CALCR_PIG
ID CALCR_PIG Reviewed; 498 AA.
AC P25117;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Calcitonin receptor {ECO:0000250|UniProtKB:P30988};
DE Short=CT-R;
DE Flags: Precursor;
GN Name=CALCR {ECO:0000250|UniProtKB:P30988};
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SHORT).
RX PubMed=1658940; DOI=10.1126/science.1658940;
RA Lin H.Y., Harris T.L., Flannery M.S., Aruffo A., Kaji E.H., Gorn A.,
RA Kolakowski L.F. Jr., Lodish H.F., Goldring S.R.;
RT "Expression cloning of an adenylate cyclase-coupled calcitonin receptor.";
RL Science 254:1022-1024(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS LONG AND SHORT).
RC TISSUE=Kidney;
RX PubMed=8034723; DOI=10.1016/s0021-9258(17)32201-9;
RA Zolnierowicz S.S., Cron P., Solinas-Toldo S., Fries R., Lin H.Y.,
RA Hemmings B.A.;
RT "Isolation, characterization, and chromosomal localization of the porcine
RT calcitonin receptor gene. Identification of two variants of the receptor
RT generated by alternative splicing.";
RL J. Biol. Chem. 269:19530-19538(1994).
CC -!- FUNCTION: This is a receptor for calcitonin. The activity of this
CC receptor is mediated by G proteins which activate adenylyl cyclase. The
CC calcitonin receptor is thought to couple to the heterotrimeric
CC guanosine triphosphate-binding protein that is sensitive to cholera
CC toxin. The receptor can also couple to an additional signaling pathway
CC via a pertussis toxin-sensitive g protein in isolated osteoclasts and
CC in LLC-PK1 cells.
CC -!- SUBUNIT: Interacts with GPRASP2. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=Long;
CC IsoId=P25117-1; Sequence=Displayed;
CC Name=Short;
CC IsoId=P25117-2; Sequence=VSP_001993;
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 2 family.
CC {ECO:0000305}.
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DR EMBL; M74420; AAA31023.1; -; mRNA.
DR EMBL; Z31356; CAA83233.1; -; Genomic_DNA.
DR EMBL; Z31356; CAA83232.1; -; Genomic_DNA.
DR PIR; A39285; A39285.
DR PIR; I47130; I47130.
DR RefSeq; NP_999519.1; NM_214354.2. [P25117-2]
DR AlphaFoldDB; P25117; -.
DR SMR; P25117; -.
DR STRING; 9823.ENSSSCP00000016247; -.
DR PaxDb; P25117; -.
DR PRIDE; P25117; -.
DR Ensembl; ENSSSCT00015097458; ENSSSCP00015040058; ENSSSCG00015072473. [P25117-1]
DR Ensembl; ENSSSCT00025038832; ENSSSCP00025016432; ENSSSCG00025028555. [P25117-1]
DR Ensembl; ENSSSCT00030051448; ENSSSCP00030023425; ENSSSCG00030036962. [P25117-1]
DR Ensembl; ENSSSCT00055052178; ENSSSCP00055041690; ENSSSCG00055026382. [P25117-1]
DR Ensembl; ENSSSCT00070026987; ENSSSCP00070022435; ENSSSCG00070013791. [P25117-2]
DR GeneID; 397638; -.
DR KEGG; ssc:397638; -.
DR CTD; 799; -.
DR eggNOG; KOG4564; Eukaryota.
DR InParanoid; P25117; -.
DR OMA; CVAWILW; -.
DR OrthoDB; 1005634at2759; -.
DR Reactome; R-SSC-418555; G alpha (s) signalling events.
DR Reactome; R-SSC-419812; Calcitonin-like ligand receptors.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Chromosome 9.
DR GO; GO:0001669; C:acrosomal vesicle; IEA:Ensembl.
DR GO; GO:0030424; C:axon; IBA:GO_Central.
DR GO; GO:0005929; C:cilium; IEA:Ensembl.
DR GO; GO:0005887; C:integral component of plasma membrane; NAS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0032841; F:calcitonin binding; IDA:UniProtKB.
DR GO; GO:0004948; F:calcitonin receptor activity; IDA:UniProtKB.
DR GO; GO:0008528; F:G protein-coupled peptide receptor activity; IBA:GO_Central.
DR GO; GO:0007202; P:activation of phospholipase C activity; IDA:UniProtKB.
DR GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; IDA:UniProtKB.
DR GO; GO:0007188; P:adenylate cyclase-modulating G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IEA:InterPro.
DR GO; GO:0030279; P:negative regulation of ossification; IEA:Ensembl.
DR GO; GO:0001503; P:ossification; IEA:Ensembl.
DR GO; GO:0030316; P:osteoclast differentiation; IEA:Ensembl.
DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IBA:GO_Central.
DR GO; GO:0043488; P:regulation of mRNA stability; IEA:Ensembl.
DR Gene3D; 4.10.1240.10; -; 1.
DR InterPro; IPR003287; GCPR_2_calcitonin_rcpt_fam.
DR InterPro; IPR017981; GPCR_2-like.
DR InterPro; IPR001688; GPCR_2_calcitonin_rcpt.
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 PANTHER; PTHR45620:SF8; PTHR45620:SF8; 1.
DR Pfam; PF00002; 7tm_2; 1.
DR Pfam; PF02793; HRM; 1.
DR PRINTS; PR00361; CALCITONINR.
DR PRINTS; PR01350; CTRFAMILY.
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 2: Evidence at transcript level;
KW Alternative splicing; Cell membrane; Disulfide bond;
KW G-protein coupled receptor; Glycoprotein; Membrane; Receptor;
KW Reference proteome; Signal; Transducer; Transmembrane; Transmembrane helix.
FT SIGNAL 1..29
FT /evidence="ECO:0000255"
FT CHAIN 30..498
FT /note="Calcitonin receptor"
FT /id="PRO_0000012808"
FT TOPO_DOM 30..154
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 155..174
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 175..197
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 198..217
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 218..237
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 238..260
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 261..277
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 278..297
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 298..313
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 314..337
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 338..360
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 361..378
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 379..390
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 391..412
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 413..498
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 74
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 126
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 131
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 56..82
FT /evidence="ECO:0000250"
FT DISULFID 73..113
FT /evidence="ECO:0000250"
FT DISULFID 96..135
FT /evidence="ECO:0000250"
FT VAR_SEQ 176..191
FT /note="Missing (in isoform Short)"
FT /evidence="ECO:0000303|PubMed:1658940"
FT /id="VSP_001993"
SQ 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
