NPR15_CAEEL
ID NPR15_CAEEL Reviewed; 345 AA.
AC Q09638; O01344;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 22-SEP-2009, sequence version 3.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Neuropeptide receptor 15;
GN Name=npr-15; ORFNames=T27D1.3;
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 [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).
CC -!- FUNCTION: Probable receptor for neuropeptide ligand nlp-8 that plays a
CC role in octopamine signaling and specifically, the octopamine
CC inhibition of aversion responses in olfactory sensory neurons.
CC {ECO:0000269|PubMed:22124329}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in pharyngeal muscle and in AWC, ASG,
CC ASE, ASI and ASJ sensory neurons. {ECO:0000269|PubMed:22124329}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown in AWC sensory neurons
CC results in reduced octopamine inhibition of the aversive response to
CC 100% 1-octanol. {ECO:0000269|PubMed:22124329}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; Z48245; CAA88290.2; -; Genomic_DNA.
DR PIR; T25354; T25354.
DR RefSeq; NP_497744.2; NM_065343.3.
DR AlphaFoldDB; Q09638; -.
DR SMR; Q09638; -.
DR BioGRID; 40710; 2.
DR STRING; 6239.T27D1.3; -.
DR PaxDb; Q09638; -.
DR EnsemblMetazoa; T27D1.3.1; T27D1.3.1; WBGene00012084.
DR GeneID; 175470; -.
DR KEGG; cel:CELE_T27D1.3; -.
DR UCSC; T27D1.3; c. elegans.
DR CTD; 175470; -.
DR WormBase; T27D1.3; CE43181; WBGene00012084; npr-15.
DR eggNOG; ENOG502S3T9; Eukaryota.
DR GeneTree; ENSGT01030000234534; -.
DR HOGENOM; CLU_009579_6_4_1; -.
DR InParanoid; Q09638; -.
DR OMA; RYLECVF; -.
DR OrthoDB; 1229764at2759; -.
DR PhylomeDB; Q09638; -.
DR Reactome; R-CEL-373076; Class A/1 (Rhodopsin-like receptors).
DR Reactome; R-CEL-375276; Peptide ligand-binding receptors.
DR Reactome; R-CEL-416476; G alpha (q) signalling events.
DR Reactome; R-CEL-418555; G alpha (s) signalling events.
DR Reactome; R-CEL-418594; G alpha (i) signalling events.
DR Reactome; R-CEL-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR Reactome; R-CEL-8856828; Clathrin-mediated endocytosis.
DR PRO; PR:Q09638; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00012084; Expressed in larva and 2 other tissues.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IEA:UniProtKB-KW.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR Pfam; PF00001; 7tm_1; 1.
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; Membrane;
KW Receptor; Reference proteome; Transducer; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..345
FT /note="Neuropeptide receptor 15"
FT /id="PRO_0000070229"
FT TOPO_DOM 1..11
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 12..32
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 33..40
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 41..61
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 62..90
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 91..111
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 112..125
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 126..146
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 147..187
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 188..208
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 209..246
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 247..267
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 268..281
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 282..304
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 305..345
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DISULFID 82..171
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 345 AA; 39233 MW; A7CB0F6D3F5FAC15 CRC64;
MSVAVGIPYV CFFIILSVVG IIGNVIVIYA IAGDRNMRKS VMNILLLNLA VADLANLIFT
IPEWIPPVFF GSTDWLFPSF LCPVCRYLEC VFLFASISTQ MIVCIERYIA IVLPMQARQL
CSRRNVLITV LVDWIFVACF ASPYAVWHSV KTKDRNTNSL RFKLFQLSAT CSNTVGKSTW
WQGYKLTEFL AFYFVPCFII TVVYTKVAKC LWCKDPTLQC ETRSCLDNKS SSRSSDALRT
RRNVVKMLIA CVAVYFVCYS PIQVIFLSKA VLNVTIHPPY DFILLMNALA MTCSASNPLL
YTLFSQKFRR RLRDVLYCPS DVENETKTYY SINNTSIVGP RASFN
