Swiss-Prot entry

ID   VDR_BOVIN      STANDARD;      PRT;   424 AA.
AC   Q28037;
DT   01-NOV-1997 (Rel. 35, Created)
DT   01-NOV-1997 (Rel. 35, Last sequence update)
DT   01-MAY-2005 (Rel. 47, Last annotation update)
DE   Vitamin D3 receptor (VDR) (1,25-dihydroxyvitamin D3 receptor).
GN   Name=VDR; Synonyms=NR1I1;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; 
OC   Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia; 
OC   Pecora; Bovidae; Bovinae; Bos. 
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RX   MEDLINE=97034797; PubMed=8880453 [NCBI, ExPASy, EBI, Israel, Japan];
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).
CC   -!- FUNCTION: Nuclear hormone receptor. VDR mediates the action of
CC       vitamin D3 by controlling the expression of hormone sensitive
CC       genes.
CC   -!- SUBUNIT: Interacts with NCOA3 and NCOA6 coactivators, leading to a
CC       strong increase of transcription of target genes (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nuclear.
CC   -!- DOMAIN: Composed of three domains: a modulating N-terminal domain,
CC       a DNA-binding domain and a C-terminal steroid-binding domain.
CC   -!- SIMILARITY: Belongs to the nuclear hormone receptor family. NR1
CC       subfamily.
CC   -!- SIMILARITY: Contains 1 nuclear receptor DNA-binding domain.
CC   --------------------------------------------------------------------------
CC   This Swiss-Prot entry is copyright. It is produced through a collaboration
CC   between  the Swiss Institute of Bioinformatics  and the  EMBL outstation -
CC   the European Bioinformatics Institute.  There are no  restrictions on  its
CC   use as long as its content is in no way modified and this statement is not
CC   removed.
CC   --------------------------------------------------------------------------
DR   EMBL; U50200; AAB01543.1; -. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR   HSSP; P11473; 1IE9. [HSSP ENTRY / SWISS-3DIMAGE / PDB]
DR   SMR; Q28037; 18-118, 168-420.
DR   InterPro; IPR000536; Hrmon_recept_lig.
DR   InterPro; IPR001723; Stdhrmn_receptor.
DR   InterPro; IPR008946; Str_ncl_receptor.
DR   InterPro; IPR000324; VitD_receptor.
DR   InterPro; IPR001628; Znf_C4steroid.
DR   InterPro; Graphical view of domain structure.
DR   Pfam; PF00104; Hormone_recep; 1.
DR   Pfam; PF00105; zf-C4; 1.
DR   Pfam; Graphical view of domain structure.
DR   PRINTS; PR00398; STRDHORMONER.
DR   PRINTS; PR00047; STROIDFINGER.
DR   PRINTS; PR00350; VITAMINDR.
DR   ProDom; PD000035; Znf_C4steroid; 1.
DR   ProDom [Domain structure / List of seq. sharing at least 1 domain ]
DR   SMART; SM00430; HOLI; 1.
DR   SMART; SM00399; ZnF_C4; 1.
DR   PROSITE; PS00031; NUCLEAR_REC_DBD_1; 1.
DR   PROSITE; PS51030; NUCLEAR_REC_DBD_2; 1.
DR   HOVERGEN [Family / Alignment / Tree]
DR   BLOCKS; Q28037.
DR   ProtoNet; Q28037.
DR   ProtoMap; Q28037.
DR   PRESAGE; Q28037.
DR   DIP; Q28037.
DR   ModBase; Q28037.
DR   SWISS-2DPAGE; GET REGION ON 2D PAGE.
KW   DNA-binding; Nuclear protein; Phosphorylation; Receptor;
KW   Transcription; Transcription regulation; Zinc-finger.
FT   DNA_BIND     18     93       Nuclear receptor-type.
FT   ZN_FING      21     41       C4-type.
FT   ZN_FING      57     81       C4-type.
FT   DOMAIN       94    188       Hinge.
FT   DOMAIN      189    424       Ligand-binding.
SQ   SEQUENCE   424 AA;  47958 MW;  E9E24926CE38CB7D CRC64;
     MAASTSLPDP GDFDRNVPRI CGVCGDRATG FHFNAMTCEG CKGFFRRSMK RKALFTCPFN
     GDCRITKDNR RHCQACRLKR CVDIGMMKEF ILTDEEVQRK REMILKRKEE EALKDSLRPK
     LSEEQQRIIA ILLDAHHKTY DPTYSDFCQF RPPVRVNDGG GSHPSRPNSR HTPSFSGDSS
     SSCSDHCITS SDMMDSSSFS NLDLSEEDSD DPSVTLELSQ LSMLPHLADL VSYSIQKVIG
     FAKMIPGFRD LTSEDQIVLL KSSAIEVIML RSNESFTMDD MSWTCGNQDY KYRVSDVTKA
     GHSLELIEPL IKFQVGLKKL NLHEEEHVLL MAICIVSPDR PGVQDAALIE AIQDRLSNTL
     QTYIRCRHPP PGSHLLYAKM IQKLADLRSL NEEHSKQYRC LSFQPECSMK LTPLVLEVFG
     NEIS
//