NTR1_CAEEL
ID NTR1_CAEEL Reviewed; 379 AA.
AC O02300;
DT 02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Nematocin receptor 1 {ECO:0000303|PubMed:23112336};
GN Name=ntr-1 {ECO:0000303|PubMed:23112336};
GN ORFNames=T07D10.2 {ECO:0000312|WormBase:T07D10.2};
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|EMBL:AFJ42569.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=23112336; DOI=10.1126/science.1226860;
RA Beets I., Janssen T., Meelkop E., Temmerman L., Suetens N., Rademakers S.,
RA Jansen G., Schoofs L.;
RT "Vasopressin/oxytocin-related signaling regulates gustatory associative
RT learning in C. elegans.";
RL Science 338:543-545(2012).
RN [2] {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 [3] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=23112335; DOI=10.1126/science.1226201;
RA Garrison J.L., Macosko E.Z., Bernstein S., Pokala N., Albrecht D.R.,
RA Bargmann C.I.;
RT "Oxytocin/vasopressin-related peptides have an ancient role in reproductive
RT behavior.";
RL Science 338:540-543(2012).
CC -!- FUNCTION: Receptor for nematocin (PubMed:23112336, PubMed:23112335).
CC The activity of this receptor is mediated by G proteins which activate
CC a phosphatidylinositol-calcium second messenger system
CC (PubMed:23112336, PubMed:23112335). The activity of this receptor may
CC be modulated by ntr-2, leading to reduced intracellular cAMP production
CC (PubMed:23112335). Plays a role in gustatory associative learning
CC (PubMed:23112336). Also plays a role in male mating behavior
CC (PubMed:23112335). {ECO:0000269|PubMed:23112336,
CC ECO:0000269|PubMed:9851916}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:23112335,
CC ECO:0000269|PubMed:23112336}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Detected in the left ASE gustatory neuron, the
CC chemosensory neuron pairs ASH and ADF, and the PQR tail neuron
CC (PubMed:23112336). In males, detected in hook and tail sensory neurons
CC involved in vulval sensing and hermaphrodite contact, and in spicule
CC protractor muscles (PubMed:23112335). {ECO:0000269|PubMed:23112335,
CC ECO:0000269|PubMed:23112336}.
CC -!- DISRUPTION PHENOTYPE: Viable and fertile (PubMed:23112336). Gustatory
CC associative learning in response to salt cues is disrupted
CC (PubMed:23112336). Males have reduced reproductive success, due to a
CC range of aberrant mating behaviors (PubMed:23112335). Double knockouts
CC with ntr-2 partially rescue the reproductive phenotypes
CC (PubMed:23112335). {ECO:0000269|PubMed:23112336}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC Vasopressin/oxytocin receptor subfamily. {ECO:0000305}.
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DR EMBL; JQ277731; AFJ42569.1; -; mRNA.
DR EMBL; BX284601; CAB04712.1; -; Genomic_DNA.
DR PIR; T24654; T24654.
DR RefSeq; NP_493193.1; NM_060792.1.
DR AlphaFoldDB; O02300; -.
DR SMR; O02300; -.
DR DIP; DIP-26414N; -.
DR IntAct; O02300; 1.
DR STRING; 6239.T07D10.2; -.
DR PaxDb; O02300; -.
DR PRIDE; O02300; -.
DR EnsemblMetazoa; T07D10.2a.1; T07D10.2a.1; WBGene00011582.
DR GeneID; 188227; -.
DR UCSC; T07D10.2; c. elegans.
DR CTD; 188227; -.
DR WormBase; T07D10.2; CE13377; WBGene00011582; ntr-1.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT00970000195859; -.
DR HOGENOM; CLU_009579_15_0_1; -.
DR InParanoid; O02300; -.
DR OMA; TLYMSFK; -.
DR OrthoDB; 890925at2759; -.
DR PhylomeDB; O02300; -.
DR PRO; PR:O02300; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00011582; Expressed in larva.
DR ExpressionAtlas; O02300; baseline and differential.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IEA:UniProtKB-KW.
DR GO; GO:0007610; P:behavior; 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 PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE 2: Evidence at transcript level;
KW Behavior; Cell membrane; Disulfide bond; G-protein coupled receptor;
KW Glycoprotein; Membrane; Receptor; Reference proteome; Transducer;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..379
FT /note="Nematocin receptor 1"
FT /id="PRO_0000438124"
FT TOPO_DOM 19..48
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 49..69
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 70..95
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 96..116
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 117..124
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 125..145
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 146..168
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 169..189
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 190..207
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 208..228
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 229..289
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 290..310
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 311..320
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 321..343
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 344..379
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT CARBOHYD 32
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 199
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 319
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 123..196
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 379 AA; 43077 MW; E420F93F8BEB439B CRC64;
MGAFFPVILL TPTPISSAHN LYLFQMLELQ ENITDSQPMD PPSLEIMMLH HLMIILVTLF
GNTLLIYVIY KNNAVLRRKR VTPVQMLMLH MCAADILFAL ISVGPTMAIT ATVPFFYGPN
LLCKLTKFLQ VIPMYASSFL LVAISADRYQ AICRPLASMK SSIYNRPALY SGIAWTAAIL
FSTPQLYLFE KRNGDCSENY TTALQYQLYV CLFNSVVWLL PSAIAGWLYL CVCKAVWKST
SFSSSLRNNM KKMEHMKLTE KNGGMQAHHK GATMQCVELD RRRVQTVKLT LTIVAANFVL
WAPFCITSVI DAVWPTAINS TFATYIMFFG NLNSCMNPWL WFHFNRKQLK RACPCRKSSE
PLIQSLVYVH VMTSEQSDF
