ID GPA4_CAEEL Reviewed; 359 AA. AC Q9BIG5; O44409; DT 27-MAY-2002, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 02-OCT-2024, entry version 159. DE RecName: Full=Guanine nucleotide-binding protein alpha-4 subunit; GN Name=gpa-4; ORFNames=T07A9.7; OS Caenorhabditis elegans. OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida; OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae; OC Caenorhabditis. OX NCBI_TaxID=6239; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=Bristol N2; RA Cuppen E., Jansen G., Plasterk R.H.A.; RT "Interaction analysis of the complete G-alpha subfamily of heterotrimeric G RT proteins from Caenorhabditis elegans."; RL Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Bristol N2; RX PubMed=9851916; DOI=10.1126/science.282.5396.2012; RG The C. elegans sequencing consortium; RT "Genome sequence of the nematode C. elegans: a platform for investigating RT biology."; RL Science 282:2012-2018(1998). RN [3] RP GENE FAMILY, AND NOMENCLATURE. RX PubMed=10192394; DOI=10.1038/7753; RA Jansen G., Thijssen K.L., Werner P., van der Horst M., Hazendonk E., RA Plasterk R.H.A.; RT "The complete family of genes encoding G proteins of Caenorhabditis RT elegans."; RL Nat. Genet. 21:414-419(1999). RN [4] {ECO:0000305} RP FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND DISRUPTION RP PHENOTYPE. RX PubMed=37060828; DOI=10.1016/j.bbrc.2023.03.080; RA Ono M., Matsushita K., Maega S., Asano N., Matsunaga Y., Bito T., RA Iwasaki T., Kawano T.; RT "The G protein-coupled receptor neuropeptide receptor-15 modulates larval RT development via the transforming growth factor-beta DAF-7 protein in RT Caenorhabditis elegans."; RL Biochem. Biophys. Res. Commun. 660:28-34(2023). CC -!- FUNCTION: Guanine nucleotide-binding proteins (G proteins) are involved CC as modulators or transducers in various transmembrane signaling CC systems. Acts in concert with npr-15 to activate TGF-beta-like daf-7 CC secretion in the ASI neuron, thereby promoting larval development and CC inhibition of dauer diapause (PubMed:37060828). CC {ECO:0000269|PubMed:37060828}. CC -!- SUBUNIT: G proteins are composed of 3 units; alpha, beta and gamma. The CC alpha chain contains the guanine nucleotide binding site. CC -!- TISSUE SPECIFICITY: Expressed in ASI neurons. CC {ECO:0000269|PubMed:37060828}. CC -!- DEVELOPMENTAL STAGE: Expressed in ASI neurons during L2 larval CC development. {ECO:0000269|PubMed:37060828}. CC -!- DISRUPTION PHENOTYPE: Increases the likelihood of dauer diapause in L2 CC larval stage animals (PubMed:37060828). Reduces the level of daf-7 CC secreted in the ASI neurons but has no effect on daf-28 secretion CC (PubMed:37060828). {ECO:0000269|PubMed:37060828}. CC -!- SIMILARITY: Belongs to the G-alpha family. G(i/o/t/z) 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; AY008127; AAG32080.1; -; mRNA. DR EMBL; FO081716; CCD73978.1; -; Genomic_DNA. DR PIR; T32578; T32578. DR RefSeq; NP_499921.2; NM_067520.6. DR AlphaFoldDB; Q9BIG5; -. DR SMR; Q9BIG5; -. DR STRING; 6239.T07A9.7.1; -. DR PaxDb; 6239-T07A9.7; -. DR EnsemblMetazoa; T07A9.7.1; T07A9.7.1; WBGene00001666. DR GeneID; 176865; -. DR KEGG; cel:CELE_T07A9.7; -. DR UCSC; T07A9.7; c. elegans. DR AGR; WB:WBGene00001666; -. DR CTD; 176865; -. DR WormBase; T07A9.7; CE31599; WBGene00001666; gpa-4. DR eggNOG; KOG0082; Eukaryota. DR GeneTree; ENSGT00940000165593; -. DR HOGENOM; CLU_014184_6_0_1; -. DR InParanoid; Q9BIG5; -. DR OMA; AHYICAT; -. DR OrthoDB; 2897309at2759; -. DR PhylomeDB; Q9BIG5; -. DR Reactome; R-CEL-170670; Adenylate cyclase inhibitory pathway. DR Reactome; R-CEL-392170; ADP signalling through P2Y purinoceptor 12. DR Reactome; R-CEL-418594; G alpha (i) signalling events. DR PRO; PR:Q9BIG5; -. DR Proteomes; UP000001940; Chromosome IV. DR GO; GO:0005929; C:cilium; IDA:UniProtKB. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005834; C:heterotrimeric G-protein complex; IBA:GO_Central. DR GO; GO:0097730; C:non-motile cilium; IDA:UniProtKB. 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-KW. DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0007188; P:adenylate cyclase-modulating G protein-coupled receptor signaling pathway; IBA:GO_Central. DR CDD; cd00066; G-alpha; 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; IPR001408; Gprotein_alpha_I. DR InterPro; IPR001019; Gprotein_alpha_su. DR InterPro; IPR011025; GproteinA_insert. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10218; GTP-BINDING PROTEIN ALPHA SUBUNIT; 1. DR PANTHER; PTHR10218:SF349; GUANINE NUCLEOTIDE-BINDING PROTEIN ALPHA-4 SUBUNIT; 1. DR Pfam; PF00503; G-alpha; 1. DR PRINTS; PR00318; GPROTEINA. DR PRINTS; PR00441; GPROTEINAI. 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 2: Evidence at transcript level; KW GTP-binding; Lipoprotein; Magnesium; Metal-binding; Myristate; KW Nucleotide-binding; Palmitate; Reference proteome; Transducer. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000255" FT CHAIN 2..359 FT /note="Guanine nucleotide-binding protein alpha-4 subunit" FT /id="PRO_0000203635" FT DOMAIN 31..359 FT /note="G-alpha" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230" FT REGION 34..47 FT /note="G1 motif" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230" FT REGION 176..184 FT /note="G2 motif" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230" FT REGION 199..208 FT /note="G3 motif" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230" FT REGION 268..275 FT /note="G4 motif" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230" FT REGION 329..334 FT /note="G5 motif" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230" FT BINDING 39..46 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250" FT BINDING 46 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250" FT BINDING 178..184 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250" FT BINDING 203..207 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250" FT BINDING 272..275 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250" FT BINDING 331 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250" FT LIPID 2 FT /note="N-myristoyl glycine" FT /evidence="ECO:0000255" FT LIPID 3 FT /note="S-palmitoyl cysteine" FT /evidence="ECO:0000255" SQ SEQUENCE 359 AA; 41671 MW; 04CD363CE9E90D2B CRC64; MGCFHSTGSE AKKRSKLIDE QLRHDHERCV GEIKLLLLGA GESGKSTIVR QMRILHETGF NKQEQMAYRP VVFSNMVQSM LAILKAMQPL NISFTDAARE EDARMFISHF LHVNNAELSE AFSLELSDLM KQLWMDEGVK KCVKRAHEYQ LNDSAEYYFN ALDRISSSSY LPTQDDILRA RVKSTGIVET TFMYKDLCFK MFDVGGQRSE RKKWIHCFDS VTAVIFCVAL SEYDLRLAED QTMNRMHESM QLFDSIVNNC WFTETSIILF LNKMDIFEER IRYTPLTVCF PEYQGGMTIT ETSTFIQSRF EILNKRQTPA QKEIYSHFTC ATDTNNIRFV FDAVTDIIIR NNLYLCGLY //