ID GPA2_CAEEL Reviewed; 356 AA.
AC P22454;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1991, sequence version 1.
DT 27-MAR-2024, entry version 161.
DE RecName: Full=Guanine nucleotide-binding protein alpha-2 subunit;
GN Name=gpa-2; ORFNames=F38E1.5;
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 [GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=2121996; DOI=10.1016/s0022-2836(05)80160-3;
RA Silva F.I., Plasterk R.H.A.;
RT "Characterization of a G-protein alpha-subunit gene from the nematode
RT Caenorhabditis elegans.";
RL J. Mol. Biol. 215:483-487(1990).
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).
RN [5]
RP FUNCTION.
RX PubMed=25303524; DOI=10.1016/j.cell.2014.09.011;
RA Meisel J.D., Panda O., Mahanti P., Schroeder F.C., Kim D.H.;
RT "Chemosensation of bacterial secondary metabolites modulates neuroendocrine
RT signaling and behavior of C. elegans.";
RL Cell 159:267-280(2014).
CC -!- FUNCTION: Guanine nucleotide-binding proteins (G proteins) are involved
CC as modulators or transducers in various transmembrane signaling
CC systems. Involved in behavioral responses to P.aeruginosa by
CC controlling the expression of daf-7, a member of the TGF-beta family,
CC in ASJ sensory neurons (PubMed:25303524).
CC {ECO:0000269|PubMed:25303524}.
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(q) subfamily.
CC {ECO:0000305}.
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DR EMBL; X53156; CAA37312.1; -; Genomic_DNA.
DR EMBL; AY008125; AAG32078.1; -; mRNA.
DR EMBL; FO080433; CCD63657.1; -; Genomic_DNA.
DR PIR; S13221; S13221.
DR RefSeq; NP_505157.1; NM_072756.3.
DR AlphaFoldDB; P22454; -.
DR SMR; P22454; -.
DR STRING; 6239.F38E1.5.1; -.
DR PaxDb; 6239-F38E1-5; -.
DR PeptideAtlas; P22454; -.
DR EnsemblMetazoa; F38E1.5.1; F38E1.5.1; WBGene00001664.
DR GeneID; 179219; -.
DR KEGG; cel:CELE_F38E1.5; -.
DR UCSC; F38E1.5; c. elegans.
DR AGR; WB:WBGene00001664; -.
DR WormBase; F38E1.5; CE04523; WBGene00001664; gpa-2.
DR eggNOG; KOG0082; Eukaryota.
DR GeneTree; ENSGT00970000196172; -.
DR HOGENOM; CLU_014184_6_0_1; -.
DR InParanoid; P22454; -.
DR OMA; YNEVLFE; -.
DR OrthoDB; 2874799at2759; -.
DR PhylomeDB; P22454; -.
DR PRO; PR:P22454; -.
DR Proteomes; UP000001940; Chromosome V.
DR GO; GO:0030424; C:axon; IDA:WormBase.
DR GO; GO:0005834; C:heterotrimeric G-protein complex; IBA:GO_Central.
DR GO; GO:0043025; C:neuronal cell body; IDA:WormBase.
DR GO; GO:0097730; C:non-motile cilium; 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 GO; GO:0050829; P:defense response to Gram-negative bacterium; IGI:UniProtKB.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IMP:WormBase.
DR GO; GO:0008355; P:olfactory learning; IGI:WormBase.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:UniProtKB.
DR CDD; cd00066; G-alpha; 1.
DR Gene3D; 1.10.400.10; GI Alpha 1, domain 2-like; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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; GTP-BINDING PROTEIN ALPHA SUBUNIT; 1.
DR PANTHER; PTHR10218:SF245; GUANINE NUCLEOTIDE-BINDING PROTEIN ALPHA-2 SUBUNIT-RELATED; 1.
DR Pfam; PF00503; G-alpha; 1.
DR PRINTS; PR00318; GPROTEINA.
DR PRINTS; PR00441; GPROTEINAI.
DR SMART; SM00275; G_alpha; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF47895; Transducin (alpha subunit), insertion domain; 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..356
FT /note="Guanine nucleotide-binding protein alpha-2 subunit"
FT /id="PRO_0000203631"
FT DOMAIN 32..356
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 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 326..331
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 178..184
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 184
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
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 328
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 356 AA; 41490 MW; B2622850B3AF04ED CRC64;
MGLCQSEEEK VGTLKSRAID KEIKQLQTSE ERTVKLLLLG AGECGKSTVL KQMRLLTSKQ
YTDEELLTQA KLVYTNIVIE MDHLVKAMPA AGLNFSDPMR EHDVHMLTLY IKDMQHKNFQ
QDAADHVEKL WKDPVVKRLY AERKELNIRD IGDNTEYFFE NLPRISKEDY HPNATDTLLL
RTKTTGIVEV GFEIKKVKFR VFDVGGQRSE RKKWIHCFED VNAIIFIAAL SEYNEVLFED
ETTNRMIESM RLFESICNSR WFHNTNIILF LNKKDLFEEK IKKENIHKAF PEYRGEQNYA
ETVAFIKTKF EALSNNPKKT FYVHETCATD TNQVQKILDS VISMIIQSNL HKSGLY
//
