Swiss-Prot entry
ID VDR_XENLA STANDARD; PRT; 422 AA.
AC O13124;
DT 15-DEC-1998 (Rel. 37, Created)
DT 15-DEC-1998 (Rel. 37, 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 Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Amphibia; Batrachia; Anura; Mesobatrachia; Pipoidea; Pipidae;
OC Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Kidney;
RX MEDLINE=97307679; PubMed=9165021 [NCBI, ExPASy, EBI, Israel, Japan]; DOI=10.1210/en.138.6.2347;
RA Li Y.C., Bergwitz C., Jueppner H., Demay M.B.;
RT "Cloning and characterization of the vitamin D receptor from Xenopus
RT laevis.";
RL Endocrinology 138:2347-2353(1997).
CC -!- FUNCTION: VDR mediates the action of vitamin D3 by controlling the
CC expression of hormone sensitive genes.
CC -!- SUBCELLULAR LOCATION: Nuclear.
CC -!- TISSUE SPECIFICITY: Detected in all tissues examined. Highest
CC level in small intestine and skin.
CC -!- DEVELOPMENTAL STAGE: First detected at stage 13. Increases
CC gradually and peaks at stage 57-61 then decreases to the level
CC seen in adult.
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; U91846; AAB58585.1; -. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR HSSP; P11473; 1KB2. [HSSP ENTRY / SWISS-3DIMAGE / PDB]
DR SMR; O13124; 22-122, 166-417.
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 PROSITE; PS00031; NUCLEAR_REC_DBD_1; 1.
DR PROSITE; PS51030; NUCLEAR_REC_DBD_2; 1.
DR HOVERGEN [Family / Alignment / Tree]
DR BLOCKS; O13124.
DR ProtoNet; O13124.
DR ProtoMap; O13124.
DR PRESAGE; O13124.
DR DIP; O13124.
DR ModBase; O13124.
DR SWISS-2DPAGE; GET REGION ON 2D PAGE.
KW DNA-binding; Nuclear protein; Receptor; Transcription;
KW Transcription regulation; Zinc-finger.
FT DNA_BIND 22 90 Nuclear receptor-type.
FT ZN_FING 25 45 C4-type.
FT ZN_FING 61 85 C4-type.
FT DOMAIN 91 188 Hinge.
FT DOMAIN 189 422 Ligand-binding.
SQ SEQUENCE 422 AA; 48188 MW; C8A9F25414FEE9D5 CRC64;
MEFMAATTSI ADTDMEFDKN VPRICGVCGD KATGFHFNAM TCEGCKGFFR RSMKRKAMFT
CPFNGDCRIT KDNRRHCQSC RLKRCVDIGM MKEFILTDEE VQRKRQMINK RKSEEALKES
MRPKISDEQQ KMIDILLEAH RKTFDTTYSD FNKFRPPVRE NVDPFRRITR SSSVHTQGSP
SEDSDVFTSS PDSSEHGFFS ASLFGQFEYS SMGGKSGELS MLPHIADLVS YSIQKIIGFA
KMIPGFRDLI AEDQIALLKS SVIEVIMLRS NQSFSLDDMS WTCGSEDFKY KVDDVTQAGH
NMELLEPLVK FQVGLKKLDL HEEEHVLLMA ICILSPDRPG LQDKALVESI QDRLSSTLQT
YILCKHPPPG SRLLYAKMIQ KLADLRSLNE EHSKQYRSIS FLPEHSMKLT PLMLEVFSDE
IP
//