Swiss-Prot entry
ID RRG2_MOUSE STANDARD; PRT; 447 AA.
AC P20787;
DT 01-FEB-1991 (Rel. 17, Created)
DT 01-FEB-1991 (Rel. 17, Last sequence update)
DT 01-MAY-2005 (Rel. 47, Last annotation update)
DE Retinoic acid receptor gamma-B (RAR-gamma-B).
GN Name=Rarg; Synonyms=Nr1b3;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC Muridae; Murinae; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE.
RX MEDLINE=90220619; PubMed=2157970 [NCBI, ExPASy, EBI, Israel, Japan];
RA Giguere V., Shago M., Zirngibl R., Tate P., Rossant J., Varmuza S.;
RT "Identification of a novel isoform of the retinoic acid receptor gamma
RT expressed in the mouse embryo.";
RL Mol. Cell. Biol. 10:2335-2340(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE OF 1-63.
RX MEDLINE=90207264; PubMed=2157210 [NCBI, ExPASy, EBI, Israel, Japan];
RA Kastner P., Krust A., Mendelsohn C., Garnier J.M., Zelent A.,
RA Leroy P., Staub A., Chambon P.;
RT "Murine isoforms of retinoic acid receptor gamma with specific
RT patterns of expression.";
RL Proc. Natl. Acad. Sci. U.S.A. 87:2700-2704(1990).
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=RAR-gamma-B;
CC IsoId=P20787-1; Sequence=Displayed;
CC Name=RAR-gamma-A;
CC IsoId=P18911-1; Sequence=External;
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; M34475; AAA40036.1; -. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR EMBL; M32069; AAA40033.1; -. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR PIR; B34714; B34714.
DR HSSP; P22932; 2LBD. [HSSP ENTRY / SWISS-3DIMAGE / PDB]
DR SMR; P20787; 78-152, 171-406.
DR TRANSFAC; T00717; -.
DR TRANSFAC; T01341; -.
DR Ensembl; ENSMUSG00000001288; Mus_musculus
DR MGD; MGI:97858; Rarg.
DR GeneLynx; Rarg..
DR SOURCE; Rarg..
DR GO; GO:0005634; C:nucleus; IDA.
DR GO; GO:0005667; C:transcription factor complex; IDA.
DR GO; GO:0003677; F:DNA binding; IDA.
DR GO; GO:0005515; F:protein binding; IPI.
DR GO; GO:0045944; P:positive regulation of transcription from P...; IDA.
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; P20787.
DR HOVERGEN [Family / Alignment / Tree]
DR BLOCKS; P20787.
DR ProtoNet; P20787.
DR ProtoMap; P20787.
DR PRESAGE; P20787.
DR DIP; P20787.
DR ModBase; P20787.
DR SWISS-2DPAGE; GET REGION ON 2D PAGE.
KW Alternative splicing; DNA-binding; Multigene family; Nuclear protein;
KW Receptor; Transcription; Transcription regulation; Zinc-finger.
FT DOMAIN 1 78 Modulating.
FT DNA_BIND 79 144 Nuclear receptor-type.
FT ZN_FING 79 99 C4-type.
FT ZN_FING 115 139 C4-type.
FT DOMAIN 145 190 Hinge.
FT DOMAIN 191 410 Ligand-binding.
SQ SEQUENCE 447 AA; 49792 MW; 9C45518BC38DAA99 CRC64;
MYDCMESFVP GPRRLYGAAG PGAGLLRRAT GSSCFAGLES FAWAQPASLQ SVETQSTSSE
EMVPSSPSPP PPPRVYKPCF VCNDKSSGYH YGVSSCEGCK GFFRRSIQKN MVYTCHRDKN
CIINKVTRNR CQYCRLQKCF EVGMSKEAVR NDRNKKKKEV KEEGSPDSYE LSPQLEELIT
KVSKAHQETF PSLCQLGKYT TNSSADHRVQ LDLGLWDKFS ELATKCIIKI VEFAKRLPGF
TGLSIADQIT LLKAACLDIL MLRICTRYTP EQDTMTFSDG LTLNRTQMHN AGFGPLTDLV
FAFAGQLLPL EMDDTETGLL SAICLICGDR MDLEEPEKVD KLQEPLLEAL RLYARRRDPA
KPYMFPRMLM KITDLRGIST KGAERAITLK MEIPGPMPPL IREMLENPEM FEDDSSKPGP
HPKASSEDEA PGGQGKRGQS PQPDQGP
//