GPA3_CAEEL
ID GPA3_CAEEL Reviewed; 353 AA.
AC P28052; Q19029;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2021, sequence version 3.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Guanine nucleotide-binding protein alpha-3 subunit;
GN Name=gpa-3 {ECO:0000312|WormBase:E02C12.5a};
GN ORFNames=E02C12.5 {ECO:0000312|WormBase:E02C12.5a};
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).
RN [5]
RP FUNCTION.
RX PubMed=14988722; DOI=10.1038/sj.emboj.7600107;
RA Hilliard M.A., Bergamasco C., Arbucci S., Plasterk R.H., Bazzicalupo P.;
RT "Worms taste bitter: ASH neurons, QUI-1, GPA-3 and ODR-3 mediate quinine
RT avoidance in Caenorhabditis elegans.";
RL EMBO J. 23:1101-1111(2004).
RN [6]
RP FUNCTION, AND MUTAGENESIS OF GLN-205.
RX PubMed=19489741; DOI=10.1111/j.1474-9726.2009.00495.x;
RA Hahm J.H., Kim S., Paik Y.K.;
RT "Endogenous cGMP regulates adult longevity via the insulin signaling
RT pathway in Caenorhabditis elegans.";
RL Aging Cell 8:473-483(2009).
RN [7]
RP FUNCTION, AND MUTAGENESIS OF GLY-40.
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. Promotes transcription of 3',5'-cyclic phosphodiesterases pde-
CC 1 and pde-5, leading to reduced cGMP levels in sensory neurons. This
CC causes suppression of insulin production and signaling which leads to
CC increased daf-16 activity and contributes to increased adult lifespan
CC and resistance to oxidative stress. In addition, by reducing cGMP
CC levels, inhibits TGF-beta signaling pathways (PubMed:19489741).
CC Involved in behavioral response to P.aeruginosa by controlling the
CC expression of daf-7, a member of the TGF-beta family, in ASJ sensory
CC neurons (PubMed:25303524). Plays a role in the avoidance response to
CC the noxious chemical quinine in ASH sensory neurons (PubMed:14988722).
CC {ECO:0000269|PubMed:14988722, ECO:0000269|PubMed:19489741,
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA28061.1; Type=Erroneous termination; Note=Extended C-terminus.; Evidence={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; M38250; AAA28061.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AY008126; AAG32079.1; -; mRNA.
DR EMBL; BX284605; CCD68590.2; -; Genomic_DNA.
DR PIR; T30140; T30140.
DR RefSeq; NP_001309498.1; NM_001322582.1.
DR AlphaFoldDB; P28052; -.
DR SMR; P28052; -.
DR BioGRID; 44357; 1.
DR STRING; 6239.E02C12.5; -.
DR PaxDb; P28052; -.
DR PeptideAtlas; P28052; -.
DR EnsemblMetazoa; E02C12.5a.1; E02C12.5a.1; WBGene00001665.
DR GeneID; 179319; -.
DR KEGG; cel:CELE_E02C12.5; -.
DR UCSC; E02C12.5; c. elegans.
DR CTD; 179319; -.
DR WormBase; E02C12.5a; CE51492; WBGene00001665; gpa-3.
DR eggNOG; KOG0082; Eukaryota.
DR GeneTree; ENSGT00970000196172; -.
DR HOGENOM; CLU_014184_6_0_1; -.
DR InParanoid; P28052; -.
DR OMA; QVQMILD; -.
DR OrthoDB; 754573at2759; -.
DR PhylomeDB; P28052; -.
DR PRO; PR:P28052; -.
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:0031849; F:olfactory receptor binding; IPI:WormBase.
DR GO; GO:0007188; P:adenylate cyclase-modulating G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0001306; P:age-dependent response to oxidative stress; IMP:UniProtKB.
DR GO; GO:0071321; P:cellular response to cGMP; IMP:UniProtKB.
DR GO; GO:0040024; P:dauer larval development; IMP:WormBase.
DR GO; GO:0050829; P:defense response to Gram-negative bacterium; IGI:UniProtKB.
DR GO; GO:0008340; P:determination of adult lifespan; IMP:UniProtKB.
DR GO; GO:1903554; P:G protein-coupled receptor signaling pathway involved in defense response to Gram-negative bacterium; IMP:WormBase.
DR GO; GO:0010629; P:negative regulation of gene expression; IMP:UniProtKB.
DR GO; GO:0007602; P:phototransduction; IGI:UniProtKB.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:UniProtKB.
DR GO; GO:0050913; P:sensory perception of bitter taste; IMP:WormBase.
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..353
FT /note="Guanine nucleotide-binding protein alpha-3 subunit"
FT /id="PRO_0000203633"
FT DOMAIN 32..353
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 324..329
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 326
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 MUTAGEN 40
FT /note="G->D: Reduced daf-7 expression in ASJ neurons."
FT /evidence="ECO:0000269|PubMed:25303524"
FT MUTAGEN 205
FT /note="Q->L: In syls25; constitutively active. In adults,
FT premature death resulting from internal egg hatching.
FT Increased lifespan and resistance to oxidative stress when
FT progeny overgrowth is prevented. Reduction in pde-1, pde-5,
FT daf-7, ins-7 and daf-28 mRNA levels."
FT /evidence="ECO:0000269|PubMed:19489741"
FT CONFLICT 200
FT /note="F -> L (in Ref. 1; AAA28061)"
FT /evidence="ECO:0000305"
FT CONFLICT 353
FT /note="L -> LY (in Ref. 1; AAA28061)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 353 AA; 40443 MW; A9EF32F337DD02F6 CRC64;
MGLCQSAEDK ELTLKSKAID KEMMQNHMSQ QKVVKLLLLG AGECGKSTVL KQMRILHDHG
FTAEEAEQQK SVVFNNTLQA MTAILKGMEA LRMTFDKPIR ENDAKFVMES HKMLQEAKVF
PEELANAIQA LWNDKAVQQV IAKGNEFQMP ESAPHFLSSL DRIKLPDYNP TEQDILLSRI
KTTGIVEVKF QMKSVDFRVF DVGGQRSERK KWIHCFEDVN AIIFIAAISE YDQVLFEDET
TNRMIESMRL FESICNSRWF INTSMILFLN KKDLFAEKIK RTSIKSAFPD YKGAQTYDES
CRYIEEKFDG LNANPEKTIY MHQTCATDTD QVQMILDSVI DMIIQANLQG CGL
