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Calcitonin receptor-like protein 1 (Pigment dispersing factor neuropeptide receptor homolog 1)

 PDFR1_CAEEL             Reviewed;         546 AA.
Q09460; B2BBX5; G5EDW6; G5EFM1;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
30-MAY-2003, sequence version 2.
23-MAY-2018, entry version 133.
RecName: Full=Calcitonin receptor-like protein 1;
AltName: Full=Pigment dispersing factor neuropeptide receptor homolog 1;
Name=pdfr-1; Synonyms=seb-1; ORFNames=C13B9.4;
Caenorhabditis elegans.
Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
Rhabditoidea; Rhabditidae; Peloderinae; Caenorhabditis.
NCBI_TaxID=6239;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A; B AND C), FUNCTION, AND TISSUE
SPECIFICITY.
PubMed=18390545; DOI=10.1074/jbc.M709060200;
Janssen T., Husson S.J., Lindemans M., Mertens I., Rademakers S.,
Donck K.V., Geysen J., Jansen G., Schoofs L.;
"Functional characterization of three G protein-coupled receptors for
pigment dispersing factors in Caenorhabditis elegans.";
J. Biol. Chem. 283:15241-15249(2008).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A; B AND C).
Mastwal S.S., Yu D., Hedgecock E.M.;
"Molecular and evolutionary characterization of family B G-protein
coupled receptors in Caenorhabditis elegans.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE
SPLICING.
STRAIN=Bristol N2;
PubMed=9851916; DOI=10.1126/science.282.5396.2012;
The C. elegans sequencing consortium;
"Genome sequence of the nematode C. elegans: a platform for
investigating biology.";
Science 282:2012-2018(1998).
[4]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=14551910; DOI=10.1371/journal.pbio.0000012;
Simmer F., Moorman C., van der Linden A.M., Kuijk E.,
van den Berghe P.V.E., Kamath R.S., Fraser A.G., Ahringer J.,
Plasterk R.H.A.;
"Genome-wide RNAi of C. elegans using the hypersensitive rrf-3 strain
reveals novel gene functions.";
PLoS Biol. 1:E12-E12(2003).
[5]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=22579613; DOI=10.1016/j.mce.2012.05.001;
Meelkop E., Temmerman L., Janssen T., Suetens N., Beets I.,
Van Rompay L., Shanmugam N., Husson S.J., Schoofs L.;
"PDF receptor signaling in Caenorhabditis elegans modulates locomotion
and egg-laying.";
Mol. Cell. Endocrinol. 361:232-240(2012).
[6]
FUNCTION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF
GLY-298.
PubMed=23143519; DOI=10.1038/nn.3253;
Barrios A., Ghosh R., Fang C., Emmons S.W., Barr M.M.;
"PDF-1 neuropeptide signaling modulates a neural circuit for mate-
searching behavior in C. elegans.";
Nat. Neurosci. 15:1675-1682(2012).
-!- FUNCTION: G-protein coupled receptor for PDF neuropeptides.
Activated by peptides PDF-1 and PDF-2 but to a lesser extent with
isoform c. Isoforms a and b are thought to act through the G-
alpha(s) type of G proteins to elevate cAMP levels whereas isoform
c inhibits cAMP levels through the G-alpha(i/o) type of G
proteins. Involved in locomotion; more specifically mate searching
behavior independent of nutritional status. Might have a role in
touch sensitivity. {ECO:0000269|PubMed:14551910,
ECO:0000269|PubMed:18390545, ECO:0000269|PubMed:22579613,
ECO:0000269|PubMed:23143519}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass
membrane protein {ECO:0000305}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=a; Synonyms=Seb-1a;
IsoId=Q09460-1; Sequence=Displayed;
Name=c; Synonyms=Seb-1c;
IsoId=Q09460-2; Sequence=VSP_046482;
Name=b; Synonyms=Seb-1b;
IsoId=Q09460-3; Sequence=VSP_046483, VSP_046484;
-!- TISSUE SPECIFICITY: Expression was observed in the mechanosensory
neuron pairs PLM, ALM, FLP, OLQD, and OLQV, the chemosensory
neurons PHA, PHB, RMEV, the ring motor neurons RMED, and the
pharyngeal interneuron pair I1. In both hermaphrodites and males
at the L4 stage expression is observed in the head, body wall
muscle cells and tail. Expression in sensory neurons PHA, PQR and
URY are responsible for mate searching behavior.
{ECO:0000269|PubMed:18390545, ECO:0000269|PubMed:23143519}.
-!- DISRUPTION PHENOTYPE: Disrupted locomotion (unc); decreased speed,
increased number of reversals and loss of mate searching behavior.
{ECO:0000269|PubMed:14551910, ECO:0000269|PubMed:22579613,
ECO:0000269|PubMed:23143519}.
-!- SIMILARITY: Belongs to the G-protein coupled receptor 2 family.
{ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AY314776; AAQ84883.1; -; mRNA.
EMBL; AY314777; AAQ84884.1; -; mRNA.
EMBL; AY314778; AAQ84885.1; -; mRNA.
EMBL; EF141317; ABO42256.1; -; mRNA.
EMBL; EF141316; ABO42255.1; -; mRNA.
EMBL; EF141318; ABO42257.1; -; mRNA.
EMBL; FO080523; CCD64378.1; -; Genomic_DNA.
EMBL; FO080523; CCD64379.1; -; Genomic_DNA.
EMBL; FO080523; CCD64380.1; -; Genomic_DNA.
PIR; E88487; E88487.
RefSeq; NP_001021170.1; NM_001025999.2. [Q09460-1]
RefSeq; NP_001021171.1; NM_001026000.2. [Q09460-3]
RefSeq; NP_001021172.1; NM_001026001.2. [Q09460-2]
UniGene; Cel.22708; -.
ProteinModelPortal; Q09460; -.
STRING; 6239.C13B9.4a.1; -.
PaxDb; Q09460; -.
PRIDE; Q09460; -.
EnsemblMetazoa; C13B9.4a.1; C13B9.4a.1; WBGene00015735. [Q09460-1]
EnsemblMetazoa; C13B9.4a.2; C13B9.4a.2; WBGene00015735. [Q09460-1]
GeneID; 175942; -.
UCSC; C13B9.4c.1; c. elegans.
CTD; 175942; -.
WormBase; C13B9.4a; CE30860; WBGene00015735; pdfr-1. [Q09460-1]
WormBase; C13B9.4b; CE37087; WBGene00015735; pdfr-1. [Q09460-3]
WormBase; C13B9.4c; CE37088; WBGene00015735; pdfr-1. [Q09460-2]
eggNOG; ENOG410J3V0; Eukaryota.
eggNOG; ENOG41115ZH; LUCA.
GeneTree; ENSGT00900000140884; -.
HOGENOM; HOG000020932; -.
InParanoid; Q09460; -.
OMA; GKTINTM; -.
OrthoDB; EOG091G07WI; -.
PhylomeDB; Q09460; -.
PRO; PR:Q09460; -.
Proteomes; UP000001940; Chromosome III.
Bgee; WBGene00015735; -.
ExpressionAtlas; Q09460; baseline and differential.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005622; C:intracellular; IEA:GOC.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0004948; F:calcitonin receptor activity; ISS:WormBase.
GO; GO:0007189; P:adenylate cyclase-activating G-protein coupled receptor signaling pathway; ISS:WormBase.
GO; GO:0007166; P:cell surface receptor signaling pathway; IEA:InterPro.
GO; GO:0006874; P:cellular calcium ion homeostasis; ISS:WormBase.
GO; GO:0045762; P:positive regulation of adenylate cyclase activity; ISS:WormBase.
Gene3D; 4.10.1240.10; -; 1.
InterPro; IPR017981; GPCR_2-like.
InterPro; IPR036445; GPCR_2_extracell_dom_sf.
InterPro; IPR001879; GPCR_2_extracellular_dom.
InterPro; IPR000832; GPCR_2_secretin-like.
InterPro; IPR017983; GPCR_2_secretin-like_CS.
Pfam; PF00002; 7tm_2; 1.
Pfam; PF02793; HRM; 1.
PRINTS; PR00249; GPCRSECRETIN.
SMART; SM00008; HormR; 1.
SUPFAM; SSF111418; SSF111418; 1.
PROSITE; PS00649; G_PROTEIN_RECEP_F2_1; 1.
PROSITE; PS00650; G_PROTEIN_RECEP_F2_2; 1.
PROSITE; PS50227; G_PROTEIN_RECEP_F2_3; 1.
PROSITE; PS50261; G_PROTEIN_RECEP_F2_4; 1.
1: Evidence at protein level;
Alternative splicing; Cell membrane; Complete proteome;
G-protein coupled receptor; Glycoprotein; Membrane; Receptor;
Reference proteome; Transducer; Transmembrane; Transmembrane helix.
CHAIN 1 546 Calcitonin receptor-like protein 1.
/FTId=PRO_0000070332.
TOPO_DOM 1 171 Cytoplasmic. {ECO:0000255}.
TRANSMEM 172 192 Helical; Name=1. {ECO:0000255}.
TOPO_DOM 193 205 Extracellular. {ECO:0000255}.
TRANSMEM 206 226 Helical; Name=2. {ECO:0000255}.
TOPO_DOM 227 251 Cytoplasmic. {ECO:0000255}.
TRANSMEM 252 272 Helical; Name=3. {ECO:0000255}.
TOPO_DOM 273 292 Extracellular. {ECO:0000255}.
TRANSMEM 293 313 Helical; Name=4. {ECO:0000255}.
TOPO_DOM 314 333 Cytoplasmic. {ECO:0000255}.
TRANSMEM 334 354 Helical; Name=5. {ECO:0000255}.
TOPO_DOM 355 377 Extracellular. {ECO:0000255}.
TRANSMEM 378 398 Helical; Name=6. {ECO:0000255}.
TOPO_DOM 399 403 Cytoplasmic. {ECO:0000255}.
TRANSMEM 404 424 Helical; Name=7. {ECO:0000255}.
TOPO_DOM 425 546 Extracellular. {ECO:0000255}.
CARBOHYD 365 365 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 366 366 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 472 472 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 476 476 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 540 540 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
VAR_SEQ 108 132 NITKDCHVSGVWSGRNAGEMGPTLP -> YIVKRCDETGRW
AGKKPGHYENPW (in isoform b).
{ECO:0000303|PubMed:18390545,
ECO:0000303|Ref.2}.
/FTId=VSP_046483.
VAR_SEQ 139 158 MCYTDEVIYIMQNLNNESLT -> VCFKIDYEDAK (in
isoform b). {ECO:0000303|PubMed:18390545,
ECO:0000303|Ref.2}.
/FTId=VSP_046484.
VAR_SEQ 539 546 SNRSTKSP -> YEE (in isoform c).
{ECO:0000303|PubMed:18390545,
ECO:0000303|Ref.2}.
/FTId=VSP_046482.
MUTAGEN 298 298 G->D: In bx142; reduced mate searching
behavior. {ECO:0000269|PubMed:23143519}.
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


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