NPR9_CAEEL
ID NPR9_CAEEL Reviewed; 431 AA.
AC Q23497;
DT 07-SEP-2016, integrated into UniProtKB/Swiss-Prot.
DT 02-DEC-2020, sequence version 2.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Galanin-like G-protein coupled receptor npr-9 {ECO:0000305|PubMed:27223098};
DE AltName: Full=Probable neuropeptide receptor 9 {ECO:0000305};
GN Name=npr-9 {ECO:0000312|WormBase:ZK455.3};
GN ORFNames=ZK455.3 {ECO:0000312|WormBase:ZK455.3};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
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 [2] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP AND DISRUPTION PHENOTYPE.
RX PubMed=18216257; DOI=10.1073/pnas.0709492105;
RA Bendena W.G., Boudreau J.R., Papanicolaou T., Maltby M., Tobe S.S.,
RA Chin-Sang I.D.;
RT "A Caenorhabditis elegans allatostatin/galanin-like receptor NPR-9 inhibits
RT local search behavior in response to feeding cues.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:1339-1342(2008).
RN [3] {ECO:0000305}
RP FUNCTION.
RX PubMed=27223098; DOI=10.1371/journal.pgen.1006050;
RA Campbell J.C., Polan-Couillard L.F., Chin-Sang I.D., Bendena W.G.;
RT "NPR-9, a galanin-like G-protein coupled receptor, and GLR-1 regulate
RT interneuronal circuitry underlying multisensory integration of
RT environmental cues in Caenorhabditis elegans.";
RL PLoS Genet. 12:E1006050-E1006050(2016).
RN [4] {ECO:0000305}
RP FUNCTION.
RX PubMed=27133473; DOI=10.1038/cmi.2016.8;
RA Yu Y., Zhi L., Wu Q., Jing L., Wang D.;
RT "NPR-9 regulates the innate immune response in Caenorhabditis elegans by
RT antagonizing the activity of AIB interneurons.";
RL Cell. Mol. Immunol. 15:27-37(2018).
CC -!- FUNCTION: Neuropeptide that controls movement such as roaming, foraging
CC and backwards locomotion or 'reversals' in response to environmental
CC cues such as food availability or volatile odorants such as octanol
CC (PubMed:18216257, PubMed:27223098). Antagonizes AIB interneuron
CC activity to control bacterial colonization and may negatively regulate
CC the expression of immunity-related genes such as pqm-1 and dod-22 in
CC response to infection by P.aeruginosa (PubMed:27133473).
CC {ECO:0000269|PubMed:18216257, ECO:0000269|PubMed:27133473,
CC ECO:0000269|PubMed:27223098}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:18216257};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Exclusively expressed in the AIB interneuron.
CC {ECO:0000269|PubMed:18216257}.
CC -!- DEVELOPMENTAL STAGE: Not expressed in embryos, but is expressed in the
CC AIB interneuron region of the head during all larval stages of
CC development. {ECO:0000269|PubMed:18216257}.
CC -!- DISRUPTION PHENOTYPE: Decreased roaming in response to food during the
CC L3 and L4 stages of larval development and adult stages, but not at the
CC L1 stage of larval development. Increased lipid accumulation.
CC {ECO:0000269|PubMed:18216257}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; BX284606; CAA91489.1; -; Genomic_DNA.
DR PIR; T27866; T27866.
DR RefSeq; NP_509896.1; NM_077495.1.
DR AlphaFoldDB; Q23497; -.
DR SMR; Q23497; -.
DR STRING; 6239.ZK455.3; -.
DR PaxDb; Q23497; -.
DR EnsemblMetazoa; ZK455.3.1; ZK455.3.1; WBGene00013974.
DR UCSC; ZK455.3; c. elegans.
DR WormBase; ZK455.3; CE53640; WBGene00013974; npr-9.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT00940000164736; -.
DR HOGENOM; CLU_009579_6_4_1; -.
DR InParanoid; Q23497; -.
DR OrthoDB; 1294084at2759; -.
DR PhylomeDB; Q23497; -.
DR Reactome; R-CEL-416476; G alpha (q) signalling events.
DR PRO; PR:Q23497; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00013974; Expressed in larva.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IBA:GO_Central.
DR GO; GO:0008188; F:neuropeptide receptor activity; IBA:GO_Central.
DR GO; GO:0060756; P:foraging behavior; IMP:WormBase.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR InterPro; IPR000405; Galanin_rcpt.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00663; GALANINR.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR SMART; SM01381; 7TM_GPCR_Srsx; 1.
DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Disulfide bond; G-protein coupled receptor; Glycoprotein;
KW Membrane; Receptor; Reference proteome; Transducer; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..431
FT /note="Galanin-like G-protein coupled receptor npr-9"
FT /evidence="ECO:0000305"
FT /id="PRO_0000437202"
FT TOPO_DOM 1..34
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 35..55
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 56..66
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 67..87
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 88..101
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 102..124
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 125..143
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 144..164
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 165..203
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 204..224
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 225..268
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 269..289
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 290..298
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 299..319
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 320..431
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REGION 235..257
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 393..431
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 5
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 101..182
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 431 AA; 48523 MW; CEEA9EEA1BF94C5E CRC64;
MEFENLTKEE MEQLQKIYDD TISFERKIGI IIPTIFAVII LVGLVGNALV VIVAFGRQMR
NSTNTLIIGL AISDLMFLLL CVPFTAVDYA APTWIFPEWT CSMINFFQHT SAYCSVWTLT
LMALDRYLAV VYPVESMTLR TPRNTVIALC FIYIIIIASQ IPVGRMHGIY VYDFIMEKRS
TCAILTIATA EATPTMARTY FMTFNVFGYV LPLGISVVLY GLMLRKLWDM PRPGNSQSVG
GRNLTNRDSG SSIRRRPEAT AAKRKVTRLV LCVLITWALC WLPLNVCFFM SGLAYPEPLV
ISHGVIMVIV QIASQVLAYT NSCLNPILYA LMSQSFREGF IRVMKMLINK LSRGRFCTNY
RRSALRTELT HYNQTPAHPA NTVVQVSNGE RSSLLKDNSS SATSVQPLRT SIQAKKTKNI
GRSKSTRSYN L
