GPA17_CAEEL
ID GPA17_CAEEL Reviewed; 356 AA.
AC Q18434; C3U544; Q867E1; Q867N8; Q868B7; Q86FY4; Q86FY5;
DT 27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Guanine nucleotide-binding protein alpha-17 subunit;
DE AltName: Full=Odorant response abnormal protein 3;
GN Name=odr-3 {ECO:0000312|WormBase:C34D1.3};
GN ORFNames=C34D1.3 {ECO:0000312|WormBase:C34D1.3};
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], FUNCTION, TISSUE SPECIFICITY, DISRUPTION
RP PHENOTYPE, AND MUTAGENESIS OF SER-47 AND GLN-206.
RX PubMed=9459442; DOI=10.1016/s0896-6273(00)80434-1;
RA Roayaie K., Crump J.G., Sagasti A., Bargmann C.I.;
RT "The G alpha protein ODR-3 mediates olfactory and nociceptive function and
RT controls cilium morphogenesis in C. elegans olfactory neurons.";
RL Neuron 20:55-67(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Bristol N2;
RX PubMed=18629017; DOI=10.1002/cfg.318;
RA Cuppen E., van der Linden A.M., Jansen G., Plasterk R.H.;
RT "Proteins interacting with Caenorhabditis elegans Galpha subunits.";
RL Comp. Funct. Genomics 4:479-491(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=PX174, PX178, and PX179;
RX PubMed=19001295; DOI=10.1534/genetics.107.082651;
RA Jovelin R., Dunham J.P., Sung F.S., Phillips P.C.;
RT "High nucleotide divergence in developmental regulatory genes contrasts
RT with the structural elements of olfactory pathways in caenorhabditis.";
RL Genetics 181:1387-1397(2009).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-350, FUNCTION, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=AB3, BO, CB4855, CB4856, CB4857, CB4932, DH424, RC301, and TR403;
RX PubMed=12694294; DOI=10.1046/j.1365-294x.2003.01805.x;
RA Jovelin R., Ajie B.C., Phillips P.C.;
RT "Molecular evolution and quantitative variation for chemosensory behaviour
RT in the nematode genus Caenorhabditis.";
RL Mol. Ecol. 12:1325-1337(2003).
RN [6]
RP GENE FAMILY, NOMENCLATURE, AND FUNCTION.
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 [7]
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 [8]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=15342507; DOI=10.1534/genetics.103.024786;
RA Lans H., Rademakers S., Jansen G.;
RT "A network of stimulatory and inhibitory Galpha-subunits regulates
RT olfaction in Caenorhabditis elegans.";
RL Genetics 167:1677-1687(2004).
RN [9]
RP MUTAGENESIS OF GLY-185.
RX PubMed=20713521; DOI=10.1101/gad.1932610;
RA Lesch B.J., Bargmann C.I.;
RT "The homeodomain protein hmbx-1 maintains asymmetric gene expression in
RT adult C. elegans olfactory neurons.";
RL Genes Dev. 24:1802-1815(2010).
RN [10]
RP FUNCTION.
RX PubMed=25009271; DOI=10.1523/jneurosci.0012-14.2014;
RA Harris G., Shen Y., Ha H., Donato A., Wallis S., Zhang X., Zhang Y.;
RT "Dissecting the signaling mechanisms underlying recognition and preference
RT of food odors.";
RL J. Neurosci. 34:9389-9403(2014).
CC -!- FUNCTION: Guanine nucleotide-binding proteins (G proteins) are involved
CC as modulators or transducers in various transmembrane signaling systems
CC (PubMed:10192394). This specific G-alpha subunit plays an important
CC role in olfaction and in cilia morphogenesis (PubMed:9459442,
CC PubMed:15342507). Involved in chemotactic responses to attractants
CC diacetyl, pyrazine, 2,4,5-trimethylthiazole, benzaldehyde, isoamyl
CC alcohol, butanone and 2,3-pentanedione (PubMed:12694294). Displays a
CC redundant function with gpa-3 in chemotactic responses
CC (PubMed:12694294). Plays a role in the avoidance response to the
CC noxious chemical quinine in ASH sensory neurons (PubMed:14988722).
CC Involved in avoidance responses to copper, sodium dodecyl sulfate and
CC linoleic acid (PubMed:12694294). Involved in osmotic avoidance and
CC mechanosensory responses (PubMed:12694294). Involved in specifying fan-
CC like morphology of cilia of head sensory neurons AWC (PubMed:9459442).
CC Plays a role in the detection of preferred food sources by mediating
CC the recognition of food odors in olfactory sensory neurons
CC (PubMed:25009271). {ECO:0000269|PubMed:10192394,
CC ECO:0000269|PubMed:12694294, ECO:0000269|PubMed:14988722,
CC ECO:0000269|PubMed:15342507, ECO:0000269|PubMed:25009271,
CC ECO:0000269|PubMed:9459442}.
CC -!- SUBUNIT: G proteins are composed of 3 units; alpha, beta and gamma. The
CC alpha chain contains the guanine nucleotide binding site (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell projection, cilium
CC {ECO:0000269|PubMed:15342507}. Cell projection, dendrite
CC {ECO:0000269|PubMed:15342507}. Note=In amphid neurons also weakly
CC expressed in cell body. In phasmid neurons found only in cilia.
CC -!- TISSUE SPECIFICITY: Expressed in sensory neurons in the head and tail.
CC Expressed in amphid AWC neurons, to a lesser extent in AWB and weakly
CC in AWA, ASH and ADF neurons (head sensory neurons). Expressed in
CC phasmid PHA and PHB neurons (tail sensory neurons).
CC {ECO:0000269|PubMed:15342507, ECO:0000269|PubMed:9459442}.
CC -!- DISRUPTION PHENOTYPE: Defective in chemotactic responses to attractants
CC and repellents and in osmotic and mechanosensory avoidance.
CC {ECO:0000269|PubMed:12694294, ECO:0000269|PubMed:15342507,
CC ECO:0000269|PubMed:9459442}.
CC -!- SIMILARITY: Belongs to the G-alpha family. {ECO:0000305}.
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DR EMBL; AY008142; AAG32095.1; -; mRNA.
DR EMBL; FJ455729; ACQ43989.1; -; Genomic_DNA.
DR EMBL; FJ455730; ACQ43990.1; -; Genomic_DNA.
DR EMBL; FJ455731; ACQ43991.1; -; Genomic_DNA.
DR EMBL; BX284605; CAB01489.1; -; Genomic_DNA.
DR EMBL; AY146558; AAN78230.1; -; Genomic_DNA.
DR EMBL; AY146559; AAN78231.1; -; Genomic_DNA.
DR EMBL; AY146560; AAN78232.1; -; Genomic_DNA.
DR EMBL; AY146561; AAN78233.1; -; Genomic_DNA.
DR EMBL; AY146562; AAN78234.1; -; Genomic_DNA.
DR EMBL; AY146563; AAN78235.1; -; Genomic_DNA.
DR EMBL; AY146564; AAN78236.1; -; Genomic_DNA.
DR EMBL; AY146565; AAN78237.1; -; Genomic_DNA.
DR EMBL; AY146566; AAN78238.1; -; Genomic_DNA.
DR PIR; T19715; T19715.
DR RefSeq; NP_506290.1; NM_073889.1.
DR AlphaFoldDB; Q18434; -.
DR SMR; Q18434; -.
DR BioGRID; 44824; 1.
DR STRING; 6239.C34D1.3; -.
DR EPD; Q18434; -.
DR PaxDb; Q18434; -.
DR PeptideAtlas; Q18434; -.
DR EnsemblMetazoa; C34D1.3.1; C34D1.3.1; WBGene00003850.
DR GeneID; 179806; -.
DR KEGG; cel:CELE_C34D1.3; -.
DR UCSC; C34D1.3; c. elegans.
DR CTD; 179806; -.
DR WormBase; C34D1.3; CE08571; WBGene00003850; odr-3.
DR eggNOG; KOG0082; Eukaryota.
DR HOGENOM; CLU_014184_6_0_1; -.
DR InParanoid; Q18434; -.
DR OMA; HEPGYRP; -.
DR OrthoDB; 754573at2759; -.
DR PhylomeDB; Q18434; -.
DR PRO; PR:Q18434; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00003850; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
DR GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
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:0006935; P:chemotaxis; IEA:UniProtKB-KW.
DR GO; GO:0060271; P:cilium assembly; IMP:UniProtKB.
DR GO; GO:0006972; P:hyperosmotic response; IMP:WormBase.
DR GO; GO:0042048; P:olfactory behavior; IMP:UniProtKB.
DR GO; GO:1990834; P:response to odorant; IMP:UniProtKB.
DR GO; GO:0007608; P:sensory perception of smell; IEA:UniProtKB-KW.
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 Cell projection; Chemotaxis; Cilium; GTP-binding; Lipoprotein; Magnesium;
KW Metal-binding; Myristate; Nucleotide-binding; Olfaction; Palmitate;
KW Reference proteome; Sensory transduction; Transducer.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000255"
FT CHAIN 2..356
FT /note="Guanine nucleotide-binding protein alpha-17 subunit"
FT /id="PRO_0000203659"
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 175..183
FT /note="G2 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 198..207
FT /note="G3 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 267..274
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 177..183
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 183
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 202..206
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 271..274
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"
FT MUTAGEN 47
FT /note="S->C: Loss of chemotactic responses."
FT /evidence="ECO:0000269|PubMed:9459442"
FT MUTAGEN 185
FT /note="G->S: In ky879; defects in GPCR expression in the
FT AWC neurons."
FT /evidence="ECO:0000269|PubMed:20713521"
FT MUTAGEN 206
FT /note="Q->L: Loss of chemotactic and osmotic avoidance
FT responses."
FT /evidence="ECO:0000269|PubMed:9459442"
SQ SEQUENCE 356 AA; 40434 MW; CB9F36F5F4FB95D9 CRC64;
MGSCQSNENS EGNARNKEIE KQLNADKRAG SSIVKLLLLG AGECGKSTVL KQMQILHSNG
FTEEEVNEKR AIVYNNTVSA MCTILRAMDG VLHLPLENGQ KEAEKAIVMK VQENGEEGEA
LTEEVSKAIQ SLWADPGVKK AFEMRSEYQL PDSAKYFLDN CQRISEPGYR PNDQDILYSR
VATTGVVEVK FKIKELDFRV FDVGGQRSER RKWIHCFDNV ESIIFITAIS EYDQVLFEDE
TTNRMIESMQ LFNSICNSTW FLSTAMILFM NKKDLFMEKI QRVNITTAFP DYEGGQNYEE
AVSFIKQKFA ELNLNPDKKT IYMHETCATD TNQVQLVISS VIDTIIQKNL QKAGMM
