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GPA4_CAEEL
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   03-AUG-2022, entry version 149.
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}.
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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; -.
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; XYLNDER; -.
DR   OrthoDB; 754573at2759; -.
DR   PhylomeDB; Q9BIG5; -.
DR   Reactome; R-CEL-170670; Adenylate cyclase inhibitory pathway.
DR   Reactome; R-CEL-2485179; Activation of the phototransduction cascade.
DR   Reactome; R-CEL-2514859; Inactivation, recovery and regulation of the phototransduction cascade.
DR   Reactome; R-CEL-392170; ADP signalling through P2Y purinoceptor 12.
DR   Reactome; R-CEL-4086398; Ca2+ pathway.
DR   Reactome; R-CEL-418594; G alpha (i) signalling events.
DR   Reactome; R-CEL-9717207; Sensory perception of sweet, bitter, and umami (glutamate) taste.
DR   PRO; PR:Q9BIG5; -.
DR   Proteomes; UP000001940; Chromosome IV.
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   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
 
 
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