VDR_BOVIN
ID VDR_BOVIN Reviewed; 426 AA.
AC Q28037;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 04-DEC-2007, sequence version 2.
DT 03-AUG-2022, entry version 153.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP PRELIMINARY NUCLEOTIDE SEQUENCE.
RX PubMed=8880453; DOI=10.3168/jds.s0022-0302(96)76486-x;
RA Neibergs H.L., Bosworth B.T., Reinhardt T.A.;
RT "Nucleotide sequence of the bovine vitamin D3 receptor.";
RL J. Dairy Sci. 79:1313-1315(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hereford;
RX PubMed=19390049; DOI=10.1126/science.1169588;
RG The bovine genome sequencing and analysis consortium;
RT "The genome sequence of taurine cattle: a window to ruminant biology and
RT evolution.";
RL Science 324:522-528(2009).
RN [3]
RP TISSUE SPECIFICITY.
RX PubMed=6250480; DOI=10.1016/0003-9861(80)90158-7;
RA Reinhardt T.A., Conrad H.R.;
RT "Specific binding protein for 1,25-dihydroxyvitamin D3 in bovine mammary
RT gland.";
RL Arch. Biochem. Biophys. 203:108-116(1980).
RN [4]
RP TISSUE SPECIFICITY.
RX PubMed=8747330; DOI=10.3168/jds.s0022-0302(95)76867-9;
RA Goff J.P., Reinhardt T.A., Horst R.L.;
RT "Milk fever and dietary cation-anion balance effects on concentration of
RT vitamin D receptor in tissue of periparturient dairy cows.";
RL J. Dairy Sci. 78:2388-2394(1995).
CC -!- FUNCTION: Nuclear receptor for calcitriol, the active form of vitamin
CC D3 which mediates the action of this vitamin on cells (By similarity).
CC Enters the nucleus upon vitamin D3 binding where it forms heterodimers
CC with the retinoid X receptor/RXR (By similarity). The VDR-RXR
CC heterodimers bind to specific response elements on DNA and activate the
CC transcription of vitamin D3-responsive target genes (By similarity).
CC Plays a central role in calcium homeostasis (By similarity).
CC {ECO:0000250|UniProtKB:P11473, ECO:0000250|UniProtKB:P13053}.
CC -!- SUBUNIT: Homodimer in the absence of bound vitamin D3. Heterodimer with
CC RXRA after vitamin D3 binding. Interacts with MED1, NCOA1, NCOA2, NCOA3
CC and NCOA6 coactivators, leading to a strong increase of transcription
CC of target genes. Interacts with the corepressor NCOR1. Interacts with
CC SNW1. Interacts with IRX4, the interaction does not affect its
CC transactivation activity (By similarity). Interacts with CRY1 (By
CC similarity). Interacts with CRY2 in a ligand-dependent manner (By
CC similarity). {ECO:0000250|UniProtKB:P11473,
CC ECO:0000250|UniProtKB:P48281}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P11473,
CC ECO:0000255|PROSITE-ProRule:PRU00407}. Cytoplasm
CC {ECO:0000250|UniProtKB:P11473}. Note=Localizes mainly to the nucleus.
CC Translocated into the nucleus via both ligand-dependent and ligand-
CC independent pathways; ligand-independent nuclear translocation is
CC mediated by IPO4. {ECO:0000250|UniProtKB:P11473}.
CC -!- TISSUE SPECIFICITY: Mammary gland, expression increases during
CC lactation. Also found in colon, expression is down-regulated at
CC parturition. {ECO:0000269|PubMed:6250480, ECO:0000269|PubMed:8747330}.
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:0000250|UniProtKB:P11473}.
CC -!- DOMAIN: The 9aaTAD motif is a transactivation domain present in a large
CC number of yeast and animal transcription factors.
CC {ECO:0000250|UniProtKB:P11473}.
CC -!- SIMILARITY: Belongs to the nuclear hormone receptor family. NR1
CC subfamily. {ECO:0000305}.
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DR EMBL; AAFC03056593; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_001161404.1; NM_001167932.1.
DR AlphaFoldDB; Q28037; -.
DR SMR; Q28037; -.
DR STRING; 9913.ENSBTAP00000021832; -.
DR BindingDB; Q28037; -.
DR ChEMBL; CHEMBL3452; -.
DR DrugCentral; Q28037; -.
DR PaxDb; Q28037; -.
DR PRIDE; Q28037; -.
DR GeneID; 533656; -.
DR KEGG; bta:533656; -.
DR CTD; 7421; -.
DR eggNOG; KOG3575; Eukaryota.
DR HOGENOM; CLU_007368_12_0_1; -.
DR InParanoid; Q28037; -.
DR OrthoDB; 297114at2759; -.
DR PRO; PR:Q28037; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0004879; F:nuclear receptor activity; ISS: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:0030154; P:cell differentiation; IBA:GO_Central.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0070561; P:vitamin D receptor signaling pathway; ISS:UniProtKB.
DR CDD; cd06955; NR_DBD_VDR; 1.
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 2: Evidence at transcript level;
KW Cytoplasm; DNA-binding; Metal-binding; Nucleus; Receptor;
KW Reference proteome; Transcription; Transcription regulation; Zinc;
KW Zinc-finger.
FT CHAIN 1..426
FT /note="Vitamin D3 receptor"
FT /id="PRO_0000053541"
FT DOMAIN 127..422
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:0000250|UniProtKB:P11473"
FT REGION 147..215
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 244..262
FT /note="Interaction with coactivator LXXLL motif"
FT /evidence="ECO:0000250|UniProtKB:P13053"
FT MOTIF 415..423
FT /note="9aaTAD"
FT /evidence="ECO:0000250|UniProtKB:P11473"
FT COMPBIAS 170..204
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:0000250|UniProtKB:P11473"
FT BINDING 225..235
FT /ligand="calciol"
FT /ligand_id="ChEBI:CHEBI:28940"
FT /evidence="ECO:0000250|UniProtKB:P11473"
FT BINDING 269..276
FT /ligand="calciol"
FT /ligand_id="ChEBI:CHEBI:28940"
FT /evidence="ECO:0000250|UniProtKB:P11473"
FT BINDING 304
FT /ligand="calciol"
FT /ligand_id="ChEBI:CHEBI:28940"
FT /evidence="ECO:0000250|UniProtKB:P11473"
FT BINDING 396
FT /ligand="calciol"
FT /ligand_id="ChEBI:CHEBI:28940"
FT /evidence="ECO:0000250|UniProtKB:P11473"
SQ SEQUENCE 426 AA; 48318 MW; 1A0E76ABE461EBF1 CRC64;
MEATAASTSL PDPGDFDRNV PRICGVCGDR ATGFHFNAMT CEGCKGFFRR SMKRKALFTC
PFNGDCRITK DNRRHCQACR LKRCIDIGMM KEFILTDEEV QRKREMILKR KEEEALKDSL
RPKLSEEQQR IITTLLEAHH KTYDDTYSDF SQFRPPVRNS EDEGNRPLRS ILTPSFSGNS
SSSCSDHCTS SPDTMEPTSF SNQDLNEEDS DDPSVTLDLS QLSMLPHLAD LVSYSIQKVI
GFAKMIPGFR DLTPEDQIVL LKSSAIEVIM LRSNQSFTLD DDMSWTCGSP DYKYQVSDVT
RAGHSLELIE PLIKFQVGLK KLNLHEEEHV LLMAICIVSP DRPGVQDAAL VEAIQDRLSN
TLQTYIRCRH PPPGSHLLYA KMIQKLADLR SLNEEHSKQY RCLSFQPESS MKLTPLLFEV
FGNEIS
