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 29-SEP-2021, entry version 146. 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). CC -!- FUNCTION: Guanine nucleotide-binding proteins (G proteins) are involved CC as modulators or transducers in various transmembrane signaling CC systems. CC -!- SUBUNIT: G proteins are composed of 3 units; alpha, beta and gamma. The CC alpha chain contains the guanine nucleotide binding site. 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 SMR; Q9BIG5; -. DR STRING; 6239.T07A9.7; -. DR PaxDb; Q9BIG5; -. DR PRIDE; Q9BIG5; -. 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 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; KIDYEEP; -. DR OrthoDB; 754573at2759; -. 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-400042; Adrenaline,noradrenaline inhibits insulin secretion. DR Reactome; R-CEL-418594; G alpha (i) signalling events. DR PRO; PR:Q9BIG5; -. DR Proteomes; UP000001940; Chromosome IV. DR Bgee; WBGene00001666; Expressed in multi-cellular organism and 4 other tissues. DR GO; GO:0005929; C:cilium; IDA:UniProtKB. 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; -; 1. DR Gene3D; 3.40.50.300; -; 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; PTHR10218; 1. DR Pfam; PF00503; G-alpha; 1. DR PRINTS; PR00318; GPROTEINA. DR PRINTS; PR00441; GPROTEINAI. DR SMART; SM00275; G_alpha; 1. DR SUPFAM; SSF47895; SSF47895; 1. DR SUPFAM; SSF52540; SSF52540; 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 NP_BIND 39..46 FT /note="GTP" FT /evidence="ECO:0000250" FT NP_BIND 178..184 FT /note="GTP" FT /evidence="ECO:0000250" FT NP_BIND 203..207 FT /note="GTP" FT /evidence="ECO:0000250" FT NP_BIND 272..275 FT /note="GTP" FT /evidence="ECO:0000250" 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 METAL 46 FT /note="Magnesium" FT /evidence="ECO:0000250" FT BINDING 331 FT /note="GTP; via amide nitrogen" 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 //