GPA7_CAEEL
ID GPA7_CAEEL Reviewed; 352 AA.
AC Q21917;
DT 27-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Guanine nucleotide-binding protein alpha-7 subunit;
GN Name=gpa-7; ORFNames=R10H10.5;
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 -!- INTERACTION:
CC Q21917; Q09587: nhr-22; NbExp=3; IntAct=EBI-6094232, EBI-323124;
CC -!- SIMILARITY: Belongs to the G-alpha family. G(i/o/t/z) subfamily.
CC {ECO:0000305}.
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DR EMBL; AY008130; AAG32083.1; -; mRNA.
DR EMBL; Z70686; CAA94612.1; -; Genomic_DNA.
DR PIR; T24154; T24154.
DR RefSeq; NP_501921.1; NM_069520.1.
DR AlphaFoldDB; Q21917; -.
DR SMR; Q21917; -.
DR BioGRID; 43033; 1.
DR IntAct; Q21917; 1.
DR STRING; 6239.R10H10.5; -.
DR iPTMnet; Q21917; -.
DR EPD; Q21917; -.
DR PaxDb; Q21917; -.
DR PeptideAtlas; Q21917; -.
DR EnsemblMetazoa; R10H10.5.1; R10H10.5.1; WBGene00001669.
DR GeneID; 177931; -.
DR KEGG; cel:CELE_R10H10.5; -.
DR UCSC; R10H10.5; c. elegans.
DR CTD; 177931; -.
DR WormBase; R10H10.5; CE06296; WBGene00001669; gpa-7.
DR eggNOG; KOG0082; Eukaryota.
DR GeneTree; ENSGT00940000168787; -.
DR HOGENOM; CLU_014184_6_0_1; -.
DR InParanoid; Q21917; -.
DR OMA; DMIIARN; -.
DR OrthoDB; 754573at2759; -.
DR PhylomeDB; Q21917; -.
DR PRO; PR:Q21917; -.
DR Proteomes; UP000001940; Chromosome IV.
DR GO; GO:0005829; C:cytosol; IDA:WormBase.
DR GO; GO:0005834; C:heterotrimeric G-protein complex; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:WormBase.
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 1: Evidence at protein 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..352
FT /note="Guanine nucleotide-binding protein alpha-7 subunit"
FT /id="PRO_0000203641"
FT DOMAIN 32..352
FT /note="G-alpha"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 35..48
FT /note="G1 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 172..180
FT /note="G2 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 195..204
FT /note="G3 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 264..271
FT /note="G4 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 322..327
FT /note="G5 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT BINDING 40..47
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 47
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 174..180
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 180
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 199..203
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 268..271
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 324
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 4
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 352 AA; 41021 MW; 375A1A4D462EFE5E CRC64;
MGHCTSKDQK EGKRLNRRID EQIKKDQSMS LRIIKLLLLG AGESGKSTIL KQMRILHKDG
FSQQDLEMIR PVVYSNCIHS MLSILRAMFH LQIEYGEPDR VRDSQLVFAT VHANKEELTE
ELAAAMQRLW HDPGVRECYR RSNEYQIDDS AKYFLDNLPR LSSPNYVPSE QDLLRTRIKT
TGITEVLFEL KGLTFRVIDV GGQRSERKKW IHCFDNVNAI IFISSLSEYD QTLREDNCTN
RMQESLKLFD SICNSPWFAD IHFILFLNKK DLFAEKIVRS PLTVCFPEYK GQQNQTECIN
YIQWKFEQLN RSSQREIYCH HTCATDTNNV QFVLDACLDM IIAKNLKSMG LC
