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Extracellular calcium-sensing receptor (CaR) (CaSR) (hCasR) (Parathyroid cell calcium-sensing receptor 1) (PCaR1)

 CASR_HUMAN              Reviewed;        1078 AA.
P41180; Q13912; Q16108; Q16109; Q16110; Q16379; Q2M1T0; Q4PJ19;
01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
10-MAY-2017, sequence version 3.
27-SEP-2017, entry version 187.
RecName: Full=Extracellular calcium-sensing receptor {ECO:0000305};
Short=CaR {ECO:0000303|PubMed:7759551, ECO:0000303|PubMed:8813042};
Short=CaSR;
Short=hCasR {ECO:0000303|PubMed:27386547};
AltName: Full=Parathyroid cell calcium-sensing receptor 1 {ECO:0000303|PubMed:8698326};
Short=PCaR1 {ECO:0000303|PubMed:8698326};
Flags: Precursor;
Name=CASR {ECO:0000312|HGNC:HGNC:1514};
Synonyms=GPRC2A, PCAR1 {ECO:0000303|PubMed:8698326};
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS HYPOC1 LYS-118; LEU-128;
MET-151; LYS-191 AND SER-612, AND CHARACTERIZATION OF VARIANTS HYPOC1
LEU-128; MET-151 AND LYS-191.
PubMed=8813042; DOI=10.1056/NEJM199610103351505;
Pearce S.H.S., Williamson C., Kifor O., Bai M., Coulthard M.G.,
Davies M., Lewis-Barned N., McCredie D., Powell H., Kendall-Taylor P.,
Brown E.M., Thakker R.V.;
"A familial syndrome of hypocalcemia with hypercalciuria due to
mutations in the calcium-sensing receptor.";
N. Engl. J. Med. 335:1115-1122(1996).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, AND VARIANT
GLY-990.
TISSUE=Parathyroid;
PubMed=7759551; DOI=10.1074/jbc.270.21.12919;
Garrett J.E., Capuano I.V., Hammerland L.G., Hung B.C., Brown E.M.,
Hebert S.C., Nemeth E.F., Fuller F.;
"Molecular cloning and functional expression of human parathyroid
calcium receptor cDNAs.";
J. Biol. Chem. 270:12919-12925(1995).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Kidney;
PubMed=7677761; DOI=10.1006/bbrc.1995.2318;
Aida K., Koishi S., Tawata M., Onaya T.;
"Molecular cloning of a putative Ca(2+)-sensing receptor cDNA from
human kidney.";
Biochem. Biophys. Res. Commun. 214:524-529(1995).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=8756555; DOI=10.1210/endo.137.9.8756555;
Freichel M., Zink-Lorenz A., Holloschi A., Hafner M., Flockerzi V.,
Raue F.;
"Expression of a calcium-sensing receptor in a human medullary thyroid
carcinoma cell line and its contribution to calcitonin secretion.";
Endocrinology 137:3842-3848(1996).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS SER-986; GLY-990 AND
GLN-1011.
SeattleSNPs variation discovery resource;
Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-61, AND VARIANT HHC1 ALA-39.
PubMed=7673400; DOI=10.1210/jcem.80.9.7673400;
Aida K., Koishi S., Inoue M., Nakazato M., Tawata M., Onaya T.;
"Familial hypocalciuric hypercalcemia associated with mutation in the
human Ca(2+)-sensing receptor gene.";
J. Clin. Endocrinol. Metab. 80:2594-2598(1995).
[8]
NUCLEOTIDE SEQUENCE [MRNA] OF 643-908.
PubMed=8613532; DOI=10.1172/JCI118501;
Bikle D.D., Ratnam A., Mauro T., Harris J., Pillai S.;
"Changes in calcium responsiveness and handling during keratinocyte
differentiation. Potential role of the calcium receptor.";
J. Clin. Invest. 97:1085-1093(1996).
[9]
INTERACTION WITH VCP AND RNF19A, GLYCOSYLATION, AND UBIQUITINATION.
PubMed=16513638; DOI=10.1074/jbc.M513552200;
Huang Y., Niwa J., Sobue G., Breitwieser G.E.;
"Calcium-sensing receptor ubiquitination and degradation mediated by
the E3 ubiquitin ligase dorfin.";
J. Biol. Chem. 281:11610-11617(2006).
[10]
DOMAIN.
PubMed=17360426; DOI=10.1073/pnas.0611577104;
Muto T., Tsuchiya D., Morikawa K., Jingami H.;
"Structures of the extracellular regions of the group II/III
metabotropic glutamate receptors.";
Proc. Natl. Acad. Sci. U.S.A. 104:3759-3764(2007).
[11]
SUBCELLULAR LOCATION, AND GLYCOSYLATION.
PubMed=20861236; DOI=10.1210/en.2010-0422;
Zhuang X., Adipietro K.A., Datta S., Northup J.K., Ray K.;
"Rab1 small GTP-binding protein regulates cell surface trafficking of
the human calcium-sensing receptor.";
Endocrinology 151:5114-5123(2010).
[12]
ENZYME REGULATION, AND MUTAGENESIS OF CYS-482.
PubMed=26290606;
Alexander S.T., Hunter T., Walter S., Dong J., Maclean D., Baruch A.,
Subramanian R., Tomlinson J.;
"Critical cysteine residues in both the calcium-sensing receptor and
the allosteric activator AMG 416 underlie the mechanism of action.";
Mol. Pharmacol. 88:853-865(2015).
[13] {ECO:0000244|PDB:5K5S, ECO:0000244|PDB:5K5T}
X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 20-607 IN COMPLEX WITH
CALCIUM; ANION AND TRYPTOPHAN, FUNCTION, ENZYME REGULATION, DOMAIN,
DISULFIDE BONDS, GLYCOSYLATION AT ASN-261; ASN-287; ASN-446; ASN-468;
ASN-488; ASN-541 AND ASN-594, MUTAGENESIS OF ARG-69; ASN-102; THR-145;
SER-147; SER-170; TYR-218; SER-417 AND TRP-458, CHARACTERIZATION OF
VARIANTS NSHPT ILE-100; LEU-227 AND LYS-551, AND CHARACTERIZATION OF
VARIANTS HHC1 HIS-66; MET-81; PRO-159; GLY-172; GLY-215; LYS-297 AND
GLU-557.
PubMed=27434672; DOI=10.7554/eLife.13662;
Geng Y., Mosyak L., Kurinov I., Zuo H., Sturchler E., Cheng T.C.,
Subramanyam P., Brown A.P., Brennan S.C., Mun H.C., Bush M., Chen Y.,
Nguyen T.X., Cao B., Chang D.D., Quick M., Conigrave A.D.,
Colecraft H.M., McDonald P., Fan Q.R.;
"Structural mechanism of ligand activation in human calcium-sensing
receptor.";
Elife 5:0-0(2016).
[14] {ECO:0000244|PDB:5FBH, ECO:0000244|PDB:5FBK}
X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 20-541 IN COMPLEX WITH
MAGNESIUM AND TRYPTOPHAN, FUNCTION, ENZYME REGULATION, DOMAIN,
DISULFIDE BONDS, AND MUTAGENESIS OF GLU-297.
PubMed=27386547; DOI=10.1126/sciadv.1600241;
Zhang C., Zhang T., Zou J., Miller C.L., Gorkhali R., Yang J.Y.,
Schilmiller A., Wang S., Huang K., Brown E.M., Moremen K.W., Hu J.,
Yang J.J.;
"Structural basis for regulation of human calcium-sensing receptor by
magnesium ions and an unexpected tryptophan derivative co-agonist.";
Sci. Adv. 2:E1600241-E1600241(2016).
[15]
VARIANTS HHC1 GLN-185; LYS-297 AND TRP-795.
PubMed=7916660; DOI=10.1016/0092-8674(93)90617-Y;
Pollak M.R., Brown E.M., Chou Y.-H.W., Hebert S.C., Marx S.J.,
Steinmann B., Levi T., Seidman C.E., Seidman J.G.;
"Mutations in the human Ca(2+)-sensing receptor gene cause familial
hypocalciuric hypercalcemia and neonatal severe hyperparathyroidism.";
Cell 75:1297-1303(1993).
[16]
VARIANT HYPOC1 ALA-127.
PubMed=7874174; DOI=10.1038/ng1194-303;
Pollak M.R., Brown E.M., Estep H.L., McLaine P.N., Kifor O., Park J.,
Hebert S.C., Seidman C.E., Seidman J.G.;
"Autosomal dominant hypocalcaemia caused by a Ca(2+)-sensing receptor
gene mutation.";
Nat. Genet. 8:303-307(1994).
[17]
VARIANTS HHC1 MET-62; CYS-66; MET-138; GLU-143 AND GLN-227.
PubMed=7726161;
Chou Y.-H.W., Pollak M.R., Brandi M.L., Toss G., Arnqvist H.,
Atkinson A.B., Papapoulos S.E., Marx S., Brown E.M., Seidman J.G.,
Seidman C.E.;
"Mutations in the human Ca(2+)-sensing-receptor gene that cause
familial hypocalciuric hypercalcemia.";
Am. J. Hum. Genet. 56:1075-1079(1995).
[18]
VARIANTS NSHPT LEU-227 AND TYR-582.
PubMed=8675635; DOI=10.1172/JCI118335;
Pearce S.H.S., Trump D., Wooding C., Besser G.M., Chew S.L.,
Grant D.B., Heath D.A., Hughes I.A., Paterson C.R., Whyte M.P.,
Thakker R.V.;
"Calcium-sensing receptor mutations in familial benign hypercalcemia
and neonatal hyperparathyroidism.";
J. Clin. Invest. 96:2683-2692(1995).
[19]
VARIANT FIH MET-151.
PubMed=8698326; DOI=10.1007/s004390050174;
Lovlie R., Eiken H.G., Sorheim J.I., Boman H.;
"The Ca(2+)-sensing receptor gene (PCAR1) mutation T151M in isolated
autosomal dominant hypoparathyroidism.";
Hum. Genet. 98:129-133(1996).
[20]
VARIANTS HYPOC1 THR-116; HIS-681 AND SER-806, AND VARIANT SER-851.
PubMed=8733126; DOI=10.1093/hmg/5.5.601;
Baron J., Winer K.K., Yanovski J.A., Cunningham A.W., Laue L.,
Zimmerman D., Cutler G.B. Jr.;
"Mutations in the Ca(2+)-sensing receptor gene cause autosomal
dominant and sporadic hypoparathyroidism.";
Hum. Mol. Genet. 5:601-606(1996).
[21]
VARIANTS HHC1 MET-62; CYS-66; MET-138; GLU-143; GLN-185; LYS-297 AND
TRP-795, VARIANT HYPOC1 ALA-127, FUNCTION, SUBCELLULAR LOCATION,
GLYCOSYLATION, CHARACTERIZATION OF VARIANTS HHC1 MET-62; CYS-66;
MET-138; GLU-143; GLN-185; LYS-297 AND TRP-795, AND CHARACTERIZATION
OF VARIANT HYPOC1 ALA-127.
PubMed=8702647;
Bai M., Quinn S., Trivedi S., Kifor O., Pearce S.H.S., Pollak M.R.,
Krapcho K., Hebert S.C., Brown E.M.;
"Expression and characterization of inactivating and activating
mutations in the human Ca2+o-sensing receptor.";
J. Biol. Chem. 271:19537-19545(1996).
[22]
VARIANTS HHC1 PRO-53; LEU-55; GLN-185; GLY-215; TYR-657 AND ARG-748,
VARIANTS SER-986; GLY-990 AND GLN-1011, AND CHARACTERIZATION OF
VARIANTS HHC1 PRO-53; LEU-55 AND GLY-215.
PubMed=8636323; DOI=10.1210/jcem.81.4.8636323;
Heath H. III, Odelberg S., Jackson C.E., Teh B.T., Hayward N.,
Larsson C., Buist N.R., Krapcho K.J., Hung B.C., Capuano I.V.,
Garrett J.E., Leppert M.F.;
"Clustered inactivating mutations and benign polymorphisms of the
calcium receptor gene in familial benign hypocalciuric hypercalcemia
suggest receptor functional domains.";
J. Clin. Endocrinol. Metab. 81:1312-1317(1996).
[23]
VARIANTS HHC1 LEU-55; ASP-178; SER-221 AND ILE-817, VARIANTS HYPOC1
LEU-128; MET-151 AND LYS-191, VARIANT NSHPT LEU-227, CHARACTERIZATION
OF VARIANTS HHC1 LEU-55; ASP-178; SER-221 AND ILE-817, FUNCTION,
CHARACTERIZATION OF VARIANTS HYPOC1 LEU-128; MET-151 AND LYS-191, AND
CHARACTERIZATION OF VARIANT NSHPT LEU-227.
PubMed=8878438; DOI=10.1172/JCI118987;
Pearce S.H.S., Bai M., Quinn S.J., Kifor O., Brown E.M., Thakker R.V.;
"Functional characterization of calcium-sensing receptor mutations
expressed in human embryonic kidney cells.";
J. Clin. Invest. 98:1860-1866(1996).
[24]
VARIANT HHC1 ARG-174.
PubMed=9298824;
DOI=10.1002/(SICI)1098-1004(1997)10:3<233::AID-HUMU9>3.3.CO;2-G;
Ward B.K., Stuckey B.G.A., Gutteridge D.H., Laing N.G., Pullan P.T.,
Ratajczak T.;
"A novel mutation (L174R) in the Ca2+-sensing receptor gene associated
with familial hypocalciuric hypercalcemia.";
Hum. Mutat. 10:233-235(1997).
[25]
VARIANTS HYPOC1 LYS-118; ARG-773 AND SER-806, AND CHARACTERIZATION OF
VARIANTS HYPOC1 LYS-118; ARG-773 AND SER-806.
PubMed=9253358; DOI=10.1210/jc.82.8.2710;
De Luca F., Ray K., Mancilla E.E., Fan G.-F., Winer K.K., Gore P.,
Spiegel A.M., Baron J.;
"Sporadic hypoparathyroidism caused by de Novo gain-of-function
mutations of the Ca(2+)-sensing receptor.";
J. Clin. Endocrinol. Metab. 82:2710-2715(1997).
[26]
VARIANT NSHPT GLU-670.
PubMed=9253359; DOI=10.1210/jcem.82.8.4135;
Kobayashi M., Tanaka H., Tsuzuki K., Tsuyuki M., Igaki H.,
Ichinose Y., Aya K., Nishioka N., Seino Y.;
"Two novel missense mutations in calcium-sensing receptor gene
associated with neonatal severe hyperparathyroidism.";
J. Clin. Endocrinol. Metab. 82:2716-2719(1997).
[27]
VARIANT HYPOC1 CYS-788, AND CHARACTERIZATION OF VARIANT HYPOC1
CYS-788.
PubMed=9661634; DOI=10.1210/jcem.83.7.4920;
Watanabe T., Bai M., Lane C.R., Matsumoto S., Minamitani K.,
Minagawa M., Niimi H., Brown E.M., Yasuda T.;
"Familial hypoparathyroidism: identification of a novel gain of
function mutation in transmembrane domain 5 of the calcium-sensing
receptor.";
J. Clin. Endocrinol. Metab. 83:2497-2502(1998).
[28]
VARIANT ARG-27, CHARACTERIZATION OF VARIANT ARG-27, AND INVOLVEMENT IN
PRIMARY HYPERPARATHYROIDISM.
PubMed=10468915; DOI=10.1046/j.1365-2265.1999.00729.x;
Chikatsu N., Fukumoto S., Suzawa M., Tanaka Y., Takeuchi Y.,
Takeda S., Tamura Y., Matsumoto T., Fujita T.;
"An adult patient with severe hypercalcaemia and hypocalciuria due to
a novel homozygous inactivating mutation of calcium-sensing
receptor.";
Clin. Endocrinol. (Oxf.) 50:537-543(1999).
[29]
VARIANT HYPOC1 ASN-47, AND CHARACTERIZATION OF VARIANT HYPOC1 ASN-47.
PubMed=9920108; DOI=10.1210/jcem.84.1.5385;
Okazaki R., Chikatsu N., Nakatsu M., Takeuchi Y., Ajima M., Miki J.,
Fujita T., Arai M., Totsuka Y., Tanaka K., Fukumoto S.;
"A novel activating mutation in calcium-sensing receptor gene
associated with a family of autosomal dominant hypocalcemia.";
J. Clin. Endocrinol. Metab. 84:363-366(1999).
[30]
VARIANT HYPOC1 VAL-616, AND CHARACTERIZATION OF VARIANT HYPOC1
VAL-616.
PubMed=10487661; DOI=10.1210/jcem.84.9.5977;
Stock J.L., Brown R.S., Baron J., Coderre J.A., Mancilla E.,
De Luca F., Ray K., Mericq M.V.;
"Autosomal dominant hypoparathyroidism associated with short stature
and premature osteoarthritis.";
J. Clin. Endocrinol. Metab. 84:3036-3040(1999).
[31]
VARIANT SER-986, AND ASSOCIATION WITH SERUM LEVEL OF CALCIUM.
PubMed=10023897; DOI=10.1016/S0140-6736(98)06434-4;
Cole D.E.C., Peltekova V.D., Rubin L.A., Hawker G.A., Vieth R.,
Liew C.C., Hwang D.M., Evrovski J., Hendy G.N.;
"A986S polymorphism of the calcium-sensing receptor and circulating
calcium concentrations.";
Lancet 353:112-115(1999).
[32]
VARIANT HYPERCALCIURIC HYPERCALCEMIA LEU-881, AND CHARACTERIZATION OF
VARIANT HYPERCALCIURIC HYPERCALCEMIA LEU-881.
PubMed=10843194; DOI=10.1210/jcem.85.5.6477;
Carling T., Szabo E., Bai M., Ridefelt P., Westin G., Gustavsson P.,
Trivedi S., Hellman P., Brown E.M., Dahl N., Rastad J.;
"Familial hypercalcemia and hypercalciuria caused by a novel mutation
in the cytoplasmic tail of the calcium receptor.";
J. Clin. Endocrinol. Metab. 85:2042-2047(2000).
[33]
VARIANT HHC1 GLU-557.
PubMed=11762699; DOI=10.1385/ENDO:15:3:277;
Nakayama T., Minato M., Nakagawa M., Soma M., Tobe H., Aoi N.,
Kosuge K., Sato M., Ozawa Y., Kanmatsuse K., Kokubun S.;
"A novel mutation in Ca2+-sensing receptor gene in familial
hypocalciuric hypercalcemia.";
Endocrine 15:277-282(2001).
[34]
VARIANT SER-986, ASSOCIATION WITH SERUM LEVEL OF CALCIUM, AND
PREDISPOSING FACTOR IN DISORDERS OF BONE AND MINERAL METABOLISM.
PubMed=11161843; DOI=10.1006/mgme.2000.3126;
Cole D.E.C., Vieth R., Trang H.M., Wong B.Y.-L., Hendy G.N.,
Rubin L.A.;
"Association between total serum calcium and the A986S polymorphism of
the calcium-sensing receptor gene.";
Mol. Genet. Metab. 72:168-174(2001).
[35]
VARIANT HYPOC1 PHE-820, CHARACTERIZATION OF VARIANT HYPOC1 PHE-820,
AND VARIANT GLY-990.
PubMed=12050233; DOI=10.1210/jcem.87.6.8531;
Nagase T., Murakami T., Tsukada T., Kitamura R., Chikatsu N.,
Takeo H., Takata N., Yasuda H., Fukumoto S., Tanaka Y., Nagata N.,
Yamaguchi K., Akatsu T., Yamamoto M.;
"A family of autosomal dominant hypocalcemia with a positive
correlation between serum calcium and magnesium: identification of a
novel gain of function mutation (Ser(820)Phe) in the calcium-sensing
receptor.";
J. Clin. Endocrinol. Metab. 87:2681-2687(2002).
[36]
VARIANTS HYPOC1 PRO-125 AND GLU-843, AND CHARACTERIZATION OF VARIANTS
HYPOC1 PRO-125 AND GLU-843.
PubMed=12107202; DOI=10.1210/jcem.87.7.8639;
Sato K., Hasegawa Y., Nakae J., Nanao K., Takahashi I., Tajima T.,
Shinohara N., Fujieda K.;
"Hydrochlorothiazide effectively reduces urinary calcium excretion in
two Japanese patients with gain-of-function mutations of the calcium-
sensing receptor gene.";
J. Clin. Endocrinol. Metab. 87:3068-3073(2002).
[37]
VARIANTS HYPOC1 TRP-131 AND GLU-843.
PubMed=12241879; DOI=10.1016/S0140-6736(02)09842-2;
Watanabe S., Fukumoto S., Chang H., Takeuchi Y., Hasegawa Y.,
Okazaki R., Chikatsu N., Fujita T.;
"Association between activating mutations of calcium-sensing receptor
and Bartter's syndrome.";
Lancet 360:692-694(2002).
[38]
VARIANT HYPOC1 LYS-604, AND CHARACTERIZATION OF VARIANT HYPOC1
LYS-604.
PubMed=12574188; DOI=10.1210/jc.2002-020081;
Tan Y.M., Cardinal J., Franks A.H., Mun H.-C., Lewis N., Harris L.B.,
Prins J.B., Conigrave A.D.;
"Autosomal dominant hypocalcemia: a novel activating mutation (E604K)
in the cysteine-rich domain of the calcium-sensing receptor.";
J. Clin. Endocrinol. Metab. 88:605-610(2003).
[39]
VARIANT HYPOC1 LEU-788, AND CHARACTERIZATION OF VARIANT HYPOC1
LEU-788.
PubMed=12915654; DOI=10.1210/jc.2003-030409;
Hendy G.N., Minutti C., Canaff L., Pidasheva S., Yang B., Nouhi Z.,
Zimmerman D., Wei C., Cole D.E.C.;
"Recurrent familial hypocalcemia due to germline mosaicism for an
activating mutation of the calcium-sensing receptor gene.";
J. Clin. Endocrinol. Metab. 88:3674-3681(2003).
[40]
VARIANTS SER-986; GLY-990 AND GLN-1011, AND ASSOCIATION WITH SERUM
LEVEL OF CALCIUM.
PubMed=15531522; DOI=10.1210/jc.2004-0129;
Scillitani A., Guarnieri V., De Geronimo S., Muscarella L.A.,
Battista C., D'Agruma L., Bertoldo F., Florio C., Minisola S.,
Hendy G.N., Cole D.E.C.;
"Blood ionized calcium is associated with clustered polymorphisms in
the carboxyl-terminal tail of the calcium-sensing receptor.";
J. Clin. Endocrinol. Metab. 89:5634-5638(2004).
[41]
VARIANT HHC1 PRO-13, AND CHARACTERIZATION OF VARIANT HHC1 PRO-13.
PubMed=15579740; DOI=10.1210/jc.2004-1046;
Miyashiro K., Kunii I., Manna T.D., de Menezes Filho H.C., Damiani D.,
Setian N., Hauache O.M.;
"Severe hypercalcemia in a 9-year-old Brazilian girl due to a novel
inactivating mutation of the calcium-sensing receptor.";
J. Clin. Endocrinol. Metab. 89:5936-5941(2004).
[42]
VARIANTS NSHPT ILE-100; LYS-336 DEL; PRO-650 AND MET-689, AND VARIANTS
SER-986; GLY-990 AND GLN-1011.
PubMed=14985373; DOI=10.1136/jmg.2003.016725;
Warner J., Epstein M., Sweet A., Singh D., Burgess J., Stranks S.,
Hill P., Perry-Keene D., Learoyd D., Robinson B., Birdsey P.,
Mackenzie E., Teh B.T., Prins J.B., Cardinal J.;
"Genetic testing in familial isolated hyperparathyroidism: unexpected
results and their implications.";
J. Med. Genet. 41:155-160(2004).
[43]
VARIANT HYPOC1 LYS-767, AND VARIANT GLY-990.
PubMed=15551332; DOI=10.1002/ajmg.a.30403;
Uckun-Kitapci A., Underwood L.E., Zhang J., Moats-Staats B.;
"A novel mutation (E767K) in the second extracellular loop of the
calcium sensing receptor in a family with autosomal dominant
hypocalcemia.";
Am. J. Med. Genet. A 132:125-129(2005).
[44]
VARIANTS HHC1 SER-11 AND PRO-13, VARIANT ALA-14, CHARACTERIZATION OF
VARIANTS HHC1 SER-11 AND PRO-13, AND CHARACTERIZATION OF VARIANT
ALA-14.
PubMed=15879434; DOI=10.1093/hmg/ddi176;
Pidasheva S., Canaff L., Simonds W.F., Marx S.J., Hendy G.N.;
"Impaired cotranslational processing of the calcium-sensing receptor
due to signal peptide missense mutations in familial hypocalciuric
hypercalcemia.";
Hum. Mol. Genet. 14:1679-1690(2005).
[45]
VARIANT HHC1 GLN-227, SUBCELLULAR LOCATION, CHARACTERIZATION OF
VARIANT NSHPT LEU-227, AND CHARACTERIZATION OF VARIANT HHC1 GLN-227.
PubMed=15572418; DOI=10.1210/jc.2004-1791;
Wystrychowski A., Pidasheva S., Canaff L., Chudek J., Kokot F.,
Wiecek A., Hendy G.N.;
"Functional characterization of calcium-sensing receptor codon 227
mutations presenting as either familial (benign) hypocalciuric
hypercalcemia or neonatal hyperparathyroidism.";
J. Clin. Endocrinol. Metab. 90:864-870(2005).
[46]
VARIANT HHC1 GLN-465, CHARACTERIZATION OF VARIANT HHC1 GLN-465, AND
VARIANT SER-986.
PubMed=16598859; DOI=10.1016/j.bbrc.2006.02.018;
Leech C., Lohse P., Stanojevic V., Lechner A., Goeke B., Spitzweg C.;
"Identification of a novel inactivating R465Q mutation of the calcium-
sensing receptor.";
Biochem. Biophys. Res. Commun. 342:996-1002(2006).
[47]
VARIANTS HHC1 CYS-66; HIS-66 AND 583-ASN--SER-1078 DEL, SUBCELLULAR
LOCATION, SUBUNIT, GLYCOSYLATION, AND CHARACTERIZATION OF VARIANTS
CYS-66; HIS-66 AND 583-ASN--SER-1078 DEL.
PubMed=16740594; DOI=10.1093/hmg/ddl145;
Pidasheva S., Grant M., Canaff L., Ercan O., Kumar U., Hendy G.N.;
"Calcium-sensing receptor dimerizes in the endoplasmic reticulum:
biochemical and biophysical characterization of CASR mutants retained
intracellularly.";
Hum. Mol. Genet. 15:2200-2209(2006).
[48]
VARIANT HYPOC1 GLN-727, AND CHARACTERIZATION OF VARIANT HYPOC1
GLN-727.
PubMed=16608894; DOI=10.1210/jc.2005-2605;
Mittelman S.D., Hendy G.N., Fefferman R.A., Canaff L., Mosesova I.,
Cole D.E., Burkett L., Geffner M.E.;
"A hypocalcemic child with a novel activating mutation of the calcium-
sensing receptor gene: successful treatment with recombinant human
parathyroid hormone.";
J. Clin. Endocrinol. Metab. 91:2474-2479(2006).
[49]
VARIANT HHC1 CYS-180, AND CHARACTERIZATION OF VARIANT HHC1 CYS-180.
PubMed=17473068; DOI=10.1210/jc.2007-0123;
Zajickova K., Vrbikova J., Canaff L., Pawelek P.D., Goltzman D.,
Hendy G.N.;
"Identification and functional characterization of a novel mutation in
the calcium-sensing receptor gene in familial hypocalciuric
hypercalcemia: modulation of clinical severity by vitamin D status.";
J. Clin. Endocrinol. Metab. 92:2616-2623(2007).
[50]
VARIANT NSHPT LYS-551, VARIANT SER-986, FUNCTION, SUBCELLULAR
LOCATION, AND CHARACTERIZATION OF VARIANT NSHPT LYS-551.
PubMed=17555508; DOI=10.1111/j.1365-2265.2007.02896.x;
Toke J., Czirjak G., Patocs A., Enyedi B., Gergics P., Csakvary V.,
Enyedi P., Toth M.;
"Neonatal severe hyperparathyroidism associated with a novel de novo
heterozygous R551K inactivating mutation and a heterozygous A986S
polymorphism of the calcium-sensing receptor gene.";
Clin. Endocrinol. (Oxf.) 67:385-392(2007).
[51]
VARIANTS HHC1 ARG-21; ASN-171; GLN-221; THR-225; PHE-271; ARG-397;
ARG-509; ARG-553; VAL-555; TYR-562; PHE-582; TYR-582; ASP-623;
ARG-670; PHE-728; ARG-742 AND TRP-886, AND VARIANTS LYS-250; SER-986;
GLY-990 AND GLN-1011.
PubMed=17698911; DOI=10.1210/jc.2007-0322;
Nissen P.H., Christensen S.E., Heickendorff L., Brixen K.,
Mosekilde L.;
"Molecular genetic analysis of the calcium sensing receptor gene in
patients clinically suspected to have familial hypocalciuric
hypercalcemia: phenotypic variation and mutation spectrum in a Danish
population.";
J. Clin. Endocrinol. Metab. 92:4373-4379(2007).
[52]
VARIANTS EIG8 ALA-354; VAL-686; GLN-898; VAL-988 AND GLY-988, VARIANTS
SER-986 AND GLY-990, AND TISSUE SPECIFICITY.
PubMed=18756473; DOI=10.1002/ana.21428;
Kapoor A., Satishchandra P., Ratnapriya R., Reddy R., Kadandale J.,
Shankar S.K., Anand A.;
"An idiopathic epilepsy syndrome linked to 3q13.3-q21 and missense
mutations in the extracellular calcium sensing receptor gene.";
Ann. Neurol. 64:158-167(2008).
[53]
VARIANT HHC1 ARG-459, VARIANTS SER-986 AND GLN-1011, FUNCTION, AND
CHARACTERIZATION OF VARIANT HHC1 ARG-459.
PubMed=19789209; DOI=10.1210/jc.2008-2484;
Lietman S.A., Tenenbaum-Rakover Y., Jap T.S., Yi-Chi W., De-Ming Y.,
Ding C., Kussiny N., Levine M.A.;
"A novel loss-of-function mutation, Gln459Arg, of the calcium-sensing
receptor gene associated with apparent autosomal recessive inheritance
of familial hypocalciuric hypercalcemia.";
J. Clin. Endocrinol. Metab. 94:4372-4379(2009).
[54]
VARIANTS HHC1 SER-42; LEU-55; HIS-66; MET-81; MET-138; ARG-143;
ARG-158; GLY-166; TRP-220; ARG-549; TYR-562; GLY-565; TYR-582;
583-ASN--SER-1078 DEL; TYR-661; HIS-680; ILE-761 DEL AND TRP-795, AND
VARIANTS HYPOC1 LYS-118; PHE-125; ARG-129; LYS-228; LYS-604; ILE-802;
SER-830; LEU-832 AND SER-832.
PubMed=19179454; DOI=10.1677/JME-08-0164;
Cole D.E., Yun F.H., Wong B.Y., Shuen A.Y., Booth R.A., Scillitani A.,
Pidasheva S., Zhou X., Canaff L., Hendy G.N.;
"Calcium-sensing receptor mutations and denaturing high performance
liquid chromatography.";
J. Mol. Endocrinol. 42:331-339(2009).
[55]
VARIANT THR-339, CHARACTERIZATION OF VARIANT THR-339, AND INVOLVEMENT
IN PRIMARY HYPERPARATHYROIDISM.
PubMed=20846291; DOI=10.1111/j.1365-2265.2010.03870.x;
Hannan F.M., Nesbit M.A., Christie P.T., Lissens W.,
Van der Schueren B., Bex M., Bouillon R., Thakker R.V.;
"A homozygous inactivating calcium-sensing receptor mutation,
Pro339Thr, is associated with isolated primary hyperparathyroidism:
correlation between location of mutations and severity of
hypercalcaemia.";
Clin. Endocrinol. (Oxf.) 73:715-722(2010).
[56]
VARIANT HHC1 ILE-550, FUNCTION, AND CHARACTERIZATION OF VARIANT HHC1
ILE-550.
PubMed=21566075; DOI=10.1530/EJE-11-0141;
Al-Salameh A., Cetani F., Pardi E., Vulpoi C., Pierre P., de Calan L.,
Guyetant S., Jeunemaitre X., Lecomte P.;
"A novel mutation in the calcium-sensing receptor in a French family
with familial hypocalciuric hypercalcaemia.";
Eur. J. Endocrinol. 165:359-363(2011).
[57]
VARIANTS HHC1 PRO-159 AND TRP-795, FUNCTION, SUBCELLULAR LOCATION, AND
CHARACTERIZATION OF VARIANTS HHC1 PRO-159 AND TRP-795.
PubMed=22114145; DOI=10.1126/scisignal.2002208;
Grant M.P., Stepanchick A., Cavanaugh A., Breitwieser G.E.;
"Agonist-driven maturation and plasma membrane insertion of calcium-
sensing receptors dynamically control signal amplitude.";
Sci. Signal. 4:RA78-RA78(2011).
[58]
VARIANT HHC1 MET-697.
PubMed=21643651; DOI=10.1007/s00431-011-1504-8;
Aparicio Lopez C., Anton-Martin P., Gil-Fournier B., Ramiro-Leon S.,
Perez-Nanclares G., Perez de Nanclares G., Martinez Menendez B.,
Castano L.;
"Familial hypocalciuric hypercalcemia: new mutation in the CASR gene
converting valine 697 to methionine.";
Eur. J. Pediatr. 171:147-150(2012).
[59]
VARIANTS HHC1 THR-110 AND GLY-172, VARIANTS HYPOC1 CYS-122; HIS-569
AND THR-839, FUNCTION, CHARACTERIZATION OF VARIANTS HHC1 THR-110 AND
GLY-172, AND CHARACTERIZATION OF VARIANTS HYPOC1 CYS-122; HIS-569 AND
THR-839.
PubMed=23966241; DOI=10.1210/jc.2013-1974;
Nakamura A., Hotsubo T., Kobayashi K., Mochizuki H., Ishizu K.,
Tajima T.;
"Loss-of-function and gain-of-function mutations of calcium-sensing
receptor: functional analysis and the effect of allosteric modulators
NPS R-568 and NPS 2143.";
J. Clin. Endocrinol. Metab. 98:E1692-E1701(2013).
[60]
VARIANT HHC1 SER-802, AND VARIANT HYPOC1 ILE-802.
PubMed=23169696; DOI=10.1530/EJE-12-0714;
Lia-Baldini A.S., Magdelaine C., Nizou A., Airault C., Salles J.P.,
Moulin P., Delemer B., Aitouares M., Funalot B., Sturtz F.,
Lienhardt-Roussie A.;
"Two novel mutations of the calcium-sensing receptor gene affecting
the same amino acid position lead to opposite phenotypes and reveal
the importance of p.N802 on receptor activity.";
Eur. J. Endocrinol. 168:K27-K34(2013).
[61]
VARIANT HHC1 MET-972, FUNCTION, AND CHARACTERIZATION OF VARIANT HHC1
MET-972.
PubMed=25292184; DOI=10.1186/1472-6823-14-81;
Mastromatteo E., Lamacchia O., Campo M.R., Conserva A., Baorda F.,
Cinque L., Guarnieri V., Scillitani A., Cignarelli M.;
"A novel mutation in calcium-sensing receptor gene associated to
hypercalcemia and hypercalciuria.";
BMC Endocr. Disord. 14:81-81(2014).
[62]
VARIANTS HHC1 VAL-707 AND SER-774, FUNCTION, SUBCELLULAR LOCATION, AND
CHARACTERIZATION OF VARIANTS HHC1 VAL-707 AND SER-774.
PubMed=25104082; DOI=10.1093/ndt/gfu065;
Stratta P., Merlotti G., Musetti C., Quaglia M., Pagani A., Izzo C.,
Radin E., Airoldi A., Baorda F., Palladino T., Leone M.P.,
Guarnieri V.;
"Calcium-sensing-related gene mutations in hypercalcaemic
hypocalciuric patients as differential diagnosis from primary
hyperparathyroidism: detection of two novel inactivating mutations in
an Italian population.";
Nephrol. Dial. Transplant. 29:1902-1909(2014).
[63]
VARIANT HHC1 TRP-571, FUNCTION, SUBCELLULAR LOCATION, AND
CHARACTERIZATION OF VARIANT HHC1 TRP-571.
PubMed=26386835; DOI=10.1007/s00774-015-0713-z;
Kim E.S., Kim S.Y., Lee J.Y., Han J.H., Sohn T.S., Son H.S.,
Moon S.D.;
"Identification and functional analysis of a novel CaSR mutation in a
family with familial hypocalciuric hypercalcemia.";
J. Bone Miner. Metab. 34:662-667(2016).
[64]
VARIANT HYPOC1 LEU-136, FUNCTION, SUBCELLULAR LOCATION, AND
CHARACTERIZATION OF VARIANT HYPOC1 LEU-136.
PubMed=25766501; DOI=10.1016/j.mce.2015.02.021;
Baran N., ter Braak M., Saffrich R., Woelfle J., Schmitz U.;
"Novel activating mutation of human calcium-sensing receptor in a
family with autosomal dominant hypocalcaemia.";
Mol. Cell. Endocrinol. 407:18-25(2015).
[65]
VARIANTS HYPOC1 LEU-221; ARG-681 AND GLN-727, FUNCTION, SUBCELLULAR
LOCATION, AND CHARACTERIZATION OF VARIANTS HYPOC1 ARG-681 AND GLN-727.
PubMed=22789683; DOI=10.1016/j.ymgme.2012.06.012;
Guarnieri V., Valentina D'Elia A., Baorda F., Pazienza V.,
Benegiamo G., Stanziale P., Copetti M., Battista C., Grimaldi F.,
Damante G., Pellegrini F., D'Agruma L., Zelante L., Carella M.,
Scillitani A.;
"CASR gene activating mutations in two families with autosomal
dominant hypocalcemia.";
Mol. Genet. Metab. 107:548-552(2012).
-!- FUNCTION: G-protein-coupled receptor that senses changes in the
extracellular concentration of calcium ions and plays a key role
in maintaining calcium homeostasis (PubMed:7759551,
PubMed:8702647, PubMed:8636323, PubMed:8878438, PubMed:17555508,
PubMed:19789209, PubMed:21566075, PubMed:22114145,
PubMed:23966241, PubMed:25292184, PubMed:25104082,
PubMed:26386835, PubMed:25766501, PubMed:22789683). Senses
fluctuations in the circulating calcium concentration and
modulates the production of parathyroid hormone (PTH) in
parathyroid glands (By similarity). The activity of this receptor
is mediated by a G-protein that activates a phosphatidylinositol-
calcium second messenger system (PubMed:7759551). The G-protein-
coupled receptor activity is activated by a co-agonist mechanism:
aromatic amino acids, such as Trp or Phe, act concertedly with
divalent cations, such as calcium or magnesium, to achieve full
receptor activation (PubMed:27434672, PubMed:27386547).
{ECO:0000250|UniProtKB:Q9QY96, ECO:0000269|PubMed:17555508,
ECO:0000269|PubMed:19789209, ECO:0000269|PubMed:21566075,
ECO:0000269|PubMed:22114145, ECO:0000269|PubMed:22789683,
ECO:0000269|PubMed:23966241, ECO:0000269|PubMed:25104082,
ECO:0000269|PubMed:25292184, ECO:0000269|PubMed:25766501,
ECO:0000269|PubMed:26386835, ECO:0000269|PubMed:27386547,
ECO:0000269|PubMed:27434672, ECO:0000269|PubMed:7759551,
ECO:0000269|PubMed:8636323, ECO:0000269|PubMed:8702647,
ECO:0000269|PubMed:8878438}.
-!- ENZYME REGULATION: In resting state, adopts an open conformation,
anion-binding promoting the inactive configuration
(PubMed:27434672). Upon aromatic amino acid-binding, the groove in
the extracellular venus flytrap module is closed, thereby inducing
the formation of a novel homodimer interface between subunits
(PubMed:27434672, PubMed:27386547). Calcium ions stabilize the
active state by enhancing homodimer interactions between membrane-
proximal domains to fully activate the receptor (PubMed:27434672,
PubMed:27386547). Activated by AMG 416, a D-amino acid-containing
peptide agonist that is being evaluated for the treatment of
secondary hyperparathyroidism in chronic kidney disease patients
receiving hemodialysis (PubMed:26290606). AMG 416 agonist acts by
forming a disulfide bond with Cys-482 (PubMed:26290606).
{ECO:0000269|PubMed:26290606, ECO:0000269|PubMed:27386547,
ECO:0000269|PubMed:27434672}.
-!- SUBUNIT: Homodimer; disulfide-linked (PubMed:27434672,
PubMed:27386547, PubMed:16740594). Interacts with VCP and RNF19A
(PubMed:16513638). Interacts with ARRB1 (By similarity).
{ECO:0000250|UniProtKB:P48442, ECO:0000269|PubMed:16513638,
ECO:0000269|PubMed:16740594, ECO:0000269|PubMed:27386547,
ECO:0000269|PubMed:27434672}.
-!- INTERACTION:
Q15363:TMED2; NbExp=3; IntAct=EBI-4400127, EBI-998485;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15572418,
ECO:0000269|PubMed:16740594, ECO:0000269|PubMed:17555508,
ECO:0000269|PubMed:19789209, ECO:0000269|PubMed:20861236,
ECO:0000269|PubMed:22114145, ECO:0000269|PubMed:22789683,
ECO:0000269|PubMed:25104082, ECO:0000269|PubMed:25766501,
ECO:0000269|PubMed:26386835, ECO:0000269|PubMed:8702647}; Multi-
pass membrane protein {ECO:0000269|PubMed:20861236}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P41180-1; Sequence=Displayed;
Name=2;
IsoId=P41180-2; Sequence=VSP_002035;
-!- TISSUE SPECIFICITY: Expressed in the temporal lobe, frontal lobe,
parietal lobe, hippocampus, and cerebellum. Also found in kidney,
lung, liver, heart, skeletal muscle, placenta.
{ECO:0000269|PubMed:18756473}.
-!- DOMAIN: The extracellular regions of the homodimer interact in a
side-by-side fashion while facing opposite directions
(PubMed:27434672, PubMed:27386547). Each extracellular region
consists of three domains, LB1 (ligand-binding 1), LB2 and CR
(cysteine-rich) (PubMed:17360426). The two lobe-shaped domains LB1
and LB2 form a venus flytrap module (PubMed:27434672,
PubMed:27386547). In the inactive configuration, the venus flytrap
modules of both protomers are in the open conformation associated
with the resting state (open-open) and the interdomain cleft is
empty (PubMed:27434672). In addition, each protomer contains three
anions, which reinforce the inactive conformation, and one calcium
ion (PubMed:27434672). In the active configuration, both protomers
of extracellular regions have the closed conformation associated
with agonist-binding (closed-closed) (PubMed:27434672,
PubMed:27386547). The ligand-binding cleft of each protomer is
solely occupied by an aromatic amino-acid (PubMed:27434672,
PubMed:27386547). Calcium is bound at four novel sites, including
one at the homodimer interface (PubMed:27434672, PubMed:27386547).
Agonist-binding induces large conformational changes within the
extracellular region homodimer: first, the venus flytrap module of
each protomer undergoes domain closure (PubMed:27434672,
PubMed:27386547). Second, the LB2 regions of the two protomers
approach each other, resulting in an expansion of the homodimer
interactions involving LB2 domains (PubMed:27434672,
PubMed:27386547). Third, the CR regions of the two subunits
interact to form a large homodimer interface that is unique to the
active state (PubMed:27434672, PubMed:27386547). The CR regions
are brought into close contact by the motion involving LB2 since
the two domains are rigidly associated within each subunit
(PubMed:27434672, PubMed:27386547). {ECO:0000269|PubMed:27386547,
ECO:0000269|PubMed:27434672, ECO:0000303|PubMed:17360426}.
-!- PTM: N-glycosylated. {ECO:0000269|PubMed:16513638,
ECO:0000269|PubMed:16740594, ECO:0000269|PubMed:20861236,
ECO:0000269|PubMed:27434672, ECO:0000269|PubMed:8702647}.
-!- PTM: Ubiquitinated by RNF19A; which induces proteasomal
degradation. {ECO:0000269|PubMed:16513638}.
-!- DISEASE: Hypocalciuric hypercalcemia, familial 1 (HHC1)
[MIM:145980]: A form of hypocalciuric hypercalcemia, a disorder of
mineral homeostasis that is transmitted as an autosomal dominant
trait with a high degree of penetrance. It is characterized
biochemically by lifelong elevation of serum calcium
concentrations and is associated with inappropriately low urinary
calcium excretion and a normal or mildly elevated circulating
parathyroid hormone level. Hypermagnesemia is typically present.
Affected individuals are usually asymptomatic and the disorder is
considered benign. However, chondrocalcinosis and pancreatitis
occur in some adults. {ECO:0000269|PubMed:11762699,
ECO:0000269|PubMed:15572418, ECO:0000269|PubMed:15579740,
ECO:0000269|PubMed:15879434, ECO:0000269|PubMed:16598859,
ECO:0000269|PubMed:16740594, ECO:0000269|PubMed:17473068,
ECO:0000269|PubMed:17698911, ECO:0000269|PubMed:19179454,
ECO:0000269|PubMed:19789209, ECO:0000269|PubMed:21566075,
ECO:0000269|PubMed:21643651, ECO:0000269|PubMed:22114145,
ECO:0000269|PubMed:23169696, ECO:0000269|PubMed:23966241,
ECO:0000269|PubMed:25104082, ECO:0000269|PubMed:25292184,
ECO:0000269|PubMed:26386835, ECO:0000269|PubMed:27434672,
ECO:0000269|PubMed:7673400, ECO:0000269|PubMed:7726161,
ECO:0000269|PubMed:7916660, ECO:0000269|PubMed:8636323,
ECO:0000269|PubMed:8702647, ECO:0000269|PubMed:8878438,
ECO:0000269|PubMed:9298824}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Hyperparathyroidism, neonatal severe (NSHPT)
[MIM:239200]: A disorder characterized by severe hypercalcemia,
bone demineralization, and failure to thrive usually manifesting
in the first 6 months of life. If untreated, NSHPT can be a
devastating neurodevelopmental disorder, which in some cases is
lethal without parathyroidectomy. {ECO:0000269|PubMed:14985373,
ECO:0000269|PubMed:15572418, ECO:0000269|PubMed:17555508,
ECO:0000269|PubMed:27434672, ECO:0000269|PubMed:8675635,
ECO:0000269|PubMed:8878438, ECO:0000269|PubMed:9253359}. Note=The
disease is caused by mutations affecting the gene represented in
this entry.
-!- DISEASE: Hypocalcemia, autosomal dominant 1 (HYPOC1) [MIM:601198]:
A disorder of mineral homeostasis characterized by blood calcium
levels below normal, and low or normal serum parathyroid hormone
concentrations. Disease manifestations include mild or
asymptomatic hypocalcemia, paresthesias, carpopedal spasm,
seizures, hypercalciuria with nephrocalcinosis or kidney stones,
and ectopic and basal ganglia calcifications. Few patients
manifest hypocalcemia and features of Bartter syndrome, including
hypomagnesemia, hypokalemia, metabolic alkalosis, hyperreninemia,
and hyperaldosteronemia. {ECO:0000269|PubMed:10487661,
ECO:0000269|PubMed:12050233, ECO:0000269|PubMed:12107202,
ECO:0000269|PubMed:12241879, ECO:0000269|PubMed:12574188,
ECO:0000269|PubMed:12915654, ECO:0000269|PubMed:15551332,
ECO:0000269|PubMed:16608894, ECO:0000269|PubMed:19179454,
ECO:0000269|PubMed:22789683, ECO:0000269|PubMed:23169696,
ECO:0000269|PubMed:23966241, ECO:0000269|PubMed:25766501,
ECO:0000269|PubMed:7874174, ECO:0000269|PubMed:8702647,
ECO:0000269|PubMed:8733126, ECO:0000269|PubMed:8813042,
ECO:0000269|PubMed:8878438, ECO:0000269|PubMed:9253358,
ECO:0000269|PubMed:9661634, ECO:0000269|PubMed:9920108}. Note=The
disease is caused by mutations affecting the gene represented in
this entry.
-!- DISEASE: Epilepsy, idiopathic generalized 8 (EIG8) [MIM:612899]: A
disorder characterized by recurring generalized seizures in the
absence of detectable brain lesions and/or metabolic
abnormalities. Seizure types are variable, but include myoclonic
seizures, absence seizures, febrile seizures, complex partial
seizures, and generalized tonic-clonic seizures.
{ECO:0000269|PubMed:18756473}. Note=Disease susceptibility is
associated with variations affecting the gene represented in this
entry.
-!- SIMILARITY: Belongs to the G-protein coupled receptor 3 family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAB29413.2; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=SeattleSNPs;
URL="http://pga.gs.washington.edu/data/casr/";
-----------------------------------------------------------------------
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EMBL; X81086; CAA56990.1; -; Genomic_DNA.
EMBL; U20759; AAA86503.1; -; mRNA.
EMBL; U20760; AAA86504.1; -; mRNA.
EMBL; D50855; BAA09453.1; -; mRNA.
EMBL; S83176; AAB46873.1; -; mRNA.
EMBL; S79217; AAB35262.2; -; mRNA.
EMBL; S81755; AAD14370.1; -; mRNA.
EMBL; S68032; AAB29413.2; ALT_SEQ; Genomic_DNA.
EMBL; S68033; AAB29414.1; -; Genomic_DNA.
EMBL; S68036; AAB29415.1; -; Genomic_DNA.
EMBL; DQ088967; AAY68221.1; -; Genomic_DNA.
EMBL; BC104999; AAI05000.1; -; mRNA.
EMBL; BC112236; AAI12237.1; -; mRNA.
CCDS; CCDS3010.1; -. [P41180-1]
CCDS; CCDS54632.1; -. [P41180-2]
PIR; A56715; A56715.
PIR; B56715; B56715.
RefSeq; NP_000379.2; NM_000388.3.
RefSeq; NP_001171536.1; NM_001178065.1.
RefSeq; XP_006713852.1; XM_006713789.3. [P41180-1]
RefSeq; XP_016862813.1; XM_017007324.1. [P41180-1]
RefSeq; XP_016862814.1; XM_017007325.1. [P41180-1]
UniGene; Hs.435615; -.
PDB; 5FBH; X-ray; 2.70 A; A/B=20-541.
PDB; 5FBK; X-ray; 2.10 A; A/B=20-541.
PDB; 5K5S; X-ray; 2.60 A; A/B=20-607.
PDB; 5K5T; X-ray; 3.10 A; A=20-607.
PDBsum; 5FBH; -.
PDBsum; 5FBK; -.
PDBsum; 5K5S; -.
PDBsum; 5K5T; -.
ProteinModelPortal; P41180; -.
SMR; P41180; -.
BioGrid; 107296; 9.
DIP; DIP-5975N; -.
ELM; P41180; -.
IntAct; P41180; 1.
MINT; MINT-201342; -.
STRING; 9606.ENSP00000420194; -.
BindingDB; P41180; -.
ChEMBL; CHEMBL1878; -.
DrugBank; DB05255; 751689.
DrugBank; DB01012; Cinacalcet.
DrugBank; DB12865; Etelcalcetide.
GuidetoPHARMACOLOGY; 54; -.
TCDB; 9.A.14.7.2; the g-protein-coupled receptor (gpcr) family.
iPTMnet; P41180; -.
PhosphoSitePlus; P41180; -.
BioMuta; CASR; -.
DMDM; 1168781; -.
PaxDb; P41180; -.
PeptideAtlas; P41180; -.
PRIDE; P41180; -.
Ensembl; ENST00000498619; ENSP00000420194; ENSG00000036828. [P41180-2]
Ensembl; ENST00000638421; ENSP00000492190; ENSG00000036828. [P41180-1]
Ensembl; ENST00000639785; ENSP00000491584; ENSG00000036828. [P41180-1]
GeneID; 846; -.
KEGG; hsa:846; -.
UCSC; uc003eev.5; human. [P41180-1]
CTD; 846; -.
DisGeNET; 846; -.
EuPathDB; HostDB:ENSG00000036828.13; -.
GeneCards; CASR; -.
H-InvDB; HIX0163457; -.
HGNC; HGNC:1514; CASR.
HPA; HPA039686; -.
HPA; HPA050335; -.
MalaCards; CASR; -.
MIM; 145980; phenotype.
MIM; 239200; phenotype.
MIM; 601198; phenotype.
MIM; 601199; gene+phenotype.
MIM; 612899; phenotype.
neXtProt; NX_P41180; -.
OpenTargets; ENSG00000036828; -.
Orphanet; 428; Autosomal dominant hypocalcemia.
Orphanet; 263417; Bartter syndrome with hypocalcemia.
Orphanet; 93372; Familial hypocalciuric hypercalcemia type 1.
Orphanet; 189466; Familial isolated hypoparathyroidism due to impaired PTH secretion.
Orphanet; 417; Neonatal severe primary hyperparathyroidism.
PharmGKB; PA26097; -.
eggNOG; KOG1056; Eukaryota.
eggNOG; ENOG410XR6W; LUCA.
GeneTree; ENSGT00760000118974; -.
HOVERGEN; HBG052876; -.
InParanoid; P41180; -.
KO; K04612; -.
PhylomeDB; P41180; -.
Reactome; R-HSA-416476; G alpha (q) signalling events.
Reactome; R-HSA-418594; G alpha (i) signalling events.
Reactome; R-HSA-420499; Class C/3 (Metabotropic glutamate/pheromone receptors).
SIGNOR; P41180; -.
GeneWiki; Calcium-sensing_receptor; -.
GenomeRNAi; 846; -.
PRO; PR:P41180; -.
Proteomes; UP000005640; Chromosome 3.
Bgee; ENSG00000036828; -.
CleanEx; HS_CASR; -.
ExpressionAtlas; P41180; baseline and differential.
Genevisible; P41180; HS.
GO; GO:0016324; C:apical plasma membrane; IEA:Ensembl.
GO; GO:0030424; C:axon; IEA:Ensembl.
GO; GO:0043679; C:axon terminus; IEA:Ensembl.
GO; GO:0016323; C:basolateral plasma membrane; IEA:Ensembl.
GO; GO:0009986; C:cell surface; IEA:Ensembl.
GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
GO; GO:0005634; C:nucleus; IEA:Ensembl.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0016597; F:amino acid binding; IDA:UniProtKB.
GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
GO; GO:0008144; F:drug binding; IEA:Ensembl.
GO; GO:0004930; F:G-protein coupled receptor activity; IDA:UniProtKB.
GO; GO:0005178; F:integrin binding; IEA:Ensembl.
GO; GO:0044325; F:ion channel binding; IEA:Ensembl.
GO; GO:0000287; F:magnesium ion binding; IEA:Ensembl.
GO; GO:0004435; F:phosphatidylinositol phospholipase C activity; TAS:ProtInc.
GO; GO:0019808; F:polyamine binding; IEA:Ensembl.
GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
GO; GO:0019901; F:protein kinase binding; IEA:Ensembl.
GO; GO:0007193; P:adenylate cyclase-inhibiting G-protein coupled receptor signaling pathway; IEA:Ensembl.
GO; GO:0009653; P:anatomical structure morphogenesis; TAS:ProtInc.
GO; GO:0006915; P:apoptotic process; IEA:Ensembl.
GO; GO:0048754; P:branching morphogenesis of an epithelial tube; IEA:Ensembl.
GO; GO:0070509; P:calcium ion import; IDA:UniProtKB.
GO; GO:0006874; P:cellular calcium ion homeostasis; IDA:UniProtKB.
GO; GO:0071333; P:cellular response to glucose stimulus; IEA:Ensembl.
GO; GO:0035729; P:cellular response to hepatocyte growth factor stimulus; IEA:Ensembl.
GO; GO:0071456; P:cellular response to hypoxia; IEA:Ensembl.
GO; GO:0071404; P:cellular response to low-density lipoprotein particle stimulus; IEA:Ensembl.
GO; GO:1901653; P:cellular response to peptide; IEA:Ensembl.
GO; GO:0071305; P:cellular response to vitamin D; IEA:Ensembl.
GO; GO:0007635; P:chemosensory behavior; TAS:ProtInc.
GO; GO:0005513; P:detection of calcium ion; IDA:UniProtKB.
GO; GO:0060613; P:fat pad development; IEA:Ensembl.
GO; GO:0007186; P:G-protein coupled receptor signaling pathway; IDA:UniProtKB.
GO; GO:0007254; P:JNK cascade; IEA:Ensembl.
GO; GO:0001503; P:ossification; TAS:ProtInc.
GO; GO:0007200; P:phospholipase C-activating G-protein coupled receptor signaling pathway; IEA:Ensembl.
GO; GO:0032781; P:positive regulation of ATPase activity; IEA:Ensembl.
GO; GO:0090280; P:positive regulation of calcium ion import; IEA:Ensembl.
GO; GO:0008284; P:positive regulation of cell proliferation; IEA:Ensembl.
GO; GO:0010628; P:positive regulation of gene expression; IEA:Ensembl.
GO; GO:0032024; P:positive regulation of insulin secretion; IEA:Ensembl.
GO; GO:0050927; P:positive regulation of positive chemotaxis; IEA:Ensembl.
GO; GO:0045907; P:positive regulation of vasoconstriction; IEA:Ensembl.
GO; GO:0071774; P:response to fibroblast growth factor; IEA:Ensembl.
GO; GO:0002931; P:response to ischemia; IEA:Ensembl.
GO; GO:0042311; P:vasodilation; IEA:Ensembl.
InterPro; IPR001828; ANF_lig-bd_rcpt.
InterPro; IPR000337; GPCR_3.
InterPro; IPR011500; GPCR_3_9-Cys_dom.
InterPro; IPR017978; GPCR_3_C.
InterPro; IPR017979; GPCR_3_CS.
InterPro; IPR028082; Peripla_BP_I.
Pfam; PF00003; 7tm_3; 1.
Pfam; PF01094; ANF_receptor; 1.
Pfam; PF07562; NCD3G; 1.
PRINTS; PR00248; GPCRMGR.
SUPFAM; SSF53822; SSF53822; 1.
PROSITE; PS00979; G_PROTEIN_RECEP_F3_1; 1.
PROSITE; PS00980; G_PROTEIN_RECEP_F3_2; 1.
PROSITE; PS00981; G_PROTEIN_RECEP_F3_3; 1.
PROSITE; PS50259; G_PROTEIN_RECEP_F3_4; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Calcium; Cell membrane;
Complete proteome; Disease mutation; Disulfide bond; Epilepsy;
G-protein coupled receptor; Glycoprotein; Membrane; Metal-binding;
Phosphoprotein; Polymorphism; Receptor; Reference proteome; Signal;
Transducer; Transmembrane; Transmembrane helix; Ubl conjugation.
SIGNAL 1 19 {ECO:0000255}.
CHAIN 20 1078 Extracellular calcium-sensing receptor.
/FTId=PRO_0000012946.
TOPO_DOM 20 612 Extracellular. {ECO:0000255}.
TRANSMEM 613 635 Helical; Name=1. {ECO:0000255}.
TOPO_DOM 636 649 Cytoplasmic. {ECO:0000255}.
TRANSMEM 650 670 Helical; Name=2. {ECO:0000255}.
TOPO_DOM 671 681 Extracellular. {ECO:0000255}.
TRANSMEM 682 700 Helical; Name=3. {ECO:0000255}.
TOPO_DOM 701 724 Cytoplasmic. {ECO:0000255}.
TRANSMEM 725 745 Helical; Name=4. {ECO:0000255}.
TOPO_DOM 746 769 Extracellular. {ECO:0000255}.
TRANSMEM 770 792 Helical; Name=5. {ECO:0000255}.
TOPO_DOM 793 805 Cytoplasmic. {ECO:0000255}.
TRANSMEM 806 828 Helical; Name=6. {ECO:0000255}.
TOPO_DOM 829 836 Extracellular. {ECO:0000255}.
TRANSMEM 837 862 Helical; Name=7. {ECO:0000255}.
TOPO_DOM 863 1078 Cytoplasmic. {ECO:0000255}.
REGION 22 188 Ligand-binding 1 (LB1).
{ECO:0000303|PubMed:17360426}.
REGION 66 70 Anion binding. {ECO:0000244|PDB:5K5S,
ECO:0000244|PDB:5K5T,
ECO:0000269|PubMed:27434672}.
REGION 189 324 Ligand-binding 2 (LB2).
{ECO:0000303|PubMed:17360426}.
REGION 415 417 Anion binding. {ECO:0000244|PDB:5K5S,
ECO:0000244|PDB:5K5T,
ECO:0000269|PubMed:27434672}.
REGION 542 612 Cysteine-rich (CR).
{ECO:0000303|PubMed:17360426}.
REGION 880 900 Interaction with RNF19A.
{ECO:0000269|PubMed:16513638}.
METAL 81 81 Calcium; via carbonyl oxygen.
{ECO:0000244|PDB:5FBH,
ECO:0000244|PDB:5FBK,
ECO:0000244|PDB:5K5S,
ECO:0000269|PubMed:27434672,
ECO:0000305|PubMed:27386547}.
METAL 84 84 Calcium. {ECO:0000244|PDB:5FBK,
ECO:0000244|PDB:5K5S,
ECO:0000269|PubMed:27434672,
ECO:0000305|PubMed:27386547}.
METAL 87 87 Calcium; via carbonyl oxygen.
{ECO:0000244|PDB:5FBH,
ECO:0000244|PDB:5FBK,
ECO:0000244|PDB:5K5S,
ECO:0000269|PubMed:27434672,
ECO:0000305|PubMed:27386547}.
METAL 88 88 Calcium; via carbonyl oxygen.
{ECO:0000244|PDB:5FBH,
ECO:0000244|PDB:5FBK,
ECO:0000244|PDB:5K5S,
ECO:0000269|PubMed:27434672,
ECO:0000305|PubMed:27386547}.
METAL 100 100 Calcium. {ECO:0000244|PDB:5K5S,
ECO:0000244|PDB:5K5T,
ECO:0000269|PubMed:27434672}.
METAL 145 145 Calcium. {ECO:0000244|PDB:5K5S,
ECO:0000269|PubMed:27434672}.
METAL 231 231 Calcium. {ECO:0000244|PDB:5K5S,
ECO:0000269|PubMed:27434672}.
METAL 234 234 Calcium. {ECO:0000244|PDB:5K5S,
ECO:0000269|PubMed:27434672}.
METAL 557 557 Calcium; via carbonyl oxygen.
{ECO:0000244|PDB:5K5S,
ECO:0000269|PubMed:27434672}.
BINDING 147 147 Aromatic amino acid.
{ECO:0000244|PDB:5FBH,
ECO:0000244|PDB:5FBK,
ECO:0000244|PDB:5K5S,
ECO:0000269|PubMed:27386547,
ECO:0000269|PubMed:27434672}.
BINDING 168 168 Aromatic amino acid; via carbonyl oxygen.
{ECO:0000244|PDB:5FBH,
ECO:0000244|PDB:5FBK,
ECO:0000244|PDB:5K5S,
ECO:0000269|PubMed:27386547,
ECO:0000269|PubMed:27434672}.
BINDING 170 170 Aromatic amino acid.
{ECO:0000244|PDB:5FBH,
ECO:0000244|PDB:5FBK,
ECO:0000244|PDB:5K5S,
ECO:0000269|PubMed:27386547,
ECO:0000269|PubMed:27434672}.
BINDING 297 297 Aromatic amino acid.
{ECO:0000244|PDB:5FBH,
ECO:0000244|PDB:5FBK,
ECO:0000244|PDB:5K5S,
ECO:0000269|PubMed:27386547,
ECO:0000269|PubMed:27434672}.
SITE 482 482 Important for ability of agonist AMG 416
to activate G-protein-coupled receptor
activity. {ECO:0000269|PubMed:26290606}.
MOD_RES 920 920 Phosphoserine.
{ECO:0000250|UniProtKB:Q9QY96}.
MOD_RES 1061 1061 Phosphoserine.
{ECO:0000250|UniProtKB:Q9QY96}.
CARBOHYD 90 90 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 130 130 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 261 261 N-linked (GlcNAc...) asparagine.
{ECO:0000255,
ECO:0000269|PubMed:27434672}.
CARBOHYD 287 287 N-linked (GlcNAc...) asparagine.
{ECO:0000255,
ECO:0000269|PubMed:27434672}.
CARBOHYD 386 386 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 400 400 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 446 446 N-linked (GlcNAc...) asparagine.
{ECO:0000255,
ECO:0000269|PubMed:27434672}.
CARBOHYD 468 468 N-linked (GlcNAc...) asparagine.
{ECO:0000255,
ECO:0000269|PubMed:27434672}.
CARBOHYD 488 488 N-linked (GlcNAc...) asparagine.
{ECO:0000255,
ECO:0000269|PubMed:27434672}.
CARBOHYD 541 541 N-linked (GlcNAc...) asparagine.
{ECO:0000255,
ECO:0000269|PubMed:27434672}.
CARBOHYD 594 594 N-linked (GlcNAc...) asparagine.
{ECO:0000255,
ECO:0000269|PubMed:27434672}.
DISULFID 60 101 {ECO:0000244|PDB:5FBH,
ECO:0000244|PDB:5FBK,
ECO:0000244|PDB:5K5S,
ECO:0000269|PubMed:27386547,
ECO:0000269|PubMed:27434672}.
DISULFID 129 129 Interchain. {ECO:0000269|PubMed:27434672,
ECO:0000305|PubMed:27386547}.
DISULFID 131 131 Interchain. {ECO:0000269|PubMed:27434672,
ECO:0000305|PubMed:27386547}.
DISULFID 236 561 {ECO:0000269|PubMed:27434672}.
DISULFID 358 395 {ECO:0000244|PDB:5FBH,
ECO:0000244|PDB:5FBK,
ECO:0000244|PDB:5K5S,
ECO:0000269|PubMed:27386547,
ECO:0000269|PubMed:27434672}.
DISULFID 437 449 {ECO:0000244|PDB:5FBH,
ECO:0000244|PDB:5FBK,
ECO:0000244|PDB:5K5S,
ECO:0000269|PubMed:27386547,
ECO:0000269|PubMed:27434672}.
DISULFID 542 562 {ECO:0000269|PubMed:27434672}.
DISULFID 546 565 {ECO:0000269|PubMed:27434672}.
DISULFID 568 582 {ECO:0000269|PubMed:27434672}.
DISULFID 585 598 {ECO:0000269|PubMed:27434672}.
VAR_SEQ 536 536 E -> EPLTFVLSVLQ (in isoform 2).
{ECO:0000303|PubMed:7759551}.
/FTId=VSP_002035.
VARIANT 11 11 L -> S (in HHC1; demonstrates reduced
intracellular and plasma membrane
expression and signaling to the MAPK
pathway in response to extracellular
calcium relative to wild-type; fails to
be inserted in the microsomes and does
not undergo proper glycosylation;
dbSNP:rs200673016).
{ECO:0000269|PubMed:15879434}.
/FTId=VAR_058046.
VARIANT 13 13 L -> P (in HHC1; has a dose-response
curve shifted to the right relative to
that of wild-type; demonstrates reduced
intracellular and plasma membrane
expression and signaling to the MAPK
pathway in response to extracellular
calcium relative to wild-type; fails to
be inserted in the microsomes and does
not undergo proper glycosylation;
dbSNP:rs104893717).
{ECO:0000269|PubMed:15579740,
ECO:0000269|PubMed:15879434}.
/FTId=VAR_058047.
VARIANT 14 14 T -> A (does not demonstrate reduced
intracellular and plasma membrane
expression and signaling to the MAPK
pathway in response to extracellular
calcium relative to wild-type; does not
fail to be inserted in the microsomes and
does undergo proper glycosylation;
dbSNP:rs199515839).
{ECO:0000269|PubMed:15879434}.
/FTId=VAR_058048.
VARIANT 21 21 G -> R (in HHC1).
{ECO:0000269|PubMed:17698911}.
/FTId=VAR_058049.
VARIANT 27 27 Q -> R (found in a patient with primary
hyperparathyroidism detected at
adulthood; mutant CASR is activated by a
higher calcium concentrations than the
wild-type).
{ECO:0000269|PubMed:10468915}.
/FTId=VAR_065198.
VARIANT 39 39 P -> A (in HHC1; dbSNP:rs121909262).
{ECO:0000269|PubMed:7673400}.
/FTId=VAR_003585.
VARIANT 42 42 F -> S (in HHC1).
{ECO:0000269|PubMed:19179454}.
/FTId=VAR_078139.
VARIANT 47 47 K -> N (in HYPOC1; the EC(50) of the
mutant is significantly lower than that
of wild-type; dbSNP:rs104893702).
{ECO:0000269|PubMed:9920108}.
/FTId=VAR_058050.
VARIANT 53 53 S -> P (in HHC1; decreased G-protein
coupled receptor signaling pathway).
{ECO:0000269|PubMed:8636323}.
/FTId=VAR_078140.
VARIANT 55 55 P -> L (in HHC1; decreased G-protein
coupled receptor signaling pathway).
{ECO:0000269|PubMed:19179454,
ECO:0000269|PubMed:8636323,
ECO:0000269|PubMed:8878438}.
/FTId=VAR_078141.
VARIANT 62 62 R -> M (in HHC1; mild; decreased G-
protein coupled receptor signaling
pathway; dbSNP:rs121909265).
{ECO:0000269|PubMed:7726161,
ECO:0000269|PubMed:8702647}.
/FTId=VAR_003586.
VARIANT 66 66 R -> C (in HHC1; does not affect
homodimerization; impaired N-
glycosylation; impaired cell membrane
localization; decreased G-protein coupled
receptor signaling pathway;
dbSNP:rs121909266).
{ECO:0000269|PubMed:16740594,
ECO:0000269|PubMed:7726161,
ECO:0000269|PubMed:8702647}.
/FTId=VAR_003587.
VARIANT 66 66 R -> H (in HHC1; does not affect
homodimerization; impaired N-
glycosylation; impaired cell membrane
localization; decreased G-protein coupled
receptor signaling pathway).
{ECO:0000269|PubMed:16740594,
ECO:0000269|PubMed:19179454,
ECO:0000269|PubMed:27434672}.
/FTId=VAR_078142.
VARIANT 81 81 I -> M (in HHC1; decreased G-protein
coupled receptor signaling pathway).
{ECO:0000269|PubMed:19179454,
ECO:0000269|PubMed:27434672}.
/FTId=VAR_078143.
VARIANT 100 100 T -> I (in NSHPT; Abolished G-protein
coupled receptor activity).
{ECO:0000269|PubMed:14985373,
ECO:0000269|PubMed:27434672}.
/FTId=VAR_065199.
VARIANT 110 110 A -> T (in HHC1; decreased G-protein
coupled receptor signaling pathway).
{ECO:0000269|PubMed:23966241}.
/FTId=VAR_078144.
VARIANT 116 116 A -> T (in HYPOC1; dbSNP:rs104893691).
{ECO:0000269|PubMed:8733126}.
/FTId=VAR_003588.
VARIANT 118 118 N -> K (in HYPOC1; the mutation shifts
the concentration-response curve to the
left and increases maximal activity;
dbSNP:rs104893695).
{ECO:0000269|PubMed:19179454,
ECO:0000269|PubMed:8813042,
ECO:0000269|PubMed:9253358}.
/FTId=VAR_058051.
VARIANT 122 122 S -> C (in HYPOC1; increased G-protein
coupled receptor signaling pathway).
{ECO:0000269|PubMed:23966241}.
/FTId=VAR_078145.
VARIANT 125 125 L -> F (in HYPOC1).
{ECO:0000269|PubMed:19179454}.
/FTId=VAR_078146.
VARIANT 125 125 L -> P (in HYPOC1; shifts the
concentration-response curve of calcium
ions to the left; dbSNP:rs104893708).
{ECO:0000269|PubMed:12107202}.
/FTId=VAR_058052.
VARIANT 127 127 E -> A (in HYPOC1; increased G-protein
coupled receptor signaling pathway;
dbSNP:rs121909260).
{ECO:0000269|PubMed:7874174,
ECO:0000269|PubMed:8702647}.
/FTId=VAR_003589.
VARIANT 128 128 F -> L (in HYPOC1; increased G-protein
coupled receptor signaling pathway;
dbSNP:rs104893696).
{ECO:0000269|PubMed:8813042,
ECO:0000269|PubMed:8878438}.
/FTId=VAR_058053.
VARIANT 129 129 C -> R (in HYPOC1).
{ECO:0000269|PubMed:19179454}.
/FTId=VAR_078147.
VARIANT 131 131 C -> W (in HYPOC1; associated with
clinical features of Bartter syndrome;
dbSNP:rs121909267).
{ECO:0000269|PubMed:12241879}.
/FTId=VAR_058054.
VARIANT 136 136 P -> L (in HYPOC1; increased G-protein
coupled receptor signaling pathway; does
not affect cell membrane localization).
{ECO:0000269|PubMed:25766501}.
/FTId=VAR_078148.
VARIANT 138 138 T -> M (in HHC1; decreased G-protein
coupled receptor signaling pathway;
dbSNP:rs121909263).
{ECO:0000269|PubMed:19179454,
ECO:0000269|PubMed:7726161,
ECO:0000269|PubMed:8702647}.
/FTId=VAR_003590.
VARIANT 143 143 G -> E (in HHC1; decreased G-protein
coupled receptor signaling pathway;
dbSNP:rs121909264).
{ECO:0000269|PubMed:7726161,
ECO:0000269|PubMed:8702647}.
/FTId=VAR_003591.
VARIANT 143 143 G -> R (in HHC1; dbSNP:rs769256610).
{ECO:0000269|PubMed:19179454}.
/FTId=VAR_078149.
VARIANT 151 151 T -> M (in HYPOC1; increased G-protein
coupled receptor signaling pathway;
dbSNP:rs104893694).
{ECO:0000269|PubMed:8698326,
ECO:0000269|PubMed:8813042,
ECO:0000269|PubMed:8878438}.
/FTId=VAR_058055.
VARIANT 158 158 G -> R (in HHC1).
{ECO:0000269|PubMed:19179454}.
/FTId=VAR_078150.
VARIANT 159 159 L -> P (in HHC1; decreased G-protein
coupled receptor signaling pathway).
{ECO:0000269|PubMed:22114145,
ECO:0000269|PubMed:27434672}.
/FTId=VAR_078151.
VARIANT 166 166 S -> G (in HHC1; dbSNP:rs193922441).
{ECO:0000269|PubMed:19179454}.
/FTId=VAR_078152.
VARIANT 171 171 S -> N (in HHC1).
{ECO:0000269|PubMed:17698911}.
/FTId=VAR_058056.
VARIANT 172 172 R -> G (in HHC1; decreased G-protein
coupled receptor signaling pathway).
{ECO:0000269|PubMed:23966241,
ECO:0000269|PubMed:27434672}.
/FTId=VAR_078153.
VARIANT 174 174 L -> R (in HHC1).
{ECO:0000269|PubMed:9298824}.
/FTId=VAR_003592.
VARIANT 178 178 N -> D (in HHC1; decreased G-protein
coupled receptor signaling pathway).
{ECO:0000269|PubMed:8878438}.
/FTId=VAR_078154.
VARIANT 180 180 F -> C (in HHC1; although the mutant
receptor is expressed normally at the
cell surface it is unresponsive with
respect to intracellular signaling (MAPK
activation) to increases in extracellular
calcium concentrations;
dbSNP:rs121909268).
{ECO:0000269|PubMed:17473068}.
/FTId=VAR_058057.
VARIANT 185 185 R -> Q (in HHC1; decreased G-protein
coupled receptor signaling pathway;
dbSNP:rs104893689).
{ECO:0000269|PubMed:7916660,
ECO:0000269|PubMed:8636323,
ECO:0000269|PubMed:8702647}.
/FTId=VAR_003593.
VARIANT 191 191 E -> K (in HYPOC1; increased G-protein
coupled receptor signaling pathway;
dbSNP:rs104893697).
{ECO:0000269|PubMed:8813042,
ECO:0000269|PubMed:8878438}.
/FTId=VAR_058058.
VARIANT 215 215 D -> G (in HHC1; decreased G-protein
coupled receptor signaling pathway).
{ECO:0000269|PubMed:27434672,
ECO:0000269|PubMed:8636323}.
/FTId=VAR_078155.
VARIANT 220 220 R -> W (in HHC1).
{ECO:0000269|PubMed:19179454}.
/FTId=VAR_078156.
VARIANT 221 221 P -> L (in HYPOC1; dbSNP:rs397514728).
{ECO:0000269|PubMed:22789683}.
/FTId=VAR_078157.
VARIANT 221 221 P -> Q (in HHC1; dbSNP:rs397514728).
{ECO:0000269|PubMed:17698911}.
/FTId=VAR_058059.
VARIANT 221 221 P -> S (in HHC1; decreased G-protein
coupled receptor signaling pathway).
{ECO:0000269|PubMed:8878438}.
/FTId=VAR_078158.
VARIANT 225 225 K -> T (in HHC1).
{ECO:0000269|PubMed:17698911}.
/FTId=VAR_058060.
VARIANT 227 227 R -> L (in NSHPT; decreased G-protein
coupled receptor signaling pathway; does
not affect cell membrane localization;
dbSNP:rs28936684).
{ECO:0000269|PubMed:15572418,
ECO:0000269|PubMed:27434672,
ECO:0000269|PubMed:8675635,
ECO:0000269|PubMed:8878438}.
/FTId=VAR_003594.
VARIANT 227 227 R -> Q (in HHC1; G-protein coupled
receptor signaling pathway; less markedly
impaired relative to wild-type than L-
227; does not affect cell membrane
localization; dbSNP:rs28936684).
{ECO:0000269|PubMed:15572418,
ECO:0000269|PubMed:7726161}.
/FTId=VAR_003595.
VARIANT 228 228 E -> K (in HYPOC1).
{ECO:0000269|PubMed:19179454}.
/FTId=VAR_078159.
VARIANT 250 250 E -> K (in dbSNP:rs62269092).
{ECO:0000269|PubMed:17698911}.
/FTId=VAR_058061.
VARIANT 271 271 S -> F (in HHC1).
{ECO:0000269|PubMed:17698911}.
/FTId=VAR_058062.
VARIANT 297 297 E -> K (in HHC1; decreased G-protein
coupled receptor signaling pathway;
dbSNP:rs121909259).
{ECO:0000269|PubMed:27434672,
ECO:0000269|PubMed:7916660,
ECO:0000269|PubMed:8702647}.
/FTId=VAR_003596.
VARIANT 336 336 Missing (in NSHPT).
{ECO:0000269|PubMed:14985373}.
/FTId=VAR_065200.
VARIANT 339 339 P -> T (mutation found in a patient with
primary hyperparathyroidism detected at
adulthood; inactivating mutation; mutant
CASR is activated by a higher calcium
concentrations than the wild-type).
{ECO:0000269|PubMed:20846291}.
/FTId=VAR_065201.
VARIANT 354 354 E -> A (in EIG8; patients present
juvenile myoclonus epilepsy).
{ECO:0000269|PubMed:18756473}.
/FTId=VAR_060206.
VARIANT 397 397 G -> R (in HHC1).
{ECO:0000269|PubMed:17698911}.
/FTId=VAR_058063.
VARIANT 459 459 Q -> R (in HHC1; decreased G-protein
coupled receptor signaling pathway; does
not affect cell membrane localization).
{ECO:0000269|PubMed:19789209}.
/FTId=VAR_078160.
VARIANT 465 465 R -> Q (in HHC1; loss-of-function
mutation; the quantity of the mutant
receptor is higher than that of the wild-
type receptor; dose-response curves show
that the mutation significantly reduces
the sensitivity of the receptor to
extracellular calcium concentrations;
dbSNP:rs104893716).
{ECO:0000269|PubMed:16598859}.
/FTId=VAR_058064.
VARIANT 509 509 G -> R (in HHC1; dbSNP:rs193922423).
{ECO:0000269|PubMed:17698911}.
/FTId=VAR_058065.
VARIANT 549 549 G -> R (in HHC1).
{ECO:0000269|PubMed:19179454}.
/FTId=VAR_078161.
VARIANT 550 550 T -> I (in HHC1; decreased G-protein
coupled receptor signaling pathway).
{ECO:0000269|PubMed:21566075}.
/FTId=VAR_078162.
VARIANT 551 551 R -> K (in NSHPT; decreased G-protein
coupled receptor signaling pathway; does
not affect cell membrane localization).
{ECO:0000269|PubMed:17555508,
ECO:0000269|PubMed:27434672}.
/FTId=VAR_078163.
VARIANT 553 553 G -> R (in HHC1; dbSNP:rs104893719).
{ECO:0000269|PubMed:17698911}.
/FTId=VAR_058066.
VARIANT 555 555 I -> V (in HHC1; dbSNP:rs777646067).
{ECO:0000269|PubMed:17698911}.
/FTId=VAR_058067.
VARIANT 557 557 G -> E (in HHC1; Abolished G-protein
coupled receptor activity).
{ECO:0000269|PubMed:11762699,
ECO:0000269|PubMed:27434672}.
/FTId=VAR_012649.
VARIANT 562 562 C -> Y (in HHC1).
{ECO:0000269|PubMed:17698911,
ECO:0000269|PubMed:19179454}.
/FTId=VAR_058068.
VARIANT 565 565 C -> G (in HHC1).
{ECO:0000269|PubMed:19179454}.
/FTId=VAR_078164.
VARIANT 569 569 P -> H (in HYPOC1; increased G-protein
coupled receptor signaling pathway).
{ECO:0000269|PubMed:23966241}.
/FTId=VAR_078165.
VARIANT 571 571 G -> W (in HHC1; decreased G-protein
coupled receptor signaling pathway; does
not affect cell membrane localization).
{ECO:0000269|PubMed:26386835}.
/FTId=VAR_078166.
VARIANT 582 582 C -> F (in HHC1; dbSNP:rs104893690).
{ECO:0000269|PubMed:17698911}.
/FTId=VAR_058069.
VARIANT 582 582 C -> Y (in NSHPT and HHC1;
dbSNP:rs104893690).
{ECO:0000269|PubMed:17698911,
ECO:0000269|PubMed:19179454,
ECO:0000269|PubMed:8675635}.
/FTId=VAR_003597.
VARIANT 583 1078 Missing (in HHC1; impaired
homodimerization; impaired cell membrane
localization).
{ECO:0000269|PubMed:16740594,
ECO:0000269|PubMed:19179454}.
/FTId=VAR_078167.
VARIANT 604 604 E -> K (in HYPOC1; there is a significant
leftward shift in the concentration
response curves for the effects of
extracellular calcium on both
intracellular calcium mobilization and
MAPK activity; dbSNP:rs104893712).
{ECO:0000269|PubMed:12574188,
ECO:0000269|PubMed:19179454}.
/FTId=VAR_058070.
VARIANT 612 612 F -> S (in HYPOC1; dbSNP:rs104893698).
{ECO:0000269|PubMed:8813042}.
/FTId=VAR_058071.
VARIANT 616 616 L -> V (in HYPOC1; does not affect the
total accumulation of inositol phosphates
as a function of extracellular calcium
concentrations in transfected cells;
dbSNP:rs104893703).
{ECO:0000269|PubMed:10487661}.
/FTId=VAR_015414.
VARIANT 623 623 G -> D (in HHC1).
{ECO:0000269|PubMed:17698911}.
/FTId=VAR_058072.
VARIANT 650 650 L -> P (in NSHPT).
{ECO:0000269|PubMed:14985373}.
/FTId=VAR_065202.
VARIANT 657 657 S -> Y (in HHC1).
{ECO:0000269|PubMed:8636323}.
/FTId=VAR_078168.
VARIANT 661 661 C -> Y (in HHC1).
{ECO:0000269|PubMed:19179454}.
/FTId=VAR_078169.
VARIANT 670 670 G -> E (in NSHPT; dbSNP:rs104893700).
{ECO:0000269|PubMed:9253359}.
/FTId=VAR_058073.
VARIANT 670 670 G -> R (in HHC1).
{ECO:0000269|PubMed:17698911}.
/FTId=VAR_058074.
VARIANT 680 680 R -> H (in HHC1; dbSNP:rs773146939).
{ECO:0000269|PubMed:19179454}.
/FTId=VAR_078170.
VARIANT 681 681 Q -> H (in HYPOC1; dbSNP:rs121909261).
{ECO:0000269|PubMed:8733126}.
/FTId=VAR_003598.
VARIANT 681 681 Q -> R (in HYPOC1; increased G-protein
coupled receptor signaling pathway; does
not affect cell membrane localization).
{ECO:0000269|PubMed:22789683}.
/FTId=VAR_078171.
VARIANT 686 686 I -> V (in EIG8; patients present
juvenile myoclonus epilepsy;
dbSNP:rs753013993).
{ECO:0000269|PubMed:18756473}.
/FTId=VAR_060207.
VARIANT 689 689 V -> M (in NSHPT).
{ECO:0000269|PubMed:14985373}.
/FTId=VAR_065203.
VARIANT 697 697 V -> M (in HHC1).
{ECO:0000269|PubMed:21643651}.
/FTId=VAR_065494.
VARIANT 707 707 E -> V (in HHC1; decreased protein
level). {ECO:0000269|PubMed:25104082}.
/FTId=VAR_078172.
VARIANT 727 727 L -> Q (in HYPOC1; increased G-protein
coupled receptor signaling pathway; does
not affect cell membrane localization;
dbSNP:rs104893718).
{ECO:0000269|PubMed:16608894,
ECO:0000269|PubMed:22789683}.
/FTId=VAR_058075.
VARIANT 728 728 V -> F (in HHC1).
{ECO:0000269|PubMed:17698911}.
/FTId=VAR_058076.
VARIANT 742 742 W -> R (in HHC1).
{ECO:0000269|PubMed:17698911}.
/FTId=VAR_058077.
VARIANT 748 748 P -> R (in HHC1).
{ECO:0000269|PubMed:8636323}.
/FTId=VAR_078173.
VARIANT 761 761 Missing (in HHC1).
{ECO:0000269|PubMed:19179454}.
/FTId=VAR_078174.
VARIANT 767 767 E -> K (in HYPOC1).
{ECO:0000269|PubMed:15551332}.
/FTId=VAR_021019.
VARIANT 773 773 L -> R (in HYPOC1; the mutation shifts
the concentration-response curve to the
left and increases maximal activity;
dbSNP:rs104893699).
{ECO:0000269|PubMed:9253358}.
/FTId=VAR_058078.
VARIANT 774 774 G -> S (in HHC1; decreased G-protein
coupled receptor signaling pathway; does
not affect cell membrane localization).
{ECO:0000269|PubMed:25104082}.
/FTId=VAR_078175.
VARIANT 788 788 F -> C (in HYPOC1; leftward shift in the
concentration-response curve for the
mutant receptor; cells cotransfected with
both the wild-type and the mutant
receptor show an EC(50) similar to the
mutant; a gain-of-function mutation
rendering the receptor more sensitive
than normal to activation;
dbSNP:rs104893701).
{ECO:0000269|PubMed:9661634}.
/FTId=VAR_058079.
VARIANT 788 788 F -> L (in HYPOC1; induces a significant
shift to the left relative to the wild-
type protein in the MAPK response to
increasing extracellular calcium
concentrations; dbSNP:rs104893711).
{ECO:0000269|PubMed:12915654}.
/FTId=VAR_058080.
VARIANT 795 795 R -> W (in HHC1; decreased G-protein
coupled receptor signaling pathway;
dbSNP:rs121909258).
{ECO:0000269|PubMed:19179454,
ECO:0000269|PubMed:22114145,
ECO:0000269|PubMed:7916660,
ECO:0000269|PubMed:8702647}.
/FTId=VAR_003599.
VARIANT 802 802 N -> I (in HYPOC1; increased G-protein
coupled receptor signaling pathway).
{ECO:0000269|PubMed:19179454,
ECO:0000269|PubMed:23169696}.
/FTId=VAR_078176.
VARIANT 802 802 N -> S (in HHC1; decreased G-protein
coupled receptor signaling pathway;
dbSNP:rs140022350).
{ECO:0000269|PubMed:23169696}.
/FTId=VAR_078177.
VARIANT 806 806 F -> S (in HYPOC1; does not produce a
significant activating effect; decreased
cell surface receptor expression;
dbSNP:rs104893693).
{ECO:0000269|PubMed:8733126,
ECO:0000269|PubMed:9253358}.
/FTId=VAR_003600.
VARIANT 817 817 V -> I (in HHC1; decreased G-protein
coupled receptor signaling pathway).
{ECO:0000269|PubMed:8878438}.
/FTId=VAR_078178.
VARIANT 820 820 S -> F (in HYPOC1; the concentration-
response curve of the mutant receptor is
left-shifted and its EC(50) is
significantly lower than that of the
wild-type; dbSNP:rs104893710).
{ECO:0000269|PubMed:12050233}.
/FTId=VAR_058081.
VARIANT 830 830 G -> S (in HYPOC1).
{ECO:0000269|PubMed:19179454}.
/FTId=VAR_078179.
VARIANT 832 832 F -> L (in HYPOC1).
{ECO:0000269|PubMed:19179454}.
/FTId=VAR_078180.
VARIANT 832 832 F -> S (in HYPOC1).
{ECO:0000269|PubMed:19179454}.
/FTId=VAR_078181.
VARIANT 839 839 I -> T (in HYPOC1; increased G-protein
coupled receptor signaling pathway).
{ECO:0000269|PubMed:23966241}.
/FTId=VAR_078182.
VARIANT 843 843 A -> E (in HYPOC1; also in HYPOC1
associated with clinical features of
Bartter syndrome; shifts the
concentration-response curve of calcium
ions to the left; dbSNP:rs104893706).
{ECO:0000269|PubMed:12107202,
ECO:0000269|PubMed:12241879}.
/FTId=VAR_058082.
VARIANT 851 851 C -> S (in dbSNP:rs200777304).
{ECO:0000269|PubMed:8733126}.
/FTId=VAR_003601.
VARIANT 881 881 F -> L (probable disease-associated
mutation found in a patient with
hypercalciuric hypercalcemia; mutant CASR
has a right-shifted dose-response to
extracellular calcium concentrations;
activated by a higher calcium
concentrations than the wild-type;
dbSNP:rs104893704).
{ECO:0000269|PubMed:10843194}.
/FTId=VAR_058083.
VARIANT 886 886 R -> W (in HHC1).
{ECO:0000269|PubMed:17698911}.
/FTId=VAR_058084.
VARIANT 898 898 R -> Q (in EIG8; dbSNP:rs121909269).
{ECO:0000269|PubMed:18756473}.
/FTId=VAR_060208.
VARIANT 951 951 P -> T (in dbSNP:rs4987051).
/FTId=VAR_020220.
VARIANT 972 972 T -> M (in HHC1; decreased G-protein
coupled receptor signaling pathway;
dbSNP:rs200620134).
{ECO:0000269|PubMed:25292184}.
/FTId=VAR_078183.
VARIANT 986 986 A -> S (common polymorphism associated
with high serum level of calcium; is also
a potential predisposing factor in
disorders of bone and mineral metabolism;
dbSNP:rs1801725).
{ECO:0000269|PubMed:10023897,
ECO:0000269|PubMed:11161843,
ECO:0000269|PubMed:14985373,
ECO:0000269|PubMed:15531522,
ECO:0000269|PubMed:16598859,
ECO:0000269|PubMed:17555508,
ECO:0000269|PubMed:17698911,
ECO:0000269|PubMed:18756473,
ECO:0000269|PubMed:19789209,
ECO:0000269|PubMed:8636323,
ECO:0000269|Ref.5}.
/FTId=VAR_014450.
VARIANT 988 988 A -> G (in EIG8; patients present
juvenile myoclonus epilepsy).
{ECO:0000269|PubMed:18756473}.
/FTId=VAR_060209.
VARIANT 988 988 A -> V (in EIG8; patients present
juvenile myoclonus epilepsy;
dbSNP:rs759027000).
{ECO:0000269|PubMed:18756473}.
/FTId=VAR_060210.
VARIANT 990 990 R -> G (common polymorphism associated
with low serum level of calcium;
dbSNP:rs1042636).
{ECO:0000269|PubMed:12050233,
ECO:0000269|PubMed:14985373,
ECO:0000269|PubMed:15531522,
ECO:0000269|PubMed:15551332,
ECO:0000269|PubMed:17698911,
ECO:0000269|PubMed:18756473,
ECO:0000269|PubMed:7759551,
ECO:0000269|PubMed:8636323,
ECO:0000269|Ref.5}.
/FTId=VAR_020221.
VARIANT 1011 1011 E -> Q (common polymorphism;
dbSNP:rs1801726).
{ECO:0000269|PubMed:14985373,
ECO:0000269|PubMed:15531522,
ECO:0000269|PubMed:17698911,
ECO:0000269|PubMed:19789209,
ECO:0000269|PubMed:8636323,
ECO:0000269|Ref.5}.
/FTId=VAR_014451.
MUTAGEN 69 69 R->E: Abolishes G-protein coupled
receptor signaling pathway.
{ECO:0000269|PubMed:27434672}.
MUTAGEN 102 102 N->I: Abolishes G-protein coupled
receptor activity.
{ECO:0000269|PubMed:27434672}.
MUTAGEN 145 145 T->A: Abolishes G-protein coupled
receptor activity.
{ECO:0000269|PubMed:27434672}.
MUTAGEN 147 147 S->A: Nearly abolished G-protein coupled
receptor activity.
{ECO:0000269|PubMed:27434672}.
MUTAGEN 170 170 S->A: Abolishes G-protein coupled
receptor activity.
{ECO:0000269|PubMed:27434672}.
MUTAGEN 218 218 Y->S: Abolishes G-protein coupled
receptor activity.
{ECO:0000269|PubMed:27434672}.
MUTAGEN 297 297 E->I: Abolishes ability to sense calcium
or magnesium levels.
{ECO:0000269|PubMed:27386547}.
MUTAGEN 417 417 S->L: Abolishes G-protein coupled
receptor signaling pathway.
{ECO:0000269|PubMed:27434672}.
MUTAGEN 458 458 W->A: Decreased G-protein coupled
receptor signaling pathway.
{ECO:0000269|PubMed:27434672}.
MUTAGEN 482 482 C->S,Y: Abolishes ability of agonist AMG
416 to activate G-protein-coupled
receptor activity.
{ECO:0000269|PubMed:26290606}.
CONFLICT 857 857 I -> T (in Ref. 3; BAA09453).
{ECO:0000305}.
CONFLICT 878 878 A -> R (in Ref. 3; BAA09453).
{ECO:0000305}.
CONFLICT 926 926 Q -> R (in Ref. 2; AAA86503).
{ECO:0000305}.
STRAND 26 28 {ECO:0000244|PDB:5FBK}.
STRAND 31 38 {ECO:0000244|PDB:5FBK}.
STRAND 40 44 {ECO:0000244|PDB:5FBK}.
STRAND 60 63 {ECO:0000244|PDB:5FBK}.
HELIX 65 82 {ECO:0000244|PDB:5FBK}.
STRAND 85 90 {ECO:0000244|PDB:5FBK}.
STRAND 93 99 {ECO:0000244|PDB:5FBK}.
HELIX 104 114 {ECO:0000244|PDB:5FBK}.
HELIX 116 123 {ECO:0000244|PDB:5FBK}.
HELIX 125 128 {ECO:0000244|PDB:5FBK}.
STRAND 138 142 {ECO:0000244|PDB:5FBK}.
HELIX 147 159 {ECO:0000244|PDB:5FBK}.
STRAND 164 168 {ECO:0000244|PDB:5FBK}.
HELIX 172 175 {ECO:0000244|PDB:5FBK}.
TURN 177 179 {ECO:0000244|PDB:5FBK}.
STRAND 183 187 {ECO:0000244|PDB:5FBK}.
HELIX 191 203 {ECO:0000244|PDB:5FBK}.
STRAND 208 216 {ECO:0000244|PDB:5FBK}.
HELIX 219 232 {ECO:0000244|PDB:5FBK}.
STRAND 237 243 {ECO:0000244|PDB:5FBK}.
HELIX 249 261 {ECO:0000244|PDB:5FBK}.
STRAND 266 270 {ECO:0000244|PDB:5FBK}.
HELIX 273 285 {ECO:0000244|PDB:5FBK}.
STRAND 292 295 {ECO:0000244|PDB:5FBK}.
HELIX 297 300 {ECO:0000244|PDB:5FBK}.
TURN 303 305 {ECO:0000244|PDB:5FBK}.
HELIX 308 310 {ECO:0000244|PDB:5FBK}.
HELIX 311 314 {ECO:0000244|PDB:5FBK}.
STRAND 318 322 {ECO:0000244|PDB:5FBK}.
HELIX 330 335 {ECO:0000244|PDB:5FBK}.
TURN 339 341 {ECO:0000244|PDB:5FBK}.
STRAND 343 345 {ECO:0000244|PDB:5FBK}.
HELIX 348 356 {ECO:0000244|PDB:5FBK}.
STRAND 358 360 {ECO:0000244|PDB:5K5T}.
HELIX 374 378 {ECO:0000244|PDB:5K5T}.
STRAND 384 386 {ECO:0000244|PDB:5K5T}.
HELIX 387 389 {ECO:0000244|PDB:5K5T}.
HELIX 401 403 {ECO:0000244|PDB:5FBK}.
TURN 407 409 {ECO:0000244|PDB:5FBK}.
HELIX 416 435 {ECO:0000244|PDB:5FBK}.
STRAND 441 444 {ECO:0000244|PDB:5FBK}.
HELIX 445 447 {ECO:0000244|PDB:5FBK}.
HELIX 452 454 {ECO:0000244|PDB:5FBK}.
HELIX 457 465 {ECO:0000244|PDB:5FBK}.
STRAND 468 470 {ECO:0000244|PDB:5FBK}.
STRAND 476 478 {ECO:0000244|PDB:5FBK}.
STRAND 481 485 {ECO:0000244|PDB:5K5T}.
STRAND 489 496 {ECO:0000244|PDB:5FBK}.
TURN 498 500 {ECO:0000244|PDB:5FBK}.
STRAND 502 511 {ECO:0000244|PDB:5FBK}.
STRAND 513 515 {ECO:0000244|PDB:5FBH}.
STRAND 519 523 {ECO:0000244|PDB:5FBK}.
HELIX 525 527 {ECO:0000244|PDB:5FBK}.
TURN 531 533 {ECO:0000244|PDB:5FBK}.
STRAND 550 554 {ECO:0000244|PDB:5K5S}.
STRAND 556 558 {ECO:0000244|PDB:5K5T}.
STRAND 563 567 {ECO:0000244|PDB:5K5S}.
STRAND 576 578 {ECO:0000244|PDB:5K5T}.
STRAND 589 591 {ECO:0000244|PDB:5K5T}.
STRAND 595 600 {ECO:0000244|PDB:5K5T}.
SEQUENCE 1078 AA; 120675 MW; D60C57C6C743FC06 CRC64;
MAFYSCCWVL LALTWHTSAY GPDQRAQKKG DIILGGLFPI HFGVAAKDQD LKSRPESVEC
IRYNFRGFRW LQAMIFAIEE INSSPALLPN LTLGYRIFDT CNTVSKALEA TLSFVAQNKI
DSLNLDEFCN CSEHIPSTIA VVGATGSGVS TAVANLLGLF YIPQVSYASS SRLLSNKNQF
KSFLRTIPND EHQATAMADI IEYFRWNWVG TIAADDDYGR PGIEKFREEA EERDICIDFS
ELISQYSDEE EIQHVVEVIQ NSTAKVIVVF SSGPDLEPLI KEIVRRNITG KIWLASEAWA
SSSLIAMPQY FHVVGGTIGF ALKAGQIPGF REFLKKVHPR KSVHNGFAKE FWEETFNCHL
QEGAKGPLPV DTFLRGHEES GDRFSNSSTA FRPLCTGDEN ISSVETPYID YTHLRISYNV
YLAVYSIAHA LQDIYTCLPG RGLFTNGSCA DIKKVEAWQV LKHLRHLNFT NNMGEQVTFD
ECGDLVGNYS IINWHLSPED GSIVFKEVGY YNVYAKKGER LFINEEKILW SGFSREVPFS
NCSRDCLAGT RKGIIEGEPT CCFECVECPD GEYSDETDAS ACNKCPDDFW SNENHTSCIA
KEIEFLSWTE PFGIALTLFA VLGIFLTAFV LGVFIKFRNT PIVKATNREL SYLLLFSLLC
CFSSSLFFIG EPQDWTCRLR QPAFGISFVL CISCILVKTN RVLLVFEAKI PTSFHRKWWG
LNLQFLLVFL CTFMQIVICV IWLYTAPPSS YRNQELEDEI IFITCHEGSL MALGFLIGYT
CLLAAICFFF AFKSRKLPEN FNEAKFITFS MLIFFIVWIS FIPAYASTYG KFVSAVEVIA
ILAASFGLLA CIFFNKIYII LFKPSRNTIE EVRCSTAAHA FKVAARATLR RSNVSRKRSS
SLGGSTGSTP SSSISSKSNS EDPFPQPERQ KQQQPLALTQ QEQQQQPLTL PQQQRSQQQP
RCKQKVIFGS GTVTFSLSFD EPQKNAMAHR NSTHQNSLEA QKSSDTLTRH EPLLPLQCGE
TDLDLTVQET GLQGPVGGDQ RPEVEDPEEL SPALVVSSSQ SFVISGGGST VTENVVNS


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CSB-EL004558MO Mouse Extracellular calcium-sensing receptor(CASR) ELISA kit 96T
CSB-EL004558PI Pig Extracellular calcium-sensing receptor(CASR) ELISA kit SpeciesPig 96T
CSB-EL004558MO Mouse Extracellular calcium-sensing receptor(CASR) ELISA kit SpeciesMouse 96T
CSB-EL004558BO Bovine Extracellular calcium-sensing receptor(CASR) ELISA kit SpeciesBovine 96T
CSB-EL004558HU Human Extracellular calcium-sensing receptor(CASR) ELISA kit SpeciesHuman 96T
E1510m ELISA Kit FOR Extracellular calcium-sensing receptor; organism: Mouse; gene name: Casr 96T
CAST CASR Gene calcium-sensing receptor
GWB-AB8E96 Calcium Sensing Receptor (CaSR), Antibody
E-EL-R0137 Rat CASR (Calcium Sensing Receptor) ELISA Kit 96T
E02C0537 Rat Calcium Sensing Receptor ELISA , CaSR 96 Tests/kit
201-20-0834 CASR{calcium-sensing receptor}rabbit.pAb 0.1ml
E02C0537 Rat Calcium Sensing Receptor ELISA , CaSR
GWB-7101AF Calcium Sensing Receptor (CaSR), Antibody
E02C0537 Rat Calcium Sensing Receptor Elisa Kit (CaSR) 96 Tests/kit


 

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