PDFR1_CAEEL
ID PDFR1_CAEEL Reviewed; 546 AA.
AC Q09460; B2BBX5; G5EDW6; G5EFM1;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2003, sequence version 2.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Calcitonin receptor-like protein 1;
DE AltName: Full=Pigment dispersing factor neuropeptide receptor homolog 1;
GN Name=pdfr-1; Synonyms=seb-1; ORFNames=C13B9.4;
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 [MRNA] (ISOFORMS A; B AND C), FUNCTION, AND TISSUE
RP SPECIFICITY.
RX PubMed=18390545; DOI=10.1074/jbc.m709060200;
RA Janssen T., Husson S.J., Lindemans M., Mertens I., Rademakers S.,
RA Donck K.V., Geysen J., Jansen G., Schoofs L.;
RT "Functional characterization of three G protein-coupled receptors for
RT pigment dispersing factors in Caenorhabditis elegans.";
RL J. Biol. Chem. 283:15241-15249(2008).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A; B AND C).
RA Mastwal S.S., Yu D., Hedgecock E.M.;
RT "Molecular and evolutionary characterization of family B G-protein coupled
RT receptors in Caenorhabditis elegans.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE SPLICING.
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 [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=14551910; DOI=10.1371/journal.pbio.0000012;
RA Simmer F., Moorman C., van der Linden A.M., Kuijk E.,
RA van den Berghe P.V.E., Kamath R.S., Fraser A.G., Ahringer J.,
RA Plasterk R.H.A.;
RT "Genome-wide RNAi of C. elegans using the hypersensitive rrf-3 strain
RT reveals novel gene functions.";
RL PLoS Biol. 1:E12-E12(2003).
RN [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=22579613; DOI=10.1016/j.mce.2012.05.001;
RA Meelkop E., Temmerman L., Janssen T., Suetens N., Beets I., Van Rompay L.,
RA Shanmugam N., Husson S.J., Schoofs L.;
RT "PDF receptor signaling in Caenorhabditis elegans modulates locomotion and
RT egg-laying.";
RL Mol. Cell. Endocrinol. 361:232-240(2012).
RN [6]
RP FUNCTION, DEVELOPMENTAL STAGE, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE,
RP AND MUTAGENESIS OF GLY-298.
RX PubMed=23143519; DOI=10.1038/nn.3253;
RA Barrios A., Ghosh R., Fang C., Emmons S.W., Barr M.M.;
RT "PDF-1 neuropeptide signaling modulates a neural circuit for mate-searching
RT behavior in C. elegans.";
RL Nat. Neurosci. 15:1675-1682(2012).
RN [7]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=23972393; DOI=10.1016/j.cell.2013.08.001;
RA Flavell S.W., Pokala N., Macosko E.Z., Albrecht D.R., Larsch J.,
RA Bargmann C.I.;
RT "Serotonin and the neuropeptide PDF initiate and extend opposing behavioral
RT states in C. elegans.";
RL Cell 154:1023-1035(2013).
RN [8] {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 [9] {ECO:0000305}
RP FUNCTION.
RX PubMed=26113231; DOI=10.1111/gbb.12231;
RA Herrero A., Romanowski A., Meelkop E., Caldart C.S., Schoofs L.,
RA Golombek D.A.;
RT "Pigment-dispersing factor signaling in the circadian system of
RT Caenorhabditis elegans.";
RL Genes Brain Behav. 14:493-501(2015).
RN [10] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=30024377; DOI=10.7554/elife.36547;
RA Hilbert Z.A., Kim D.H.;
RT "PDF-1 neuropeptide signaling regulates sexually dimorphic gene expression
RT in shared sensory neurons of C. elegans.";
RL Elife 7:0-0(2018).
CC -!- FUNCTION: G-protein coupled receptor for PDF neuropeptides
CC (PubMed:18390545). Plays a role in responses to environmental signals,
CC including chemicals and touch, and in modulating locomotory behaviors
CC (PubMed:30024377, PubMed:18390545, PubMed:14551910, PubMed:22579613,
CC PubMed:23143519, PubMed:23972393, PubMed:26113231). Capable of
CC transducing signals via an adenylate cyclase acy-1 cAMP-dependent
CC pathway (PubMed:23972393, PubMed:30024377). Required to regulate the
CC sex-specific expression of TGFbeta-like daf-7 in the ASJ chemosensory
CC neurons, perhaps acting via acy-1 (PubMed:30024377). Involved in
CC modulating mate searching behavior independent of nutritional status
CC (PubMed:18390545, PubMed:22579613, PubMed:23143519, PubMed:14551910).
CC In the presence of food, plays a role in initiating and extending
CC exploratory roaming behavior, perhaps acting in AIY, RIM, RIA, and
CC other neurons, in opposition to 5-hydroxytryptamine (serotonin)
CC signaling (PubMed:23972393). Involved in mediating arousal from the
CC sleep-like state called lethargus, which occurs during molting between
CC larval and adult stages, in part by regulating touch sensitivity
CC (PubMed:18390545, PubMed:23764289). May play a role in circadian
CC rhythms of locomotor activity (PubMed:26113231).
CC {ECO:0000269|PubMed:14551910, ECO:0000269|PubMed:18390545,
CC ECO:0000269|PubMed:22579613, ECO:0000269|PubMed:23143519,
CC ECO:0000269|PubMed:23764289, ECO:0000269|PubMed:23972393,
CC ECO:0000269|PubMed:26113231, ECO:0000269|PubMed:30024377}.
CC -!- FUNCTION: [Isoform a]: G-protein coupled receptor which is activated by
CC neuropeptides PDF-1 and PDF-2 (PubMed:18390545). Probably acts through
CC the G-alpha(s) type of G proteins to elevate cAMP levels
CC (PubMed:18390545). {ECO:0000269|PubMed:18390545}.
CC -!- FUNCTION: [Isoform b]: G-protein coupled receptor which is activated by
CC neuropeptides PDF-1 and PDF-2 (PubMed:18390545). Probably acts through
CC the G-alpha(s) type of G proteins to elevate cAMP levels
CC (PubMed:18390545). {ECO:0000269|PubMed:18390545}.
CC -!- FUNCTION: [Isoform c]: G-protein coupled receptor which is activated by
CC neuropeptides PDF-1 and PDF-2; however, activation is lower compared to
CC isoforms a and b (PubMed:18390545). Probably inhibits cAMP levels
CC through the G-alpha(i/o) type of G proteins (PubMed:18390545).
CC {ECO:0000269|PubMed:18390545}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=a; Synonyms=Seb-1a;
CC IsoId=Q09460-1; Sequence=Displayed;
CC Name=c; Synonyms=Seb-1c;
CC IsoId=Q09460-2; Sequence=VSP_046482;
CC Name=b; Synonyms=Seb-1b;
CC IsoId=Q09460-3; Sequence=VSP_046483, VSP_046484;
CC -!- TISSUE SPECIFICITY: Expression was observed in the mechanosensory
CC neuron pairs PLM, ALM, FLP, OLQD, and OLQV, the chemosensory neurons
CC PHA, PHB, RMEV, the ring motor neurons RMED, and the pharyngeal
CC interneuron pair I1 (PubMed:18390545). Expression in sensory neurons
CC PHA, PQR and URY are responsible for mate searching behavior
CC (PubMed:23143519). Expressed in AIY, RIM, RIA, and other neurons.
CC {ECO:0000269|PubMed:18390545, ECO:0000269|PubMed:23143519,
CC ECO:0000269|PubMed:23972393}.
CC -!- DEVELOPMENTAL STAGE: Expressed in both hermaphrodites and males at the
CC L4 stage in the head, body wall muscle cells and tail.
CC {ECO:0000269|PubMed:23143519}.
CC -!- DISRUPTION PHENOTYPE: Disrupted locomotion (unc); decreased speed,
CC increased number of reversals and loss of mate searching behavior
CC (PubMed:14551910, PubMed:22579613, PubMed:23143519). RNAi-mediated
CC knockdown causes reduced expression of TGFbeta-like daf-7 in ASJ
CC chemosensory neurons (PubMed:30024377). {ECO:0000269|PubMed:14551910,
CC ECO:0000269|PubMed:22579613, ECO:0000269|PubMed:23143519,
CC ECO:0000269|PubMed:30024377}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 2 family.
CC {ECO:0000305}.
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DR EMBL; AY314776; AAQ84883.1; -; mRNA.
DR EMBL; AY314777; AAQ84884.1; -; mRNA.
DR EMBL; AY314778; AAQ84885.1; -; mRNA.
DR EMBL; EF141317; ABO42256.1; -; mRNA.
DR EMBL; EF141316; ABO42255.1; -; mRNA.
DR EMBL; EF141318; ABO42257.1; -; mRNA.
DR EMBL; FO080523; CCD64378.1; -; Genomic_DNA.
DR EMBL; FO080523; CCD64379.1; -; Genomic_DNA.
DR EMBL; FO080523; CCD64380.1; -; Genomic_DNA.
DR PIR; E88487; E88487.
DR RefSeq; NP_001021170.1; NM_001025999.2. [Q09460-1]
DR RefSeq; NP_001021171.1; NM_001026000.2. [Q09460-3]
DR RefSeq; NP_001021172.1; NM_001026001.2.
DR AlphaFoldDB; Q09460; -.
DR SMR; Q09460; -.
DR STRING; 6239.C13B9.4a.2; -.
DR PaxDb; Q09460; -.
DR PRIDE; Q09460; -.
DR EnsemblMetazoa; C13B9.4a.1; C13B9.4a.1; WBGene00015735. [Q09460-1]
DR EnsemblMetazoa; C13B9.4a.2; C13B9.4a.2; WBGene00015735. [Q09460-1]
DR EnsemblMetazoa; C13B9.4a.3; C13B9.4a.3; WBGene00015735. [Q09460-1]
DR EnsemblMetazoa; C13B9.4b.1; C13B9.4b.1; WBGene00015735. [Q09460-3]
DR EnsemblMetazoa; C13B9.4b.2; C13B9.4b.2; WBGene00015735. [Q09460-3]
DR EnsemblMetazoa; C13B9.4b.3; C13B9.4b.3; WBGene00015735. [Q09460-3]
DR EnsemblMetazoa; C13B9.4c.1; C13B9.4c.1; WBGene00015735. [Q09460-2]
DR EnsemblMetazoa; C13B9.4c.2; C13B9.4c.2; WBGene00015735. [Q09460-2]
DR EnsemblMetazoa; C13B9.4c.3; C13B9.4c.3; WBGene00015735. [Q09460-2]
DR GeneID; 175942; -.
DR UCSC; C13B9.4c.1; c. elegans.
DR CTD; 175942; -.
DR WormBase; C13B9.4a; CE30860; WBGene00015735; pdfr-1. [Q09460-1]
DR WormBase; C13B9.4b; CE37087; WBGene00015735; pdfr-1. [Q09460-3]
DR WormBase; C13B9.4c; CE37088; WBGene00015735; pdfr-1. [Q09460-2]
DR eggNOG; KOG4564; Eukaryota.
DR InParanoid; Q09460; -.
DR OMA; RIWCNAT; -.
DR OrthoDB; 651627at2759; -.
DR PhylomeDB; Q09460; -.
DR PRO; PR:Q09460; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00015735; Expressed in larva and 14 other tissues.
DR ExpressionAtlas; Q09460; baseline and differential.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IMP:UniProtKB.
DR GO; GO:0097642; F:calcitonin family receptor activity; IMP:UniProtKB.
DR GO; GO:0004948; F:calcitonin receptor activity; ISS:WormBase.
DR GO; GO:0008528; F:G protein-coupled peptide receptor activity; IBA:GO_Central.
DR GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; IMP:UniProtKB.
DR GO; GO:0007188; P:adenylate cyclase-modulating G protein-coupled receptor signaling pathway; IMP:UniProtKB.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IMP:UniProtKB.
DR GO; GO:0006874; P:cellular calcium ion homeostasis; IMP:UniProtKB.
DR GO; GO:0040011; P:locomotion; IMP:UniProtKB.
DR GO; GO:0031987; P:locomotion involved in locomotory behavior; IMP:UniProtKB.
DR GO; GO:0060179; P:male mating behavior; IMP:UniProtKB.
DR GO; GO:0045762; P:positive regulation of adenylate cyclase activity; ISS:WormBase.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:UniProtKB.
DR GO; GO:0030431; P:sleep; IMP:UniProtKB.
DR Gene3D; 4.10.1240.10; -; 1.
DR InterPro; IPR017981; GPCR_2-like.
DR InterPro; IPR036445; GPCR_2_extracell_dom_sf.
DR InterPro; IPR001879; GPCR_2_extracellular_dom.
DR InterPro; IPR000832; GPCR_2_secretin-like.
DR InterPro; IPR017983; GPCR_2_secretin-like_CS.
DR Pfam; PF00002; 7tm_2; 1.
DR Pfam; PF02793; HRM; 1.
DR PRINTS; PR00249; GPCRSECRETIN.
DR SMART; SM00008; HormR; 1.
DR SUPFAM; SSF111418; SSF111418; 1.
DR PROSITE; PS00649; G_PROTEIN_RECEP_F2_1; 1.
DR PROSITE; PS00650; G_PROTEIN_RECEP_F2_2; 1.
DR PROSITE; PS50227; G_PROTEIN_RECEP_F2_3; 1.
DR PROSITE; PS50261; G_PROTEIN_RECEP_F2_4; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; G-protein coupled receptor;
KW Glycoprotein; Membrane; Receptor; Reference proteome; Transducer;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..546
FT /note="Calcitonin receptor-like protein 1"
FT /id="PRO_0000070332"
FT TOPO_DOM 1..171
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 172..192
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 193..205
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 206..226
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 227..251
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 252..272
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 273..292
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 293..313
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 314..333
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 334..354
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 355..377
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 378..398
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 399..403
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 404..424
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 425..546
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT REGION 472..546
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 472..489
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 501..518
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 521..546
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 365
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 366
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 472
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 476
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 540
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 108..132
FT /note="NITKDCHVSGVWSGRNAGEMGPTLP -> YIVKRCDETGRWAGKKPGHYENP
FT W (in isoform b)"
FT /evidence="ECO:0000303|PubMed:18390545, ECO:0000303|Ref.2"
FT /id="VSP_046483"
FT VAR_SEQ 139..158
FT /note="MCYTDEVIYIMQNLNNESLT -> VCFKIDYEDAK (in isoform b)"
FT /evidence="ECO:0000303|PubMed:18390545, ECO:0000303|Ref.2"
FT /id="VSP_046484"
FT VAR_SEQ 539..546
FT /note="SNRSTKSP -> YEE (in isoform c)"
FT /evidence="ECO:0000303|PubMed:18390545, ECO:0000303|Ref.2"
FT /id="VSP_046482"
FT MUTAGEN 298
FT /note="G->D: In bx142; reduced mate searching behavior."
FT /evidence="ECO:0000269|PubMed:23143519"
SQ SEQUENCE 546 AA; 61694 MW; 82F7E88CA18A1319 CRC64;
MADATSPFNV SILDNSTKLS EMVESGWNVL ASTSVQAFNE AMDVLEESYP LCKKMLDHNN
LFPERDPNDT RIWCNATYDT VLCWPPTPAN SSVTLQCPHM KGLDPNKNIT KDCHVSGVWS
GRNAGEMGPT LPGWTNFTMC YTDEVIYIMQ NLNNESLTIA QEVARNARKL EFVGLGLSLV
SLILAISIFS YFRRLRVFRN LLHLHLMIAM LMVVILRLVL YIDLIFTGEN GPHTNSAEGK
TINTMPIVCE GMFFFLEYFK TVTFCWMFLE GIYLNNQIVF GFFNSEPKLL PYFIAGYGIP
LVHTMLWLLV VLIKKDFKVE RCLGSYYLEP EFWILDGPRM AELVINLFFI CNVIRVLYSK
VRESNNTSEA GLKKSVKAAM MLLPLLGVPN IMQTIPFAPT RDNIMVFAVW TYTASFTYMY
QGLMVASIYC FTNKEVNHVL KTFYARYRLL HKSQNELRRG SRSVASHYAA KNGTANASAP
QTNNADEFGK LSPFPSRSKK GSDDSTTKLM KDAVMEEEKN ANNNGYGSAG EMTPLREGSN
RSTKSP
