NPR18_CAEEL
ID NPR18_CAEEL Reviewed; 498 AA.
AC Q09502;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Neuropeptide receptor 18 {ECO:0000305};
GN Name=npr-18 {ECO:0000312|WormBase:C43C3.2a};
GN ORFNames=C43C3.2 {ECO:0000312|WormBase:C43C3.2a};
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 [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 [2]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=22124329; DOI=10.1038/emboj.2011.422;
RA Mills H., Wragg R., Hapiak V., Castelletto M., Zahratka J., Harris G.,
RA Summers P., Korchnak A., Law W., Bamber B., Komuniecki R.;
RT "Monoamines and neuropeptides interact to inhibit aversive behaviour in
RT Caenorhabditis elegans.";
RL EMBO J. 31:667-678(2012).
RN [3]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
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: Probable receptor for neuropeptide ligand nlp-9 that plays a
CC role in octopamine signaling and specifically, the octapamine
CC inhibition of aversion responses in olfactory sensory neurons
CC (PubMed:22124329, PubMed:25009271). In AWB olfactory sensory neurons,
CC required for the detection of preferred food sources (PubMed:25009271).
CC {ECO:0000269|PubMed:22124329, ECO:0000269|PubMed:25009271}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in sensory neurons including ASER.
CC {ECO:0000269|PubMed:22124329}.
CC -!- DISRUPTION PHENOTYPE: Defective octopamine signaling characterized by
CC reduced octopamine inhibition of the aversive response initiated by ASH
CC sensory neurons when exposed to 100% 1-octanol (PubMed:22124329). RNAi-
CC mediated knockdown results in an inability to distinguish between
CC different food odors (PubMed:25009271). {ECO:0000269|PubMed:22124329,
CC ECO:0000269|PubMed:25009271}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; Z47067; CAA87329.1; -; Genomic_DNA.
DR PIR; T19901; T19901.
DR RefSeq; NP_001257089.1; NM_001270160.1.
DR AlphaFoldDB; Q09502; -.
DR SMR; Q09502; -.
DR STRING; 6239.C43C3.2f; -.
DR PaxDb; Q09502; -.
DR UCSC; C43C3.2; c. elegans.
DR WormBase; C43C3.2a; CE01524; WBGene00008065; npr-18.
DR eggNOG; KOG3656; Eukaryota.
DR InParanoid; Q09502; -.
DR OrthoDB; 780509at2759; -.
DR PhylomeDB; Q09502; -.
DR Reactome; R-CEL-202040; G-protein activation.
DR Reactome; R-CEL-391908; Prostanoid ligand receptors.
DR Reactome; R-CEL-416476; G alpha (q) signalling events.
DR Reactome; R-CEL-418594; G alpha (i) signalling events.
DR Reactome; R-CEL-5620922; BBSome-mediated cargo-targeting to cilium.
DR PRO; PR:Q09502; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00008065; Expressed in pharyngeal muscle cell (C elegans) and 2 other tissues.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IBA:GO_Central.
DR GO; GO:0042277; F:peptide binding; IBA:GO_Central.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00237; GPCRRHODOPSN.
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; G-protein coupled receptor; Glycoprotein; Membrane;
KW Receptor; Reference proteome; Transducer; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..498
FT /note="Neuropeptide receptor 18"
FT /evidence="ECO:0000305"
FT /id="PRO_0000070228"
FT TOPO_DOM 1..52
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 53..73
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 74..93
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 94..114
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 115..130
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 131..151
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 152..170
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 171..191
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 192..258
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 259..279
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 280..313
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 314..334
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 335..356
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 357..377
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 378..498
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 48
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 498 AA; 57463 MW; 7F13584348FB54A6 CRC64;
MQLFLEQSFK KLHIEQSTPA RENLPNREIY QIFQFTLVYA LPLSNHDNSS LMLIAGFYAL
LFMFGTCGNA AILAVVHHVK GQDPRSRHNT TLTYICILSI VDFLSMLPIP MTIIDQILGF
WMFDTFACKL FRLLEHIGKI FSTFILVAFS IDRYCAVCHP LQVRVRNQRT VFVFLGIMFF
VTCVMLSPIL LYAHSKVHFI ITETYRHLIM QKCLRFFEGS VTFFGLQELV MHEKVDLDQE
VITRMHLYKC VDDLGRELFV VFTLYSFVLA YLMPLLFMIY FYYEMLIRLF KQANVIKQTL
VGRRSGGEEK KLTIPVGHIA IYTLAICSFH FICWTPYWIS ILYSLYEELY QDTKSTASPP
TYAFIYFMYG VHALPYINSA SNFILYGLLN RQLHNAPERK YTRNGVGGRQ MSHALTTNTR
PEYSELIAIP SSSCRPDSRV SAMIHNNNNN TESLPLAQNI SNMTNKDSAT IVPMPMSANV
DGNEIYNWIT PDTESVIL