RARG_HUMAN
ID RARG_HUMAN Reviewed; 454 AA.
AC P13631; B7Z492; B7Z4F1; B7ZAE4; J3KNP6; P22932; Q15281; Q52LZ8; Q9BYX8;
AC Q9H1I3; Q9UJ38;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1990, sequence version 1.
DT 03-AUG-2022, entry version 242.
DE RecName: Full=Retinoic acid receptor gamma;
DE Short=RAR-gamma;
DE AltName: Full=Nuclear receptor subfamily 1 group B member 3;
GN Name=RARG; Synonyms=NR1B3;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=2546152; DOI=10.1073/pnas.86.14.5310;
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 [MRNA] (ISOFORM 1).
RX PubMed=2172793; DOI=10.1210/mend-4-6-837;
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 [MRNA] (ISOFORM 1), AND ALTERNATIVE SPLICING.
RC TISSUE=Placenta;
RX PubMed=1849262; DOI=10.1093/nar/19.3.573;
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] (ISOFORMS 2; 3 AND 4).
RC TISSUE=Brain, Tongue, and Umbilical cord blood;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Colon;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-63 (ISOFORM 2).
RX PubMed=2157210; DOI=10.1073/pnas.87.7.2700;
RA Kastner P., Krust A., Mendelsohn C., Garnier J.-M., Zelent A., Leroy P.,
RA Staub A., Chambon P.;
RT "Murine isoforms of retinoic acid receptor gamma with specific patterns of
RT expression.";
RL Proc. Natl. Acad. Sci. U.S.A. 87:2700-2704(1990).
RN [9]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-55, AND ALTERNATIVE SPLICING.
RC TISSUE=Placenta;
RX PubMed=1320193; DOI=10.1128/mcb.12.7.2976-2985.1992;
RA Lehmann J.M., Zhang X.K., Pfahl M.;
RT "RAR-gamma-2 expression is regulated through a retinoic acid response
RT element embedded in Sp1 sites.";
RL Mol. Cell. Biol. 12:2976-2985(1992).
RN [10]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 74-454.
RC TISSUE=Lung carcinoma;
RA Gebhard W.;
RL Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases.
RN [11]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 134-191 AND 394-411.
RA Xu H., Clifford J.L.;
RT "Genomic organization of the human retinoic acid receptor gamma gene.";
RL Submitted (JAN-2001) to the EMBL/GenBank/DDBJ databases.
RN [12]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-172 AND LYS-401, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 178-423.
RX PubMed=7501014; 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 all-
RT trans retinoic acid.";
RL Nature 378:681-689(1995).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 178-423.
RX PubMed=9501913; DOI=10.1038/nsb0398-199;
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 RAR
RT gamma.";
RL Nat. Struct. Biol. 5:199-202(1998).
RN [15]
RP VARIANT [LARGE SCALE ANALYSIS] SER-430.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
RN [16]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=28167758; DOI=10.1073/pnas.1621425114;
RA Lee D.Y., Lin T.E., Lee C.I., Zhou J., Huang Y.H., Lee P.L., Shih Y.T.,
RA Chien S., Chiu J.J.;
RT "MicroRNA-10a is crucial for endothelial response to different flow
RT patterns via interaction of retinoid acid receptors and histone
RT deacetylases.";
RL Proc. Natl. Acad. Sci. U.S.A. 114:2072-2077(2017).
CC -!- FUNCTION: Receptor for retinoic acid. Retinoic acid receptors bind as
CC heterodimers to their target response elements in response to their
CC ligands, all-trans or 9-cis retinoic acid, and regulate gene expression
CC in various biological processes. The RAR/RXR heterodimers bind to the
CC retinoic acid response elements (RARE) composed of tandem 5'-AGGTCA-3'
CC sites known as DR1-DR5. In the absence of ligand, acts mainly as an
CC activator of gene expression due to weak binding to corepressors.
CC Required for limb bud development. In concert with RARA or RARB,
CC required for skeletal growth, matrix homeostasis and growth plate
CC function (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homodimer. Heterodimer with a RXR molecule. Binds DNA
CC preferentially as a RAR/RXR heterodimer. Forms a complex with PUS1 and
CC the SRA1 RNA in the nucleus. {ECO:0000250}.
CC -!- INTERACTION:
CC P13631; Q96RK4: BBS4; NbExp=5; IntAct=EBI-2568901, EBI-1805814;
CC P13631; P13349: MYF5; NbExp=3; IntAct=EBI-2568901, EBI-17491620;
CC P13631; P31321: PRKAR1B; NbExp=5; IntAct=EBI-2568901, EBI-2805516;
CC P13631; P28702: RXRB; NbExp=7; IntAct=EBI-2568901, EBI-748576;
CC P13631; P48443: RXRG; NbExp=5; IntAct=EBI-2568901, EBI-712405;
CC P13631; O60504-2: SORBS3; NbExp=2; IntAct=EBI-2568901, EBI-1222956;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:28167758}. Cytoplasm
CC {ECO:0000269|PubMed:28167758}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Comment=Isoforms differ only in their N-terminal regions.;
CC Name=1;
CC IsoId=P13631-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P13631-2; Sequence=VSP_031080;
CC Name=3;
CC IsoId=P13631-3; Sequence=VSP_044777;
CC Name=4;
CC IsoId=P13631-4; Sequence=VSP_044776;
CC -!- TISSUE SPECIFICITY: Expressed in aortic endothelial cells (at protein
CC level). {ECO:0000269|PubMed:28167758}.
CC -!- DOMAIN: Composed of three domains: a modulating N-terminal domain, a
CC DNA-binding domain and a C-terminal ligand-binding domain.
CC -!- SIMILARITY: Belongs to the nuclear hormone receptor family. NR1
CC subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA40548.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Wikipedia; Note=Retinoic acid receptor entry;
CC URL="https://en.wikipedia.org/wiki/Retinoic_acid_receptor";
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DR EMBL; M24857; AAA52692.1; -; mRNA.
DR EMBL; M57707; AAA63254.1; -; mRNA.
DR EMBL; M38258; AAA60254.1; -; mRNA.
DR EMBL; AK297023; BAH12478.1; -; mRNA.
DR EMBL; AK297277; BAH12537.1; -; mRNA.
DR EMBL; AK316259; BAH14630.1; -; mRNA.
DR EMBL; AC021072; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC073573; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471054; EAW96676.1; -; Genomic_DNA.
DR EMBL; BC093727; AAH93727.1; -; mRNA.
DR EMBL; BC093729; AAH93729.1; -; mRNA.
DR EMBL; M32074; AAA60253.1; -; mRNA.
DR EMBL; X57280; CAA40548.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AJ250835; CAB60726.1; -; Genomic_DNA.
DR EMBL; AY013703; AAG41594.2; -; Genomic_DNA.
DR EMBL; AY013704; AAG41595.1; -; Genomic_DNA.
DR CCDS; CCDS41790.1; -. [P13631-2]
DR CCDS; CCDS58236.1; -. [P13631-3]
DR CCDS; CCDS58237.1; -. [P13631-4]
DR CCDS; CCDS8850.1; -. [P13631-1]
DR PIR; A33903; A33903.
DR PIR; C35991; C35991.
DR RefSeq; NP_000957.1; NM_000966.5. [P13631-1]
DR RefSeq; NP_001036193.1; NM_001042728.2. [P13631-2]
DR RefSeq; NP_001230659.1; NM_001243730.1. [P13631-3]
DR RefSeq; NP_001230661.1; NM_001243732.1. [P13631-4]
DR PDB; 1EXA; X-ray; 1.59 A; A=178-423.
DR PDB; 1EXX; X-ray; 1.67 A; A=178-423.
DR PDB; 1FCX; X-ray; 1.47 A; A=183-417.
DR PDB; 1FCY; X-ray; 1.30 A; A=183-417.
DR PDB; 1FCZ; X-ray; 1.38 A; A=183-417.
DR PDB; 1FD0; X-ray; 1.38 A; A=183-417.
DR PDB; 2LBD; X-ray; 2.06 A; A=178-423.
DR PDB; 3LBD; X-ray; 2.40 A; A=178-423.
DR PDB; 4LBD; X-ray; 2.50 A; A=178-423.
DR PDB; 5M24; X-ray; 1.69 A; A=178-423.
DR PDB; 6FX0; X-ray; 1.90 A; A=1-454.
DR PDBsum; 1EXA; -.
DR PDBsum; 1EXX; -.
DR PDBsum; 1FCX; -.
DR PDBsum; 1FCY; -.
DR PDBsum; 1FCZ; -.
DR PDBsum; 1FD0; -.
DR PDBsum; 2LBD; -.
DR PDBsum; 3LBD; -.
DR PDBsum; 4LBD; -.
DR PDBsum; 5M24; -.
DR PDBsum; 6FX0; -.
DR AlphaFoldDB; P13631; -.
DR SMR; P13631; -.
DR BioGRID; 111851; 41.
DR IntAct; P13631; 25.
DR MINT; P13631; -.
DR STRING; 9606.ENSP00000388510; -.
DR BindingDB; P13631; -.
DR ChEMBL; CHEMBL2003; -.
DR DrugBank; DB07294; 3-fluoro-4-[2-hydroxy-2-(5,5,8,8-tetramethyl-5,6,7,8,-tetrahydro-naphtalen-2-yl)-acetylamino]-benzoic acid.
DR DrugBank; DB07031; 3-Fluoro-4-{[(2R)-2-hydroxy-2-(5,5,8,8-tetramethyl-5,6,7,8-tetrahydro-2-naphthalenyl)acetyl]amino}benzoic acid.
DR DrugBank; DB00459; Acitretin.
DR DrugBank; DB00210; Adapalene.
DR DrugBank; DB00523; Alitretinoin.
DR DrugBank; DB02466; BMS-181156.
DR DrugBank; DB03466; BMS184394.
DR DrugBank; DB02741; CD564.
DR DrugBank; DB03279; Dodecyl-Alpha-D-Maltoside.
DR DrugBank; DB00926; Etretinate.
DR DrugBank; DB00982; Isotretinoin.
DR DrugBank; DB05785; LGD-1550.
DR DrugBank; DB05467; R667.
DR DrugBank; DB02258; SR11254.
DR DrugBank; DB00799; Tazarotene.
DR DrugBank; DB00755; Tretinoin.
DR DrugBank; DB12808; Trifarotene.
DR DrugCentral; P13631; -.
DR GuidetoPHARMACOLOGY; 592; -.
DR iPTMnet; P13631; -.
DR PhosphoSitePlus; P13631; -.
DR BioMuta; RARG; -.
DR DMDM; 133498; -.
DR EPD; P13631; -.
DR jPOST; P13631; -.
DR MassIVE; P13631; -.
DR MaxQB; P13631; -.
DR PaxDb; P13631; -.
DR PeptideAtlas; P13631; -.
DR PRIDE; P13631; -.
DR ProteomicsDB; 52944; -. [P13631-1]
DR ProteomicsDB; 52945; -. [P13631-2]
DR ProteomicsDB; 6597; -.
DR ABCD; P13631; 1 sequenced antibody.
DR Antibodypedia; 15142; 219 antibodies from 37 providers.
DR DNASU; 5916; -.
DR Ensembl; ENST00000338561.9; ENSP00000343698.5; ENSG00000172819.17. [P13631-2]
DR Ensembl; ENST00000394426.5; ENSP00000377947.2; ENSG00000172819.17. [P13631-3]
DR Ensembl; ENST00000425354.7; ENSP00000388510.2; ENSG00000172819.17. [P13631-1]
DR Ensembl; ENST00000543726.1; ENSP00000444335.1; ENSG00000172819.17. [P13631-4]
DR GeneID; 5916; -.
DR KEGG; hsa:5916; -.
DR MANE-Select; ENST00000425354.7; ENSP00000388510.2; NM_000966.6; NP_000957.1.
DR UCSC; uc001scd.4; human. [P13631-1]
DR CTD; 5916; -.
DR DisGeNET; 5916; -.
DR GeneCards; RARG; -.
DR HGNC; HGNC:9866; RARG.
DR HPA; ENSG00000172819; Tissue enhanced (esophagus, skin).
DR MIM; 180190; gene.
DR neXtProt; NX_P13631; -.
DR OpenTargets; ENSG00000172819; -.
DR PharmGKB; PA34227; -.
DR VEuPathDB; HostDB:ENSG00000172819; -.
DR eggNOG; KOG3575; Eukaryota.
DR GeneTree; ENSGT00940000156458; -.
DR HOGENOM; CLU_007368_18_2_1; -.
DR InParanoid; P13631; -.
DR OMA; MQYTCHK; -.
DR OrthoDB; 1165737at2759; -.
DR PhylomeDB; P13631; -.
DR TreeFam; TF328382; -.
DR PathwayCommons; P13631; -.
DR Reactome; R-HSA-383280; Nuclear Receptor transcription pathway.
DR Reactome; R-HSA-5362517; Signaling by Retinoic Acid.
DR Reactome; R-HSA-5617472; Activation of anterior HOX genes in hindbrain development during early embryogenesis.
DR SignaLink; P13631; -.
DR SIGNOR; P13631; -.
DR BioGRID-ORCS; 5916; 17 hits in 1111 CRISPR screens.
DR ChiTaRS; RARG; human.
DR EvolutionaryTrace; P13631; -.
DR GeneWiki; Retinoic_acid_receptor_gamma; -.
DR GenomeRNAi; 5916; -.
DR Pharos; P13631; Tclin.
DR PRO; PR:P13631; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; P13631; protein.
DR Bgee; ENSG00000172819; Expressed in lower esophagus mucosa and 130 other tissues.
DR ExpressionAtlas; P13631; baseline and differential.
DR Genevisible; P13631; HS.
DR GO; GO:0000785; C:chromatin; IDA:ARUK-UCL.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; NAS:BHF-UCL.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005667; C:transcription regulator complex; ISS:BHF-UCL.
DR GO; GO:0003682; F:chromatin binding; IEA:Ensembl.
DR GO; GO:0003677; F:DNA binding; ISS:BHF-UCL.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISS:BHF-UCL.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB.
DR GO; GO:0004879; F:nuclear receptor activity; IBA:GO_Central.
DR GO; GO:0046965; F:nuclear retinoid X receptor binding; ISS:BHF-UCL.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IDA:ARUK-UCL.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0009952; P:anterior/posterior pattern specification; IEA:Ensembl.
DR GO; GO:0006915; P:apoptotic process; IEA:Ensembl.
DR GO; GO:0060070; P:canonical Wnt signaling pathway; TAS:BHF-UCL.
DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR GO; GO:1990830; P:cellular response to leukemia inhibitory factor; IEA:Ensembl.
DR GO; GO:0071300; P:cellular response to retinoic acid; IEA:Ensembl.
DR GO; GO:0031076; P:embryonic camera-type eye development; IEA:Ensembl.
DR GO; GO:0048048; P:embryonic eye morphogenesis; ISS:BHF-UCL.
DR GO; GO:0035116; P:embryonic hindlimb morphogenesis; ISS:BHF-UCL.
DR GO; GO:0060324; P:face development; IEA:Ensembl.
DR GO; GO:0002068; P:glandular epithelial cell development; IEA:Ensembl.
DR GO; GO:0003430; P:growth plate cartilage chondrocyte growth; IEA:Ensembl.
DR GO; GO:0070384; P:Harderian gland development; IEA:Ensembl.
DR GO; GO:0009755; P:hormone-mediated signaling pathway; IBA:GO_Central.
DR GO; GO:0035264; P:multicellular organism growth; IEA:Ensembl.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; ISS:BHF-UCL.
DR GO; GO:0032331; P:negative regulation of chondrocyte differentiation; IEA:Ensembl.
DR GO; GO:2000647; P:negative regulation of stem cell proliferation; IEA:Ensembl.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISS:BHF-UCL.
DR GO; GO:0001843; P:neural tube closure; IEA:Ensembl.
DR GO; GO:0043065; P:positive regulation of apoptotic process; ISS:BHF-UCL.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IEA:Ensembl.
DR GO; GO:0010628; P:positive regulation of gene expression; IEA:Ensembl.
DR GO; GO:0043068; P:positive regulation of programmed cell death; ISS:BHF-UCL.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:BHF-UCL.
DR GO; GO:0060740; P:prostate gland epithelium morphogenesis; IEA:Ensembl.
DR GO; GO:0008361; P:regulation of cell size; TAS:BHF-UCL.
DR GO; GO:0031641; P:regulation of myelination; IEA:Ensembl.
DR GO; GO:0045637; P:regulation of myeloid cell differentiation; IEA:Ensembl.
DR GO; GO:0032526; P:response to retinoic acid; IDA:BHF-UCL.
DR GO; GO:0048384; P:retinoic acid receptor signaling pathway; IDA:BHF-UCL.
DR GO; GO:0072089; P:stem cell proliferation; IEA:Ensembl.
DR GO; GO:0060534; P:trachea cartilage development; IEA:Ensembl.
DR Gene3D; 1.10.565.10; -; 1.
DR Gene3D; 3.30.50.10; -; 1.
DR InterPro; IPR035500; NHR-like_dom_sf.
DR InterPro; IPR000536; Nucl_hrmn_rcpt_lig-bd.
DR InterPro; IPR001723; Nuclear_hrmn_rcpt.
DR InterPro; IPR003078; Retinoic_acid_rcpt.
DR InterPro; IPR001628; Znf_hrmn_rcpt.
DR InterPro; IPR013088; Znf_NHR/GATA.
DR Pfam; PF00104; Hormone_recep; 1.
DR Pfam; PF00105; zf-C4; 1.
DR PRINTS; PR01292; RETNOICACIDR.
DR PRINTS; PR00398; STRDHORMONER.
DR PRINTS; PR00047; STROIDFINGER.
DR SMART; SM00430; HOLI; 1.
DR SMART; SM00399; ZnF_C4; 1.
DR SUPFAM; SSF48508; SSF48508; 1.
DR PROSITE; PS51843; NR_LBD; 1.
DR PROSITE; PS00031; NUCLEAR_REC_DBD_1; 1.
DR PROSITE; PS51030; NUCLEAR_REC_DBD_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cytoplasm; DNA-binding;
KW Isopeptide bond; Metal-binding; Methylation; Nucleus; Receptor;
KW Reference proteome; Transcription; Transcription regulation;
KW Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..454
FT /note="Retinoic acid receptor gamma"
FT /id="PRO_0000053472"
FT DOMAIN 185..419
FT /note="NR LBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01189"
FT DNA_BIND 90..155
FT /note="Nuclear receptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT ZN_FING 90..110
FT /note="NR C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT ZN_FING 126..150
FT /note="NR C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT REGION 1..89
FT /note="Modulating"
FT REGION 58..83
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 156..184
FT /note="Hinge"
FT REGION 161..180
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 408..454
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 60..74
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 161..177
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 34
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:P18911"
FT CROSSLNK 172
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 401
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1..111
FT /note="MATNKERLFAAGALGPGSGYPGAGFPFAFPGALRGSPPFEMLSPSFRGLGQP
FT DLPKEMASLSVETQSTSSEEMVPSSPSPPPPPRVYKPCFVCNDKSSGYHYGVSSCEGCK
FT -> MLALPLPPCWSGAPPGEEGESAAGPWCFQHPVSLQAGSRCTTVWKRLPRVRDGCTG
FT RPGPGPACCAEPPAAPVSPDLNLLPGRNPPACN (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_044776"
FT VAR_SEQ 1..72
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_044777"
FT VAR_SEQ 1..61
FT /note="MATNKERLFAAGALGPGSGYPGAGFPFAFPGALRGSPPFEMLSPSFRGLGQP
FT DLPKEMASL -> MYDCMETFAPGPRRLYGAAGPGAGLLRRATGGSCFAGLESFAWPQP
FT ASLQ (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:2157210"
FT /id="VSP_031080"
FT VARIANT 427
FT /note="S -> L (in dbSNP:rs2229774)"
FT /id="VAR_038554"
FT VARIANT 430
FT /note="G -> S (in a breast cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036061"
FT CONFLICT 118
FT /note="I -> T (in Ref. 10; CAB60726)"
FT /evidence="ECO:0000305"
FT CONFLICT 172
FT /note="K -> R (in Ref. 11; AAG41594)"
FT /evidence="ECO:0000305"
FT CONFLICT 252
FT /note="T -> A (in Ref. 10; CAB60726)"
FT /evidence="ECO:0000305"
FT CONFLICT 342
FT /note="M -> V (in Ref. 4; BAH12478)"
FT /evidence="ECO:0000305"
FT CONFLICT 421
FT /note="M -> L (in Ref. 10; CAB60726)"
FT /evidence="ECO:0000305"
FT HELIX 184..200
FT /evidence="ECO:0007829|PDB:1FCY"
FT HELIX 204..206
FT /evidence="ECO:0007829|PDB:1FCY"
FT HELIX 224..246
FT /evidence="ECO:0007829|PDB:1FCY"
FT HELIX 251..253
FT /evidence="ECO:0007829|PDB:1FCY"
FT HELIX 256..277
FT /evidence="ECO:0007829|PDB:1FCY"
FT TURN 281..284
FT /evidence="ECO:0007829|PDB:1FCY"
FT STRAND 285..287
FT /evidence="ECO:0007829|PDB:1FCY"
FT STRAND 292..295
FT /evidence="ECO:0007829|PDB:1FCY"
FT HELIX 296..302
FT /evidence="ECO:0007829|PDB:1FCY"
FT HELIX 305..307
FT /evidence="ECO:0007829|PDB:1FCY"
FT HELIX 308..318
FT /evidence="ECO:0007829|PDB:1FCY"
FT HELIX 319..321
FT /evidence="ECO:0007829|PDB:1FCY"
FT HELIX 325..336
FT /evidence="ECO:0007829|PDB:1FCY"
FT HELIX 347..368
FT /evidence="ECO:0007829|PDB:1FCY"
FT HELIX 375..401
FT /evidence="ECO:0007829|PDB:1FCY"
FT STRAND 404..406
FT /evidence="ECO:0007829|PDB:1FCY"
FT HELIX 410..416
FT /evidence="ECO:0007829|PDB:1FCY"
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
