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Calcitonin receptor (CT-R)

 CALCR_PIG               Reviewed;         498 AA.
P25117;
01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
01-OCT-1996, sequence version 2.
25-OCT-2017, entry version 114.
RecName: Full=Calcitonin receptor;
Short=CT-R;
Flags: Precursor;
Name=CALCR;
Sus scrofa (Pig).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae;
Sus.
NCBI_TaxID=9823;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SHORT).
PubMed=1658940; DOI=10.1126/science.1658940;
Lin H.Y., Harris T.L., Flannery M.S., Aruffo A., Kaji E.H., Gorn A.,
Kolakowski L.F. Jr., Lodish H.F., Goldring S.R.;
"Expression cloning of an adenylate cyclase-coupled calcitonin
receptor.";
Science 254:1022-1024(1991).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS LONG AND SHORT).
TISSUE=Kidney;
PubMed=8034723;
Zolnierowicz S.S., Cron P., Solinas-Toldo S., Fries R., Lin H.Y.,
Hemmings B.A.;
"Isolation, characterization, and chromosomal localization of the
porcine calcitonin receptor gene. Identification of two variants of
the receptor generated by alternative splicing.";
J. Biol. Chem. 269:19530-19538(1994).
-!- FUNCTION: This is a receptor for calcitonin. The activity of this
receptor is mediated by G proteins which activate adenylyl
cyclase. The calcitonin receptor is thought to couple to the
heterotrimeric guanosine triphosphate-binding protein that is
sensitive to cholera toxin. The receptor can also couple to an
additional signaling pathway via a pertussis toxin-sensitive g
protein in isolated osteoclasts and in LLC-PK1 cells.
-!- SUBUNIT: Interacts with GPRASP2. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=Long;
IsoId=P25117-1; Sequence=Displayed;
Name=Short;
IsoId=P25117-2; Sequence=VSP_001993;
-!- SIMILARITY: Belongs to the G-protein coupled receptor 2 family.
{ECO:0000305}.
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EMBL; M74420; AAA31023.1; -; mRNA.
EMBL; Z31356; CAA83233.1; -; Genomic_DNA.
EMBL; Z31356; CAA83232.1; -; Genomic_DNA.
PIR; A39285; A39285.
PIR; I47130; I47130.
RefSeq; NP_999519.1; NM_214354.2. [P25117-2]
UniGene; Ssc.60684; -.
ProteinModelPortal; P25117; -.
SMR; P25117; -.
STRING; 9823.ENSSSCP00000016247; -.
PaxDb; P25117; -.
PRIDE; P25117; -.
GeneID; 397638; -.
KEGG; ssc:397638; -.
CTD; 799; -.
eggNOG; KOG4564; Eukaryota.
eggNOG; ENOG410XRS2; LUCA.
HOGENOM; HOG000230695; -.
HOVERGEN; HBG102129; -.
InParanoid; P25117; -.
KO; K04576; -.
Proteomes; UP000008227; Unplaced.
GO; GO:0005887; C:integral component of plasma membrane; NAS:UniProtKB.
GO; GO:0032841; F:calcitonin binding; IDA:UniProtKB.
GO; GO:0004948; F:calcitonin receptor activity; IDA:UniProtKB.
GO; GO:0007202; P:activation of phospholipase C activity; IDA:UniProtKB.
GO; GO:0007166; P:cell surface receptor signaling pathway; IEA:InterPro.
GO; GO:0045762; P:positive regulation of adenylate cyclase activity; IDA:UniProtKB.
CDD; cd15274; 7tmB1_calcitonin_R; 1.
Gene3D; 4.10.1240.10; -; 1.
InterPro; IPR003287; GCPR_2_calcitonin_rcpt_fam.
InterPro; IPR017981; GPCR_2-like.
InterPro; IPR001688; GPCR_2_calcitonin_rcpt.
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.
PANTHER; PTHR12011:SF84; PTHR12011:SF84; 1.
Pfam; PF00002; 7tm_2; 1.
Pfam; PF02793; HRM; 1.
PRINTS; PR00361; CALCITONINR.
PRINTS; PR01350; CTRFAMILY.
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.
2: Evidence at transcript level;
Alternative splicing; Cell membrane; Complete proteome;
Disulfide bond; G-protein coupled receptor; Glycoprotein; Membrane;
Receptor; Reference proteome; Signal; Transducer; Transmembrane;
Transmembrane helix.
SIGNAL 1 29 {ECO:0000255}.
CHAIN 30 498 Calcitonin receptor.
/FTId=PRO_0000012808.
TOPO_DOM 30 154 Extracellular. {ECO:0000255}.
TRANSMEM 155 174 Helical; Name=1. {ECO:0000255}.
TOPO_DOM 175 197 Cytoplasmic. {ECO:0000255}.
TRANSMEM 198 217 Helical; Name=2. {ECO:0000255}.
TOPO_DOM 218 237 Extracellular. {ECO:0000255}.
TRANSMEM 238 260 Helical; Name=3. {ECO:0000255}.
TOPO_DOM 261 277 Cytoplasmic. {ECO:0000255}.
TRANSMEM 278 297 Helical; Name=4. {ECO:0000255}.
TOPO_DOM 298 313 Extracellular. {ECO:0000255}.
TRANSMEM 314 337 Helical; Name=5. {ECO:0000255}.
TOPO_DOM 338 360 Cytoplasmic. {ECO:0000255}.
TRANSMEM 361 378 Helical; Name=6. {ECO:0000255}.
TOPO_DOM 379 390 Extracellular. {ECO:0000255}.
TRANSMEM 391 412 Helical; Name=7. {ECO:0000255}.
TOPO_DOM 413 498 Cytoplasmic. {ECO:0000255}.
COMPBIAS 213 216 Poly-Ile.
COMPBIAS 439 454 Poly-Ala.
CARBOHYD 74 74 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 126 126 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 131 131 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 56 82 {ECO:0000250}.
DISULFID 73 113 {ECO:0000250}.
DISULFID 96 135 {ECO:0000250}.
VAR_SEQ 176 191 Missing (in isoform Short).
{ECO:0000303|PubMed:1658940}.
/FTId=VSP_001993.
SEQUENCE 498 AA; 57155 MW; 618CE50EC4B5E7C3 CRC64;
MRFTLTRWCL TLFIFLNRPL PVLPDSADGA HTPTLEPEPF LYILGKQRML EAQHRCYDRM
QKLPPYQGEG LYCNRTWDGW SCWDDTPAGV LAEQYCPDYF PDFDAAEKVT KYCGEDGDWY
RHPESNISWS NYTMCNAFTP DKLQNAYILY YLAIVGHSLS ILTLLISLGI FMFLRYFNLL
APFNALLYPT RSISCQRVTL HKNMFLTYVL NSIIIIVHLV VIVPNGELVK RDPPICKVLH
FFHQYMMSCN YFWMLCEGVY LHTLIVVSVF AEGQRLWWYH VLGWGFPLIP TTAHAITRAV
LFNDNCWLSV DTNLLYIIHG PVMAALVVNF FFLLNILRVL VKKLKESQEA ESHMYLKAVR
ATLILVPLLG VQFVVLPWRP STPLLGKIYD YVVHSLIHFQ GFFVAIIYCF CNHEVQGALK
RQWNQYQAQR WAGRRSTRAA NAAAATAAAA AALAETVEIP VYICHQEPRE EPAGEEPVVE
VEGVEVIAME VLEQETSA


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