CALCR_RAT
ID CALCR_RAT Reviewed; 516 AA.
AC P32214; P32213;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Calcitonin receptor {ECO:0000305};
DE Short=CT-R;
DE AltName: Full=C1A/C1B;
DE Flags: Precursor;
GN Name=Calcr {ECO:0000312|RGD:621001};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Wistar; TISSUE=Brain;
RX PubMed=8391477; DOI=10.1016/0014-5793(93)81078-e;
RA Albrandt K.G., Mull E., Brady E.M., Herich J., Moore C.X., Beaumont K.;
RT "Molecular cloning of two receptors from rat brain with high affinity for
RT salmon calcitonin.";
RL FEBS Lett. 325:225-232(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RX PubMed=8395656; DOI=10.1210/mend.7.6.8395656;
RA Sexton P.M., Housammi S., Hilton J.M., O'Keeffe L.M., Center R.J.,
RA Gillespie M.T., Darcy P., Findlay D.M.;
RT "Identification of brain isoforms of the rat calcitonin receptor.";
RL Mol. Endocrinol. 7:815-821(1993).
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.
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=B;
CC IsoId=P32214-1; Sequence=Displayed;
CC Name=A;
CC IsoId=P32214-2; Sequence=VSP_001995;
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 2 family.
CC {ECO:0000305}.
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DR EMBL; L14618; AAA65965.1; -; mRNA.
DR EMBL; L14617; AAA65964.1; -; mRNA.
DR EMBL; L13040; AAA03031.1; -; mRNA.
DR EMBL; L13041; AAA03030.1; -; mRNA.
DR PIR; A37430; A37430.
DR PIR; I60800; I60800.
DR PIR; S33746; S33746.
DR RefSeq; NP_001029187.1; NM_001034015.1.
DR RefSeq; NP_446268.2; NM_053816.2.
DR AlphaFoldDB; P32214; -.
DR SMR; P32214; -.
DR BioGRID; 250474; 1.
DR ComplexPortal; CPX-246; Amylin receptor 1 complex.
DR ComplexPortal; CPX-247; Amylin receptor 2 complex.
DR ComplexPortal; CPX-249; Amylin receptor 3 complex.
DR STRING; 10116.ENSRNOP00000013910; -.
DR BindingDB; P32214; -.
DR ChEMBL; CHEMBL2204; -.
DR GuidetoPHARMACOLOGY; 43; -.
DR GlyGen; P32214; 4 sites.
DR PhosphoSitePlus; P32214; -.
DR PaxDb; P32214; -.
DR PRIDE; P32214; -.
DR GeneID; 116506; -.
DR KEGG; rno:116506; -.
DR UCSC; RGD:621001; rat. [P32214-1]
DR CTD; 799; -.
DR RGD; 621001; Calcr.
DR eggNOG; KOG4564; Eukaryota.
DR HOGENOM; CLU_002753_4_2_1; -.
DR InParanoid; P32214; -.
DR OrthoDB; 1005634at2759; -.
DR PhylomeDB; P32214; -.
DR Reactome; R-RNO-419812; Calcitonin-like ligand receptors.
DR PRO; PR:P32214; -.
DR Proteomes; UP000002494; Unplaced.
DR Genevisible; P32214; RN.
DR GO; GO:0001669; C:acrosomal vesicle; ISO:RGD.
DR GO; GO:0150056; C:amylin receptor complex 1; ISO:RGD.
DR GO; GO:0150057; C:amylin receptor complex 2; ISO:RGD.
DR GO; GO:0150058; C:amylin receptor complex 3; ISO:RGD.
DR GO; GO:0030424; C:axon; IDA:RGD.
DR GO; GO:0005929; C:cilium; ISO:RGD.
DR GO; GO:0043005; C:neuron projection; IDA:RGD.
DR GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0097643; F:amylin receptor activity; ISO:RGD.
DR GO; GO:0032841; F:calcitonin binding; IDA:RGD.
DR GO; GO:0001635; F:calcitonin gene-related peptide receptor activity; ISO:RGD.
DR GO; GO:0004948; F:calcitonin receptor activity; IDA:RGD.
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; ISO:RGD.
DR GO; GO:0007188; P:adenylate cyclase-modulating G protein-coupled receptor signaling pathway; IDA:RGD.
DR GO; GO:0097647; P:amylin receptor signaling pathway; ISO:RGD.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IEA:InterPro.
DR GO; GO:0038041; P:cross-receptor inhibition within G protein-coupled receptor heterodimer; ISO:RGD.
DR GO; GO:0030279; P:negative regulation of ossification; ISO:RGD.
DR GO; GO:0030316; P:osteoclast differentiation; ISO:RGD.
DR GO; GO:0045762; P:positive regulation of adenylate cyclase activity; ISO:RGD.
DR GO; GO:1905665; P:positive regulation of calcium ion import across plasma membrane; ISO:RGD.
DR GO; GO:0010942; P:positive regulation of cell death; ISO:RGD.
DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; ISO:RGD.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; ISO:RGD.
DR GO; GO:0010628; P:positive regulation of gene expression; ISO:RGD.
DR GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; ISO:RGD.
DR GO; GO:0010739; P:positive regulation of protein kinase A signaling; ISO:RGD.
DR GO; GO:0051897; P:positive regulation of protein kinase B signaling; ISO:RGD.
DR GO; GO:0043488; P:regulation of mRNA stability; ISO:RGD.
DR GO; GO:1904645; P:response to amyloid-beta; ISO:RGD.
DR GO; GO:0051384; P:response to glucocorticoid; ISO:RGD.
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..24
FT /evidence="ECO:0000255"
FT CHAIN 25..516
FT /note="Calcitonin receptor"
FT /id="PRO_0000012810"
FT TOPO_DOM 25..153
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 154..173
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 174..180
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 181..200
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 201..257
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 258..280
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 281..297
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 298..317
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 318..333
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 334..357
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 358..380
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 381..398
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 399..410
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 411..432
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 433..516
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 489..516
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 28
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 73
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 125
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 130
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 55..81
FT /evidence="ECO:0000250"
FT DISULFID 72..112
FT /evidence="ECO:0000250"
FT DISULFID 95..134
FT /evidence="ECO:0000250"
FT VAR_SEQ 217..253
FT /note="Missing (in isoform A)"
FT /evidence="ECO:0000305"
FT /id="VSP_001995"
FT CONFLICT 148
FT /note="L -> S (in Ref. 2; AAA03031/AAA03030)"
FT /evidence="ECO:0000305"
FT CONFLICT 459
FT /note="Missing (in Ref. 2; AAA03031/AAA03030)"
FT /evidence="ECO:0000305"
FT CONFLICT 479
FT /note="L -> R (in Ref. 2; AAA03031/AAA03030)"
FT /evidence="ECO:0000305"
SQ 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
