Swiss-Prot entry
ID RRG_BRARE STANDARD; PRT; 499 AA.
AC Q91392;
DT 15-JUL-1999 (Rel. 38, Created)
DT 15-JUL-1999 (Rel. 38, Last sequence update)
DT 01-MAY-2005 (Rel. 47, Last annotation update)
DE Retinoic acid receptor gamma (RAR-gamma) (ZRAR gamma).
GN Name=rarg; Synonyms=nr1b3;
OS Brachydanio rerio (Zebrafish) (Danio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Cyprinidae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE.
RX MEDLINE=95001557; PubMed=7918098 [NCBI, ExPASy, EBI, Israel, Japan]; DOI=10.1016/0925-4773(94)90082-5;
RA Joore J., der Lans G.B., Lanser P.H., Vervaart J.M., Zivkovic D.,
RA Speksnijder J.E., Kruijer W.;
RT "Effects of retinoic acid on the expression of retinoic acid receptors
RT during zebrafish embryogenesis.";
RL Mech. Dev. 46:137-150(1994).
CC -!- FUNCTION: This is a receptor for retinoic acid. This metabolite
CC has profound effects on vertebrate development. Retinoic acid is a
CC morphogen and is a powerful teratogen. This receptor controls cell
CC function by directly regulating gene expression.
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; S74156; AAB32277.1; -. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR PIR; I51257; I51257.
DR HSSP; P19793; 1DSZ. [HSSP ENTRY / SWISS-3DIMAGE / PDB]
DR SMR; Q91392; 71-149, 170-405.
DR TRANSFAC; T04895; -.
DR Ensembl; ENSDARG00000034117; Danio_rerio
DR ZFIN; ZDB-GENE-980526-531; rarg.
DR InterPro; IPR000536; Hrmon_recept_lig.
DR InterPro; IPR001723; Stdhrmn_receptor.
DR InterPro; IPR008946; Str_ncl_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; PR01292; RETNOICACIDR.
DR PRINTS; PR00398; STRDHORMONER.
DR PRINTS; PR00047; STROIDFINGER.
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 CMR; Q91392.
DR HOVERGEN [Family / Alignment / Tree]
DR BLOCKS; Q91392.
DR ProtoNet; Q91392.
DR ProtoMap; Q91392.
DR PRESAGE; Q91392.
DR DIP; Q91392.
DR ModBase; Q91392.
DR SWISS-2DPAGE; GET REGION ON 2D PAGE.
KW DNA-binding; Nuclear protein; Receptor; Transcription;
KW Transcription regulation; Zinc-finger.
FT DOMAIN 1 76 Modulating.
FT DNA_BIND 77 142 Nuclear receptor-type.
FT ZN_FING 77 97 C4-type.
FT ZN_FING 113 137 C4-type.
FT DOMAIN 143 188 Hinge.
FT DOMAIN 189 409 Ligand-binding.
SQ SEQUENCE 499 AA; 56179 MW; 83540619FB45A537 CRC64;
MFDCMEALGM GPRQLYDVTN RGACMLRKAS PFYAGLDPFA WTGTASVRSV ETQSTSSEEM
VPSSPSPPPP PRVYKPCFVC QDKSSGYHYG VSSCEGCKGF FRRSIQKNMV YTCHRDKNCQ
INKVTRNRCQ YCRLQKCFEV GMSKEAVRND RNKKKKDVKD EVIPPESYEL SGELEELVNK
VSKAHQETFP SLCQLGKYTT NSSSDHRIQL DLGLWDKFSE LSTKCIIKIV EFAKRLPGFT
TLTIADQITL LKSACLDILM LRICTRYTPE QDTMTFSDGL TLNRTQMHNA GFGPLTDLVF
AFAGQLLPLE MDDTETGLLS AICLICGDRM DLEEPERVDR LQEPLLEALK IYARRRRPNK
PHMFPRMLMK ITDLRGISTK GAERAITLKM EIPGPMPPLI REMLENPEAF EDQSEATEKK
PEPEPPAPPP PALLTMKKEQ EDEDDSWATE NGSEPSPEEE DDDDEDGEEE RGTDSDGEAW
GGQEPNADVS RKSHGGRAQ
//