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VDR_HUMAN
ID   VDR_HUMAN               Reviewed;         427 AA.
AC   P11473; B2R5Q1; G3V1V9; Q5PSV3;
DT   01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1989, sequence version 1.
DT   03-AUG-2022, entry version 248.
DE   RecName: Full=Vitamin D3 receptor;
DE            Short=VDR;
DE   AltName: Full=1,25-dihydroxyvitamin D3 receptor;
DE   AltName: Full=Nuclear receptor subfamily 1 group I member 1;
GN   Name=VDR; Synonyms=NR1I1;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX   PubMed=2835767; DOI=10.1073/pnas.85.10.3294;
RA   Baker A.R., McDonnell D.P., Hughes M., Crisp T.M., Mangelsdorf D.J.,
RA   Haussler M.R., Pike J.W., Shine J., O'Malley B.W.;
RT   "Cloning and expression of full-length cDNA encoding human vitamin D
RT   receptor.";
RL   Proc. Natl. Acad. Sci. U.S.A. 85:3294-3298(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX   PubMed=1324736; DOI=10.1016/0167-4781(92)90063-6;
RA   Goto H., Chen K.S., Prahl J.M., Deluca H.F.;
RT   "A single receptor identical with that from intestine/T47D cells mediates
RT   the action of 1,25-dihydroxyvitamin D-3 in HL-60 cells.";
RL   Biochim. Biophys. Acta 1132:103-108(1992).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   TISSUE=Lens epithelium;
RA   Rae J.L., Shepard A.R.;
RL   Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9212063; DOI=10.1210/mend.11.8.9951;
RA   Miyamoto K., Kesterson R.A., Yamamoto H., Taketani Y., Nishiwaki E.,
RA   Tatsumi S., Inoue Y., Morita K., Takeda E., Pike J.W.;
RT   "Structural organization of the human vitamin D receptor chromosomal gene
RT   and its promoter.";
RL   Mol. Endocrinol. 11:1165-1179(1997).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS VAL-230 AND ILE-362.
RG   NIEHS SNPs program;
RL   Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16541075; DOI=10.1038/nature04569;
RA   Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA   Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA   Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA   Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA   Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA   Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA   Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA   Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA   Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA   Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA   Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA   Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA   Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA   Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA   Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA   Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA   Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA   David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA   D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA   Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA   Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA   Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA   LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA   Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA   Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA   Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA   Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA   Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA   Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA   Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA   Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA   Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA   Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA   Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA   Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA   Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA   Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA   Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA   Gibbs R.A.;
RT   "The finished DNA sequence of human chromosome 12.";
RL   Nature 440:346-351(2006).
RN   [8]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [9]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Placenta;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [10]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 24-90 (ISOFORM 1/2).
RC   TISSUE=Peripheral blood;
RX   PubMed=1850412; DOI=10.1016/s0021-9258(20)89488-5;
RA   Yu X.-P., Mocharla H., Hustmyer F.G., Manolagas S.C.;
RT   "Vitamin D receptor expression in human lymphocytes. Signal requirements
RT   and characterization by western blots and DNA sequencing.";
RL   J. Biol. Chem. 266:7588-7595(1991).
RN   [11]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 343-427.
RX   PubMed=16252240; DOI=10.1086/497438;
RA   Fang Y., van Meurs J.B., d'Alesio A., Jhamai M., Zhao H., Rivadeneira F.,
RA   Hofman A., van Leeuwen J.P., Jehan F., Pols H.A., Uitterlinden A.G.;
RT   "Promoter and 3'-untranslated-region haplotypes in the vitamin D receptor
RT   gene predispose to osteoporotic fracture: the Rotterdam study.";
RL   Am. J. Hum. Genet. 77:807-823(2005).
RN   [12]
RP   INTERACTION WITH NCOA3.
RX   PubMed=9267036; DOI=10.1016/s0092-8674(00)80516-4;
RA   Chen H., Lin R.J., Schiltz R.L., Chakravarti D., Nash A., Nagy L.,
RA   Privalsky M.L., Nakatani Y., Evans R.M.;
RT   "Nuclear receptor coactivator ACTR is a novel histone acetyltransferase and
RT   forms a multimeric activation complex with P/CAF and CBP/p300.";
RL   Cell 90:569-580(1997).
RN   [13]
RP   INTERACTION WITH SNW1.
RX   PubMed=9632709; DOI=10.1074/jbc.273.26.16434;
RA   Baudino T.A., Kraichely D.M., Jefcoat S.C. Jr., Winchester S.K.,
RA   Partridge N.C., Macdonald P.N.;
RT   "Isolation and characterization of a novel coactivator protein, NCoA-62,
RT   involved in vitamin D-mediated transcription.";
RL   J. Biol. Chem. 273:16434-16441(1998).
RN   [14]
RP   INTERACTION WITH NCOA6.
RX   PubMed=10866662; DOI=10.1128/mcb.20.14.5048-5063.2000;
RA   Mahajan M.A., Samuels H.H.;
RT   "A new family of nuclear receptor coregulators that integrates nuclear
RT   receptor signaling through CBP.";
RL   Mol. Cell. Biol. 20:5048-5063(2000).
RN   [15]
RP   SUBCELLULAR LOCATION, AND MUTAGENESIS OF 47-PHE-PHE-48.
RX   PubMed=12145331; DOI=10.1210/me.2001-0345;
RA   Pruefer K., Barsony J.;
RT   "Retinoid X receptor dominates the nuclear import and export of the
RT   unliganded vitamin D receptor.";
RL   Mol. Endocrinol. 16:1738-1751(2002).
RN   [16]
RP   RETRACTED PAPER.
RX   PubMed=16252006; DOI=10.1038/sj.emboj.7600853;
RA   Fujiki R., Kim M.-S., Sasaki Y., Yoshimura K., Kitagawa H., Kato S.;
RT   "Ligand-induced transrepression by VDR through association of WSTF with
RT   acetylated histones.";
RL   EMBO J. 24:3881-3894(2005).
RN   [17]
RP   RETRACTION NOTICE OF PUBMED:16252006.
RX   PubMed=25452584; DOI=10.15252/embj.201470110;
RA   Fujiki R., Kim M.-S., Sasaki Y., Yoshimura K., Kitagawa H., Kato S.;
RT   "Retraction: 'Ligand-induced transrepression by VDR through association of
RT   WSTF with acetylated histones'.";
RL   EMBO J. 33:2881-2881(2014).
RN   [18]
RP   SUBCELLULAR LOCATION.
RX   PubMed=16207705; DOI=10.1074/jbc.m509347200;
RA   Miyauchi Y., Michigami T., Sakaguchi N., Sekimoto T., Yoneda Y., Pike J.W.,
RA   Yamagata M., Ozono K.;
RT   "Importin 4 is responsible for ligand-independent nuclear translocation of
RT   vitamin D receptor.";
RL   J. Biol. Chem. 280:40901-40908(2005).
RN   [19]
RP   INTERACTION WITH IRX4.
RC   TISSUE=Prostate;
RX   PubMed=22323358; DOI=10.1093/hmg/dds025;
RA   Nguyen H.H., Takata R., Akamatsu S., Shigemizu D., Tsunoda T., Furihata M.,
RA   Takahashi A., Kubo M., Kamatani N., Ogawa O., Fujioka T., Nakamura Y.,
RA   Nakagawa H.;
RT   "IRX4 at 5p15 suppresses prostate cancer growth through the interaction
RT   with vitamin D receptor, conferring prostate cancer susceptibility.";
RL   Hum. Mol. Genet. 21:2076-2085(2012).
RN   [20]
RP   9AATAD MOTIF.
RX   PubMed=30468856; DOI=10.1016/j.jsbmb.2018.11.008;
RA   Piskacek M., Havelka M., Jendruchova K., Knight A.;
RT   "Nuclear hormone receptors: Ancient 9aaTAD and evolutionally gained NCoA
RT   activation pathways.";
RL   J. Steroid Biochem. Mol. Biol. 187:118-123(2019).
RN   [21]
RP   X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 118-427 IN COMPLEX WITH
RP   DIHYDROXYVITAMIN D3, IDENTIFICATION BY MASS SPECTROMETRY, AND FUNCTION.
RX   PubMed=10678179; DOI=10.1016/s1097-2765(00)80413-x;
RA   Rochel N., Wurtz J.-M., Mitschler A., Klaholz B., Moras D.;
RT   "The crystal structure of the nuclear receptor for vitamin D bound to its
RT   natural ligand.";
RL   Mol. Cell 5:173-179(2000).
RN   [22]
RP   X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF 118-427 IN COMPLEXES WITH VITAMIN
RP   D3 AND VITAMIN D3 ANALOGS.
RX   PubMed=11344298; DOI=10.1073/pnas.091018698;
RA   Tocchini-Valentini G., Rochel N., Wurtz J.-M., Mitschler A., Moras D.;
RT   "Crystal structures of the vitamin D receptor complexed to superagonist 20-
RT   epi ligands.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:5491-5496(2001).
RN   [23]
RP   X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 16-125 IN COMPLEX WITH DNA,
RP   MUTAGENESIS OF 61-PRO-PHE-62 AND HIS-75, AND SUBUNIT.
RX   PubMed=11980721; DOI=10.1093/emboj/21.9.2242;
RA   Shaffer P.L., Gewirth D.T.;
RT   "Structural basis of VDR-DNA interactions on direct repeat response
RT   elements.";
RL   EMBO J. 21:2242-2252(2002).
RN   [24]
RP   X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 188-427 IN COMPLEXES WITH VITAMIN
RP   D3 ANALOGS.
RX   PubMed=15055995; DOI=10.1021/jm0310582;
RA   Tocchini-Valentini G., Rochel N., Wurtz J.-M., Moras D.;
RT   "Crystal structures of the vitamin D nuclear receptor liganded with the
RT   vitamin D side chain analogues calcipotriol and seocalcitol, receptor
RT   agonists of clinical importance. Insights into a structural basis for the
RT   switching of calcipotriol to a receptor antagonist by further side chain
RT   modification.";
RL   J. Med. Chem. 47:1956-1961(2004).
RN   [25]
RP   X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 16-125 OF MUTANT
RP   ALA-61/ALA-62/ALA-75 IN COMPLEX WITH RXRA AND DNA, AND SUBUNIT.
RX   PubMed=15225774; DOI=10.1016/j.jsbmb.2004.03.084;
RA   Shaffer P.L., Gewirth D.T.;
RT   "Structural analysis of RXR-VDR interactions on DR3 DNA.";
RL   J. Steroid Biochem. Mol. Biol. 89:215-219(2004).
RN   [26]
RP   X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 188-427 IN COMPLEX WITH VITAMIN D3
RP   ANALOG, IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, AND INTERACTION WITH
RP   NCOA1; NCOA2 AND MED1.
RX   PubMed=15728261; DOI=10.1124/mol.104.008730;
RA   Eelen G., Verlinden L., Rochel N., Claessens F., De Clercq P.,
RA   Vandewalle M., Tocchini-Valentini G., Moras D., Bouillon R., Verstuyf A.;
RT   "Superagonistic action of 14-epi-analogs of 1,25-dihydroxyvitamin D
RT   explained by vitamin D receptor-coactivator interaction.";
RL   Mol. Pharmacol. 67:1566-1573(2005).
RN   [27]
RP   X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 188-427 IN COMPLEXES WITH
RP   DIHYDROXYVITAMIN D3 AND VITAMIN D3 ANALOGS, AND FUNCTION.
RX   PubMed=16913708; DOI=10.1021/jm0604070;
RA   Hourai S., Fujishima T., Kittaka A., Suhara Y., Takayama H., Rochel N.,
RA   Moras D.;
RT   "Probing a water channel near the A-ring of receptor-bound 1 alpha,25-
RT   dihydroxyvitamin D3 with selected 2 alpha-substituted analogues.";
RL   J. Med. Chem. 49:5199-5205(2006).
RN   [28]
RP   VARIANTS VDDR2A ASP-33 AND GLN-73.
RX   PubMed=2849209; DOI=10.1126/science.2849209;
RA   Hughes M.R., Malloy P.J., Kieback D.G., Kesterson R.A., Pike J.W.,
RA   Feldman D., O'Malley B.W.;
RT   "Point mutations in the human vitamin D receptor gene associated with
RT   hypocalcemic rickets.";
RL   Science 242:1702-1705(1988).
RN   [29]
RP   VARIANT VDDR2A GLN-35.
RX   PubMed=8381803; DOI=10.1210/jcem.76.2.8381803;
RA   Yagi H., Ozono K., Miyake H., Nagashima K., Kuroume T., Pike J.W.;
RT   "A new point mutation in the deoxyribonucleic acid-binding domain of the
RT   vitamin D receptor in a kindred with hereditary 1,25-dihydroxyvitamin D-
RT   resistant rickets.";
RL   J. Clin. Endocrinol. Metab. 76:509-512(1993).
RN   [30]
RP   VARIANT VDDR2A GLN-50.
RX   PubMed=1652893;
RA   Saijo T., Ito M., Takeda E., Mahbubul Huq A.H.M., Naito E., Yokota I.,
RA   Sone T., Pike J.W., Kuroda Y.;
RT   "A unique mutation in the vitamin D receptor gene in three Japanese
RT   patients with vitamin D-dependent rickets type II: utility of single-strand
RT   conformation polymorphism analysis for heterozygous carrier detection.";
RL   Am. J. Hum. Genet. 49:668-673(1991).
RN   [31]
RP   VARIANT VDDR2A GLN-80.
RX   PubMed=2177843; DOI=10.1210/mend-4-4-623;
RA   Sone T., Marx S.J., Liberman U.A., Pike J.W.;
RT   "A unique point mutation in the human vitamin D receptor chromosomal gene
RT   confers hereditary resistance to 1,25-dihydroxyvitamin D3.";
RL   Mol. Endocrinol. 4:623-631(1990).
RN   [32]
RP   VARIANT VDDR2A GLN-80.
RX   PubMed=8106618; DOI=10.1210/jcem.78.2.8106618;
RA   Malloy P.J., Weisman Y., Feldman D.;
RT   "Hereditary 1 alpha,25-dihydroxyvitamin D-resistant rickets resulting from
RT   a mutation in the vitamin D receptor deoxyribonucleic acid-binding
RT   domain.";
RL   J. Clin. Endocrinol. Metab. 78:313-316(1994).
RN   [33]
RP   VARIANTS VDDR2A 152-GLN--SER-427 DEL AND LEU-274.
RX   PubMed=8392085; DOI=10.1172/jci116539;
RA   Kristjansson K., Rut A.R., Hewison M., O'Riordan J.L.H., Hughes M.R.;
RT   "Two mutations in the hormone binding domain of the vitamin D receptor
RT   cause tissue resistance to 1,25 dihydroxyvitamin D3.";
RL   J. Clin. Invest. 92:12-16(1993).
RN   [34]
RP   VARIANTS VDDR2A GLU-45 AND ILE-47.
RX   PubMed=7828346; DOI=10.1111/j.1365-2265.1994.tb01822.x;
RA   Rut A.R., Hewison M., Kristjansson K., Luisi B., Hughes M.R.,
RA   O'Riordan J.L.H.;
RT   "Two mutations causing vitamin D resistant rickets: modelling on the basis
RT   of steroid hormone receptor DNA-binding domain crystal structures.";
RL   Clin. Endocrinol. (Oxf.) 41:581-590(1994).
RN   [35]
RP   VARIANT VDDR2A ASP-46.
RX   PubMed=8675579; DOI=10.1210/jcem.81.7.8675579;
RA   Lin U.-T., Malloy P.J., Sakati N., Al-Ashwal A., Feldman D.;
RT   "A novel mutation in the deoxyribonucleic acid-binding domain of the
RT   vitamin D receptor causes hereditary 1,25-dihydroxyvitamin D-resistant
RT   rickets.";
RL   J. Clin. Endocrinol. Metab. 81:2564-2569(1996).
RN   [36]
RP   VARIANTS VDDR2A SER-314 AND CYS-391.
RX   PubMed=8961271; DOI=10.1210/mend.10.12.8961271;
RA   Whitfield G.K., Selznick S.H., Haussler C.A., Hsieh J.-C., Galligan M.A.,
RA   Jurutka P.W., Thompson P.D., Lee S.M., Zerwekh J.E., Haussler M.R.;
RT   "Vitamin D receptors from patients with resistance to 1,25-dihydroxyvitamin
RT   D(3): point mutations confer reduced transactivation in response to ligand
RT   and impaired interaction with the retinoid X receptor heterodimeric
RT   partner.";
RL   Mol. Endocrinol. 10:1617-1631(1996).
RN   [37]
RP   VARIANT VDDR2A GLN-305.
RX   PubMed=9005998; DOI=10.1172/jci119158;
RA   Malloy P.J., Eccleshall T.R., Gross C., van Maldergem L., Bouillon R.,
RA   Feldman D.;
RT   "Hereditary vitamin D resistant rickets caused by a novel mutation in the
RT   vitamin D receptor that results in decreased affinity for hormone and
RT   cellular hyporesponsiveness.";
RL   J. Clin. Invest. 99:297-304(1997).
RN   [38]
RP   INVOLVEMENT IN MYCOBACTERIUM TUBERCULOSIS SUSCEPTIBILITY.
RX   PubMed=15032981; DOI=10.1111/j.2004.00183.x;
RA   Selvaraj P., Kurian S.M., Chandra G., Reetha A.M., Charles N.,
RA   Narayanan P.R.;
RT   "Vitamin D receptor gene variants of BsmI, ApaI, TaqI, and FokI
RT   polymorphisms in spinal tuberculosis.";
RL   Clin. Genet. 65:73-76(2004).
RN   [39]
RP   VARIANT VDDR2A MET-346.
RX   PubMed=17970811; DOI=10.1111/j.1365-2133.2007.08232.x;
RA   Arita K., Nanda A., Wessagowit V., Akiyama M., Alsaleh Q.A., McGrath J.A.;
RT   "A novel mutation in the VDR gene in hereditary vitamin D-resistant
RT   rickets.";
RL   Br. J. Dermatol. 158:168-171(2008).
RN   [40]
RP   VARIANT VDDR2A PRO-360, CHARACTERIZATION OF VARIANT VDDR2A 152-GLN--SER-427
RP   DEL; LEU-274; GLN-305; MET-346 AND PRO-360, FUNCTION, INTERACTION WITH
RP   NCOA1; NCOR1 AND RXR, AND SUBCELLULAR LOCATION.
RX   PubMed=28698609; DOI=10.1038/s41598-017-05081-x;
RA   Tamura M., Ishizawa M., Isojima T., Oezen S., Oka A., Makishima M.,
RA   Kitanaka S.;
RT   "Functional analyses of a novel missense and other mutations of the vitamin
RT   D receptor in association with alopecia.";
RL   Sci. Rep. 7:5102-5102(2017).
CC   -!- FUNCTION: Nuclear receptor for calcitriol, the active form of vitamin
CC       D3 which mediates the action of this vitamin on cells (PubMed:28698609,
CC       PubMed:16913708, PubMed:15728261, PubMed:10678179). Enters the nucleus
CC       upon vitamin D3 binding where it forms heterodimers with the retinoid X
CC       receptor/RXR (PubMed:28698609). The VDR-RXR heterodimers bind to
CC       specific response elements on DNA and activate the transcription of
CC       vitamin D3-responsive target genes (PubMed:28698609). Plays a central
CC       role in calcium homeostasis (By similarity).
CC       {ECO:0000250|UniProtKB:P13053, ECO:0000269|PubMed:10678179,
CC       ECO:0000269|PubMed:15728261, ECO:0000269|PubMed:16913708,
CC       ECO:0000269|PubMed:28698609}.
CC   -!- SUBUNIT: Homodimer in the absence of bound vitamin D3
CC       (PubMed:11980721). Heterodimer with RXRA after vitamin D3 binding
CC       (PubMed:15225774, PubMed:11980721, PubMed:10678179). Interacts with
CC       MED1, NCOA1, NCOA2, NCOA3 and NCOA6 coactivators, leading to a strong
CC       increase of transcription of target genes (PubMed:10866662,
CC       PubMed:15728261, PubMed:28698609, PubMed:9267036). Interacts with the
CC       corepressor NCOR1 (PubMed:28698609). Interacts with SNW1
CC       (PubMed:9632709). Interacts with IRX4, the interaction does not affect
CC       its transactivation activity (PubMed:22323358). Interacts with CRY1 (By
CC       similarity). Interacts with CRY2 in a ligand-dependent manner (By
CC       similarity). {ECO:0000250|UniProtKB:P48281,
CC       ECO:0000269|PubMed:10678179, ECO:0000269|PubMed:10866662,
CC       ECO:0000269|PubMed:11980721, ECO:0000269|PubMed:15225774,
CC       ECO:0000269|PubMed:15728261, ECO:0000269|PubMed:22323358,
CC       ECO:0000269|PubMed:28698609, ECO:0000269|PubMed:9267036,
CC       ECO:0000269|PubMed:9632709}.
CC   -!- INTERACTION:
CC       P11473; Q09472: EP300; NbExp=3; IntAct=EBI-286357, EBI-447295;
CC       P11473; Q15648: MED1; NbExp=4; IntAct=EBI-286357, EBI-394459;
CC       P11473; P50222: MEOX2; NbExp=3; IntAct=EBI-286357, EBI-748397;
CC       P11473; Q15788: NCOA1; NbExp=3; IntAct=EBI-286357, EBI-455189;
CC       P11473; P26045: PTPN3; NbExp=4; IntAct=EBI-286357, EBI-1047946;
CC       P11473; P19793: RXRA; NbExp=6; IntAct=EBI-286357, EBI-78598;
CC       P11473; Q13573: SNW1; NbExp=5; IntAct=EBI-286357, EBI-632715;
CC       P11473; Q13501: SQSTM1; NbExp=4; IntAct=EBI-286357, EBI-307104;
CC       P11473; P04637: TP53; NbExp=6; IntAct=EBI-286357, EBI-366083;
CC       P11473; Q15645: TRIP13; NbExp=3; IntAct=EBI-286357, EBI-358993;
CC       P11473; Q9JLI4: Ncoa6; Xeno; NbExp=2; IntAct=EBI-286357, EBI-286271;
CC       P11473; P28700: Rxra; Xeno; NbExp=3; IntAct=EBI-286357, EBI-346715;
CC       P11473-2; X5D778: ANKRD11; NbExp=3; IntAct=EBI-12874016, EBI-17183751;
CC       P11473-2; Q96HA8: NTAQ1; NbExp=3; IntAct=EBI-12874016, EBI-741158;
CC       P11473-2; Q01804: OTUD4; NbExp=3; IntAct=EBI-12874016, EBI-1054396;
CC       P11473-2; Q96S38: RPS6KC1; NbExp=3; IntAct=EBI-12874016, EBI-347731;
CC       P11473-2; P48443: RXRG; NbExp=4; IntAct=EBI-12874016, EBI-712405;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00407,
CC       ECO:0000269|PubMed:12145331, ECO:0000269|PubMed:16207705,
CC       ECO:0000269|PubMed:28698609}. Cytoplasm {ECO:0000269|PubMed:12145331,
CC       ECO:0000269|PubMed:16207705, ECO:0000269|PubMed:28698609}.
CC       Note=Localizes mainly to the nucleus (PubMed:28698609,
CC       PubMed:12145331). Translocated into the nucleus via both ligand-
CC       dependent and ligand-independent pathways; ligand-independent nuclear
CC       translocation is mediated by IPO4 (PubMed:16207705).
CC       {ECO:0000269|PubMed:12145331, ECO:0000269|PubMed:16207705,
CC       ECO:0000269|PubMed:28698609}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=P11473-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P11473-2; Sequence=VSP_047218;
CC   -!- DOMAIN: Composed of three domains: a modulating N-terminal domain, a
CC       DNA-binding domain and a C-terminal ligand-binding domain.
CC       {ECO:0000269|PubMed:10678179}.
CC   -!- DOMAIN: The 9aaTAD motif is a transactivation domain present in a large
CC       number of yeast and animal transcription factors.
CC       {ECO:0000305|PubMed:30468856}.
CC   -!- POLYMORPHISM: Genetic variations in VDR may determine Mycobacterium
CC       tuberculosis susceptibility [MIM:607948].
CC       {ECO:0000269|PubMed:15032981}.
CC   -!- DISEASE: Rickets vitamin D-dependent 2A (VDDR2A) [MIM:277440]: A
CC       disorder of vitamin D metabolism resulting in severe rickets,
CC       hypocalcemia and secondary hyperparathyroidism. Most patients have
CC       total alopecia in addition to rickets. {ECO:0000269|PubMed:1652893,
CC       ECO:0000269|PubMed:17970811, ECO:0000269|PubMed:2177843,
CC       ECO:0000269|PubMed:2849209, ECO:0000269|PubMed:28698609,
CC       ECO:0000269|PubMed:7828346, ECO:0000269|PubMed:8106618,
CC       ECO:0000269|PubMed:8381803, ECO:0000269|PubMed:8392085,
CC       ECO:0000269|PubMed:8675579, ECO:0000269|PubMed:8961271,
CC       ECO:0000269|PubMed:9005998}. Note=The disease is caused by variants
CC       affecting the gene represented in this entry.
CC   -!- SIMILARITY: Belongs to the nuclear hormone receptor family. NR1
CC       subfamily. {ECO:0000305}.
CC   -!- CAUTION: It is uncertain whether Met-1 or Met-4 is the initiator.
CC       {ECO:0000305}.
CC   -!- CAUTION: Was thought to be recruited to promoters via its interaction
CC       with BAZ1B/WSTF, but this work has later been retracted.
CC       {ECO:0000305|PubMed:16252006, ECO:0000305|PubMed:25452584}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH60832.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=AAP88938.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC   -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC       URL="http://egp.gs.washington.edu/data/vdr/";
CC   ---------------------------------------------------------------------------
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DR   EMBL; J03258; AAA61273.1; -; mRNA.
DR   EMBL; X67482; CAA47824.1; -; mRNA.
DR   EMBL; AF026260; AAB95155.1; -; mRNA.
DR   EMBL; AB002168; BAA83389.1; -; Genomic_DNA.
DR   EMBL; AY342401; AAP88938.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AK312267; BAG35198.1; -; mRNA.
DR   EMBL; AC004466; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC121338; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471111; EAW57960.1; -; Genomic_DNA.
DR   EMBL; CH471111; EAW57961.1; -; Genomic_DNA.
DR   EMBL; BC060832; AAH60832.1; ALT_INIT; mRNA.
DR   EMBL; M65208; AAA61274.1; -; mRNA.
DR   EMBL; AY827087; AAV85448.1; -; Genomic_DNA.
DR   CCDS; CCDS55820.1; -. [P11473-2]
DR   CCDS; CCDS8757.1; -. [P11473-1]
DR   PIR; A28200; A28200.
DR   RefSeq; NP_000367.1; NM_000376.2. [P11473-1]
DR   RefSeq; NP_001017535.1; NM_001017535.1. [P11473-1]
DR   RefSeq; NP_001017536.1; NM_001017536.1. [P11473-2]
DR   RefSeq; XP_006719650.1; XM_006719587.3.
DR   RefSeq; XP_011537022.1; XM_011538720.2. [P11473-1]
DR   PDB; 1DB1; X-ray; 1.80 A; A=118-427.
DR   PDB; 1IE8; X-ray; 1.52 A; A=118-427.
DR   PDB; 1IE9; X-ray; 1.40 A; A=118-427.
DR   PDB; 1KB2; X-ray; 2.70 A; A/B=16-125.
DR   PDB; 1KB4; X-ray; 2.80 A; A/B=16-125.
DR   PDB; 1KB6; X-ray; 2.70 A; A/B=16-125.
DR   PDB; 1S0Z; X-ray; 2.50 A; A=118-427.
DR   PDB; 1S19; X-ray; 2.10 A; A=118-427.
DR   PDB; 1TXI; X-ray; 1.90 A; A=118-427.
DR   PDB; 1YNW; X-ray; 3.00 A; A=16-125.
DR   PDB; 2HAM; X-ray; 1.90 A; A=118-427.
DR   PDB; 2HAR; X-ray; 1.90 A; A=118-427.
DR   PDB; 2HAS; X-ray; 1.96 A; A=118-427.
DR   PDB; 2HB7; X-ray; 1.80 A; A=118-427.
DR   PDB; 2HB8; X-ray; 2.00 A; A=118-427.
DR   PDB; 3A2I; X-ray; 3.27 A; A=118-427.
DR   PDB; 3A2J; X-ray; 2.70 A; A=118-427.
DR   PDB; 3A3Z; X-ray; 1.72 A; X=118-427.
DR   PDB; 3A40; X-ray; 1.45 A; X=118-427.
DR   PDB; 3A78; X-ray; 1.90 A; A=118-427.
DR   PDB; 3AUQ; X-ray; 2.64 A; A=118-427.
DR   PDB; 3AUR; X-ray; 2.21 A; A=118-427.
DR   PDB; 3AX8; X-ray; 2.60 A; A=118-427.
DR   PDB; 3AZ1; X-ray; 1.50 A; A=120-423.
DR   PDB; 3AZ2; X-ray; 1.69 A; A=120-423.
DR   PDB; 3AZ3; X-ray; 1.36 A; A=120-423.
DR   PDB; 3B0T; X-ray; 1.30 A; A=120-423.
DR   PDB; 3CS4; X-ray; 2.00 A; A=118-427.
DR   PDB; 3CS6; X-ray; 1.80 A; A=118-427.
DR   PDB; 3KPZ; X-ray; 1.90 A; A=118-427.
DR   PDB; 3M7R; X-ray; 1.80 A; A=120-423.
DR   PDB; 3OGT; X-ray; 1.75 A; A=118-427.
DR   PDB; 3P8X; X-ray; 1.70 A; A=118-164, A=217-427.
DR   PDB; 3TKC; X-ray; 1.75 A; A=118-427.
DR   PDB; 3VHW; X-ray; 2.43 A; A=118-427.
DR   PDB; 3W0A; X-ray; 1.80 A; A=120-423.
DR   PDB; 3W0C; X-ray; 1.90 A; A=120-423.
DR   PDB; 3W0Y; X-ray; 1.98 A; A=120-423.
DR   PDB; 3WGP; X-ray; 2.00 A; A=120-423.
DR   PDB; 3WWR; X-ray; 3.18 A; A=118-427.
DR   PDB; 3X31; X-ray; 2.11 A; A=118-427.
DR   PDB; 3X36; X-ray; 1.93 A; A=118-427.
DR   PDB; 4G2I; X-ray; 1.80 A; A=118-427.
DR   PDB; 4ITE; X-ray; 2.49 A; A=118-427.
DR   PDB; 4ITF; X-ray; 2.84 A; A=118-427.
DR   PDB; 5GT4; X-ray; 1.83 A; A=118-423.
DR   PDB; 5V39; X-ray; 2.20 A; A=119-425.
DR   PDB; 5YSY; X-ray; 2.00 A; A=118-423.
DR   PDB; 5YT2; X-ray; 2.00 A; A=118-423.
DR   PDBsum; 1DB1; -.
DR   PDBsum; 1IE8; -.
DR   PDBsum; 1IE9; -.
DR   PDBsum; 1KB2; -.
DR   PDBsum; 1KB4; -.
DR   PDBsum; 1KB6; -.
DR   PDBsum; 1S0Z; -.
DR   PDBsum; 1S19; -.
DR   PDBsum; 1TXI; -.
DR   PDBsum; 1YNW; -.
DR   PDBsum; 2HAM; -.
DR   PDBsum; 2HAR; -.
DR   PDBsum; 2HAS; -.
DR   PDBsum; 2HB7; -.
DR   PDBsum; 2HB8; -.
DR   PDBsum; 3A2I; -.
DR   PDBsum; 3A2J; -.
DR   PDBsum; 3A3Z; -.
DR   PDBsum; 3A40; -.
DR   PDBsum; 3A78; -.
DR   PDBsum; 3AUQ; -.
DR   PDBsum; 3AUR; -.
DR   PDBsum; 3AX8; -.
DR   PDBsum; 3AZ1; -.
DR   PDBsum; 3AZ2; -.
DR   PDBsum; 3AZ3; -.
DR   PDBsum; 3B0T; -.
DR   PDBsum; 3CS4; -.
DR   PDBsum; 3CS6; -.
DR   PDBsum; 3KPZ; -.
DR   PDBsum; 3M7R; -.
DR   PDBsum; 3OGT; -.
DR   PDBsum; 3P8X; -.
DR   PDBsum; 3TKC; -.
DR   PDBsum; 3VHW; -.
DR   PDBsum; 3W0A; -.
DR   PDBsum; 3W0C; -.
DR   PDBsum; 3W0Y; -.
DR   PDBsum; 3WGP; -.
DR   PDBsum; 3WWR; -.
DR   PDBsum; 3X31; -.
DR   PDBsum; 3X36; -.
DR   PDBsum; 4G2I; -.
DR   PDBsum; 4ITE; -.
DR   PDBsum; 4ITF; -.
DR   PDBsum; 5GT4; -.
DR   PDBsum; 5V39; -.
DR   PDBsum; 5YSY; -.
DR   PDBsum; 5YT2; -.
DR   AlphaFoldDB; P11473; -.
DR   SMR; P11473; -.
DR   BioGRID; 113264; 197.
DR   ComplexPortal; CPX-631; RXRalpha-VDR nuclear hormone receptor complex.
DR   ComplexPortal; CPX-871; RXRbeta-VDR nuclear hormone receptor complex.
DR   CORUM; P11473; -.
DR   DIP; DIP-32624N; -.
DR   ELM; P11473; -.
DR   IntAct; P11473; 34.
DR   MINT; P11473; -.
DR   STRING; 9606.ENSP00000447173; -.
DR   BindingDB; P11473; -.
DR   ChEMBL; CHEMBL1977; -.
DR   DrugBank; DB07530; (1R,3R)-5-[(2E)-3-{(1S,3R)-2,2,3-trimethyl-3-[6,6,6-trifluoro-5-hydroxy-5-(trifluoromethyl)hex-3-yn-1-yl]cyclopentyl}prop-2-en-1-ylidene]cyclohexane-1,3-diol.
DR   DrugBank; DB08742; 1,3-CYCLOHEXANEDIOL, 4-METHYLENE-5-[(2E)-[(1S,3AS,7AS)-OCTAHYDRO-1-(5-HYDROXY-5-METHYL-1,3-HEXADIYNYL)-7A-METHYL-4H-INDEN-4-YLIDENE]ETHYLIDENE]-, (1R,3S,5Z).
DR   DrugBank; DB01436; Alfacalcidol.
DR   DrugBank; DB04891; Becocalcidiol.
DR   DrugBank; DB00146; Calcifediol.
DR   DrugBank; DB02300; Calcipotriol.
DR   DrugBank; DB00136; Calcitriol.
DR   DrugBank; DB00169; Cholecalciferol.
DR   DrugBank; DB04540; Cholesterol.
DR   DrugBank; DB05024; CTA018.
DR   DrugBank; DB11672; Curcumin.
DR   DrugBank; DB14635; Curcumin sulfate.
DR   DrugBank; DB01070; Dihydrotachysterol.
DR   DrugBank; DB06410; Doxercalciferol.
DR   DrugBank; DB05295; Eldecalcitol.
DR   DrugBank; DB06194; Elocalcitol.
DR   DrugBank; DB00153; Ergocalciferol.
DR   DrugBank; DB04796; Inecalcitol.
DR   DrugBank; DB03451; Lexacalcitol.
DR   DrugBank; DB00910; Paricalcitol.
DR   DrugBank; DB04258; Seocalcitol.
DR   DrugBank; DB11094; Vitamin D.
DR   DrugCentral; P11473; -.
DR   GuidetoPHARMACOLOGY; 605; -.
DR   SwissLipids; SLP:000001571; -.
DR   MoonDB; P11473; Predicted.
DR   TCDB; 9.B.208.1.1; the vitamin d3 receptor (vdr) family.
DR   iPTMnet; P11473; -.
DR   PhosphoSitePlus; P11473; -.
DR   BioMuta; VDR; -.
DR   DMDM; 137617; -.
DR   EPD; P11473; -.
DR   jPOST; P11473; -.
DR   MassIVE; P11473; -.
DR   MaxQB; P11473; -.
DR   PaxDb; P11473; -.
DR   PeptideAtlas; P11473; -.
DR   PRIDE; P11473; -.
DR   ProteomicsDB; 32456; -.
DR   ProteomicsDB; 52780; -. [P11473-1]
DR   Antibodypedia; 3902; 818 antibodies from 44 providers.
DR   DNASU; 7421; -.
DR   Ensembl; ENST00000395324.6; ENSP00000378734.2; ENSG00000111424.12. [P11473-1]
DR   Ensembl; ENST00000549336.6; ENSP00000449573.2; ENSG00000111424.12. [P11473-1]
DR   Ensembl; ENST00000550325.5; ENSP00000447173.1; ENSG00000111424.12. [P11473-2]
DR   GeneID; 7421; -.
DR   KEGG; hsa:7421; -.
DR   MANE-Select; ENST00000549336.6; ENSP00000449573.2; NM_000376.3; NP_000367.1.
DR   UCSC; uc001rql.4; human. [P11473-1]
DR   CTD; 7421; -.
DR   DisGeNET; 7421; -.
DR   GeneCards; VDR; -.
DR   HGNC; HGNC:12679; VDR.
DR   HPA; ENSG00000111424; Tissue enriched (parathyroid).
DR   MalaCards; VDR; -.
DR   MIM; 277440; phenotype.
DR   MIM; 601769; gene.
DR   MIM; 607948; phenotype.
DR   neXtProt; NX_P11473; -.
DR   OpenTargets; ENSG00000111424; -.
DR   Orphanet; 93160; Hypocalcemic vitamin D-resistant rickets.
DR   PharmGKB; PA37301; -.
DR   VEuPathDB; HostDB:ENSG00000111424; -.
DR   eggNOG; KOG3575; Eukaryota.
DR   GeneTree; ENSGT00940000155473; -.
DR   InParanoid; P11473; -.
DR   OMA; CITSPDM; -.
DR   OrthoDB; 297114at2759; -.
DR   PhylomeDB; P11473; -.
DR   TreeFam; TF316304; -.
DR   PathwayCommons; P11473; -.
DR   Reactome; R-HSA-196791; Vitamin D (calciferol) metabolism.
DR   Reactome; R-HSA-383280; Nuclear Receptor transcription pathway.
DR   Reactome; R-HSA-4090294; SUMOylation of intracellular receptors.
DR   SignaLink; P11473; -.
DR   SIGNOR; P11473; -.
DR   BioGRID-ORCS; 7421; 9 hits in 1090 CRISPR screens.
DR   ChiTaRS; VDR; human.
DR   EvolutionaryTrace; P11473; -.
DR   GeneWiki; Calcitriol_receptor; -.
DR   GenomeRNAi; 7421; -.
DR   Pharos; P11473; Tclin.
DR   PRO; PR:P11473; -.
DR   Proteomes; UP000005640; Chromosome 12.
DR   RNAct; P11473; protein.
DR   Bgee; ENSG00000111424; Expressed in tibia and 150 other tissues.
DR   ExpressionAtlas; P11473; baseline and differential.
DR   Genevisible; P11473; HS.
DR   GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
DR   GO; GO:0005829; C:cytosol; IDA:HPA.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0043235; C:receptor complex; IDA:BHF-UCL.
DR   GO; GO:0090575; C:RNA polymerase II transcription regulator complex; IDA:BHF-UCL.
DR   GO; GO:1902098; F:calcitriol binding; IDA:UniProtKB.
DR   GO; GO:0003677; F:DNA binding; IDA:MGI.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB.
DR   GO; GO:1902121; F:lithocholic acid binding; IDA:UniProtKB.
DR   GO; GO:0038186; F:lithocholic acid receptor activity; IDA:UniProtKB.
DR   GO; GO:0004879; F:nuclear receptor activity; IDA:UniProtKB.
DR   GO; GO:0046965; F:nuclear retinoid X receptor binding; IDA:UniProtKB.
DR   GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0060057; P:apoptotic process involved in mammary gland involution; IEA:Ensembl.
DR   GO; GO:0038183; P:bile acid signaling pathway; IDA:UniProtKB.
DR   GO; GO:0006816; P:calcium ion transport; IEA:Ensembl.
DR   GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR   GO; GO:0000902; P:cell morphogenesis; IMP:UniProtKB.
DR   GO; GO:0006874; P:cellular calcium ion homeostasis; IEA:Ensembl.
DR   GO; GO:0046697; P:decidualization; IEP:BHF-UCL.
DR   GO; GO:0050892; P:intestinal absorption; IEA:Ensembl.
DR   GO; GO:0007595; P:lactation; IEA:Ensembl.
DR   GO; GO:0060745; P:mammary gland branching involved in pregnancy; IEA:Ensembl.
DR   GO; GO:0042789; P:mRNA transcription by RNA polymerase II; IDA:ComplexPortal.
DR   GO; GO:0008285; P:negative regulation of cell population proliferation; IDA:BHF-UCL.
DR   GO; GO:0010839; P:negative regulation of keratinocyte proliferation; IMP:UniProtKB.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:BHF-UCL.
DR   GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:MGI.
DR   GO; GO:0060058; P:positive regulation of apoptotic process involved in mammary gland involution; IEA:Ensembl.
DR   GO; GO:0030501; P:positive regulation of bone mineralization; IC:ComplexPortal.
DR   GO; GO:0010628; P:positive regulation of gene expression; IMP:UniProtKB.
DR   GO; GO:0045618; P:positive regulation of keratinocyte differentiation; IMP:UniProtKB.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:ComplexPortal.
DR   GO; GO:0010980; P:positive regulation of vitamin D 24-hydroxylase activity; IDA:BHF-UCL.
DR   GO; GO:0070564; P:positive regulation of vitamin D receptor signaling pathway; IDA:ComplexPortal.
DR   GO; GO:0060558; P:regulation of calcidiol 1-monooxygenase activity; ISS:BHF-UCL.
DR   GO; GO:0001501; P:skeletal system development; IEA:Ensembl.
DR   GO; GO:0070561; P:vitamin D receptor signaling pathway; IDA:BHF-UCL.
DR   CDD; cd06955; NR_DBD_VDR; 1.
DR   DisProt; DP00184; -.
DR   Gene3D; 1.10.565.10; -; 1.
DR   Gene3D; 3.30.50.10; -; 1.
DR   InterPro; IPR042153; DBD_VDR.
DR   InterPro; IPR035500; NHR-like_dom_sf.
DR   InterPro; IPR000536; Nucl_hrmn_rcpt_lig-bd.
DR   InterPro; IPR001723; Nuclear_hrmn_rcpt.
DR   InterPro; IPR000324; VitD_rcpt.
DR   InterPro; IPR001628; Znf_hrmn_rcpt.
DR   InterPro; IPR013088; Znf_NHR/GATA.
DR   Pfam; PF00104; Hormone_recep; 1.
DR   Pfam; PF00105; zf-C4; 1.
DR   PRINTS; PR00398; STRDHORMONER.
DR   PRINTS; PR00047; STROIDFINGER.
DR   PRINTS; PR00350; VITAMINDR.
DR   SMART; SM00430; HOLI; 1.
DR   SMART; SM00399; ZnF_C4; 1.
DR   SUPFAM; SSF48508; SSF48508; 1.
DR   PROSITE; PS51843; NR_LBD; 1.
DR   PROSITE; PS00031; NUCLEAR_REC_DBD_1; 1.
DR   PROSITE; PS51030; NUCLEAR_REC_DBD_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Cytoplasm; Disease variant;
KW   DNA-binding; Metal-binding; Nucleus; Receptor; Reference proteome;
KW   Transcription; Transcription regulation; Zinc; Zinc-finger.
FT   CHAIN           1..427
FT                   /note="Vitamin D3 receptor"
FT                   /id="PRO_0000053542"
FT   DOMAIN          127..423
FT                   /note="NR LBD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01189"
FT   DNA_BIND        21..96
FT                   /note="Nuclear receptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT   ZN_FING         24..44
FT                   /note="NR C4-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT   ZN_FING         60..84
FT                   /note="NR C4-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT   REGION          97..126
FT                   /note="Hinge"
FT                   /evidence="ECO:0000269|PubMed:10678179"
FT   REGION          158..190
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          246..264
FT                   /note="Interaction with coactivator LXXLL motif"
FT                   /evidence="ECO:0000250|UniProtKB:P13053"
FT   MOTIF           416..424
FT                   /note="9aaTAD"
FT                   /evidence="ECO:0000269|PubMed:30468856"
FT   COMPBIAS        165..190
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         143
FT                   /ligand="calciol"
FT                   /ligand_id="ChEBI:CHEBI:28940"
FT                   /evidence="ECO:0000269|PubMed:10678179,
FT                   ECO:0000269|PubMed:11344298"
FT   BINDING         227..237
FT                   /ligand="calciol"
FT                   /ligand_id="ChEBI:CHEBI:28940"
FT                   /evidence="ECO:0000269|PubMed:10678179,
FT                   ECO:0000269|PubMed:11344298"
FT   BINDING         271..278
FT                   /ligand="calciol"
FT                   /ligand_id="ChEBI:CHEBI:28940"
FT                   /evidence="ECO:0000269|PubMed:10678179,
FT                   ECO:0000269|PubMed:11344298"
FT   BINDING         305
FT                   /ligand="calciol"
FT                   /ligand_id="ChEBI:CHEBI:28940"
FT                   /evidence="ECO:0000269|PubMed:10678179,
FT                   ECO:0000269|PubMed:11344298"
FT   BINDING         397
FT                   /ligand="calciol"
FT                   /ligand_id="ChEBI:CHEBI:28940"
FT                   /evidence="ECO:0000269|PubMed:10678179,
FT                   ECO:0000269|PubMed:11344298"
FT   VAR_SEQ         1
FT                   /note="M -> MEWRNKKRSDWLSMVLRTAGVEEAFGSEVSVRPHRRAPLGSTYLPPA
FT                   PSGM (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_047218"
FT   VARIANT         33
FT                   /note="G -> D (in VDDR2A; dbSNP:rs121909790)"
FT                   /evidence="ECO:0000269|PubMed:2849209"
FT                   /id="VAR_004656"
FT   VARIANT         35
FT                   /note="H -> Q (in VDDR2A)"
FT                   /evidence="ECO:0000269|PubMed:8381803"
FT                   /id="VAR_004657"
FT   VARIANT         45
FT                   /note="K -> E (in VDDR2A)"
FT                   /evidence="ECO:0000269|PubMed:7828346"
FT                   /id="VAR_004658"
FT   VARIANT         46
FT                   /note="G -> D (in VDDR2A; dbSNP:rs121909797)"
FT                   /evidence="ECO:0000269|PubMed:8675579"
FT                   /id="VAR_004659"
FT   VARIANT         47
FT                   /note="F -> I (in VDDR2A)"
FT                   /evidence="ECO:0000269|PubMed:7828346"
FT                   /id="VAR_004660"
FT   VARIANT         50
FT                   /note="R -> Q (in VDDR2A; dbSNP:rs121909794)"
FT                   /evidence="ECO:0000269|PubMed:1652893"
FT                   /id="VAR_004661"
FT   VARIANT         73
FT                   /note="R -> Q (in VDDR2A; dbSNP:rs121909791)"
FT                   /evidence="ECO:0000269|PubMed:2849209"
FT                   /id="VAR_004662"
FT   VARIANT         80
FT                   /note="R -> Q (in VDDR2A; dbSNP:rs121909793)"
FT                   /evidence="ECO:0000269|PubMed:2177843,
FT                   ECO:0000269|PubMed:8106618"
FT                   /id="VAR_004663"
FT   VARIANT         152..427
FT                   /note="Missing (in VDDR2A; loss of calcitriol receptor
FT                   activity; loss of affinity for calcitriol; no effect on
FT                   ligand-independent localization to the nucleus;
FT                   dbSNP:rs121909795)"
FT                   /evidence="ECO:0000269|PubMed:28698609,
FT                   ECO:0000269|PubMed:8392085"
FT                   /id="VAR_079325"
FT   VARIANT         230
FT                   /note="L -> V (in dbSNP:rs11574090)"
FT                   /evidence="ECO:0000269|Ref.5"
FT                   /id="VAR_029309"
FT   VARIANT         274
FT                   /note="R -> L (in VDDR2A; loss of calcitriol receptor
FT                   activity; decreased affinity for calcitriol by a factor of
FT                   1000; no effect on interaction with RXRA; changed
FT                   interaction with NCOR1; loss of interaction with NCOA1; no
FT                   effect on sequence-specific DNA-binding;
FT                   dbSNP:rs121909796)"
FT                   /evidence="ECO:0000269|PubMed:28698609,
FT                   ECO:0000269|PubMed:8392085"
FT                   /id="VAR_004664"
FT   VARIANT         305
FT                   /note="H -> Q (in VDDR2A; loss of calcitriol receptor
FT                   activity; no effect on interaction with RXRA; changed
FT                   interaction with NCOR1; loss of interaction with NCOA1; no
FT                   effect on sequence-specific DNA-binding;
FT                   dbSNP:rs121909798)"
FT                   /evidence="ECO:0000269|PubMed:28698609,
FT                   ECO:0000269|PubMed:9005998"
FT                   /id="VAR_004665"
FT   VARIANT         314
FT                   /note="I -> S (in VDDR2A; dbSNP:rs121909799)"
FT                   /evidence="ECO:0000269|PubMed:8961271"
FT                   /id="VAR_004666"
FT   VARIANT         346
FT                   /note="V -> M (in VDDR2A; decreased calcitriol receptor
FT                   activity; decreased affinity for calcitriol; decreased
FT                   ligand-independent localization to the nucleus; loss of
FT                   interaction with RXRA; decreased interaction with NCOR1;
FT                   decreased interaction with NCOA1; decreased sequence-
FT                   specific DNA-binding; dbSNP:rs267607169)"
FT                   /evidence="ECO:0000269|PubMed:17970811,
FT                   ECO:0000269|PubMed:28698609"
FT                   /id="VAR_079326"
FT   VARIANT         360
FT                   /note="S -> P (in VDDR2A; loss of calcitriol receptor
FT                   activity; loss of affinity for calcitriol; decreased
FT                   ligand-independent localization to the nucleus; loss of
FT                   interaction with RXRA; loss of interaction with NCOR1; loss
FT                   of interaction with NCOA1; loss of sequence-specific DNA-
FT                   binding)"
FT                   /evidence="ECO:0000269|PubMed:28698609"
FT                   /id="VAR_079327"
FT   VARIANT         362
FT                   /note="T -> I (in dbSNP:rs11574115)"
FT                   /evidence="ECO:0000269|Ref.5"
FT                   /id="VAR_029310"
FT   VARIANT         391
FT                   /note="R -> C (in VDDR2A; dbSNP:rs121909800)"
FT                   /evidence="ECO:0000269|PubMed:8961271"
FT                   /id="VAR_004667"
FT   MUTAGEN         47..48
FT                   /note="FF->AA: Abolishes nuclear export."
FT                   /evidence="ECO:0000269|PubMed:12145331"
FT   MUTAGEN         61..62
FT                   /note="PF->AA: Promotes heterodimerization with RXRA; when
FT                   associated with A-75."
FT                   /evidence="ECO:0000269|PubMed:11980721"
FT   MUTAGEN         75
FT                   /note="H->A: Promotes heterodimerization with RXRA; when
FT                   associated with A-61 and A-62."
FT                   /evidence="ECO:0000269|PubMed:11980721"
FT   TURN            25..27
FT                   /evidence="ECO:0007829|PDB:1KB2"
FT   STRAND          33..35
FT                   /evidence="ECO:0007829|PDB:1KB2"
FT   STRAND          38..40
FT                   /evidence="ECO:0007829|PDB:1KB6"
FT   HELIX           42..53
FT                   /evidence="ECO:0007829|PDB:1KB2"
FT   STRAND          61..64
FT                   /evidence="ECO:0007829|PDB:1KB4"
FT   TURN            70..75
FT                   /evidence="ECO:0007829|PDB:1KB2"
FT   HELIX           77..86
FT                   /evidence="ECO:0007829|PDB:1KB2"
FT   HELIX           91..93
FT                   /evidence="ECO:0007829|PDB:1KB2"
FT   HELIX           97..107
FT                   /evidence="ECO:0007829|PDB:1KB2"
FT   STRAND          108..110
FT                   /evidence="ECO:0007829|PDB:1KB6"
FT   TURN            111..113
FT                   /evidence="ECO:0007829|PDB:1KB6"
FT   HELIX           115..119
FT                   /evidence="ECO:0007829|PDB:1KB6"
FT   HELIX           126..142
FT                   /evidence="ECO:0007829|PDB:3B0T"
FT   HELIX           150..152
FT                   /evidence="ECO:0007829|PDB:3B0T"
FT   TURN            162..164
FT                   /evidence="ECO:0007829|PDB:5V39"
FT   HELIX           217..223
FT                   /evidence="ECO:0007829|PDB:3B0T"
FT   HELIX           227..247
FT                   /evidence="ECO:0007829|PDB:3B0T"
FT   HELIX           251..253
FT                   /evidence="ECO:0007829|PDB:3B0T"
FT   HELIX           256..274
FT                   /evidence="ECO:0007829|PDB:3B0T"
FT   HELIX           275..277
FT                   /evidence="ECO:0007829|PDB:3B0T"
FT   TURN            281..284
FT                   /evidence="ECO:0007829|PDB:3B0T"
FT   STRAND          285..287
FT                   /evidence="ECO:0007829|PDB:3B0T"
FT   HELIX           291..293
FT                   /evidence="ECO:0007829|PDB:3B0T"
FT   HELIX           297..301
FT                   /evidence="ECO:0007829|PDB:3B0T"
FT   TURN            302..304
FT                   /evidence="ECO:0007829|PDB:3B0T"
FT   HELIX           307..321
FT                   /evidence="ECO:0007829|PDB:3B0T"
FT   TURN            322..324
FT                   /evidence="ECO:0007829|PDB:2HAR"
FT   HELIX           327..338
FT                   /evidence="ECO:0007829|PDB:3B0T"
FT   STRAND          341..343
FT                   /evidence="ECO:0007829|PDB:3AUQ"
FT   HELIX           349..370
FT                   /evidence="ECO:0007829|PDB:3B0T"
FT   TURN            373..378
FT                   /evidence="ECO:0007829|PDB:3B0T"
FT   HELIX           379..404
FT                   /evidence="ECO:0007829|PDB:3B0T"
FT   HELIX           410..413
FT                   /evidence="ECO:0007829|PDB:3B0T"
FT   HELIX           416..422
FT                   /evidence="ECO:0007829|PDB:3B0T"
SQ   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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