CALCR_HUMAN
ID CALCR_HUMAN Reviewed; 474 AA.
AC P30988; A4D1G6; F5H605; O14585; Q13941; Q5ZGL8; Q659U6; Q6DJU8; Q6T712;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 03-JUL-2019, sequence version 3.
DT 03-AUG-2022, entry version 215.
DE RecName: Full=Calcitonin receptor {ECO:0000305};
DE Short=CT-R;
DE Flags: Precursor;
GN Name=CALCR {ECO:0000312|HGNC:HGNC:1440};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC TISSUE=Ovarian carcinoma;
RX PubMed=1331173; DOI=10.1172/jci116046;
RA Gorn A.H., Lin H.Y., Yamin M., Auron P.E., Flannery M.R., Tapp D.R.,
RA Manning C.A., Lodish H.F., Krane S.M., Goldring S.R.;
RT "Cloning, characterization, and expression of a human calcitonin receptor
RT from an ovarian carcinoma cell line.";
RL J. Clin. Invest. 90:1726-1735(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT LEU-447.
RX PubMed=8078488;
RA Kuestner R.E., Elrod R.D., Grant F.J., Hagen F.S., Kuijper J.L.,
RA Mathewes S.L., O'Hara P.J., Sheppard P.O., Stroop S.D., Thompson D.L.,
RA Whitmore T.E., Findlays D.M., Houssamis S., Sexton P.M., Moore E.E.;
RT "Cloning and characterization of an abundant subtype of the human
RT calcitonin receptor.";
RL Mol. Pharmacol. 46:246-255(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3), ALTERNATIVE SPLICING, AND
RP VARIANT LEU-447.
RC TISSUE=Mammary carcinoma;
RX PubMed=7588285; DOI=10.1210/endo.136.12.7588285;
RA Albrandt K., Brady E.M.G., Moore C.X., Mull E., Sierzega M.E., Beaumont K.;
RT "Molecular cloning and functional expression of a third isoform of the
RT human calcitonin receptor and partial characterization of the calcitonin
RT receptor gene.";
RL Endocrinology 136:5377-5384(1995).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT LEU-447.
RX PubMed=8143880; DOI=10.1016/0014-5793(94)80503-2;
RA Frendo J.L., Pichaud F., Delage-Mourroux R., Bouizar Z., Segond N.,
RA Moukhtar M.S., Jullienne A.;
RT "An isoform of the human calcitonin receptor is expressed in TT cells and
RT in medullary carcinoma of the thyroid.";
RL FEBS Lett. 342:214-216(1994).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Mammary carcinoma;
RX PubMed=10570950; DOI=10.1016/s0014-5793(99)01176-x;
RA Nishikawa T., Ishikawa H., Yamamoto S., Koshihara Y.;
RT "A novel calcitonin receptor gene in human osteoclasts from normal bone
RT marrow.";
RL FEBS Lett. 458:409-414(1999).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 5 AND 6).
RX PubMed=15563840; DOI=10.1016/j.gene.2004.08.019;
RA Beaudreuil J., Balasubramanian S., Chenais J., Taboulet J., Frenkian M.,
RA Orcel P., Jullienne A., Horne W., de Vernejoul M.C., Cressent M.;
RT "Molecular characterization of two novel isoforms of the human calcitonin
RT receptor.";
RL Gene 343:143-151(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT LEU-447.
RC TISSUE=Cartilage;
RA Bonnefond C.;
RT "Identification of the human calcitonin receptor expressed in
RT osteoarthritis chondrocytes.";
RL Submitted (JUN-2010) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT LEU-447.
RC TISSUE=Kidney;
RA King M.M., Aronstam R.S., Sharma S.V.;
RT "cDNA clones of human proteins involved in signal transduction sequenced by
RT the Guthrie cDNA resource center (www.cdna.org).";
RL Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT LEU-447.
RC TISSUE=Amygdala;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT LEU-447.
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [11]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT LEU-447.
RX PubMed=12690205; DOI=10.1126/science.1083423;
RA Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K.,
RA Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R.,
RA Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A.,
RA Kanematsu E., Gentles S., Christopoulos C.C., Choufani S., Kwasnicka D.,
RA Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S.,
RA Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R.,
RA Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N.,
RA Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E.,
RA Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R.,
RA Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T.,
RA Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W.,
RA Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A.,
RA Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X.,
RA Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E.,
RA Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H.,
RA Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J.,
RA Adams M.D., Tsui L.-C.;
RT "Human chromosome 7: DNA sequence and biology.";
RL Science 300:767-772(2003).
RN [12]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT LEU-447.
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [13]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT LEU-447.
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).
RN [14]
RP PROTEIN SEQUENCE OF 25-39.
RX PubMed=15340161; DOI=10.1110/ps.04682504;
RA Zhang Z., Henzel W.J.;
RT "Signal peptide prediction based on analysis of experimentally verified
RT cleavage sites.";
RL Protein Sci. 13:2819-2824(2004).
RN [15]
RP ALTERNATIVE SPLICING.
RC TISSUE=Placenta;
RX PubMed=7720653; DOI=10.1210/endo.136.5.7720653;
RA Nussenzveig D.R., Mathew S., Gershengorn M.C.;
RT "Alternative splicing of a 48-nucleotide exon generates two isoforms of the
RT human calcitonin receptor.";
RL Endocrinology 136:2047-2051(1995).
RN [16]
RP ALTERNATIVE SPLICING.
RX PubMed=7733946; DOI=10.1006/bbrc.1995.1562;
RA Nakamura M., Hashimoto T., Nakajima T., Ichii S., Furuyama J., Ishihara Y.,
RA Kakudo K.;
RT "A new type of human calcitonin receptor isoform generated by alternative
RT splicing.";
RL Biochem. Biophys. Res. Commun. 209:744-751(1995).
RN [17]
RP ALTERNATIVE SPLICING, AND FUNCTION.
RX PubMed=7476993; DOI=10.1210/mend.9.8.7476993;
RA Moore E.E., Kuestner R.E., Stroop S.D., Grant F.J., Matthewes S.L.,
RA Brady C.L., Sexton P.M., Findlay D.M.;
RT "Functionally different isoforms of the human calcitonin receptor result
RT from alternative splicing of the gene transcript.";
RL Mol. Endocrinol. 9:959-968(1995).
RN [18]
RP ALTERNATIVE PROMOTER USAGE.
RX PubMed=10860825; DOI=10.1006/bbrc.2000.2842;
RA Hebden C., Smalt R., Chambers T., Pondel M.D.;
RT "Multiple promoters regulate human calcitonin receptor gene expression.";
RL Biochem. Biophys. Res. Commun. 272:738-743(2000).
RN [19]
RP INTERACTION WITH GPRASP2.
RX PubMed=15086532; DOI=10.1111/j.1471-4159.2004.02411.x;
RA Simonin F., Karcher P., Boeuf J.J.-M., Matifas A., Kieffer B.L.;
RT "Identification of a novel family of G protein-coupled receptor associated
RT sorting proteins.";
RL J. Neurochem. 89:766-775(2004).
RN [20]
RP INVOLVEMENT IN LUMBAR BMD.
RX PubMed=9675109; DOI=10.1006/bbrc.1998.8880;
RA Masi L., Becherini L., Colli E., Gennari L., Mansani R., Falchetti A.,
RA Becorpi A.M., Cepollaro C., Gonnelli S., Tanini A., Brandi M.L.;
RT "Polymorphisms of the calcitonin receptor gene are associated with bone
RT mineral density in postmenopausal Italian women.";
RL Biochem. Biophys. Res. Commun. 248:190-195(1998).
RN [21]
RP ALTERNATIVE SPLICING (ISOFORM 4).
RX PubMed=22946511; DOI=10.1111/j.1476-5381.2012.02197.x;
RA Qi T., Dong M., Watkins H.A., Wootten D., Miller L.J., Hay D.L.;
RT "Receptor activity-modifying protein-dependent impairment of calcitonin
RT receptor splice variant Delta(1-47)hCT((a)) function.";
RL Br. J. Pharmacol. 168:644-657(2013).
RN [22]
RP ASSOCIATION OF VARIANT LEU-447 WITH LOWER LUMBAR BMD.
RX PubMed=9571205; DOI=10.1006/bbrc.1998.8445;
RA Masi L., Becherini L., Gennari L., Colli E., Mansani R., Falchetti A.,
RA Cepollaro C., Gonnelli S., Tanini A., Brandi M.L.;
RT "Allelic variants of human calcitonin receptor: distribution and
RT association with bone mass in postmenopausal Italian women.";
RL Biochem. Biophys. Res. Commun. 245:622-626(1998).
RN [23]
RP VARIANT LEU-447.
RX PubMed=9817931; DOI=10.1093/hmg/7.13.2129;
RA Taboulet J., Frenkian M., Frendo J.L., Feingold N., Jullienne A.,
RA de Vernejoul M.-C.;
RT "Calcitonin receptor polymorphism is associated with a decreased fracture
RT risk in post-menopausal women.";
RL Hum. Mol. Genet. 7:2129-2133(1998).
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 -!- FUNCTION: [Isoform 2]: Receptor for calcitonin but is unable to couple
CC to G proteins and activate adenylyl cyclase (PubMed:7476993). Does not
CC undergo receptor internalization following ligand binding
CC (PubMed:7476993). {ECO:0000269|PubMed:7476993}.
CC -!- SUBUNIT: Interacts with GPRASP2. {ECO:0000269|PubMed:15086532}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative promoter usage, Alternative splicing; Named isoforms=6;
CC Name=1;
CC IsoId=P30988-2; Sequence=Displayed;
CC Name=2;
CC IsoId=P30988-1; Sequence=VSP_060211;
CC Name=3;
CC IsoId=P30988-3; Sequence=VSP_060209;
CC Name=4; Synonyms=Delta(1-47)hCT((a));
CC IsoId=P30988-4; Sequence=VSP_060209, VSP_060211;
CC Name=5; Synonyms=HCTR-5;
CC IsoId=P30988-5; Sequence=VSP_060212, VSP_060213;
CC Name=6; Synonyms=HCTR-6;
CC IsoId=P30988-6; Sequence=VSP_060211, VSP_060212, VSP_060213;
CC -!- POLYMORPHISM: Genetic variations in CALCR may be correlated with bone
CC mineral density (BMD). Low BMD is a risk factor for osteoporotic
CC fracture. Osteoporosis is characterized by reduced bone mineral
CC density, disruption of bone microarchitecture, and the alteration of
CC the amount and variety of non-collagenous proteins in bone.
CC Osteoporotic bones are more at risk of fracture.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 2 family.
CC {ECO:0000305}.
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DR EMBL; L00587; AAA35640.1; -; mRNA.
DR EMBL; X69920; CAA49541.1; -; mRNA.
DR EMBL; U26553; AAC50300.1; -; mRNA.
DR EMBL; U26554; AAC50301.1; -; mRNA.
DR EMBL; X82466; CAA57849.1; -; mRNA.
DR EMBL; S77876; AAD14268.1; -; Genomic_DNA.
DR EMBL; S77875; AAD14268.1; JOINED; Genomic_DNA.
DR EMBL; AB022177; BAA86929.1; -; mRNA.
DR EMBL; AB022178; BAA86928.1; -; mRNA.
DR EMBL; AJ831406; CAH40796.1; -; mRNA.
DR EMBL; AJ831407; CAH40797.1; -; mRNA.
DR EMBL; FN994995; CBN80567.1; -; mRNA.
DR EMBL; FN994996; CBN80568.1; -; mRNA.
DR EMBL; AY430048; AAR06949.1; -; mRNA.
DR EMBL; AK313996; BAG36708.1; -; mRNA.
DR EMBL; AC003078; AAB83945.1; -; Genomic_DNA.
DR EMBL; AC005024; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH236949; EAL24142.1; -; Genomic_DNA.
DR EMBL; CH471091; EAW76814.1; -; Genomic_DNA.
DR EMBL; BC069611; AAH69611.1; -; mRNA.
DR EMBL; BC075028; AAH75028.2; -; mRNA.
DR CCDS; CCDS55125.1; -. [P30988-1]
DR CCDS; CCDS5631.1; -. [P30988-2]
DR PIR; I37217; I37217.
DR PIR; S34486; S34486.
DR RefSeq; NP_001158209.1; NM_001164737.1.
DR RefSeq; NP_001158210.1; NM_001164738.1.
DR RefSeq; NP_001733.1; NM_001742.3.
DR PDB; 5II0; X-ray; 2.10 A; A/B/C=25-144.
DR PDB; 5UZ7; EM; 4.10 A; R=25-474.
DR PDB; 6NIY; EM; 3.34 A; R=1-474.
DR PDB; 6PFO; X-ray; 1.78 A; A/B=38-141.
DR PDB; 6PGQ; X-ray; 2.85 A; A=39-141.
DR PDB; 7TYF; EM; 2.20 A; R=25-474.
DR PDB; 7TYH; EM; 3.30 A; R=25-474.
DR PDB; 7TYI; EM; 3.30 A; R=25-474.
DR PDB; 7TYL; EM; 3.30 A; R=25-474.
DR PDB; 7TYN; EM; 2.60 A; R=25-474.
DR PDB; 7TYO; EM; 2.70 A; R=25-474.
DR PDB; 7TYW; EM; 3.00 A; R=25-474.
DR PDB; 7TYX; EM; 2.55 A; R=25-474.
DR PDB; 7TYY; EM; 3.00 A; R=25-474.
DR PDB; 7TZF; EM; 2.40 A; R=25-474.
DR PDBsum; 5II0; -.
DR PDBsum; 5UZ7; -.
DR PDBsum; 6NIY; -.
DR PDBsum; 6PFO; -.
DR PDBsum; 6PGQ; -.
DR PDBsum; 7TYF; -.
DR PDBsum; 7TYH; -.
DR PDBsum; 7TYI; -.
DR PDBsum; 7TYL; -.
DR PDBsum; 7TYN; -.
DR PDBsum; 7TYO; -.
DR PDBsum; 7TYW; -.
DR PDBsum; 7TYX; -.
DR PDBsum; 7TYY; -.
DR PDBsum; 7TZF; -.
DR AlphaFoldDB; P30988; -.
DR SMR; P30988; -.
DR BioGRID; 107250; 6.
DR ComplexPortal; CPX-2173; Amylin receptor 1 complex.
DR ComplexPortal; CPX-3186; Amylin receptor 2 complex.
DR ComplexPortal; CPX-3187; Amylin receptor 3 complex.
DR IntAct; P30988; 11.
DR MINT; P30988; -.
DR STRING; 9606.ENSP00000352561; -.
DR ChEMBL; CHEMBL1832; -.
DR DrugBank; DB01278; Pramlintide.
DR DrugBank; DB00017; Salmon calcitonin.
DR DrugCentral; P30988; -.
DR GuidetoPHARMACOLOGY; 43; -.
DR TCDB; 9.A.14.4.1; the g-protein-coupled receptor (gpcr) family.
DR GlyGen; P30988; 4 sites.
DR iPTMnet; P30988; -.
DR PhosphoSitePlus; P30988; -.
DR BioMuta; CALCR; -.
DR DMDM; 550544247; -.
DR MassIVE; P30988; -.
DR PaxDb; P30988; -.
DR PeptideAtlas; P30988; -.
DR PRIDE; P30988; -.
DR ProteomicsDB; 27039; -.
DR ProteomicsDB; 54752; -. [P30988-1]
DR ProteomicsDB; 54753; -. [P30988-2]
DR ProteomicsDB; 54754; -. [P30988-3]
DR ProteomicsDB; 620; -.
DR DNASU; 799; -.
DR Ensembl; ENST00000415529.2; ENSP00000413179.1; ENSG00000004948.16. [P30988-5]
DR Ensembl; ENST00000423724.5; ENSP00000391369.1; ENSG00000004948.16. [P30988-6]
DR GeneID; 799; -.
DR KEGG; hsa:799; -.
DR UCSC; uc003umw.3; human. [P30988-2]
DR CTD; 799; -.
DR DisGeNET; 799; -.
DR GeneCards; CALCR; -.
DR HGNC; HGNC:1440; CALCR.
DR MalaCards; CALCR; -.
DR MIM; 114131; gene.
DR neXtProt; NX_P30988; -.
DR OpenTargets; ENSG00000004948; -.
DR PharmGKB; PA26032; -.
DR VEuPathDB; HostDB:ENSG00000004948; -.
DR eggNOG; KOG4564; Eukaryota.
DR GeneTree; ENSGT00940000155380; -.
DR HOGENOM; CLU_002753_4_6_1; -.
DR InParanoid; P30988; -.
DR OrthoDB; 1005634at2759; -.
DR TreeFam; TF315710; -.
DR PathwayCommons; P30988; -.
DR Reactome; R-HSA-418555; G alpha (s) signalling events.
DR Reactome; R-HSA-419812; Calcitonin-like ligand receptors.
DR Reactome; R-HSA-9660821; ADORA2B mediated anti-inflammatory cytokines production.
DR SignaLink; P30988; -.
DR BioGRID-ORCS; 799; 7 hits in 1064 CRISPR screens.
DR GeneWiki; Calcitonin_receptor; -.
DR GenomeRNAi; 799; -.
DR Pharos; P30988; Tclin.
DR PRO; PR:P30988; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; P30988; protein.
DR Bgee; ENSG00000004948; Expressed in tibia and 49 other tissues.
DR ExpressionAtlas; P30988; baseline and differential.
DR Genevisible; P30988; HS.
DR GO; GO:0150056; C:amylin receptor complex 1; IDA:ARUK-UCL.
DR GO; GO:0150057; C:amylin receptor complex 2; IDA:ARUK-UCL.
DR GO; GO:0150058; C:amylin receptor complex 3; IDA:ARUK-UCL.
DR GO; GO:0030424; C:axon; IBA:GO_Central.
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:0097643; F:amylin receptor activity; IPI:UniProtKB.
DR GO; GO:0001540; F:amyloid-beta binding; IC:ARUK-UCL.
DR GO; GO:0032841; F:calcitonin binding; IDA:UniProtKB.
DR GO; GO:0001635; F:calcitonin gene-related peptide receptor activity; IPI: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: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:0097647; P:amylin receptor signaling pathway; IDA:UniProtKB.
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; IPI:UniProtKB.
DR GO; GO:0045762; P:positive regulation of adenylate cyclase activity; IDA:UniProtKB.
DR GO; GO:1905665; P:positive regulation of calcium ion import across plasma membrane; IGI:ARUK-UCL.
DR GO; GO:0010942; P:positive regulation of cell death; IGI:ARUK-UCL.
DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IDA:UniProtKB.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IGI:ARUK-UCL.
DR GO; GO:0010628; P:positive regulation of gene expression; IGI:ARUK-UCL.
DR GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; IGI:ARUK-UCL.
DR GO; GO:0010739; P:positive regulation of protein kinase A signaling; IGI:ARUK-UCL.
DR GO; GO:0051897; P:positive regulation of protein kinase B signaling; IGI:ARUK-UCL.
DR GO; GO:1904645; P:response to amyloid-beta; IGI:ARUK-UCL.
DR GO; GO:0051384; P:response to glucocorticoid; IDA:UniProtKB.
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 1: Evidence at protein level;
KW 3D-structure; Alternative promoter usage; Alternative splicing;
KW Cell membrane; Direct protein sequencing; 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:0000269|PubMed:15340161"
FT CHAIN 25..474
FT /note="Calcitonin receptor"
FT /id="PRO_0000447620"
FT TOPO_DOM 25..152
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 153..173
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 174..186
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 187..207
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 208..233
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 234..254
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 255..258
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 259..279
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 280..296
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 297..317
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 318..340
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 341..361
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 362..373
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 374..394
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 395..474
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
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 1..47
FT /note="Missing (in isoform 3 and isoform 4)"
FT /id="VSP_060209"
FT VAR_SEQ 174
FT /note="R -> RKLTTIFPLNWKYRKAL (in isoform 2, isoform 4 and
FT isoform 6)"
FT /id="VSP_060211"
FT VAR_SEQ 268..274
FT /note="GFPLVPT -> APAFHRD (in isoform 5 and isoform 6)"
FT /id="VSP_060212"
FT VAR_SEQ 275..474
FT /note="Missing (in isoform 5 and isoform 6)"
FT /id="VSP_060213"
FT VARIANT 447
FT /note="P -> L (may be correlated with low bone mineral
FT density (BMD); dbSNP:rs1801197)"
FT /evidence="ECO:0000269|PubMed:12690205,
FT ECO:0000269|PubMed:12853948, ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:7588285,
FT ECO:0000269|PubMed:8078488, ECO:0000269|PubMed:8143880,
FT ECO:0000269|PubMed:9817931, ECO:0000269|Ref.12,
FT ECO:0000269|Ref.7, ECO:0000269|Ref.8"
FT /id="VAR_003580"
FT CONFLICT 347
FT /note="I -> T (in Ref. 3; AAC50301)"
FT /evidence="ECO:0000305"
FT HELIX 38..40
FT /evidence="ECO:0007829|PDB:6PFO"
FT HELIX 46..61
FT /evidence="ECO:0007829|PDB:6PFO"
FT STRAND 67..69
FT /evidence="ECO:0007829|PDB:6PFO"
FT STRAND 90..94
FT /evidence="ECO:0007829|PDB:6PFO"
FT STRAND 97..99
FT /evidence="ECO:0007829|PDB:6PFO"
FT STRAND 106..112
FT /evidence="ECO:0007829|PDB:6PFO"
FT TURN 122..124
FT /evidence="ECO:0007829|PDB:6PFO"
FT HELIX 132..134
FT /evidence="ECO:0007829|PDB:6PFO"
FT HELIX 139..172
FT /evidence="ECO:0007829|PDB:6NIY"
FT HELIX 174..176
FT /evidence="ECO:0007829|PDB:6NIY"
FT HELIX 179..204
FT /evidence="ECO:0007829|PDB:6NIY"
FT HELIX 218..248
FT /evidence="ECO:0007829|PDB:6NIY"
FT HELIX 259..266
FT /evidence="ECO:0007829|PDB:6NIY"
FT TURN 267..270
FT /evidence="ECO:0007829|PDB:6NIY"
FT HELIX 271..284
FT /evidence="ECO:0007829|PDB:6NIY"
FT HELIX 296..298
FT /evidence="ECO:0007829|PDB:6NIY"
FT HELIX 299..329
FT /evidence="ECO:0007829|PDB:6NIY"
FT HELIX 337..352
FT /evidence="ECO:0007829|PDB:6NIY"
FT HELIX 355..358
FT /evidence="ECO:0007829|PDB:6NIY"
FT HELIX 366..381
FT /evidence="ECO:0007829|PDB:6NIY"
FT HELIX 383..392
FT /evidence="ECO:0007829|PDB:6NIY"
FT HELIX 396..411
FT /evidence="ECO:0007829|PDB:6NIY"
SQ SEQUENCE 474 AA; 55329 MW; 0D9FA80FF16E82D9 CRC64;
MRFTFTSRCL ALFLLLNHPT PILPAFSNQT YPTIEPKPFL YVVGRKKMMD AQYKCYDRMQ
QLPAYQGEGP YCNRTWDGWL CWDDTPAGVL SYQFCPDYFP DFDPSEKVTK YCDEKGVWFK
HPENNRTWSN YTMCNAFTPE KLKNAYVLYY LAIVGHSLSI FTLVISLGIF VFFRSLGCQR
VTLHKNMFLT YILNSMIIII HLVEVVPNGE LVRRDPVSCK ILHFFHQYMM ACNYFWMLCE
GIYLHTLIVV AVFTEKQRLR WYYLLGWGFP LVPTTIHAIT RAVYFNDNCW LSVETHLLYI
IHGPVMAALV VNFFFLLNIV RVLVTKMRET HEAESHMYLK AVKATMILVP LLGIQFVVFP
WRPSNKMLGK IYDYVMHSLI HFQGFFVATI YCFCNNEVQT TVKRQWAQFK IQWNQRWGRR
PSNRSARAAA AAAEAGDIPI YICHQEPRNE PANNQGEESA EIIPLNIIEQ ESSA
