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 07-JUN-2017, entry version 120. 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 Rhabditoidea; Rhabditidae; Peloderinae; 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 RT heterotrimeric G 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 RT investigating 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 CC involved as modulators or transducers in various transmembrane CC signaling systems. CC -!- SUBUNIT: G proteins are composed of 3 units; alpha, beta and CC gamma. The alpha chain contains the guanine nucleotide binding CC 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 UniGene; Cel.39186; -. DR ProteinModelPortal; Q9BIG5; -. DR SMR; Q9BIG5; -. DR STRING; 6239.T07A9.7; -. DR PaxDb; Q9BIG5; -. DR PRIDE; Q9BIG5; -. DR EnsemblMetazoa; T07A9.7; T07A9.7; 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 eggNOG; ENOG410XNVQ; LUCA. DR GeneTree; ENSGT00760000118851; -. DR HOGENOM; HOG000038730; -. DR InParanoid; Q9BIG5; -. DR KO; K04630; -. DR OMA; CFTRARE; -. DR OrthoDB; EOG091G0VUT; -. DR PhylomeDB; Q9BIG5; -. DR Reactome; R-CEL-112043; PLC beta mediated events. DR Reactome; R-CEL-170670; Adenylate cyclase inhibitory pathway. DR Reactome; R-CEL-202040; G-protein activation. DR Reactome; R-CEL-2514859; Inactivation, recovery and regulation of the phototransduction cascade. DR Reactome; R-CEL-418594; G alpha (i) signalling events. DR Reactome; R-CEL-418597; G alpha (z) signalling events. DR PRO; PR:Q9BIG5; -. DR Proteomes; UP000001940; Chromosome IV. DR Bgee; WBGene00001666; -. 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:0031683; F:G-protein beta/gamma-subunit complex binding; IBA:GO_Central. DR GO; GO:0001664; F:G-protein coupled receptor 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:0004871; F:signal transducer activity; IBA:GO_Central. 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 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; 2. PE 2: Evidence at transcript level; KW Complete proteome; GTP-binding; Lipoprotein; Magnesium; Metal-binding; KW Myristate; Nucleotide-binding; Palmitate; Reference proteome; KW Transducer. FT INIT_MET 1 1 Removed. {ECO:0000255}. FT CHAIN 2 359 Guanine nucleotide-binding protein alpha- FT 4 subunit. FT /FTId=PRO_0000203635. FT NP_BIND 39 46 GTP. {ECO:0000250}. FT NP_BIND 178 184 GTP. {ECO:0000250}. FT NP_BIND 203 207 GTP. {ECO:0000250}. FT NP_BIND 272 275 GTP. {ECO:0000250}. FT METAL 46 46 Magnesium. {ECO:0000250}. FT BINDING 331 331 GTP; via amide nitrogen. {ECO:0000250}. FT LIPID 2 2 N-myristoyl glycine. {ECO:0000255}. FT LIPID 3 3 S-palmitoyl cysteine. {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 //