO:RGD.
GO; GO:0071870; P:cellular response to catecholamine stimulus; IDA:BHF-UCL.
GO; GO:0071380; P:cellular response to prostaglandin E stimulus; IDA:BHF-UCL.
GO; GO:0050890; P:cognition; ISO:RGD.
GO; GO:0048589; P:developmental growth; ISO:RGD.
GO; GO:0006306; P:DNA methylation; ISO:RGD.
GO; GO:0048701; P:embryonic cranial skeleton morphogenesis; ISO:RGD.
GO; GO:0035116; P:embryonic hindlimb morphogenesis; ISO:RGD.
GO; GO:0001958; P:endochondral ossification; ISO:RGD.
GO; GO:0006112; P:energy reserve metabolic process; ISO:RGD.
GO; GO:0007186; P:G-protein coupled receptor signaling pathway; IMP:RGD.
GO; GO:0071514; P:genetic imprinting; ISO:RGD.
GO; GO:0060789; P:hair follicle placode formation; ISO:RGD.
GO; GO:0035264; P:multicellular organism growth; ISO:RGD.
GO; GO:0045776; P:negative regulation of blood pressure; IMP:RGD.
GO; GO:0040015; P:negative regulation of multicellular organism growth; ISO:RGD.
GO; GO:0035814; P:negative regulation of renal sodium excretion; IMP:RGD.
GO; GO:0070527; P:platelet aggregation; ISO:RGD.
GO; GO:0030819; P:positive regulation of cAMP biosynthetic process; IMP:RGD.
GO; GO:0043950; P:positive regulation of cAMP-mediated signaling; ISS:UniProtKB.
GO; GO:0008284; P:positive regulation of cell proliferation; IDA:RGD.
GO; GO:0043547; P:positive regulation of GTPase activity; ISS:UniProtKB.
GO; GO:0045669; P:positive regulation of osteoblast differentiation; ISO:RGD.
GO; GO:0045672; P:positive regulation of osteoclast differentiation; ISO:RGD.
GO; GO:0001934; P:positive regulation of protein phosphorylation; IMP:RGD.
GO; GO:0010765; P:positive regulation of sodium ion transport; IMP:RGD.
GO; GO:0040032; P:post-embryonic body morphogenesis; ISO:RGD.
GO; GO:0009791; P:post-embryonic development; ISO:RGD.
GO; GO:2000828; P:regulation of parathyroid hormone secretion; ISO:RGD.
GO; GO:0009966; P:regulation of signal transduction; ISO:RGD.
GO; GO:0006357; P:regulation of transcription from RNA polymerase II promoter; IMP:RGD.
GO; GO:0042493; P:response to drug; ISO:RGD.
GO; GO:0071107; P:response to parathyroid hormone; ISO:RGD.
GO; GO:0001501; P:skeletal system development; ISO:RGD.
GO; GO:0043588; P:skin development; ISO:RGD.
GO; GO:0001894; P:tissue homeostasis; ISO:RGD.
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; GTP-binding;
Isopeptide bond; Lipoprotein; Magnesium; Membrane; Metal-binding;
Nucleotide-binding; Palmitate; Phosphoprotein; 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_0000203725.
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:0000244|PubMed:22673903}.
LIPID 2 2 N-palmitoyl glycine.
{ECO:0000250|UniProtKB:P04896}.
LIPID 3 3 S-palmitoyl cysteine.
{ECO:0000269|PubMed:8347607}.
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-
2). {ECO:0000303|Ref.4}.
/FTId=VSP_021154.
VAR_SEQ 87 91 EKATK -> VYYPH (in isoform Gnas-3).
{ECO:0000303|PubMed:8486667}.
/FTId=VSP_021155.
VAR_SEQ 92 394 Missing (in isoform Gnas-3).
{ECO:0000303|PubMed:8486667}.
/FTId=VSP_021156.
MUTAGEN 3 3 C->A: Abolishes S-palmitoylation.
{ECO:0000269|PubMed:8347607}.
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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