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Vitamin D3 receptor (VDR) (1,25-dihydroxyvitamin D3 receptor) (Nuclear receptor subfamily 1 group I member 1)

 VDR_HUMAN               Reviewed;         427 AA.
P11473; B2R5Q1; G3V1V9; Q5PSV3;
01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
01-OCT-1989, sequence version 1.
20-DEC-2017, entry version 215.
RecName: Full=Vitamin D3 receptor;
Short=VDR;
AltName: Full=1,25-dihydroxyvitamin D3 receptor;
AltName: Full=Nuclear receptor subfamily 1 group I member 1;
Name=VDR; Synonyms=NR1I1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=2835767; DOI=10.1073/pnas.85.10.3294;
Baker A.R., McDonnell D.P., Hughes M., Crisp T.M., Mangelsdorf D.J.,
Haussler M.R., Pike J.W., Shine J., O'Malley B.W.;
"Cloning and expression of full-length cDNA encoding human vitamin D
receptor.";
Proc. Natl. Acad. Sci. U.S.A. 85:3294-3298(1988).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=1324736; DOI=10.1016/0167-4781(92)90063-6;
Goto H., Chen K.S., Prahl J.M., Deluca H.F.;
"A single receptor identical with that from intestine/T47D cells
mediates the action of 1,25-dihydroxyvitamin D-3 in HL-60 cells.";
Biochim. Biophys. Acta 1132:103-108(1992).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Lens epithelium;
Rae J.L., Shepard A.R.;
Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=9212063; DOI=10.1210/mend.11.8.9951;
Miyamoto K., Kesterson R.A., Yamamoto H., Taketani Y., Nishiwaki E.,
Tatsumi S., Inoue Y., Morita K., Takeda E., Pike J.W.;
"Structural organization of the human vitamin D receptor chromosomal
gene and its promoter.";
Mol. Endocrinol. 11:1165-1179(1997).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS VAL-230 AND ILE-362.
NIEHS SNPs program;
Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16541075; DOI=10.1038/nature04569;
Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M.,
Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B.,
Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D.,
Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z.,
Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H.,
Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H.,
Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V.,
Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J.,
Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A.,
Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M.,
Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E.,
Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M.,
Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R.,
Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J.,
Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C.,
Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M.,
Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M.,
Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P.,
Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L.,
Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E.,
Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C.,
Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F.,
Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M.,
Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S.,
Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D.,
Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I.,
Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T.,
Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S.,
Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D.,
Kucherlapati R., Weinstock G., Gibbs R.A.;
"The finished DNA sequence of human chromosome 12.";
Nature 440:346-351(2006).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Placenta;
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).
[10]
NUCLEOTIDE SEQUENCE [MRNA] OF 24-90 (ISOFORM 1/2).
TISSUE=Peripheral blood;
PubMed=1850412;
Yu X.-P., Mocharla H., Hustmyer F.G., Manolagas S.C.;
"Vitamin D receptor expression in human lymphocytes. Signal
requirements and characterization by western blots and DNA
sequencing.";
J. Biol. Chem. 266:7588-7595(1991).
[11]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 343-427.
PubMed=16252240; DOI=10.1086/497438;
Fang Y., van Meurs J.B., d'Alesio A., Jhamai M., Zhao H.,
Rivadeneira F., Hofman A., van Leeuwen J.P., Jehan F., Pols H.A.,
Uitterlinden A.G.;
"Promoter and 3'-untranslated-region haplotypes in the vitamin D
receptor gene predispose to osteoporotic fracture: the Rotterdam
study.";
Am. J. Hum. Genet. 77:807-823(2005).
[12]
INTERACTION WITH NCOA3.
PubMed=9267036; DOI=10.1016/S0092-8674(00)80516-4;
Chen H., Lin R.J., Schiltz R.L., Chakravarti D., Nash A., Nagy L.,
Privalsky M.L., Nakatani Y., Evans R.M.;
"Nuclear receptor coactivator ACTR is a novel histone
acetyltransferase and forms a multimeric activation complex with P/CAF
and CBP/p300.";
Cell 90:569-580(1997).
[13]
INTERACTION WITH SNW1.
PubMed=9632709; DOI=10.1074/jbc.273.26.16434;
Baudino T.A., Kraichely D.M., Jefcoat S.C. Jr., Winchester S.K.,
Partridge N.C., Macdonald P.N.;
"Isolation and characterization of a novel coactivator protein, NCoA-
62, involved in vitamin D-mediated transcription.";
J. Biol. Chem. 273:16434-16441(1998).
[14]
INTERACTION WITH NCOA6.
PubMed=10866662; DOI=10.1128/MCB.20.14.5048-5063.2000;
Mahajan M.A., Samuels H.H.;
"A new family of nuclear receptor coregulators that integrates nuclear
receptor signaling through CBP.";
Mol. Cell. Biol. 20:5048-5063(2000).
[15]
FUNCTION, AND INTERACTION WITH BAZ1B.
PubMed=16252006; DOI=10.1038/sj.emboj.7600853;
Fujiki R., Kim M.-S., Sasaki Y., Yoshimura K., Kitagawa H., Kato S.;
"Ligand-induced transrepression by VDR through association of WSTF
with acetylated histones.";
EMBO J. 24:3881-3894(2005).
[16]
INTERACTION WITH IRX4.
TISSUE=Prostate;
PubMed=22323358; DOI=10.1093/hmg/dds025;
Nguyen H.H., Takata R., Akamatsu S., Shigemizu D., Tsunoda T.,
Furihata M., Takahashi A., Kubo M., Kamatani N., Ogawa O., Fujioka T.,
Nakamura Y., Nakagawa H.;
"IRX4 at 5p15 suppresses prostate cancer growth through the
interaction with vitamin D receptor, conferring prostate cancer
susceptibility.";
Hum. Mol. Genet. 21:2076-2085(2012).
[17]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 118-427 IN COMPLEX WITH
DIHYDROXYVITAMIN D3, IDENTIFICATION BY MASS SPECTROMETRY, AND
FUNCTION.
PubMed=10678179; DOI=10.1016/S1097-2765(00)80413-X;
Rochel N., Wurtz J.-M., Mitschler A., Klaholz B., Moras D.;
"The crystal structure of the nuclear receptor for vitamin D bound to
its natural ligand.";
Mol. Cell 5:173-179(2000).
[18]
X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF 118-427 IN COMPLEXES WITH
VITAMIN D3 AND VITAMIN D3 ANALOGS.
PubMed=11344298; DOI=10.1073/pnas.091018698;
Tocchini-Valentini G., Rochel N., Wurtz J.-M., Mitschler A., Moras D.;
"Crystal structures of the vitamin D receptor complexed to
superagonist 20-epi ligands.";
Proc. Natl. Acad. Sci. U.S.A. 98:5491-5496(2001).
[19]
X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 16-125 IN COMPLEX WITH DNA,
MUTAGENESIS OF 61-PRO-PHE-62 AND HIS-75, AND SUBUNIT.
PubMed=11980721; DOI=10.1093/emboj/21.9.2242;
Shaffer P.L., Gewirth D.T.;
"Structural basis of VDR-DNA interactions on direct repeat response
elements.";
EMBO J. 21:2242-2252(2002).
[20]
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 188-427 IN COMPLEXES WITH
VITAMIN D3 ANALOGS.
PubMed=15055995; DOI=10.1021/jm0310582;
Tocchini-Valentini G., Rochel N., Wurtz J.-M., Moras D.;
"Crystal structures of the vitamin D nuclear receptor liganded with
the vitamin D side chain analogues calcipotriol and seocalcitol,
receptor agonists of clinical importance. Insights into a structural
basis for the switching of calcipotriol to a receptor antagonist by
further side chain modification.";
J. Med. Chem. 47:1956-1961(2004).
[21]
X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 16-125 OF MUTANT
ALA-61/ALA-62/ALA-75 IN COMPLEX WITH RXRA AND DNA, AND SUBUNIT.
PubMed=15225774; DOI=10.1016/j.jsbmb.2004.03.084;
Shaffer P.L., Gewirth D.T.;
"Structural analysis of RXR-VDR interactions on DR3 DNA.";
J. Steroid Biochem. Mol. Biol. 89:215-219(2004).
[22]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 188-427 IN COMPLEX WITH
VITAMIN D3 ANALOG, IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, AND
INTERACTION WITH NCOA1; NCOA2 AND MED1.
PubMed=15728261; DOI=10.1124/mol.104.008730;
Eelen G., Verlinden L., Rochel N., Claessens F., De Clercq P.,
Vandewalle M., Tocchini-Valentini G., Moras D., Bouillon R.,
Verstuyf A.;
"Superagonistic action of 14-epi-analogs of 1,25-dihydroxyvitamin D
explained by vitamin D receptor-coactivator interaction.";
Mol. Pharmacol. 67:1566-1573(2005).
[23]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 188-427 IN COMPLEXES WITH
DIHYDROXYVITAMIN D3 AND VITAMIN D3 ANALOGS, AND FUNCTION.
PubMed=16913708; DOI=10.1021/jm0604070;
Hourai S., Fujishima T., Kittaka A., Suhara Y., Takayama H.,
Rochel N., Moras D.;
"Probing a water channel near the A-ring of receptor-bound 1 alpha,25-
dihydroxyvitamin D3 with selected 2 alpha-substituted analogues.";
J. Med. Chem. 49:5199-5205(2006).
[24]
VARIANTS VDDR2A ASP-33 AND GLN-73.
PubMed=2849209; DOI=10.1126/science.2849209;
Hughes M.R., Malloy P.J., Kieback D.G., Kesterson R.A., Pike J.W.,
Feldman D., O'Malley B.W.;
"Point mutations in the human vitamin D receptor gene associated with
hypocalcemic rickets.";
Science 242:1702-1705(1988).
[25]
VARIANT VDDR2A GLN-35.
PubMed=8381803; DOI=10.1210/jcem.76.2.8381803;
Yagi H., Ozono K., Miyake H., Nagashima K., Kuroume T., Pike J.W.;
"A new point mutation in the deoxyribonucleic acid-binding domain of
the vitamin D receptor in a kindred with hereditary 1,25-
dihydroxyvitamin D-resistant rickets.";
J. Clin. Endocrinol. Metab. 76:509-512(1993).
[26]
VARIANT VDDR2A GLN-50.
PubMed=1652893;
Saijo T., Ito M., Takeda E., Mahbubul Huq A.H.M., Naito E., Yokota I.,
Sone T., Pike J.W., Kuroda Y.;
"A unique mutation in the vitamin D receptor gene in three Japanese
patients with vitamin D-dependent rickets type II: utility of single-
strand conformation polymorphism analysis for heterozygous carrier
detection.";
Am. J. Hum. Genet. 49:668-673(1991).
[27]
VARIANT VDDR2A GLN-80.
PubMed=2177843; DOI=10.1210/mend-4-4-623;
Sone T., Marx S.J., Liberman U.A., Pike J.W.;
"A unique point mutation in the human vitamin D receptor chromosomal
gene confers hereditary resistance to 1,25-dihydroxyvitamin D3.";
Mol. Endocrinol. 4:623-631(1990).
[28]
VARIANT VDDR2A GLN-80.
PubMed=8106618; DOI=10.1210/jcem.78.2.8106618;
Malloy P.J., Weisman Y., Feldman D.;
"Hereditary 1 alpha,25-dihydroxyvitamin D-resistant rickets resulting
from a mutation in the vitamin D receptor deoxyribonucleic acid-
binding domain.";
J. Clin. Endocrinol. Metab. 78:313-316(1994).
[29]
VARIANTS VDDR2A 152-GLN--SER-427 DEL AND LEU-274.
PubMed=8392085; DOI=10.1172/JCI116539;
Kristjansson K., Rut A.R., Hewison M., O'Riordan J.L.H., Hughes M.R.;
"Two mutations in the hormone binding domain of the vitamin D receptor
cause tissue resistance to 1,25 dihydroxyvitamin D3.";
J. Clin. Invest. 92:12-16(1993).
[30]
VARIANTS VDDR2A GLU-45 AND ILE-47.
PubMed=7828346; DOI=10.1111/j.1365-2265.1994.tb01822.x;
Rut A.R., Hewison M., Kristjansson K., Luisi B., Hughes M.R.,
O'Riordan J.L.H.;
"Two mutations causing vitamin D resistant rickets: modelling on the
basis of steroid hormone receptor DNA-binding domain crystal
structures.";
Clin. Endocrinol. (Oxf.) 41:581-590(1994).
[31]
VARIANT VDDR2A ASP-46.
PubMed=8675579; DOI=10.1210/jcem.81.7.8675579;
Lin U.-T., Malloy P.J., Sakati N., Al-Ashwal A., Feldman D.;
"A novel mutation in the deoxyribonucleic acid-binding domain of the
vitamin D receptor causes hereditary 1,25-dihydroxyvitamin D-resistant
rickets.";
J. Clin. Endocrinol. Metab. 81:2564-2569(1996).
[32]
VARIANTS VDDR2A SER-314 AND CYS-391.
PubMed=8961271; DOI=10.1210/mend.10.12.8961271;
Whitfield G.K., Selznick S.H., Haussler C.A., Hsieh J.-C.,
Galligan M.A., Jurutka P.W., Thompson P.D., Lee S.M., Zerwekh J.E.,
Haussler M.R.;
"Vitamin D receptors from patients with resistance to 1,25-
dihydroxyvitamin D(3): point mutations confer reduced transactivation
in response to ligand and impaired interaction with the retinoid X
receptor heterodimeric partner.";
Mol. Endocrinol. 10:1617-1631(1996).
[33]
VARIANT VDDR2A GLN-305.
PubMed=9005998; DOI=10.1172/JCI119158;
Malloy P.J., Eccleshall T.R., Gross C., van Maldergem L., Bouillon R.,
Feldman D.;
"Hereditary vitamin D resistant rickets caused by a novel mutation in
the vitamin D receptor that results in decreased affinity for hormone
and cellular hyporesponsiveness.";
J. Clin. Invest. 99:297-304(1997).
[34]
INVOLVEMENT IN MYCOBACTERIUM TUBERCULOSIS SUSCEPTIBILITY.
PubMed=15032981; DOI=10.1111/j..2004.00183.x;
Selvaraj P., Kurian S.M., Chandra G., Reetha A.M., Charles N.,
Narayanan P.R.;
"Vitamin D receptor gene variants of BsmI, ApaI, TaqI, and FokI
polymorphisms in spinal tuberculosis.";
Clin. Genet. 65:73-76(2004).
[35]
VARIANT VDDR2A MET-346.
PubMed=17970811; DOI=10.1111/j.1365-2133.2007.08232.x;
Arita K., Nanda A., Wessagowit V., Akiyama M., Alsaleh Q.A.,
McGrath J.A.;
"A novel mutation in the VDR gene in hereditary vitamin D-resistant
rickets.";
Br. J. Dermatol. 158:168-171(2008).
[36]
VARIANT VDDR2A PRO-360, CHARACTERIZATION OF VARIANT VDDR2A
152-GLN--SER-427 DEL; LEU-274; GLN-305; MET-346 AND PRO-360, FUNCTION,
INTERACTION WITH NCOA1; NCOR1 AND RXR, AND SUBCELLULAR LOCATION.
PubMed=28698609; DOI=10.1038/s41598-017-05081-x;
Tamura M., Ishizawa M., Isojima T., Oezen S., Oka A., Makishima M.,
Kitanaka S.;
"Functional analyses of a novel missense and other mutations of the
vitamin D receptor in association with alopecia.";
Sci. Rep. 7:5102-5102(2017).
-!- FUNCTION: Nuclear receptor for calcitriol, the active form of
vitamin D3 which mediates the action of this vitamin on cells.
Enters the nucleus upon vitamin D3 binding where it forms
heterodimers with the retinoid X receptor/RXR. The VDR-RXR
heterodimers bind to specific response elements on DNA and
activate the transcription of vitamin D3-responsive target genes.
Recruited to promoters via its interaction with BAZ1B/WSTF which
mediates the interaction with acetylated histones, an essential
step for VDR-promoter association. Plays a central role in calcium
homeostasis. {ECO:0000269|PubMed:10678179,
ECO:0000269|PubMed:15728261, ECO:0000269|PubMed:16252006,
ECO:0000269|PubMed:16913708, ECO:0000269|PubMed:28698609}.
-!- SUBUNIT: Homodimer in the absence of bound vitamin D3. Heterodimer
with RXRA after vitamin D3 binding. Interacts with SMAD3.
Interacts with MED1, NCOA1, NCOA2, NCOA3 and NCOA6 coactivators,
leading to a strong increase of transcription of target genes.
Interacts with the corepressor NCOR1. Interacts (in a ligand-
dependent manner) with BAZ1B/WSTF. Interacts with SNW1. Interacts
with IRX4, the interaction doesn't affect its transactivation
activity. {ECO:0000269|PubMed:10678179,
ECO:0000269|PubMed:10866662, ECO:0000269|PubMed:11980721,
ECO:0000269|PubMed:15225774, ECO:0000269|PubMed:15728261,
ECO:0000269|PubMed:16252006, ECO:0000269|PubMed:22323358,
ECO:0000269|PubMed:28698609, ECO:0000269|PubMed:9267036,
ECO:0000269|PubMed:9632709}.
-!- INTERACTION:
Q09472:EP300; NbExp=3; IntAct=EBI-286357, EBI-447295;
Q15648:MED1; NbExp=3; IntAct=EBI-286357, EBI-394459;
P50222:MEOX2; NbExp=3; IntAct=EBI-286357, EBI-748397;
Q9JLI4:Ncoa6 (xeno); NbExp=2; IntAct=EBI-286357, EBI-286271;
P26045:PTPN3; NbExp=4; IntAct=EBI-286357, EBI-1047946;
P19793:RXRA; NbExp=6; IntAct=EBI-286357, EBI-78598;
P28700:Rxra (xeno); NbExp=3; IntAct=EBI-286357, EBI-346715;
Q13573:SNW1; NbExp=5; IntAct=EBI-286357, EBI-632715;
Q13501:SQSTM1; NbExp=4; IntAct=EBI-286357, EBI-307104;
P04637:TP53; NbExp=6; IntAct=EBI-286357, EBI-366083;
Q15645:TRIP13; NbExp=3; IntAct=EBI-286357, EBI-358993;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-
ProRule:PRU00407, ECO:0000269|PubMed:28698609}. Cytoplasm
{ECO:0000269|PubMed:28698609}. Note=Localizes mainly to the
nucleus. Localization to the nucleus is enhanced by vitamin D3.
{ECO:0000269|PubMed:28698609}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P11473-1; Sequence=Displayed;
Name=2;
IsoId=P11473-2; Sequence=VSP_047218;
Note=No experimental confirmation available.;
-!- DOMAIN: Composed of three domains: a modulating N-terminal domain,
a DNA-binding domain and a C-terminal ligand-binding domain.
-!- POLYMORPHISM: Genetic variations in VDR may determine
Mycobacterium tuberculosis susceptibility [MIM:607948].
{ECO:0000269|PubMed:15032981}.
-!- DISEASE: Rickets vitamin D-dependent 2A (VDDR2A) [MIM:277440]: A
disorder of vitamin D metabolism resulting in severe rickets,
hypocalcemia and secondary hyperparathyroidism. Most patients have
total alopecia in addition to rickets.
{ECO:0000269|PubMed:1652893, ECO:0000269|PubMed:17970811,
ECO:0000269|PubMed:2177843, ECO:0000269|PubMed:2849209,
ECO:0000269|PubMed:28698609, ECO:0000269|PubMed:7828346,
ECO:0000269|PubMed:8106618, ECO:0000269|PubMed:8381803,
ECO:0000269|PubMed:8392085, ECO:0000269|PubMed:8675579,
ECO:0000269|PubMed:8961271, ECO:0000269|PubMed:9005998}. Note=The
disease is caused by mutations affecting the gene represented in
this entry.
-!- SIMILARITY: Belongs to the nuclear hormone receptor family. NR1
subfamily. {ECO:0000305}.
-!- CAUTION: It is uncertain whether Met-1 or Met-4 is the initiator.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAH60832.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=AAP88938.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/vdr/";
-!- WEB RESOURCE: Name=SHMPD; Note=The Singapore human mutation and
polymorphism database;
URL="http://shmpd.bii.a-star.edu.sg/gene.php?genestart=A&genename=VDR";
-----------------------------------------------------------------------
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EMBL; J03258; AAA61273.1; -; mRNA.
EMBL; X67482; CAA47824.1; -; mRNA.
EMBL; AF026260; AAB95155.1; -; mRNA.
EMBL; AB002168; BAA83389.1; -; Genomic_DNA.
EMBL; AY342401; AAP88938.1; ALT_SEQ; Genomic_DNA.
EMBL; AK312267; BAG35198.1; -; mRNA.
EMBL; AC004466; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC121338; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471111; EAW57960.1; -; Genomic_DNA.
EMBL; CH471111; EAW57961.1; -; Genomic_DNA.
EMBL; BC060832; AAH60832.1; ALT_INIT; mRNA.
EMBL; M65208; AAA61274.1; -; mRNA.
EMBL; AY827087; AAV85448.1; -; Genomic_DNA.
CCDS; CCDS55820.1; -. [P11473-2]
CCDS; CCDS8757.1; -. [P11473-1]
PIR; A28200; A28200.
RefSeq; NP_000367.1; NM_000376.2. [P11473-1]
RefSeq; NP_001017535.1; NM_001017535.1. [P11473-1]
RefSeq; NP_001017536.1; NM_001017536.1. [P11473-2]
RefSeq; XP_006719650.1; XM_006719587.3. [P11473-1]
RefSeq; XP_011537022.1; XM_011538720.2. [P11473-1]
UniGene; Hs.524368; -.
PDB; 1DB1; X-ray; 1.80 A; A=118-427.
PDB; 1IE8; X-ray; 1.52 A; A=118-427.
PDB; 1IE9; X-ray; 1.40 A; A=118-427.
PDB; 1KB2; X-ray; 2.70 A; A/B=16-125.
PDB; 1KB4; X-ray; 2.80 A; A/B=16-125.
PDB; 1KB6; X-ray; 2.70 A; A/B=16-125.
PDB; 1S0Z; X-ray; 2.50 A; A=118-427.
PDB; 1S19; X-ray; 2.10 A; A=118-427.
PDB; 1TXI; X-ray; 1.90 A; A=118-427.
PDB; 1YNW; X-ray; 3.00 A; A=16-125.
PDB; 2HAM; X-ray; 1.90 A; A=118-427.
PDB; 2HAR; X-ray; 1.90 A; A=118-427.
PDB; 2HAS; X-ray; 1.96 A; A=118-427.
PDB; 2HB7; X-ray; 1.80 A; A=118-427.
PDB; 2HB8; X-ray; 2.00 A; A=118-427.
PDB; 3A2I; X-ray; 3.27 A; A=118-427.
PDB; 3A2J; X-ray; 2.70 A; A=118-427.
PDB; 3A3Z; X-ray; 1.72 A; X=118-427.
PDB; 3A40; X-ray; 1.45 A; X=118-427.
PDB; 3A78; X-ray; 1.90 A; A=118-427.
PDB; 3AUQ; X-ray; 2.64 A; A=118-427.
PDB; 3AUR; X-ray; 2.21 A; A=118-427.
PDB; 3AX8; X-ray; 2.60 A; A=118-427.
PDB; 3AZ1; X-ray; 1.50 A; A=120-423.
PDB; 3AZ2; X-ray; 1.69 A; A=120-423.
PDB; 3AZ3; X-ray; 1.36 A; A=120-423.
PDB; 3B0T; X-ray; 1.30 A; A=120-423.
PDB; 3CS4; X-ray; 2.00 A; A=118-427.
PDB; 3CS6; X-ray; 1.80 A; A=118-427.
PDB; 3KPZ; X-ray; 1.90 A; A=118-427.
PDB; 3M7R; X-ray; 1.80 A; A=120-423.
PDB; 3OGT; X-ray; 1.75 A; A=118-427.
PDB; 3P8X; X-ray; 1.70 A; A=118-164, A=217-427.
PDB; 3TKC; X-ray; 1.75 A; A=118-427.
PDB; 3VHW; X-ray; 2.43 A; A=118-427.
PDB; 3W0A; X-ray; 1.80 A; A=120-423.
PDB; 3W0C; X-ray; 1.90 A; A=120-423.
PDB; 3W0Y; X-ray; 1.98 A; A=120-423.
PDB; 3WGP; X-ray; 2.00 A; A=120-423.
PDB; 3WWR; X-ray; 3.18 A; A=118-427.
PDB; 3X31; X-ray; 2.11 A; A=118-427.
PDB; 3X36; X-ray; 1.93 A; A=118-427.
PDB; 4G2I; X-ray; 1.80 A; A=118-427.
PDB; 4ITE; X-ray; 2.49 A; A=118-427.
PDB; 4ITF; X-ray; 2.84 A; A=118-427.
PDB; 5GT4; X-ray; 1.83 A; A=118-423.
PDBsum; 1DB1; -.
PDBsum; 1IE8; -.
PDBsum; 1IE9; -.
PDBsum; 1KB2; -.
PDBsum; 1KB4; -.
PDBsum; 1KB6; -.
PDBsum; 1S0Z; -.
PDBsum; 1S19; -.
PDBsum; 1TXI; -.
PDBsum; 1YNW; -.
PDBsum; 2HAM; -.
PDBsum; 2HAR; -.
PDBsum; 2HAS; -.
PDBsum; 2HB7; -.
PDBsum; 2HB8; -.
PDBsum; 3A2I; -.
PDBsum; 3A2J; -.
PDBsum; 3A3Z; -.
PDBsum; 3A40; -.
PDBsum; 3A78; -.
PDBsum; 3AUQ; -.
PDBsum; 3AUR; -.
PDBsum; 3AX8; -.
PDBsum; 3AZ1; -.
PDBsum; 3AZ2; -.
PDBsum; 3AZ3; -.
PDBsum; 3B0T; -.
PDBsum; 3CS4; -.
PDBsum; 3CS6; -.
PDBsum; 3KPZ; -.
PDBsum; 3M7R; -.
PDBsum; 3OGT; -.
PDBsum; 3P8X; -.
PDBsum; 3TKC; -.
PDBsum; 3VHW; -.
PDBsum; 3W0A; -.
PDBsum; 3W0C; -.
PDBsum; 3W0Y; -.
PDBsum; 3WGP; -.
PDBsum; 3WWR; -.
PDBsum; 3X31; -.
PDBsum; 3X36; -.
PDBsum; 4G2I; -.
PDBsum; 4ITE; -.
PDBsum; 4ITF; -.
PDBsum; 5GT4; -.
DisProt; DP00184; -.
ProteinModelPortal; P11473; -.
SMR; P11473; -.
BioGrid; 113264; 93.
CORUM; P11473; -.
DIP; DIP-32624N; -.
ELM; P11473; -.
IntAct; P11473; 29.
MINT; MINT-236408; -.
STRING; 9606.ENSP00000447173; -.
BindingDB; P11473; -.
ChEMBL; CHEMBL1977; -.
DrugBank; DB01436; Alfacalcidol.
DrugBank; DB00146; Calcidiol.
DrugBank; DB02300; Calcipotriol.
DrugBank; DB00136; Calcitriol.
DrugBank; DB00169; Cholecalciferol.
DrugBank; DB05024; CTA018.
DrugBank; DB01070; Dihydrotachysterol.
DrugBank; DB06410; Doxercalciferol.
DrugBank; DB05295; Eldecalcitol.
DrugBank; DB00153; Ergocalciferol.
DrugBank; DB04796; Inecalcitol.
DrugBank; DB00910; Paricalcitol.
DrugBank; DB04258; Seocalcitol.
GuidetoPHARMACOLOGY; 605; -.
SwissLipids; SLP:000001571; -.
TCDB; 9.B.208.1.1; the vitamin d3 receptor (vdr) family.
iPTMnet; P11473; -.
PhosphoSitePlus; P11473; -.
BioMuta; VDR; -.
DMDM; 137617; -.
MaxQB; P11473; -.
PaxDb; P11473; -.
PeptideAtlas; P11473; -.
PRIDE; P11473; -.
DNASU; 7421; -.
Ensembl; ENST00000229022; ENSP00000229022; ENSG00000111424. [P11473-1]
Ensembl; ENST00000395324; ENSP00000378734; ENSG00000111424. [P11473-1]
Ensembl; ENST00000549336; ENSP00000449573; ENSG00000111424. [P11473-1]
Ensembl; ENST00000550325; ENSP00000447173; ENSG00000111424. [P11473-2]
GeneID; 7421; -.
KEGG; hsa:7421; -.
UCSC; uc001rql.4; human. [P11473-1]
CTD; 7421; -.
DisGeNET; 7421; -.
EuPathDB; HostDB:ENSG00000111424.10; -.
GeneCards; VDR; -.
HGNC; HGNC:12679; VDR.
HPA; CAB004617; -.
HPA; HPA047740; -.
MalaCards; VDR; -.
MIM; 277440; phenotype.
MIM; 601769; gene.
MIM; 607948; phenotype.
neXtProt; NX_P11473; -.
OpenTargets; ENSG00000111424; -.
Orphanet; 93160; Hypocalcemic vitamin D-resistant rickets.
PharmGKB; PA37301; -.
eggNOG; KOG3575; Eukaryota.
eggNOG; ENOG410XRZC; LUCA.
GeneTree; ENSGT00870000136372; -.
HOGENOM; HOG000220844; -.
HOVERGEN; HBG108655; -.
InParanoid; P11473; -.
KO; K08539; -.
OMA; PECSMKL; -.
OrthoDB; EOG091G05X3; -.
PhylomeDB; P11473; -.
TreeFam; TF316304; -.
Reactome; R-HSA-383280; Nuclear Receptor transcription pathway.
SignaLink; P11473; -.
SIGNOR; P11473; -.
ChiTaRS; VDR; human.
EvolutionaryTrace; P11473; -.
GeneWiki; Calcitriol_receptor; -.
GenomeRNAi; 7421; -.
PRO; PR:P11473; -.
Proteomes; UP000005640; Chromosome 12.
Bgee; ENSG00000111424; -.
CleanEx; HS_VDR; -.
ExpressionAtlas; P11473; baseline and differential.
Genevisible; P11473; HS.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0043235; C:receptor complex; IDA:BHF-UCL.
GO; GO:0090575; C:RNA polymerase II transcription factor complex; IDA:BHF-UCL.
GO; GO:1902098; F:calcitriol binding; IDA:UniProtKB.
GO; GO:0008434; F:calcitriol receptor activity; IDA:UniProtKB.
GO; GO:0003677; F:DNA binding; IDA:MGI.
GO; GO:1902121; F:lithocholic acid binding; IDA:UniProtKB.
GO; GO:0038186; F:lithocholic acid receptor activity; IDA:UniProtKB.
GO; GO:0046965; F:retinoid X receptor binding; IDA:UniProtKB.
GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
GO; GO:0003707; F:steroid hormone receptor activity; IEA:InterPro.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0038183; P:bile acid signaling pathway; IDA:UniProtKB.
GO; GO:0006816; P:calcium ion transport; IEA:Ensembl.
GO; GO:0000902; P:cell morphogenesis; IMP:UniProtKB.
GO; GO:0006874; P:cellular calcium ion homeostasis; IEA:Ensembl.
GO; GO:0046697; P:decidualization; IEP:BHF-UCL.
GO; GO:0050892; P:intestinal absorption; IEA:Ensembl.
GO; GO:0007595; P:lactation; IEA:Ensembl.
GO; GO:0060745; P:mammary gland branching involved in pregnancy; IEA:Ensembl.
GO; GO:0008285; P:negative regulation of cell proliferation; IDA:BHF-UCL.
GO; GO:0010839; P:negative regulation of keratinocyte proliferation; IMP:UniProtKB.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IDA:BHF-UCL.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:MGI.
GO; GO:0060058; P:positive regulation of apoptotic process involved in mammary gland involution; IEA:Ensembl.
GO; GO:0010628; P:positive regulation of gene expression; IMP:UniProtKB.
GO; GO:0045618; P:positive regulation of keratinocyte differentiation; IMP:UniProtKB.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IMP:UniProtKB.
GO; GO:0010980; P:positive regulation of vitamin D 24-hydroxylase activity; IDA:BHF-UCL.
GO; GO:0060558; P:regulation of calcidiol 1-monooxygenase activity; ISS:BHF-UCL.
GO; GO:0007165; P:signal transduction; TAS:ProtInc.
GO; GO:0001501; P:skeletal system development; IEA:Ensembl.
GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; TAS:Reactome.
GO; GO:0070561; P:vitamin D receptor signaling pathway; IDA:BHF-UCL.
Gene3D; 1.10.565.10; -; 1.
Gene3D; 3.30.50.10; -; 1.
InterPro; IPR035500; NHR_like_dom_sf.
InterPro; IPR000536; Nucl_hrmn_rcpt_lig-bd.
InterPro; IPR001723; Nuclear_hrmn_rcpt.
InterPro; IPR000324; VitD_rcpt.
InterPro; IPR001628; Znf_hrmn_rcpt.
InterPro; IPR013088; Znf_NHR/GATA.
Pfam; PF00104; Hormone_recep; 1.
Pfam; PF00105; zf-C4; 1.
PRINTS; PR00398; STRDHORMONER.
PRINTS; PR00047; STROIDFINGER.
PRINTS; PR00350; VITAMINDR.
SMART; SM00430; HOLI; 1.
SMART; SM00399; ZnF_C4; 1.
SUPFAM; SSF48508; SSF48508; 1.
PROSITE; PS51843; NR_LBD; 1.
PROSITE; PS00031; NUCLEAR_REC_DBD_1; 1.
PROSITE; PS51030; NUCLEAR_REC_DBD_2; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Complete proteome; Cytoplasm;
Disease mutation; DNA-binding; Metal-binding; Nucleus; Polymorphism;
Receptor; Reference proteome; Transcription; Transcription regulation;
Zinc; Zinc-finger.
CHAIN 1 427 Vitamin D3 receptor.
/FTId=PRO_0000053542.
DOMAIN 127 423 NR LBD. {ECO:0000255|PROSITE-
ProRule:PRU01189}.
DNA_BIND 21 96 Nuclear receptor. {ECO:0000255|PROSITE-
ProRule:PRU00407}.
ZN_FING 24 44 NR C4-type. {ECO:0000255|PROSITE-
ProRule:PRU00407}.
ZN_FING 60 84 NR C4-type. {ECO:0000255|PROSITE-
ProRule:PRU00407}.
REGION 97 126 Hinge.
REGION 227 237 Vitamin D3 binding.
REGION 271 278 Vitamin D3 binding.
BINDING 143 143 Vitamin D3.
BINDING 305 305 Vitamin D3.
BINDING 397 397 Vitamin D3.
VAR_SEQ 1 1 M -> MEWRNKKRSDWLSMVLRTAGVEEAFGSEVSVRPHRR
APLGSTYLPPAPSGM (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_047218.
VARIANT 33 33 G -> D (in VDDR2A; dbSNP:rs121909790).
{ECO:0000269|PubMed:2849209}.
/FTId=VAR_004656.
VARIANT 35 35 H -> Q (in VDDR2A).
{ECO:0000269|PubMed:8381803}.
/FTId=VAR_004657.
VARIANT 45 45 K -> E (in VDDR2A).
{ECO:0000269|PubMed:7828346}.
/FTId=VAR_004658.
VARIANT 46 46 G -> D (in VDDR2A; dbSNP:rs121909797).
{ECO:0000269|PubMed:8675579}.
/FTId=VAR_004659.
VARIANT 47 47 F -> I (in VDDR2A).
{ECO:0000269|PubMed:7828346}.
/FTId=VAR_004660.
VARIANT 50 50 R -> Q (in VDDR2A; dbSNP:rs121909794).
{ECO:0000269|PubMed:1652893}.
/FTId=VAR_004661.
VARIANT 73 73 R -> Q (in VDDR2A; dbSNP:rs121909791).
{ECO:0000269|PubMed:2849209}.
/FTId=VAR_004662.
VARIANT 80 80 R -> Q (in VDDR2A; dbSNP:rs121909793).
{ECO:0000269|PubMed:2177843,
ECO:0000269|PubMed:8106618}.
/FTId=VAR_004663.
VARIANT 152 427 Missing (in VDDR2A; loss of calcitriol
receptor activity; loss of affinity for
calcitriol; no effect on ligand-
independent localization to the nucleus;
dbSNP:rs121909795).
{ECO:0000269|PubMed:28698609,
ECO:0000269|PubMed:8392085}.
/FTId=VAR_079325.
VARIANT 230 230 L -> V (in dbSNP:rs11574090).
{ECO:0000269|Ref.5}.
/FTId=VAR_029309.
VARIANT 274 274 R -> L (in VDDR2A; loss of calcitriol
receptor activity; decreased affinity for
calcitriol by a factor of 1000; no effect
on interaction with RXRA; changed
interaction with NCOR1; loss of
interaction with NCOA1; no effect on
sequence-specific DNA-binding;
dbSNP:rs121909796).
{ECO:0000269|PubMed:28698609,
ECO:0000269|PubMed:8392085}.
/FTId=VAR_004664.
VARIANT 305 305 H -> Q (in VDDR2A; loss of calcitriol
receptor activity; no effect on
interaction with RXRA; changed
interaction with NCOR1; loss of
interaction with NCOA1; no effect on
sequence-specific DNA-binding;
dbSNP:rs121909798).
{ECO:0000269|PubMed:28698609,
ECO:0000269|PubMed:9005998}.
/FTId=VAR_004665.
VARIANT 314 314 I -> S (in VDDR2A; dbSNP:rs121909799).
{ECO:0000269|PubMed:8961271}.
/FTId=VAR_004666.
VARIANT 346 346 V -> M (in VDDR2A; decreased calcitriol
receptor activity; decreased affinity for
calcitriol; decreased ligand-independent
localization to the nucleus; loss of
interaction with RXRA; decreased
interaction with NCOR1; decreased
interaction with NCOA1; decreased
sequence-specific DNA-binding;
dbSNP:rs267607169).
{ECO:0000269|PubMed:17970811,
ECO:0000269|PubMed:28698609}.
/FTId=VAR_079326.
VARIANT 360 360 S -> P (in VDDR2A; loss of calcitriol
receptor activity; loss of affinity for
calcitriol; decreased ligand-independent
localization to the nucleus; loss of
interaction with RXRA; loss of
interaction with NCOR1; loss of
interaction with NCOA1; loss of sequence-
specific DNA-binding).
{ECO:0000269|PubMed:28698609}.
/FTId=VAR_079327.
VARIANT 362 362 T -> I (in dbSNP:rs11574115).
{ECO:0000269|Ref.5}.
/FTId=VAR_029310.
VARIANT 391 391 R -> C (in VDDR2A; dbSNP:rs121909800).
{ECO:0000269|PubMed:8961271}.
/FTId=VAR_004667.
MUTAGEN 61 62 PF->AA: Promotes heterodimerization with
RXRA; when associated with A-75.
{ECO:0000269|PubMed:11980721}.
MUTAGEN 75 75 H->A: Promotes heterodimerization with
RXRA; when associated with A-61 and A-62.
{ECO:0000269|PubMed:11980721}.
TURN 25 27 {ECO:0000244|PDB:1KB2}.
STRAND 33 35 {ECO:0000244|PDB:1KB2}.
STRAND 38 40 {ECO:0000244|PDB:1KB6}.
HELIX 42 53 {ECO:0000244|PDB:1KB2}.
STRAND 61 64 {ECO:0000244|PDB:1KB4}.
TURN 70 75 {ECO:0000244|PDB:1KB2}.
HELIX 77 86 {ECO:0000244|PDB:1KB2}.
HELIX 91 93 {ECO:0000244|PDB:1KB2}.
HELIX 97 107 {ECO:0000244|PDB:1KB2}.
STRAND 108 110 {ECO:0000244|PDB:1KB6}.
TURN 111 113 {ECO:0000244|PDB:1KB6}.
HELIX 115 119 {ECO:0000244|PDB:1KB6}.
HELIX 126 142 {ECO:0000244|PDB:3B0T}.
HELIX 150 152 {ECO:0000244|PDB:3B0T}.
HELIX 217 223 {ECO:0000244|PDB:3B0T}.
HELIX 227 247 {ECO:0000244|PDB:3B0T}.
HELIX 251 253 {ECO:0000244|PDB:3B0T}.
HELIX 256 274 {ECO:0000244|PDB:3B0T}.
HELIX 275 277 {ECO:0000244|PDB:3B0T}.
TURN 281 284 {ECO:0000244|PDB:3B0T}.
STRAND 285 287 {ECO:0000244|PDB:3B0T}.
HELIX 291 293 {ECO:0000244|PDB:3B0T}.
HELIX 297 301 {ECO:0000244|PDB:3B0T}.
TURN 302 304 {ECO:0000244|PDB:3B0T}.
HELIX 307 321 {ECO:0000244|PDB:3B0T}.
TURN 322 324 {ECO:0000244|PDB:2HAR}.
HELIX 327 338 {ECO:0000244|PDB:3B0T}.
STRAND 341 343 {ECO:0000244|PDB:3AUQ}.
HELIX 349 370 {ECO:0000244|PDB:3B0T}.
TURN 373 378 {ECO:0000244|PDB:3B0T}.
HELIX 379 404 {ECO:0000244|PDB:3B0T}.
HELIX 410 413 {ECO:0000244|PDB:3B0T}.
HELIX 416 422 {ECO:0000244|PDB:3B0T}.
SEQUENCE 427 AA; 48289 MW; F95F300D042C4CB7 CRC64;
MEAMAASTSL PDPGDFDRNV PRICGVCGDR ATGFHFNAMT CEGCKGFFRR SMKRKALFTC
PFNGDCRITK DNRRHCQACR LKRCVDIGMM KEFILTDEEV QRKREMILKR KEEEALKDSL
RPKLSEEQQR IIAILLDAHH KTYDPTYSDF CQFRPPVRVN DGGGSHPSRP NSRHTPSFSG
DSSSSCSDHC ITSSDMMDSS SFSNLDLSEE DSDDPSVTLE LSQLSMLPHL ADLVSYSIQK
VIGFAKMIPG FRDLTSEDQI VLLKSSAIEV IMLRSNESFT MDDMSWTCGN QDYKYRVSDV
TKAGHSLELI EPLIKFQVGL KKLNLHEEEH VLLMAICIVS PDRPGVQDAA LIEAIQDRLS
NTLQTYIRCR HPPPGSHLLY AKMIQKLADL RSLNEEHSKQ YRCLSFQPEC SMKLTPLVLE
VFGNEIS


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