ID Q7KPV0_CAEEL Unreviewed; 378 AA. AC Q7KPV0; DT 06-FEB-2013, integrated into UniProtKB/TrEMBL. DT 06-FEB-2013, sequence version 1. DT 27-NOV-2024, entry version 81. DE RecName: Full=Guanine nucleotide-binding protein G(s) subunit alpha {ECO:0000256|RuleBase:RU369121}; DE AltName: Full=Adenylate cyclase-stimulating G alpha protein {ECO:0000256|RuleBase:RU369121}; GN Name=gsa-1 {ECO:0000313|EMBL:CCD73235.2, GN ECO:0000313|WormBase:R06A10.2a}; GN ORFNames=CELE_R06A10.2 {ECO:0000313|EMBL:CCD73235.2}, R06A10.2 GN {ECO:0000313|WormBase:R06A10.2a}; OS Caenorhabditis elegans. OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida; OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae; OC Caenorhabditis. OX NCBI_TaxID=6239 {ECO:0000313|EMBL:CCD73235.2, ECO:0000313|Proteomes:UP000001940}; RN [1] {ECO:0000313|EMBL:CCD73235.2, ECO:0000313|Proteomes:UP000001940} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Bristol N2 {ECO:0000313|EMBL:CCD73235.2, RC ECO:0000313|Proteomes:UP000001940}; RX PubMed=9851916; DOI=10.1126/science.282.5396.2012; RG The C. elegans sequencing consortium; RA Sulson J.E., Waterston R.; RT "Genome sequence of the nematode C. elegans: a platform for investigating RT biology."; RL Science 282:2012-2018(1998). CC -!- FUNCTION: Guanine nucleotide-binding proteins (G proteins) function as CC transducers in numerous signaling pathways controlled by G protein- CC coupled receptors (GPCRs). {ECO:0000256|RuleBase:RU369121}. CC -!- SUBUNIT: G proteins are composed of 3 units; alpha, beta and gamma. The CC alpha chain contains the guanine nucleotide binding site. CC {ECO:0000256|ARBA:ARBA00011356, ECO:0000256|RuleBase:RU369121}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|RuleBase:RU369121}. CC -!- SIMILARITY: Belongs to the G-alpha family. G(s) subfamily. CC {ECO:0000256|ARBA:ARBA00007172, ECO:0000256|RuleBase:RU369121}. 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; BX284601; CCD73235.2; -; Genomic_DNA. DR PIR; D87723; D87723. DR PIR; T37243; T37245. DR RefSeq; NP_490817.4; NM_058416.5. DR AlphaFoldDB; Q7KPV0; -. DR SMR; Q7KPV0; -. DR STRING; 6239.R06A10.2a.1; -. DR PaxDb; 6239-R06A10.2.1; -. DR EnsemblMetazoa; R06A10.2a.1; R06A10.2a.1; WBGene00001745. DR AGR; WB:WBGene00001745; -. DR WormBase; R06A10.2a; CE47896; WBGene00001745; gsa-1. DR eggNOG; KOG0099; Eukaryota. DR HOGENOM; CLU_014184_3_0_1; -. DR InParanoid; Q7KPV0; -. DR OMA; TEFYDHT; -. DR OrthoDB; 2897309at2759; -. DR PhylomeDB; Q7KPV0; -. DR Reactome; R-CEL-170660; Adenylate cyclase activating pathway. DR Reactome; R-CEL-170670; Adenylate cyclase inhibitory pathway. DR Reactome; R-CEL-418555; G alpha (s) signalling events. DR Proteomes; UP000001940; Chromosome I. DR ExpressionAtlas; Q7KPV0; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005834; C:heterotrimeric G-protein complex; IBA:GO_Central. DR GO; GO:0001664; F:G protein-coupled receptor binding; IBA:GO_Central. DR GO; GO:0031683; F:G-protein beta/gamma-subunit complex binding; IBA:GO_Central. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule. DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0007191; P:adenylate cyclase-activating dopamine receptor signaling pathway; IBA:GO_Central. DR GO; GO:0043050; P:nematode pharyngeal pumping; IMP:UniProtKB. DR GO; GO:0001555; P:oocyte growth; IGI:UniProtKB. DR GO; GO:1900195; P:positive regulation of oocyte maturation; IMP:UniProtKB. DR GO; GO:2000292; P:regulation of defecation; IGI:UniProtKB. DR GO; GO:2000114; P:regulation of establishment of cell polarity; IGI:WormBase. DR GO; GO:0007606; P:sensory perception of chemical stimulus; IBA:GO_Central. DR GO; GO:0007210; P:serotonin receptor signaling pathway; IMP:UniProtKB. DR CDD; cd00066; G-alpha; 1. DR FunFam; 3.40.50.300:FF:000720; Guanine nucleotide-binding protein G(k) subunit alpha; 1. DR FunFam; 1.10.400.10:FF:000003; Guanine nucleotide-binding protein G(S) subunit alpha; 1. DR FunFam; 3.40.50.300:FF:006178; Guanine nucleotide-binding protein G(s) subunit alpha isoforms short; 1. DR Gene3D; 1.10.400.10; GI Alpha 1, domain 2-like; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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:SF212; G PROTEIN ALPHA S SUBUNIT; 1. DR PANTHER; PTHR10218; GTP-BINDING PROTEIN ALPHA SUBUNIT; 1. DR Pfam; PF00503; G-alpha; 1. DR PRINTS; PR00318; GPROTEINA. DR PRINTS; PR00443; GPROTEINAS. DR SMART; SM00275; G_alpha; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR SUPFAM; SSF47895; Transducin (alpha subunit), insertion domain; 1. DR PROSITE; PS51882; G_ALPHA; 1. PE 1: Evidence at protein level; KW Cell membrane {ECO:0000256|RuleBase:RU369121}; KW GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|PIRSR:PIRSR601019- KW 1}; KW Magnesium {ECO:0000256|PIRSR:PIRSR601019-2, ECO:0000256|RuleBase:RU369121}; KW Membrane {ECO:0000256|RuleBase:RU369121}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, KW ECO:0000256|PIRSR:PIRSR601019-2}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, KW ECO:0000256|PIRSR:PIRSR601019-1}; KW Proteomics identification {ECO:0007829|PeptideAtlas:Q7KPV0}; KW Reference proteome {ECO:0000313|Proteomes:UP000001940}; KW Transducer {ECO:0000256|ARBA:ARBA00023224, ECO:0000256|RuleBase:RU369121}. FT BINDING 49..54 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000256|PIRSR:PIRSR601019-1" FT BINDING 53 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|PIRSR:PIRSR601019-2" FT BINDING 182..188 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000256|PIRSR:PIRSR601019-1" FT BINDING 188 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|PIRSR:PIRSR601019-2" FT BINDING 207..211 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000256|PIRSR:PIRSR601019-1" FT BINDING 276..279 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000256|PIRSR:PIRSR601019-1" FT BINDING 350 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000256|PIRSR:PIRSR601019-1" SQ SEQUENCE 378 AA; 44413 MW; A75AE7370820EB9C CRC64; MRLMGCVGAG ADAEGREARK VNKQIEEQLA KDKQVMRATH RLLLLGAGES GKSTIVKQMR ILHINGFNEA EKREKITDIR RNVRDAMQVI LRAMDEIVPK VSLDDPSTAI SRDYILRITN DPEDNYPSEF YDHILTCWKD KGVMACYERS SEYQLIDCAQ YFLDKVDVVR QNNYDPSEQD ILRCRVMTTG IFETKFEVDK VRFHMFDVGG QRDERRKWIQ CFNDVTAIIF VCASSSYNLV LWEDNTQNRL RESLALFKNI WNNRWLKTIS VILFLNKQDL LSEKIKAKRY LLESFFPEFE GYNLPNDAVF DNQEDKDVVR AKYFIRGEFL RISTANSDGR HHCYPHFTCA VDTENIRRVF NDCRDIIQRI HLRQYELL //