VDR_PIG
ID VDR_PIG Reviewed; 427 AA.
AC A3RGC1;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2007, sequence version 1.
DT 03-AUG-2022, entry version 107.
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 Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Fernandez A.I., Silio L., Rodriguez C., Ovilo C.;
RT "Vitamin D receptor characterization.";
RL Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases.
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 -!- 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; EF405627; ABN80095.1; -; mRNA.
DR RefSeq; NP_001090883.1; NM_001097414.1.
DR AlphaFoldDB; A3RGC1; -.
DR SMR; A3RGC1; -.
DR STRING; 9823.ENSSSCP00000019810; -.
DR BindingDB; A3RGC1; -.
DR ChEMBL; CHEMBL5304; -.
DR DrugCentral; A3RGC1; -.
DR PaxDb; A3RGC1; -.
DR PRIDE; A3RGC1; -.
DR Ensembl; ENSSSCT00000032274; ENSSSCP00000019810; ENSSSCG00000020864.
DR Ensembl; ENSSSCT00015054074; ENSSSCP00015021680; ENSSSCG00015040270.
DR Ensembl; ENSSSCT00025006974; ENSSSCP00025002860; ENSSSCG00025005173.
DR Ensembl; ENSSSCT00030012596; ENSSSCP00030005651; ENSSSCG00030009207.
DR Ensembl; ENSSSCT00035071430; ENSSSCP00035028984; ENSSSCG00035053536.
DR Ensembl; ENSSSCT00040018729; ENSSSCP00040007652; ENSSSCG00040013967.
DR Ensembl; ENSSSCT00045000388; ENSSSCP00045000190; ENSSSCG00045000290.
DR Ensembl; ENSSSCT00055012508; ENSSSCP00055009853; ENSSSCG00055006377.
DR Ensembl; ENSSSCT00055012543; ENSSSCP00055009877; ENSSSCG00055006377.
DR Ensembl; ENSSSCT00060049451; ENSSSCP00060021161; ENSSSCG00060036478.
DR Ensembl; ENSSSCT00065086338; ENSSSCP00065037748; ENSSSCG00065062920.
DR GeneID; 396628; -.
DR KEGG; ssc:396628; -.
DR CTD; 7421; -.
DR VGNC; VGNC:94814; VDR.
DR eggNOG; KOG3575; Eukaryota.
DR GeneTree; ENSGT00940000155473; -.
DR HOGENOM; CLU_007368_12_0_1; -.
DR InParanoid; A3RGC1; -.
DR OrthoDB; 297114at2759; -.
DR TreeFam; TF316304; -.
DR Reactome; R-SSC-196791; Vitamin D (calciferol) metabolism.
DR Reactome; R-SSC-383280; Nuclear Receptor transcription pathway.
DR PRO; PR:A3RGC1; -.
DR Proteomes; UP000008227; Chromosome 5.
DR Proteomes; UP000314985; Unplaced.
DR Bgee; ENSSSCG00000020864; Expressed in adult mammalian kidney and 25 other tissues.
DR ExpressionAtlas; A3RGC1; baseline and differential.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0043235; C:receptor complex; IEA:Ensembl.
DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; IEA:Ensembl.
DR GO; GO:1902098; F:calcitriol binding; IEA:Ensembl.
DR GO; GO:1902121; F:lithocholic acid binding; IEA:Ensembl.
DR GO; GO:0038186; F:lithocholic acid receptor activity; IEA:Ensembl.
DR GO; GO:0004879; F:nuclear receptor activity; ISS:UniProtKB.
DR GO; GO:0046965; F:nuclear retinoid X receptor binding; IEA:Ensembl.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0070644; F:vitamin D response element binding; IEA:Ensembl.
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:0006816; P:calcium ion transport; IEA:Ensembl.
DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR GO; GO:0000902; P:cell morphogenesis; IEA:Ensembl.
DR GO; GO:0006874; P:cellular calcium ion homeostasis; IEA:Ensembl.
DR GO; GO:0046697; P:decidualization; IEA:Ensembl.
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; IEA:Ensembl.
DR GO; GO:0010839; P:negative regulation of keratinocyte proliferation; IEA:Ensembl.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0060058; P:positive regulation of apoptotic process involved in mammary gland involution; IEA:Ensembl.
DR GO; GO:0010628; P:positive regulation of gene expression; IEA:Ensembl.
DR GO; GO:0045618; P:positive regulation of keratinocyte differentiation; IEA:Ensembl.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0010980; P:positive regulation of vitamin D 24-hydroxylase activity; IEA:Ensembl.
DR GO; GO:0070564; P:positive regulation of vitamin D receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0060558; P:regulation of calcidiol 1-monooxygenase activity; IEA:Ensembl.
DR GO; GO:0001501; P:skeletal system development; IEA:Ensembl.
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..427
FT /note="Vitamin D3 receptor"
FT /id="PRO_0000337877"
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..79
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 149..201
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:0000250|UniProtKB:P11473"
FT COMPBIAS 168..199
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 227..237
FT /ligand="calciol"
FT /ligand_id="ChEBI:CHEBI:28940"
FT /evidence="ECO:0000250|UniProtKB:P11473"
FT BINDING 271..278
FT /ligand="calciol"
FT /ligand_id="ChEBI:CHEBI:28940"
FT /evidence="ECO:0000250|UniProtKB:P11473"
FT BINDING 305
FT /ligand="calciol"
FT /ligand_id="ChEBI:CHEBI:28940"
FT /evidence="ECO:0000250|UniProtKB:P11473"
FT BINDING 397
FT /ligand="calciol"
FT /ligand_id="ChEBI:CHEBI:28940"
FT /evidence="ECO:0000250|UniProtKB:P11473"
SQ SEQUENCE 427 AA; 48128 MW; 79670A39FE013858 CRC64;
MEATAASTSL PDPGDFDRNV PRICGVCGDR ATGFHFNAMT CEGCKGFFRR SMKRKALFTC
PFNGDCRITK DNRRHCQACR LKRCVDIGMM KEFILTDEEV QRKREMILKR KEEEALKDSL
RPKLSEEQQR IIAILLDAHH KTYDPTYADF GQFRPPVRGD EEEGTLPSRS SSAHAPSFSG
SSSSSCSDQY TSSPDTMEPA SFSHLDLSEE DSDDPSVTLD LSQLSMLPHL ADLVSYSIQK
VIGFAKMIPG FRDLTAEDQI VLLKSSAIEV IMLRSNQSFT MDDMSWTCGS RDYKYQVSDV
AKAGHSLELI EPLIKFQVGL KKLNLHEEEH VLLMAICIVS PDRPGVQDPT LIEAIQDRLS
NTLQTYIRCR HPPPGSHLLY AKMIQKLADL RSLNEEHSKQ YRCLSFQPEC SMKLTPLVLE
VFGNEIS
