NPR1_CAEEL
ID NPR1_CAEEL Reviewed; 457 AA.
AC Q18534;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Neuropeptide receptor npr-1 {ECO:0000312|WormBase:C39E6.6};
DE AltName: Full=Neuropeptide Y receptor homolog npr-1 {ECO:0000303|PubMed:9741632};
GN Name=npr-1 {ECO:0000312|WormBase:C39E6.6};
GN Synonyms=AF9-R1 {ECO:0000303|PubMed:12821653};
GN ORFNames=C39E6.6 {ECO:0000312|WormBase:C39E6.6};
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, TISSUE SPECIFICITY, AND MUTAGENESIS OF 61-GLN--VAL-457; THR-83;
RP GLY-118; THR-144 AND VAL-215.
RC STRAIN=AB1 {ECO:0000269|PubMed:9741632}, AB3 {ECO:0000269|PubMed:9741632},
RC Bristol N2 {ECO:0000312|Proteomes:UP000001940},
RC CB4852 {ECO:0000269|PubMed:9741632}, CB4853 {ECO:0000269|PubMed:9741632},
RC CB4854 {ECO:0000269|PubMed:9741632}, CB4855 {ECO:0000269|PubMed:9741632},
RC CB4856 {ECO:0000269|PubMed:9741632}, CB4857 {ECO:0000269|PubMed:9741632},
RC CB4858 {ECO:0000269|PubMed:9741632}, CB4932 {ECO:0000269|PubMed:9741632},
RC KR314 {ECO:0000269|PubMed:9741632}, RC301 {ECO:0000269|PubMed:9741632}, and
RC TR403 {ECO:0000269|PubMed:9741632};
RX PubMed=9741632; DOI=10.1016/s0092-8674(00)81609-8;
RA de Bono M., Bargmann C.I.;
RT "Natural variation in a neuropeptide Y receptor homolog modifies social
RT behavior and food response in C. elegans.";
RL Cell 94:679-689(1998).
RN [3] {ECO:0000305}
RP FUNCTION, AND MUTAGENESIS OF VAL-215.
RX PubMed=12821653; DOI=10.1074/jbc.m304861200;
RA Kubiak T.M., Larsen M.J., Nulf S.C., Zantello M.R., Burton K.J.,
RA Bowman J.W., Modric T., Lowery D.E.;
RT "Differential activation of 'social' and 'solitary' variants of the
RT Caenorhabditis elegans G protein-coupled receptor NPR-1 by its cognate
RT ligand AF9.";
RL J. Biol. Chem. 278:33724-33729(2003).
RN [4] {ECO:0000305}
RP FUNCTION, AND MUTAGENESIS OF VAL-215.
RX PubMed=14555955; DOI=10.1038/nn1140;
RA Rogers C., Reale V., Kim K., Chatwin H., Li C., Evans P., de Bono M.;
RT "Inhibition of Caenorhabditis elegans social feeding by FMRFamide-related
RT peptide activation of NPR-1.";
RL Nat. Neurosci. 6:1178-1185(2003).
RN [5] {ECO:0000305}
RP FUNCTION.
RX PubMed=23764289; DOI=10.1016/j.neuron.2013.04.002;
RA Choi S., Chatzigeorgiou M., Taylor K.P., Schafer W.R., Kaplan J.M.;
RT "Analysis of NPR-1 reveals a circuit mechanism for behavioral quiescence in
RT C. elegans.";
RL Neuron 78:869-880(2013).
RN [6] {ECO:0000305}
RP REVIEW OF FUNCTION.
RX PubMed=25804345; DOI=10.1016/j.tig.2015.02.009;
RA Sterken M.G., Snoek L.B., Kammenga J.E., Andersen E.C.;
RT "The laboratory domestication of Caenorhabditis elegans.";
RL Trends Genet. 31:224-231(2015).
RN [7] {ECO:0000305}
RP FUNCTION, AND MUTAGENESIS OF 61-GLN--VAL-457.
RX PubMed=27585848; DOI=10.1534/genetics.116.192898;
RA Chen D., Taylor K.P., Hall Q., Kaplan J.M.;
RT "The Neuropeptides FLP-2 and PDF-1 Act in Concert To Arouse Caenorhabditis
RT elegans Locomotion.";
RL Genetics 204:1151-1159(2016).
CC -!- FUNCTION: G-protein coupled receptor for FARP(FMRFamide related
CC peptide) neuropeptides (PubMed:12821653, PubMed:14555955). Activated by
CC FARP neuropeptides flp-18 and flp-21 (PubMed:12821653,
CC PubMed:14555955). Plays a role in modulating social and feeding
CC behavior (PubMed:9741632). Required to modulate locomotion quiescence
CC during the sleep-like state called lethargus, which occurs during
CC molting between larval and adult stages, in part by regulating touch
CC sensitivity (PubMed:23764289, PubMed:27585848).
CC {ECO:0000269|PubMed:12821653, ECO:0000269|PubMed:14555955,
CC ECO:0000269|PubMed:23764289, ECO:0000269|PubMed:27585848,
CC ECO:0000269|PubMed:9741632}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in neurons, including neurons in the
CC head, the ventral nerve cord, and the preanal ganglion.
CC {ECO:0000269|PubMed:9741632}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000305}.
CC -!- CAUTION: It has been reported that many phenotypes associated with the
CC Bristol N2 reference allele of npr-1 may reflect a neomorphic gain-of-
CC function sensitivity of the receptor to flp-18 in addition to
CC sensitivity to flp-21. {ECO:0000303|PubMed:25804345}.
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DR EMBL; BX284606; CCD67081.1; -; Genomic_DNA.
DR PIR; T29741; T29741.
DR RefSeq; NP_508816.1; NM_076415.4.
DR AlphaFoldDB; Q18534; -.
DR SMR; Q18534; -.
DR STRING; 6239.C39E6.6; -.
DR PaxDb; Q18534; -.
DR EnsemblMetazoa; C39E6.6.1; C39E6.6.1; WBGene00003807.
DR GeneID; 180752; -.
DR KEGG; cel:CELE_C39E6.6; -.
DR UCSC; C39E6.6; c. elegans.
DR CTD; 180752; -.
DR WormBase; C39E6.6; CE06941; WBGene00003807; npr-1.
DR eggNOG; KOG3656; Eukaryota.
DR HOGENOM; CLU_009579_6_1_1; -.
DR InParanoid; Q18534; -.
DR OMA; LPYAFNM; -.
DR OrthoDB; 609835at2759; -.
DR PhylomeDB; Q18534; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00003807; Expressed in larva and 1 other tissue.
DR GO; GO:0030424; C:axon; IDA:WormBase.
DR GO; GO:0030425; C:dendrite; IDA:WormBase.
DR GO; GO:0005887; C:integral component of plasma membrane; IC:WormBase.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0043025; C:neuronal cell body; IDA:WormBase.
DR GO; GO:0005886; C:plasma membrane; IDA:WormBase.
DR GO; GO:0042923; F:neuropeptide binding; IBA:GO_Central.
DR GO; GO:0008188; F:neuropeptide receptor activity; IDA:WormBase.
DR GO; GO:0004983; F:neuropeptide Y receptor activity; IEA:InterPro.
DR GO; GO:0048149; P:behavioral response to ethanol; IMP:WormBase.
DR GO; GO:0007631; P:feeding behavior; IMP:UniProtKB.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:1904068; P:G protein-coupled receptor signaling pathway involved in social behavior; IMP:WormBase.
DR GO; GO:0050709; P:negative regulation of protein secretion; IMP:UniProtKB.
DR GO; GO:0007218; P:neuropeptide signaling pathway; IDA:WormBase.
DR GO; GO:0006937; P:regulation of muscle contraction; IGI:UniProtKB.
DR GO; GO:0070482; P:response to oxygen levels; IMP:WormBase.
DR GO; GO:0030431; P:sleep; IMP:UniProtKB.
DR GO; GO:0035176; P:social behavior; IMP:UniProtKB.
DR GO; GO:0043052; P:thermotaxis; IMP:CACAO.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR InterPro; IPR000611; NPY_rcpt.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR PRINTS; PR01012; NRPEPTIDEYR.
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 1: Evidence at protein level;
KW Disulfide bond; G-protein coupled receptor; Membrane; Receptor;
KW Reference proteome; Transducer; Transmembrane; Transmembrane helix.
FT CHAIN 1..457
FT /note="Neuropeptide receptor npr-1"
FT /id="PRO_0000454188"
FT TOPO_DOM 1..22
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 23..43
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 44..62
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 63..83
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 84..100
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 101..121
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 122..140
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 141..161
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 162..193
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 194..214
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 215..279
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 280..300
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 301..324
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 325..345
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 346..457
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DISULFID 99..178
FT /evidence="ECO:0000305"
FT MUTAGEN 61..457
FT /note="Missing: In ky13; clumping behavior. Abnormally
FT active during the sleep-like state called lethargus, which
FT occurs during molting between larval and adult stages;
FT normal quiescence restored in FMRFamide peptide receptor
FT frpr-18 mutant background."
FT /evidence="ECO:0000269|PubMed:27585848,
FT ECO:0000269|PubMed:9741632"
FT MUTAGEN 83
FT /note="T->I: In ad609; clumping behavior; when associated
FT with A-144."
FT /evidence="ECO:0000269|PubMed:9741632"
FT MUTAGEN 118
FT /note="G->D: In n1353; clumping behavior."
FT /evidence="ECO:0000269|PubMed:9741632"
FT MUTAGEN 144
FT /note="T->A: In ad609; clumping behavior; when associated
FT with I-83."
FT /evidence="ECO:0000269|PubMed:9741632"
FT MUTAGEN 215
FT /note="V->F: Clumping behavior; behavior more similar to
FT many wild-isolated strains of C. elegans than the
FT laboratory reference Bristol N2 strain. Binds GLGPRPLRF-
FT amide flp-21 peptide with lower affinity, in vitro. Not
FT activated by EMPGVLRF-amide flp-18 peptide, in vitro."
FT /evidence="ECO:0000269|PubMed:12821653,
FT ECO:0000269|PubMed:14555955, ECO:0000269|PubMed:9741632"
SQ SEQUENCE 457 AA; 52464 MW; 6EB950A91BB10BE8 CRC64;
MEVENFTDCQ VYWKVYPDPS QSIYAIVPFL TVYLFLFFLG LFGNVTLIYV TCSHKALLSV
QNIFILNLAA SDCMMCILSL PITPITNVYK NWYFGNLLCH LIPCIQGISI FVCTFSLGAI
ALDRYILVVR PHSTPLSQRG AFLTTVLLWI LSFVVTLPYA FNMQMIEYTE ERICGYFCTE
KWESAKSRRA YTMIVMLAQF VVPFAVMAFC YANIVSVLSK RAQTKIRKMV ERTSALESSC
AFPSHGLEQY ENELNEFLDK QEKEKQRVVL QNRRTTSILV TMVVWFGITW LPHNVISLII
EYDDTQSFFR LYGRDDYDIS YLLNLFTHSI AMSNNVLNPV LYAWLNPSFR QLVIKTYFGD
RRKSDRIINQ TSVYKTKIVH DTKHLNGRAK IGGGGSHEAL KERELNSCSE NLSYHVNGHT
RTPTPEVQLN EVSSPEISKL VAEPEELIEF SVNDTLV
