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 29-MAY-2024, entry version 151. 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:15342507, CC PubMed:9459442). 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}. 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; 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.C34D1.3.1; -. DR EPD; Q18434; -. DR PaxDb; 6239-C34D1-3; -. 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 AGR; WB:WBGene00003850; -. 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; 2897309at2759; -. 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 cell types or tissues. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. 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; 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:SF215; GUANINE NUCLEOTIDE-BINDING PROTEIN ALPHA-17 SUBUNIT; 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 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 //