UniProt functional annotation for P04896



	UniProt functional annotation for P04896

UniProt code: P04896.

Organism: Bos taurus (Bovine).

Taxonomy: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae; Bovinae; Bos.

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 (PubMed:2022671, PubMed:9395396, PubMed:11087399, PubMed:15591060, PubMed:16766715, PubMed:19243146). GNAS functions downstream of several GPCRs, including beta-adrenergic receptors. Stimulates the Ras signaling pathway via RAPGEF2 (By similarity). {ECO:0000250|UniProtKB:P63092, ECO:0000269|PubMed:11087399, ECO:0000269|PubMed:2022671, ECO:0000269|PubMed:9395396, ECO:0000305|PubMed:15591060, ECO:0000305|PubMed:16766715, ECO:0000305|PubMed:19243146}.

Subunit: Heterotrimeric G proteins are composed of 3 units; alpha, beta and gamma. The alpha chain contains the guanine nucleotide binding site (PubMed:9395396, PubMed:9417641, PubMed:10427002, PubMed:11087399, PubMed:15591060, PubMed:16766715, PubMed:19243146). 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 (PubMed:9395396, PubMed:9417641, PubMed:10427002, PubMed:11087399, PubMed:15591060, PubMed:16766715, PubMed:19243146). Stimulates the ADCY5 adenylyl cyclase activity (By similarity). Interaction with SASH1 (By similarity). Interacts with GASL2L2 (By similarity). {ECO:0000250|UniProtKB:P63092, ECO:0000269|PubMed:10427002, ECO:0000269|PubMed:11087399, ECO:0000269|PubMed:15591060, ECO:0000269|PubMed:16766715, ECO:0000269|PubMed:19243146, ECO:0000269|PubMed:9395396, ECO:0000269|PubMed:9417641}.

Subcellular location: Cell membrane {ECO:0000250|UniProtKB:P63094}; Lipid-anchor {ECO:0000250|UniProtKB:P63094}.

Miscellaneous: The GNAS locus is imprinted in a complex manner, giving rise to distinct paternally, maternally and biallelically expressed proteins.

Miscellaneous: Crystal structures were determined for GNAS in complex with an adenylyl cyclase catalytic domain that was reconstructed from ADCY2 and ADCY5 N- and C-terminal domains. {ECO:0000269|PubMed:10427002, ECO:0000269|PubMed:11087399, ECO:0000269|PubMed:15591060, ECO:0000269|PubMed:16766715, ECO:0000269|PubMed:19243146, ECO:0000269|PubMed:9395396, ECO:0000269|PubMed:9417641}.

Similarity: Belongs to the G-alpha family. G(s) subfamily. {ECO:0000305}.

Annotations taken from UniProtKB at the EBI.


Organism:		Bos taurus (Bovine).
Taxonomy:		Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae; Bovinae; Bos.



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 (PubMed:2022671, PubMed:9395396, PubMed:11087399, PubMed:15591060, PubMed:16766715, PubMed:19243146). GNAS functions downstream of several GPCRs, including beta-adrenergic receptors. Stimulates the Ras signaling pathway via RAPGEF2 (By similarity). {ECO:0000250\|UniProtKB:P63092, ECO:0000269\|PubMed:11087399, ECO:0000269\|PubMed:2022671, ECO:0000269\|PubMed:9395396, ECO:0000305\|PubMed:15591060, ECO:0000305\|PubMed:16766715, ECO:0000305\|PubMed:19243146}.


Subunit:		Heterotrimeric G proteins are composed of 3 units; alpha, beta and gamma. The alpha chain contains the guanine nucleotide binding site (PubMed:9395396, PubMed:9417641, PubMed:10427002, PubMed:11087399, PubMed:15591060, PubMed:16766715, PubMed:19243146). 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 (PubMed:9395396, PubMed:9417641, PubMed:10427002, PubMed:11087399, PubMed:15591060, PubMed:16766715, PubMed:19243146). Stimulates the ADCY5 adenylyl cyclase activity (By similarity). Interaction with SASH1 (By similarity). Interacts with GASL2L2 (By similarity). {ECO:0000250\|UniProtKB:P63092, ECO:0000269\|PubMed:10427002, ECO:0000269\|PubMed:11087399, ECO:0000269\|PubMed:15591060, ECO:0000269\|PubMed:16766715, ECO:0000269\|PubMed:19243146, ECO:0000269\|PubMed:9395396, ECO:0000269\|PubMed:9417641}.
Subcellular location:		Cell membrane {ECO:0000250\|UniProtKB:P63094}; Lipid-anchor {ECO:0000250\|UniProtKB:P63094}.
Miscellaneous:		The GNAS locus is imprinted in a complex manner, giving rise to distinct paternally, maternally and biallelically expressed proteins.
Miscellaneous:		Crystal structures were determined for GNAS in complex with an adenylyl cyclase catalytic domain that was reconstructed from ADCY2 and ADCY5 N- and C-terminal domains. {ECO:0000269\|PubMed:10427002, ECO:0000269\|PubMed:11087399, ECO:0000269\|PubMed:15591060, ECO:0000269\|PubMed:16766715, ECO:0000269\|PubMed:19243146, ECO:0000269\|PubMed:9395396, ECO:0000269\|PubMed:9417641}.
Similarity:		Belongs to the G-alpha family. G(s) subfamily. {ECO:0000305}.