Swiss-Prot entry
ID VDR_SAGOE STANDARD; PRT; 427 AA.
AC Q95MH5;
DT 05-JUL-2004 (Rel. 44, Created)
DT 05-JUL-2004 (Rel. 44, 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 Saguinus oedipus (Cotton-top tamarin).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Platyrrhini;
OC Callitrichidae; Saguinus.
OX NCBI_TaxID=9490;
RN [1]
RP NUCLEOTIDE SEQUENCE.
RX MEDLINE=21269858; PubMed=11376448 [NCBI, ExPASy, EBI, Israel, Japan]; DOI=10.1002/ajp.1016;
RA Chun R.F., Chen H., Boldrick L., Sweet C., Adams J.S.;
RT "Cloning, sequencing, and functional characterization of the vitamin D
RT receptor in vitamin D-resistant New World primates.";
RL Am. J. Primatol. 54:107-118(2001).
CC -!- FUNCTION: Nuclear hormone receptor. VDR mediates the action of
CC vitamin D3 by controlling the expression of hormone sensitive
CC genes (By similarity).
CC -!- SUBUNIT: Interacts with SMAD3. Interacts with NCOA3 and NCOA6
CC coactivators, leading to a strong increase of transcription of
CC target genes (By similarity).
CC -!- SUBCELLULAR LOCATION: Nuclear (By similarity).
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; AF354232; AAK48863.1; -. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR HSSP; P11473; 1KB6. [HSSP ENTRY / SWISS-3DIMAGE / PDB]
DR SMR; Q95MH5; 21-121, 171-423.
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; Q95MH5.
DR ProtoNet; Q95MH5.
DR ProtoMap; Q95MH5.
DR PRESAGE; Q95MH5.
DR DIP; Q95MH5.
DR ModBase; Q95MH5.
DR SWISS-2DPAGE; GET REGION ON 2D PAGE.
KW DNA-binding; Nuclear protein; Phosphorylation; Receptor;
KW Transcription; Transcription regulation; Zinc-finger.
FT DNA_BIND 21 96 Nuclear receptor-type.
FT ZN_FING 24 44 C4-type.
FT ZN_FING 60 84 C4-type.
FT DOMAIN 97 191 Hinge.
FT DOMAIN 192 427 Ligand-binding.
SQ SEQUENCE 427 AA; 48383 MW; 5B933C4F023B5199 CRC64;
MEAMAASTSL PDPGDFDRNV PRICGVCGDR ATGFHFNAMT CEGCKGFFRR SMKRKALFTC
PFNGDCRITK DNRRHCQACR LKRCVDIGMM KEFILTDEEV QRKREMILKR KEEEALKDSL
RPKLSEEQQR IIAILLDAHH KTYDPTYSDF CQFRPPVRVN DGGGSHPSRP NSRHTPSFSG
DSSSCCSDHY ITSPDMMDSS SFSNLDLSEE DSDDPSLTLE LSQLSMLPHL ADLVSYSIQK
VIGFAKMIPG FRDLTSEDQI VLLKSSAIEV IMLRSNESFT MDDMSWTCGN PDYKYRISDV
TKAGHNLELI EPLIKFQVGL KKLNLHEEEH VLLMAICIVS PDRPGVQDAA LIEAIQDRLS
NTLQTYIRCR HPPPGSHLLY AKMIQKLADL RSLNEEHSKQ YRCLSFQPES SMKLTPLVLE
VFGNEIS
//