GPA17_CAEBR
ID GPA17_CAEBR Reviewed; 356 AA.
AC Q86FX7; A8X960; C3U547; Q867F2;
DT 27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Guanine nucleotide-binding protein alpha-17 subunit;
DE AltName: Full=Odorant response abnormal protein 3;
GN Name=odr-3; ORFNames=CBG09409;
OS Caenorhabditis briggsae.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6238;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=AF16, DH1300, HK104, and VT847;
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 [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=HK105;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AF16;
RX PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA Durbin R.M., Waterston R.H.;
RT "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT genomics.";
RL PLoS Biol. 1:166-192(2003).
CC -!- FUNCTION: Guanine nucleotide-binding proteins (G proteins) are involved
CC as modulators or transducers in various transmembrane signaling
CC systems. This specific G-alpha subunit plays an important role in
CC olfaction and in cilia morphogenesis. Involved in chemotactic responses
CC to attractants diacetyl, pyrazine, 2,4,5-trimethylthiazole,
CC benzaldehyde, isoamyl alcohol, butanone and 2,3-pentanedione. Displays
CC a redundant function with gpa-3 in chemotactic responses. Involved in
CC avoidance responses to copper, sodium dodecyl sulfate and linoleic
CC acid. Involved in osmotic avoidance and mechanosensory responses.
CC Involved in specifying fan-like morphology of cilia of head sensory
CC neurons AWC (By similarity). {ECO:0000250}.
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 {ECO:0000250}. Cell
CC projection, dendrite {ECO:0000250}. Note=In amphid neurons also weakly
CC expressed in cell body. In phasmid neurons found only in cilia.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the G-alpha family. {ECO:0000305}.
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DR EMBL; AY146578; AAN78250.1; -; Genomic_DNA.
DR EMBL; AY146579; AAN78251.1; -; Genomic_DNA.
DR EMBL; AY146580; AAN78252.1; -; Genomic_DNA.
DR EMBL; AY146581; AAN78253.1; -; Genomic_DNA.
DR EMBL; FJ455732; ACQ43992.1; -; Genomic_DNA.
DR EMBL; HE600954; CAP29172.3; -; Genomic_DNA.
DR RefSeq; XP_002636938.1; XM_002636892.1.
DR AlphaFoldDB; Q86FX7; -.
DR SMR; Q86FX7; -.
DR STRING; 6238.CBG09409; -.
DR EnsemblMetazoa; CBG09409.1; CBG09409.1; WBGene00030998.
DR GeneID; 8578933; -.
DR KEGG; cbr:CBG_09409; -.
DR CTD; 8578933; -.
DR WormBase; CBG09409; CBP02303; WBGene00030998; Cbr-odr-3.
DR eggNOG; KOG0082; Eukaryota.
DR HOGENOM; CLU_014184_6_0_1; -.
DR InParanoid; Q86FX7; -.
DR OMA; HEPGYRP; -.
DR OrthoDB; 754573at2759; -.
DR Proteomes; UP000008549; Chromosome V.
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; IEA:EnsemblMetazoa.
DR GO; GO:0097730; C:non-motile cilium; IEA:EnsemblMetazoa.
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; IEA:EnsemblMetazoa.
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; IEA:EnsemblMetazoa.
DR GO; GO:0006972; P:hyperosmotic response; IEA:EnsemblMetazoa.
DR GO; GO:0042048; P:olfactory behavior; IEA:EnsemblMetazoa.
DR GO; GO:1990834; P:response to odorant; IEA:EnsemblMetazoa.
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 3: Inferred from homology;
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_0000203658"
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"
SQ SEQUENCE 356 AA; 40446 MW; E18AE988033ED226 CRC64;
MGSCQSNENS EGNARNKEIE KQLNADKRAG SSIVKLLLLG AGECGKSTVL KQMQILHSNG
FTEEEVNEKR AIVYNNTVSA MCTILRAMDG VLHLPLENGQ KEAEKAIVMK VQENGEEGEA
LTEEVSRAIQ SLWADPGVKK AFEMRSEYQL PDSAKYFLDN CQRISEPGYR PNDQDILYSR
VATTGVVEVK FKIKELDFRV FDVGGQRSER RKWIHCFDNV ESIIFITAIS EYDQVLFEDE
TTNRMIESMQ LFNSICNSTW FLSTAMILFM NKKDLFMEKI QRVNITTAFP DYEGGQNYEE
AVAFIKQKFA ELNLNPDKKT IYMHETCATD TNQVQLVISS VIDTIIQKNL QKAGMM
