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Calcitonin receptor (CT-R) (C1A/C1B)

 CALCR_RAT               Reviewed;         516 AA.
P32214; P32213;
01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
01-OCT-1993, sequence version 1.
22-NOV-2017, entry version 145.
RecName: Full=Calcitonin receptor;
Short=CT-R;
AltName: Full=C1A/C1B;
Flags: Precursor;
Name=Calcr;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Wistar; TISSUE=Brain;
PubMed=8391477; DOI=10.1016/0014-5793(93)81078-E;
Albrandt K.G., Mull E., Brady E.M., Herich J., Moore C.X.,
Beaumont K.;
"Molecular cloning of two receptors from rat brain with high affinity
for salmon calcitonin.";
FEBS Lett. 325:225-232(1993).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Brain;
PubMed=8395656; DOI=10.1210/mend.7.6.8395656;
Sexton P.M., Housammi S., Hilton J.M., O'Keeffe L.M., Center R.J.,
Gillespie M.T., Darcy P., Findlay D.M.;
"Identification of brain isoforms of the rat calcitonin receptor.";
Mol. Endocrinol. 7:815-821(1993).
-!- 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.
-!- SUBUNIT: Interacts with GPRASP2. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=B;
IsoId=P32214-1; Sequence=Displayed;
Name=A;
IsoId=P32214-2; Sequence=VSP_001995;
-!- SIMILARITY: Belongs to the G-protein coupled receptor 2 family.
{ECO:0000305}.
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EMBL; L14618; AAA65965.1; -; mRNA.
EMBL; L14617; AAA65964.1; -; mRNA.
EMBL; L13040; AAA03031.1; -; mRNA.
EMBL; L13041; AAA03030.1; -; mRNA.
PIR; A37430; A37430.
PIR; I60800; I60800.
PIR; S33746; S33746.
RefSeq; NP_001029187.1; NM_001034015.1.
RefSeq; NP_446268.2; NM_053816.2.
UniGene; Rn.10062; -.
ProteinModelPortal; P32214; -.
SMR; P32214; -.
BioGrid; 250474; 1.
STRING; 10116.ENSRNOP00000013910; -.
BindingDB; P32214; -.
ChEMBL; CHEMBL2204; -.
GuidetoPHARMACOLOGY; 43; -.
PhosphoSitePlus; P32214; -.
PaxDb; P32214; -.
PRIDE; P32214; -.
GeneID; 116506; -.
KEGG; rno:116506; -.
UCSC; RGD:621001; rat. [P32214-1]
CTD; 799; -.
RGD; 621001; Calcr.
eggNOG; KOG4564; Eukaryota.
eggNOG; ENOG410XRS2; LUCA.
HOGENOM; HOG000230695; -.
HOVERGEN; HBG102129; -.
InParanoid; P32214; -.
KO; K04576; -.
OrthoDB; EOG091G027C; -.
PhylomeDB; P32214; -.
PRO; PR:P32214; -.
Proteomes; UP000002494; Unplaced.
Genevisible; P32214; RN.
GO; GO:0001669; C:acrosomal vesicle; ISO:RGD.
GO; GO:1903440; C:amylin receptor complex; ISO:RGD.
GO; GO:0030424; C:axon; IDA:RGD.
GO; GO:0005929; C:cilium; ISO:RGD.
GO; GO:0043005; C:neuron projection; IDA:RGD.
GO; GO:0043025; C:neuronal cell body; IDA:RGD.
GO; GO:0032841; F:calcitonin binding; IDA:RGD.
GO; GO:0004948; F:calcitonin receptor activity; IDA:RGD.
GO; GO:0008565; F:protein transporter activity; ISO:RGD.
GO; GO:0004872; F:receptor activity; ISO:RGD.
GO; GO:0007189; P:adenylate cyclase-activating G-protein coupled receptor signaling pathway; ISO:RGD.
GO; GO:0007188; P:adenylate cyclase-modulating G-protein coupled receptor signaling pathway; IDA:RGD.
GO; GO:0097647; P:amylin receptor signaling pathway; ISO:RGD.
GO; GO:0007166; P:cell surface receptor signaling pathway; IEA:InterPro.
GO; GO:0030279; P:negative regulation of ossification; ISO:RGD.
GO; GO:0030316; P:osteoclast differentiation; ISO:RGD.
GO; GO:0045762; P:positive regulation of adenylate cyclase activity; ISO:RGD.
GO; GO:1905665; P:positive regulation of calcium ion import across plasma membrane; ISO:RGD.
GO; GO:0030819; P:positive regulation of cAMP biosynthetic process; ISO:RGD.
GO; GO:0030816; P:positive regulation of cAMP metabolic process; ISO:RGD.
GO; GO:0010942; P:positive regulation of cell death; ISO:RGD.
GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; ISO:RGD.
GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; ISO:RGD.
GO; GO:0010628; P:positive regulation of gene expression; ISO:RGD.
GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; ISO:RGD.
GO; GO:0010739; P:positive regulation of protein kinase A signaling; ISO:RGD.
GO; GO:0051897; P:positive regulation of protein kinase B signaling; ISO:RGD.
GO; GO:0072659; P:protein localization to plasma membrane; ISO:RGD.
GO; GO:0015031; P:protein transport; ISO:RGD.
GO; GO:0031623; P:receptor internalization; ISO:RGD.
GO; GO:0043488; P:regulation of mRNA stability; ISO:RGD.
GO; GO:0051384; P:response to glucocorticoid; ISO:RGD.
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 24 {ECO:0000255}.
CHAIN 25 516 Calcitonin receptor.
/FTId=PRO_0000012810.
TOPO_DOM 25 153 Extracellular. {ECO:0000255}.
TRANSMEM 154 173 Helical; Name=1. {ECO:0000255}.
TOPO_DOM 174 180 Cytoplasmic. {ECO:0000255}.
TRANSMEM 181 200 Helical; Name=2. {ECO:0000255}.
TOPO_DOM 201 257 Extracellular. {ECO:0000255}.
TRANSMEM 258 280 Helical; Name=3. {ECO:0000255}.
TOPO_DOM 281 297 Cytoplasmic. {ECO:0000255}.
TRANSMEM 298 317 Helical; Name=4. {ECO:0000255}.
TOPO_DOM 318 333 Extracellular. {ECO:0000255}.
TRANSMEM 334 357 Helical; Name=5. {ECO:0000255}.
TOPO_DOM 358 380 Cytoplasmic. {ECO:0000255}.
TRANSMEM 381 398 Helical; Name=6. {ECO:0000255}.
TOPO_DOM 399 410 Extracellular. {ECO:0000255}.
TRANSMEM 411 432 Helical; Name=7. {ECO:0000255}.
TOPO_DOM 433 516 Cytoplasmic. {ECO:0000255}.
CARBOHYD 28 28 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 73 73 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 125 125 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 130 130 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 55 81 {ECO:0000250}.
DISULFID 72 112 {ECO:0000250}.
DISULFID 95 134 {ECO:0000250}.
VAR_SEQ 217 253 Missing (in isoform A). {ECO:0000305}.
/FTId=VSP_001995.
CONFLICT 148 148 L -> S (in Ref. 2; AAA03031/AAA03030).
{ECO:0000305}.
CONFLICT 459 459 Missing (in Ref. 2; AAA03031/AAA03030).
{ECO:0000305}.
CONFLICT 479 479 L -> R (in Ref. 2; AAA03031/AAA03030).
{ECO:0000305}.
SEQUENCE 516 AA; 60292 MW; 9B057B860E574378 CRC64;
MRFLLLNRFT LLLLLLVSPT PVLQAPTNLT DSGLDQEPFL YLVGRKKLLD AQYKCYDRIQ
QLPPYEGEGP YCNRTWDGWM CWDDTPAGVM SYQHCPDYFP DFDPTEKVSK YCDENGEWFR
HPDSNRTWSN YTLCNAFTPD KLHNAYVLYY LALVGHSMSI AALIASMGIF LFFKNLSCQR
VTLHKNMFLT YILNSIIIII HLVEVVPNGD LVRRDPMHIF HHNTYMWTMQ WELSPPLPLS
AHEGKMDPHD SEVISCKILH FFHQYMMACN YFWMLCEGIY LHTLIVMAVF TEDQRLRWYY
LLGWGFPIVP TIIHAITRAV YYNDNCWLST ETHLLYIIHG PVMAALVVNF FFLLNIVRVL
VTKMRQTHEA EAYMYLKAVK ATMVLVPLLG IQFVVFPWRP SNKVLGKIYD YLMHSLIHFQ
GFFVATIYCF CNHEVQVTLK RQWAQFKIQW SHRWGRRRRP TNRVVSAPRA VAFAEPGGLP
IYICHQEPRN PPVSNNEGEE GTEMIPMNVI QQDSSA


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