Swiss-Prot entry
ID RRG1_MOUSE STANDARD; PRT; 458 AA.
AC P18911; Q91VK5;
DT 01-NOV-1990 (Rel. 16, Created)
DT 01-FEB-1991 (Rel. 17, Last sequence update)
DT 01-MAY-2005 (Rel. 47, Last annotation update)
DE Retinoic acid receptor gamma-A (RAR-gamma-A).
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=89295563; PubMed=2544807 [NCBI, ExPASy, EBI, Israel, Japan]; DOI=10.1038/339714a0;
RA Zelent A., Krust A., Petkovich M., Kastner P., Chambon P.;
RT "Cloning of murine alpha and beta retinoic acid receptors and a novel
RT receptor gamma predominantly expressed in skin.";
RL Nature 339:714-717(1989).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX MEDLINE=22388257; PubMed=12477932 [NCBI, ExPASy, EBI, Israel, Japan]; DOI=10.1073/pnas.242603899;
RA Strausberg R.L., Feingold E.A., Grouse L.H., Derge J.G.,
RA Klausner R.D., Collins F.S., Wagner L., Shenmen C.M., Schuler G.D.,
RA Altschul S.F., Zeeberg B., Buetow K.H., Schaefer C.F., Bhat N.K.,
RA Hopkins R.F., Jordan H., Moore T., Max S.I., Wang J., Hsieh F.,
RA Diatchenko L., Marusina K., Farmer A.A., Rubin G.M., Hong L.,
RA Stapleton M., Soares M.B., Bonaldo M.F., Casavant T.L., Scheetz T.E.,
RA Brownstein M.J., Usdin T.B., Toshiyuki S., Carninci P., Prange C.,
RA Raha S.S., Loquellano N.A., Peters G.J., Abramson R.D., Mullahy S.J.,
RA Bosak S.A., McEwan P.J., McKernan K.J., Malek J.A., Gunaratne P.H.,
RA Richards S., Worley K.C., Hale S., Garcia A.M., Gay L.J., Hulyk S.W.,
RA Villalon D.K., Muzny D.M., Sodergren E.J., Lu X., Gibbs R.A.,
RA Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A.,
RA Whiting M., Madan A., Young A.C., Shevchenko Y., Bouffard G.G.,
RA Blakesley R.W., Touchman J.W., Green E.D., Dickson M.C.,
RA Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M.,
RA Butterfield Y.S.N., Krzywinski M.I., Skalska U., Smailus D.E.,
RA Schnerch A., Schein J.E., Jones S.J.M., Marra M.A.;
RT "Generation and initial analysis of more than 15,000 full-length human
RT and mouse cDNA sequences.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:16899-16903(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE OF 1-74.
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-A;
CC IsoId=P18911-1; Sequence=Displayed;
CC Name=RAR-gamma-B;
CC IsoId=P20787-1; 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; X15848; CAA33845.1; -. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR EMBL; M34476; AAA40035.1; -. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR EMBL; BC012923; AAH12923.1; -. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR EMBL; M32068; AAA40032.1; -. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR HSSP; P22932; 2LBD. [HSSP ENTRY / SWISS-3DIMAGE / PDB]
DR SMR; P18911; 89-163, 182-417.
DR TRANSFAC; T00717; -.
DR TRANSFAC; T01340; -.
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; P18911.
DR HOVERGEN [Family / Alignment / Tree]
DR BLOCKS; P18911.
DR ProtoNet; P18911.
DR ProtoMap; P18911.
DR PRESAGE; P18911.
DR DIP; P18911.
DR ModBase; P18911.
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 89 Modulating.
FT DNA_BIND 90 155 Nuclear receptor-type.
FT ZN_FING 90 110 C4-type.
FT ZN_FING 126 150 C4-type.
FT DOMAIN 156 201 Hinge.
FT DOMAIN 202 421 Ligand-binding.
FT CONFLICT 369 372 DPAK -> RPSQ (in Ref. 1 and 3).
SQ SEQUENCE 458 AA; 50834 MW; F4B63FCF80697636 CRC64;
MATNKERLFA PGALGPGSGY PGAGFPFAFP GALRGSPPFE MLSPSFRGLG QPDLPKEMAS
LSVETQSTSS EEMVPSSPSP PPPPRVYKPC FVCNDKSSGY HYGVSSCEGC KGFFRRSIQK
NMVYTCHRDK NCIINKVTRN RCQYCRLQKC FEVGMSKEAV RNDRNKKKKE VKEEGSPDSY
ELSPQLEELI TKVSKAHQET FPSLCQLGKY TTNSSADHRV QLDLGLWDKF SELATKCIIK
IVEFAKRLPG FTGLSIADQI TLLKAACLDI LMLRICTRYT PEQDTMTFSD GLTLNRTQMH
NAGFGPLTDL VFAFAGQLLP LEMDDTETGL LSAICLICGD RMDLEEPEKV DKLQEPLLEA
LRLYARRRDP AKPYMFPRML MKITDLRGIS TKGAERAITL KMEIPGPMPP LIREMLENPE
MFEDDSSKPG PHPKASSEDE APGGQGKRGQ SPQPDQGP
//