GPA1_CAEEL
ID GPA1_CAEEL Reviewed; 357 AA.
AC P28051; Q22567;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 27-MAY-2002, sequence version 2.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Guanine nucleotide-binding protein alpha-1 subunit;
GN Name=gpa-1; ORFNames=T19C4.6;
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 [GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=1907494; DOI=10.1091/mbc.2.2.135;
RA Lochrie M.A., Mendel J.E., Sternberg P.W., Simon M.I.;
RT "Homologous and unique G protein alpha subunits in the nematode
RT Caenorhabditis elegans.";
RL Cell Regul. 2:135-154(1991).
RN [2]
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 [3]
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 [4]
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. {ECO:0000305}.
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DR EMBL; M38249; AAA28060.1; -; Genomic_DNA.
DR EMBL; AY008124; AAG32077.1; -; mRNA.
DR EMBL; Z75549; CAA99914.1; -; Genomic_DNA.
DR PIR; T24992; T24992.
DR RefSeq; NP_505840.1; NM_073439.1.
DR AlphaFoldDB; P28051; -.
DR SMR; P28051; -.
DR BioGRID; 44573; 1.
DR STRING; 6239.T19C4.6a; -.
DR PaxDb; P28051; -.
DR PeptideAtlas; P28051; -.
DR EnsemblMetazoa; T19C4.6a.1; T19C4.6a.1; WBGene00001663.
DR GeneID; 179546; -.
DR KEGG; cel:CELE_T19C4.6; -.
DR UCSC; T19C4.6a; c. elegans.
DR CTD; 179546; -.
DR WormBase; T19C4.6a; CE06470; WBGene00001663; gpa-1.
DR eggNOG; KOG0082; Eukaryota.
DR GeneTree; ENSGT00940000168787; -.
DR HOGENOM; CLU_014184_6_0_1; -.
DR InParanoid; P28051; -.
DR OMA; HDSAKYF; -.
DR OrthoDB; 754573at2759; -.
DR PhylomeDB; P28051; -.
DR PRO; PR:P28051; -.
DR Proteomes; UP000001940; Chromosome V.
DR ExpressionAtlas; P28051; baseline and differential.
DR GO; GO:0005834; C:heterotrimeric G-protein complex; IBA:GO_Central.
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; 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 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..357
FT /note="Guanine nucleotide-binding protein alpha-1 subunit"
FT /id="PRO_0000203629"
FT DOMAIN 32..357
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 174..182
FT /note="G2 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 197..206
FT /note="G3 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 266..273
FT /note="G4 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 327..332
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 176..182
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 182
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 201..205
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 270..273
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 329
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"
FT CONFLICT 157..159
FT /note="FDA -> LDR (in Ref. 1; AAA28060)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 357 AA; 40660 MW; ADD8FEEED1932700 CRC64;
MGNCESRELV AQAKQNKIIN TELDKAKKTD ENIIKLLLLG AGESGKSTVL KQMKIIHNSG
FSQEEISNKR NVVCANTVQA MGALLDGMKQ LQFDFSTRVC NAHEKLIRET LNDKAEYGPF
SDAMFNALTE LWADKGVQCA YDKREFFYLH DSAKYFFDAI ARVHTPNYVP TENDILHTRV
PTMGVIEVNF TIKGKFFRVF DVGGQRSQRK KWIHCFDDAK AMIYVASLSE YDQVLLEDNT
TNRMHESIQL FKQVINNKYF VNTSVILFLN KIDLFEEKIV TKKRSLGIAF ESFSGPSQDL
NAAVAFVEKK YRSMAENKEK NIYCHHTCAT DTQQVQYVLD AVLDTILSTK LKGCGLY
