CALCR_MOUSE
ID CALCR_MOUSE Reviewed; 533 AA.
AC Q60755; F6X7J4; Q3UUL9; Q8CAB0;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 16-OCT-2013, sequence version 2.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Calcitonin receptor {ECO:0000305};
DE Short=CT-R;
DE Flags: Precursor;
GN Name=Calcr {ECO:0000312|MGI:MGI:101950};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC STRAIN=BALB/cJ; TISSUE=Brain;
RX PubMed=7988453; DOI=10.1210/endo.135.6.7988453;
RA Yamin M., Gorn A.H., Flannery M.R., Jenkins N.A., Gilbert D.J.,
RA Copeland N.G., Tapp D.R., Krane S.M., Goldring S.R.;
RT "Cloning and characterization of a mouse brain calcitonin receptor
RT complementary deoxyribonucleic acid and mapping of the calcitonin receptor
RT gene.";
RL Endocrinology 135:2635-2643(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Diencephalon, and Hypothalamus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
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=1;
CC IsoId=Q60755-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q60755-2; Sequence=VSP_053294;
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 2 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA69521.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; U18542; AAA69521.1; ALT_INIT; mRNA.
DR EMBL; AK039161; BAC30261.1; -; mRNA.
DR EMBL; AK162391; BAE36888.1; -; mRNA.
DR EMBL; AK133983; BAE21967.1; -; mRNA.
DR EMBL; AK138275; BAE23606.1; -; mRNA.
DR EMBL; AC066688; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC161368; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466533; EDL13991.1; -; Genomic_DNA.
DR EMBL; CH466533; EDL13992.1; -; Genomic_DNA.
DR EMBL; BC119232; AAI19233.1; -; mRNA.
DR EMBL; BC119272; AAI19273.1; -; mRNA.
DR CCDS; CCDS39416.1; -. [Q60755-2]
DR CCDS; CCDS39417.1; -. [Q60755-1]
DR PIR; I49154; I49154.
DR RefSeq; NP_001036190.1; NM_001042725.1. [Q60755-2]
DR RefSeq; NP_031614.2; NM_007588.2. [Q60755-1]
DR RefSeq; XP_006505035.1; XM_006504972.1.
DR RefSeq; XP_006505036.1; XM_006504973.2.
DR AlphaFoldDB; Q60755; -.
DR SMR; Q60755; -.
DR ComplexPortal; CPX-3235; Amylin receptor 1 complex.
DR ComplexPortal; CPX-3236; Amylin receptor 2 complex.
DR ComplexPortal; CPX-3237; Amylin receptor 3 complex.
DR STRING; 10090.ENSMUSP00000075070; -.
DR GlyGen; Q60755; 4 sites.
DR iPTMnet; Q60755; -.
DR PhosphoSitePlus; Q60755; -.
DR PaxDb; Q60755; -.
DR PRIDE; Q60755; -.
DR Antibodypedia; 15689; 424 antibodies from 25 providers.
DR DNASU; 12311; -.
DR Ensembl; ENSMUST00000075644; ENSMUSP00000075070; ENSMUSG00000023964. [Q60755-1]
DR Ensembl; ENSMUST00000115622; ENSMUSP00000111285; ENSMUSG00000023964. [Q60755-2]
DR Ensembl; ENSMUST00000168592; ENSMUSP00000130243; ENSMUSG00000023964. [Q60755-2]
DR Ensembl; ENSMUST00000170266; ENSMUSP00000132124; ENSMUSG00000023964. [Q60755-1]
DR Ensembl; ENSMUST00000171613; ENSMUSP00000130083; ENSMUSG00000023964. [Q60755-2]
DR GeneID; 12311; -.
DR KEGG; mmu:12311; -.
DR UCSC; uc009ave.1; mouse. [Q60755-2]
DR UCSC; uc009avf.1; mouse. [Q60755-1]
DR CTD; 799; -.
DR MGI; MGI:101950; Calcr.
DR VEuPathDB; HostDB:ENSMUSG00000023964; -.
DR eggNOG; KOG4564; Eukaryota.
DR GeneTree; ENSGT00940000155380; -.
DR HOGENOM; CLU_002753_4_2_1; -.
DR InParanoid; Q60755; -.
DR OMA; CVAWILW; -.
DR OrthoDB; 1005634at2759; -.
DR PhylomeDB; Q60755; -.
DR TreeFam; TF315710; -.
DR Reactome; R-MMU-418555; G alpha (s) signalling events.
DR Reactome; R-MMU-419812; Calcitonin-like ligand receptors.
DR BioGRID-ORCS; 12311; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Calcr; mouse.
DR PRO; PR:Q60755; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q60755; protein.
DR Bgee; ENSMUSG00000023964; Expressed in arcuate nucleus of hypothalamus and 40 other tissues.
DR Genevisible; Q60755; MM.
DR GO; GO:0001669; C:acrosomal vesicle; IDA:MGI.
DR GO; GO:0150056; C:amylin receptor complex 1; ISO:MGI.
DR GO; GO:0150057; C:amylin receptor complex 2; ISO:MGI.
DR GO; GO:0150058; C:amylin receptor complex 3; ISO:MGI.
DR GO; GO:0030424; C:axon; ISO:MGI.
DR GO; GO:0005929; C:cilium; IDA:MGI.
DR GO; GO:0043005; C:neuron projection; ISO:MGI.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0097643; F:amylin receptor activity; ISO:MGI.
DR GO; GO:0032841; F:calcitonin binding; ISO:MGI.
DR GO; GO:0001635; F:calcitonin gene-related peptide receptor activity; ISO:MGI.
DR GO; GO:0004948; F:calcitonin receptor activity; IDA:MGI.
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; IDA:MGI.
DR GO; GO:0007188; P:adenylate cyclase-modulating G protein-coupled receptor signaling pathway; ISO:MGI.
DR GO; GO:0097647; P:amylin receptor signaling pathway; ISO:MGI.
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:MGI.
DR GO; GO:0030279; P:negative regulation of ossification; IMP:MGI.
DR GO; GO:0001503; P:ossification; IMP:MGI.
DR GO; GO:0030316; P:osteoclast differentiation; IDA:MGI.
DR GO; GO:0045762; P:positive regulation of adenylate cyclase activity; ISO:MGI.
DR GO; GO:1905665; P:positive regulation of calcium ion import across plasma membrane; ISO:MGI.
DR GO; GO:0010942; P:positive regulation of cell death; ISO:MGI.
DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IDA:MGI.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; ISO:MGI.
DR GO; GO:0010628; P:positive regulation of gene expression; ISO:MGI.
DR GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; ISO:MGI.
DR GO; GO:0010739; P:positive regulation of protein kinase A signaling; ISO:MGI.
DR GO; GO:0051897; P:positive regulation of protein kinase B signaling; ISO:MGI.
DR GO; GO:0043488; P:regulation of mRNA stability; IDA:MGI.
DR GO; GO:1904645; P:response to amyloid-beta; ISO:MGI.
DR GO; GO:0051384; P:response to glucocorticoid; ISO:MGI.
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..41
FT /evidence="ECO:0000255"
FT CHAIN 42..533
FT /note="Calcitonin receptor"
FT /id="PRO_0000012807"
FT TOPO_DOM 42..170
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 171..190
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 191..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..274
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 275..297
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 298..314
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 315..334
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 335..350
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 351..374
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 375..397
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 398..415
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 416..427
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 428..449
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 450..533
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 45
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 90
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 142
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 147
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 72..98
FT /evidence="ECO:0000250"
FT DISULFID 89..129
FT /evidence="ECO:0000250"
FT DISULFID 112..151
FT /evidence="ECO:0000250"
FT VAR_SEQ 234..270
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_053294"
FT CONFLICT 257
FT /note="S -> C (in Ref. 1; AAA69521)"
FT /evidence="ECO:0000305"
FT CONFLICT 473
FT /note="Missing (in Ref. 1; AAA69521)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 533 AA; 62469 MW; 2598AF1EC7AA570B CRC64;
MTPRRSRVKR RNLRKPKMRF LLVNRFTLLL LLLVSPTPVL QAPTNLTDSG LDQEPFLYLV
GRKKLLDAQY KCYDRIHQLP SYEGEGLYCN RTWDGWMCWD DTPAGATAYQ HCPDYFPDFD
TAEKVSKYCD ENGEWFRHPD SNRTWSNYTL CNAFTSEKLQ NAYVLYYLAL VGHSLSIAAL
VASMLIFWIF KNLSCQRVTL HKHMFLTYIL NSIIIIIHLV EVVPNGDLVR RDPMHIFHHN
THMWTMQWEL SPPLPLSAHE GKMDPHASEV ISCKVLHFLH QYMMSCNYFW MLCEGIYLHT
LIVMAVFTDE QRLRWYYLLG WGFPIVPTII HAITRALYYN DNCWLSAETH LLYIIHGPVM
VALVVNFFFL LNIVRVLVTK MRQTHEAESY MYLKAVKATM VLVPLLGIQF VVFPWRPSNK
VLGKIYDYLM HSLIHFQGFF VATIYCFCNH EVQVTLKRQW TQFKIQWSQR WGRRRRPTNR
VVSAPRAVAF AEPDGLPIYI CHQEPRNPPI SNNEGEESTE MIPMNVIQQD ASA
