Swiss-Prot entry
ID RRG1_HUMAN STANDARD; PRT; 454 AA.
AC P13631;
DT 01-JAN-1990 (Rel. 13, Created)
DT 01-JAN-1990 (Rel. 13, Last sequence update)
DT 01-MAY-2005 (Rel. 47, Last annotation update)
DE Retinoic acid receptor gamma-1 (RAR-gamma-1).
GN Name=RARG; Synonyms=NR1B3;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE.
RX MEDLINE=89315787; PubMed=2546152 [NCBI, ExPASy, EBI, Israel, Japan];
RA Krust A., Kastner P., Petkovich M., Zelent A., Chambon P.;
RT "A third human retinoic acid receptor, hRAR-gamma.";
RL Proc. Natl. Acad. Sci. U.S.A. 86:5310-5314(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE.
RX MEDLINE=91042616; PubMed=2172793 [NCBI, ExPASy, EBI, Israel, Japan];
RA Ishikawa T., Umesono K., Mangelsdorf D.J., Aburatani H., Stanger B.Z.,
RA Shibasaki Y., Imawari M., Evans R.M., Takaku F.;
RT "A functional retinoic acid receptor encoded by the gene on human
RT chromosome 12.";
RL Mol. Endocrinol. 4:837-844(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE.
RX MEDLINE=91187677; PubMed=1849262 [NCBI, ExPASy, EBI, Israel, Japan];
RA Lehmann J.M., Hoffmann B., Pfahl M.;
RT "Genomic organization of the retinoic acid receptor gamma gene.";
RL Nucleic Acids Res. 19:573-578(1991).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 [5]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 178-423.
RX MEDLINE=96107307; PubMed=7501014 [NCBI, ExPASy, EBI, Israel, Japan]; DOI=10.1038/378681a0;
RA Renaud J.-P., Rochel N., Ruff M., Vivat V., Chambon P., Gronemeyer H.,
RA Moras D.;
RT "Crystal structure of the RAR-gamma ligand-binding domain bound to
RT all-trans retinoic acid.";
RL Nature 378:681-689(1995).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 178-423.
RX MEDLINE=98162555; PubMed=9501913 [NCBI, ExPASy, EBI, Israel, Japan];
RA Klaholz B.P., Renaud J.-P., Mitschler A., Zusi C., Chambon P.,
RA Gronemeyer H., Moras D.;
RT "Conformational adaptation of agonists to the human nuclear receptor
RT RAR gamma.";
RL Nat. Struct. Biol. 5:199-202(1998).
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 Comment=Isoforms differ only in their N-terminal regions;
CC Name=RAR-gamma1;
CC IsoId=P13631-1; Sequence=Displayed;
CC Name=RAR-gamma2;
CC IsoId=P22932-1; 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; M24857; AAA52692.1; -. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR EMBL; M38258; AAA60254.1; -. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR EMBL; M57707; AAA63254.1; -. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR EMBL; BC019098; AAH19098.2; ALT_INIT. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR PIR; A33903; A33903.
DR PDB; 1FCX; X-ray; A=183-417. [ExPASy / RCSB]
DR PDB; 1FCY; X-ray; A=182-417. [ExPASy / RCSB]
DR PDB; 1FCZ; X-ray; A=183-417. [ExPASy / RCSB]
DR PDB; 1FD0; X-ray; A=183-417. [ExPASy / RCSB]
DR PDB; 3LBD; X-ray; -. [ExPASy / RCSB]
DR PDB; 4LBD; X-ray; -. [ExPASy / RCSB]
DR SMR; P13631; 89-163.
DR TRANSFAC; T00720; -.
DR TRANSFAC; T01330; -.
DR Ensembl; ENSG00000172819; Homo_sapiens
DR Genew; HGNC:9866; RARG.
DR CleanEx; HGNC:9866; RARG.
DR MIM; 180190; -. [NCBI / EBI]
DR GeneCards; RARG.
DR GeneLynx; RARG.
DR GenAtlas; RARG.
DR SOURCE; RARG.
DR GO; GO:0003708; F:retinoic acid receptor activity; TAS.
DR GO; GO:0007275; P:development; TAS.
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; P13631.
DR HOVERGEN [Family / Alignment / Tree]
DR BLOCKS; P13631.
DR ProtoNet; P13631.
DR ProtoMap; P13631.
DR PRESAGE; P13631.
DR DIP; P13631.
DR ModBase; P13631.
DR SWISS-2DPAGE; GET REGION ON 2D PAGE.
KW 3D-structure; Alternative splicing; DNA-binding; Multigene family;
KW Nuclear protein; Receptor; Transcription; Transcription regulation;
KW 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 HELIX 184 200
FT HELIX 204 206
FT STRAND 210 210
FT TURN 214 215
FT HELIX 224 246
FT TURN 247 247
FT TURN 249 250
FT HELIX 251 253
FT HELIX 256 277
FT TURN 278 278
FT STRAND 279 280
FT TURN 281 284
FT STRAND 285 287
FT TURN 289 290
FT STRAND 292 295
FT HELIX 296 302
FT TURN 303 304
FT HELIX 305 307
FT HELIX 308 318
FT HELIX 319 321
FT HELIX 325 336
FT TURN 339 340
FT TURN 342 343
FT HELIX 347 368
FT TURN 370 371
FT TURN 373 374
FT HELIX 375 401
FT TURN 402 403
FT HELIX 410 416
SQ SEQUENCE 454 AA; 50342 MW; 1EE27B22772D4AFD CRC64;
MATNKERLFA AGALGPGSGY 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
LRLYARRRRP SQPYMFPRML MKITDLRGIS TKGAERAITL KMEIPGPMPP LIREMLENPE
MFEDDSSQPG PHPNASSEDE VPGGQGKGGL KSPA
//