ID NR1I3_HUMAN Reviewed; 352 AA. AC Q14994; E9PB75; E9PC13; E9PDU3; E9PGH6; E9PH10; E9PHC8; E9PHN4; F1D8Q0; AC F1D8Q1; Q0VAC9; Q4U0F0; Q5VTW5; Q5VTW6; Q6GZ68; Q6GZ76; Q6GZ77; Q6GZ78; AC Q6GZ79; Q6GZ82; Q6GZ83; Q6GZ84; Q6GZ85; Q6GZ87; Q6GZ89; DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot. DT 21-JUN-2004, sequence version 2. DT 27-MAR-2024, entry version 218. DE RecName: Full=Nuclear receptor subfamily 1 group I member 3; DE AltName: Full=Constitutive activator of retinoid response; DE Short=Constitutive active response; DE AltName: Full=Constitutive androstane receptor; DE Short=CAR; DE AltName: Full=Orphan nuclear receptor MB67; GN Name=NR1I3; Synonyms=CAR; 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 2). RC TISSUE=Liver; RX PubMed=8114692; DOI=10.1128/mcb.14.3.1544-1552.1994; RA Baes M., Gulick T., Choi H.S., Martinoli M.G., Simha D., Moore D.D.; RT "A new orphan member of the nuclear hormone receptor superfamily that RT interacts with a subset of retinoic acid response elements."; RL Mol. Cell. Biol. 14:1544-1552(1994). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 4; 5; 6 AND 7), NUCLEOTIDE SEQUENCE RP [MRNA] OF 1-288 (ISOFORM 9), NUCLEOTIDE SEQUENCE [MRNA] OF 1-293 (ISOFORM RP 10), NUCLEOTIDE SEQUENCE [MRNA] OF 1-297 (ISOFORM 11), NUCLEOTIDE SEQUENCE RP [MRNA] OF 1-321 (ISOFORM 12), NUCLEOTIDE SEQUENCE [MRNA] OF 1-322 (ISOFORM RP 13), NUCLEOTIDE SEQUENCE [MRNA] OF 1-279 (ISOFORM 14), NUCLEOTIDE SEQUENCE RP [MRNA] OF 1-266 (ISOFORM 15), AND ALTERNATIVE SPLICING. RX PubMed=15194709; DOI=10.1124/jpet.104.069310; RA Lamba J.K., Lamba V., Yasuda K., Lin Y.S., Assem M., Thompson E., Strom S., RA Schuetz E.G.; RT "Expression of constitutive androstane receptor splice variants in human RT tissues and their functional consequences."; RL J. Pharmacol. Exp. Ther. 311:811-821(2004). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 8). RA Zhou G., Nong W., Li H., Ke R., Shen C., Zhong G., Zheng Z., Liang M., RA Huang B., Lin L., Yang S.; RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2; 3 AND 7). RC TISSUE=Eye, and Small intestine; RA Kaighin V.A., Martin A.L., Aronstam R.S.; RT "Isolation of cDNA coding for multiple human nuclear receptor clones."; RL Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16710414; DOI=10.1038/nature04727; RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K., RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.; RT "The DNA sequence and biological annotation of human chromosome 1."; RL Nature 441:315-321(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 (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 3 AND 7). 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 INTERACTION WITH PSMC4. RX PubMed=8603043; DOI=10.1016/0960-0760(95)00220-0; RA Choi H.S., Seol W., Moore D.D.; RT "A component of the 26S proteasome binds on orphan member of the nuclear RT hormone receptor superfamily."; RL J. Steroid Biochem. Mol. Biol. 56:23-30(1996). RN [9] RP INTERACTION WITH DNAJC7, AND SUBCELLULAR LOCATION. RX PubMed=14573755; DOI=10.1124/mol.64.5.1069; RA Kobayashi K., Sueyoshi T., Inoue K., Moore R., Negishi M.; RT "Cytoplasmic accumulation of the nuclear receptor CAR by a RT tetratricopeptide repeat protein in HepG2 cells."; RL Mol. Pharmacol. 64:1069-1075(2003). RN [10] RP PHOSPHORYLATION AT THR-38, AND SUBCELLULAR LOCATION. RX PubMed=19858220; DOI=10.1074/jbc.m109.048108; RA Mutoh S., Osabe M., Inoue K., Moore R., Pedersen L., Perera L., RA Rebolloso Y., Sueyoshi T., Negishi M.; RT "Dephosphorylation of threonine 38 is required for nuclear translocation RT and activation of human xenobiotic receptor CAR (NR1I3)."; RL J. Biol. Chem. 284:34785-34792(2009). RN [11] RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 103-352. RX PubMed=15610735; DOI=10.1016/j.molcel.2004.11.042; RA Xu R.X., Lambert M.H., Wisely B.B., Warren E.N., Weinert E.E., Waitt G.M., RA Williams J.D., Collins J.L., Moore L.B., Willson T.M., Moore J.T.; RT "A structural basis for constitutive activity in the human CAR/RXRalpha RT heterodimer."; RL Mol. Cell 16:919-928(2004). RN [12] RP VARIANT GLY-133. RX PubMed=15618763; DOI=10.2133/dmpk.18.413; RA Ikeda S., Kurose K., Ozawa S., Sai K., Hasegawa R., Komamura K., Ueno K., RA Kamakura S., Kitakaze M., Tomoike H., Nakajima T., Matsumoto K., Saito H., RA Goto Y., Kimura H., Katoh M., Sugai K., Minami N., Shirao K., Tamura T., RA Yamamoto N., Minami H., Ohtsu A., Yoshida T., Saijo N., Saito Y., RA Sawada J.; RT "Twenty-six novel single nucleotide polymorphisms and their frequencies of RT the NR1I3 (CAR) gene in a Japanese population."; RL Drug Metab. Pharmacokinet. 18:413-418(2003). RN [13] RP VARIANT SER-247. RX PubMed=22726846; DOI=10.1016/j.ajhg.2012.05.003; RA Kleefstra T., Kramer J.M., Neveling K., Willemsen M.H., Koemans T.S., RA Vissers L.E., Wissink-Lindhout W., Fenckova M., van den Akker W.M., RA Kasri N.N., Nillesen W.M., Prescott T., Clark R.D., Devriendt K., RA van Reeuwijk J., de Brouwer A.P., Gilissen C., Zhou H., Brunner H.G., RA Veltman J.A., Schenck A., van Bokhoven H.; RT "Disruption of an EHMT1-associated chromatin-modification module causes RT intellectual disability."; RL Am. J. Hum. Genet. 91:73-82(2012). CC -!- FUNCTION: Binds and transactivates the retinoic acid response elements CC that control expression of the retinoic acid receptor beta 2 and CC alcohol dehydrogenase 3 genes. Transactivates both the phenobarbital CC responsive element module of the human CYP2B6 gene and the CYP3A4 CC xenobiotic response element. CC -!- SUBUNIT: Interacts with ECT2 (By similarity). Heterodimer of NR1I3 and CC RXR. Interacts with PSMC4. Directly interacts with DNAJC7. The DNAJC7- CC NR1I3 complex may also include HSP90 (By similarity). Interacts with CC CRY1 (By similarity). Interacts with CRY2 in a ligand-dependent manner CC (By similarity). {ECO:0000250|UniProtKB:O35627}. CC -!- INTERACTION: CC Q14994; P01100: FOS; NbExp=3; IntAct=EBI-960794, EBI-852851; CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Cytoplasm, cytoskeleton. CC Note=Recruited to the cytoplasm by DNAJC7. {ECO:0000250}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=15; CC Name=1; CC IsoId=Q14994-1; Sequence=Displayed; CC Name=2; CC IsoId=Q14994-2; Sequence=VSP_010634; CC Name=3; CC IsoId=Q14994-3; Sequence=VSP_043144; CC Name=4; CC IsoId=Q14994-4; Sequence=VSP_043730, VSP_043731; CC Name=5; CC IsoId=Q14994-5; Sequence=VSP_043730, VSP_010634; CC Name=6; CC IsoId=Q14994-6; Sequence=VSP_043730, VSP_010634, VSP_043732; CC Name=7; CC IsoId=Q14994-7; Sequence=VSP_043731; CC Name=8; CC IsoId=Q14994-8; Sequence=VSP_043732; CC Name=9; CC IsoId=Q14994-9; Sequence=VSP_043730, VSP_010634, VSP_046144; CC Name=10; CC IsoId=Q14994-10; Sequence=VSP_043730, VSP_010634, VSP_043732, CC VSP_046144; CC Name=11; CC IsoId=Q14994-11; Sequence=VSP_043730, VSP_043732, VSP_046144; CC Name=12; CC IsoId=Q14994-12; Sequence=VSP_046144; CC Name=13; CC IsoId=Q14994-13; Sequence=VSP_055180, VSP_043732, VSP_046144; CC Name=14; CC IsoId=Q14994-15; Sequence=VSP_043731, VSP_046144; CC Name=15; CC IsoId=Q14994-16; Sequence=VSP_043730, VSP_043731, VSP_046144; CC -!- TISSUE SPECIFICITY: Predominantly expressed in liver. CC -!- INDUCTION: By dexamethasone. CC -!- DOMAIN: Composed by a short N-terminal domain followed by the DNA CC binding, hinge, and ligand binding/dimerization domains. CC -!- PTM: Phosphorylated at Thr-38 by PKC, dephosphorylation of Thr-38 is CC required for nuclear translocation and activation. CC {ECO:0000269|PubMed:19858220}. CC -!- SIMILARITY: Belongs to the nuclear hormone receptor family. NR1 CC subfamily. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; Z30425; CAA83016.1; -; mRNA. DR EMBL; AY572806; AAT47159.1; -; mRNA. DR EMBL; AY572808; AAT47161.1; -; mRNA. DR EMBL; AY572810; AAT47163.1; -; mRNA. DR EMBL; AY572811; AAT47164.1; -; mRNA. DR EMBL; AY572812; AAT47165.1; -; mRNA. DR EMBL; AY572813; AAT47166.1; -; mRNA. DR EMBL; AY572816; AAT47169.1; -; mRNA. DR EMBL; AY572817; AAT47170.1; -; mRNA. DR EMBL; AY572818; AAT47171.1; -; mRNA. DR EMBL; AY572819; AAT47172.1; -; mRNA. DR EMBL; AY572827; AAT47180.1; -; mRNA. DR EMBL; DQ022681; AAY56401.1; -; mRNA. DR EMBL; HQ692838; ADZ17349.1; -; mRNA. DR EMBL; HQ692839; ADZ17350.1; -; mRNA. DR EMBL; HQ692840; ADZ17351.1; -; mRNA. DR EMBL; HQ692841; ADZ17352.1; -; mRNA. DR EMBL; AL590714; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471121; EAW52608.1; -; Genomic_DNA. DR EMBL; CH471121; EAW52609.1; -; Genomic_DNA. DR EMBL; BC069626; AAH69626.1; -; mRNA. DR EMBL; BC121120; AAI21121.1; -; mRNA. DR EMBL; BC121121; AAI21122.1; -; mRNA. DR CCDS; CCDS1228.1; -. [Q14994-2] DR CCDS; CCDS41427.1; -. [Q14994-6] DR CCDS; CCDS41428.1; -. [Q14994-3] DR CCDS; CCDS41429.1; -. [Q14994-8] DR CCDS; CCDS41430.1; -. [Q14994-1] DR CCDS; CCDS44260.1; -. [Q14994-12] DR CCDS; CCDS44261.1; -. [Q14994-13] DR CCDS; CCDS44262.1; -. [Q14994-7] DR CCDS; CCDS53405.1; -. [Q14994-15] DR CCDS; CCDS53406.1; -. [Q14994-16] DR CCDS; CCDS53407.1; -. [Q14994-4] DR CCDS; CCDS53408.1; -. [Q14994-9] DR CCDS; CCDS53409.1; -. [Q14994-5] DR CCDS; CCDS53410.1; -. [Q14994-10] DR CCDS; CCDS53411.1; -. [Q14994-11] DR PIR; A56197; A56197. DR RefSeq; NP_001070937.1; NM_001077469.2. [Q14994-13] DR RefSeq; NP_001070938.1; NM_001077470.2. [Q14994-4] DR RefSeq; NP_001070939.1; NM_001077471.2. [Q14994-7] DR RefSeq; NP_001070940.1; NM_001077472.2. [Q14994-6] DR RefSeq; NP_001070941.1; NM_001077473.2. [Q14994-11] DR RefSeq; NP_001070942.1; NM_001077474.2. [Q14994-15] DR RefSeq; NP_001070943.1; NM_001077475.2. [Q14994-16] DR RefSeq; NP_001070944.1; NM_001077476.2. [Q14994-10] DR RefSeq; NP_001070945.1; NM_001077477.2. [Q14994-9] DR RefSeq; NP_001070946.1; NM_001077478.2. [Q14994-12] DR RefSeq; NP_001070947.1; NM_001077479.2. [Q14994-5] DR RefSeq; NP_001070948.1; NM_001077480.2. [Q14994-1] DR RefSeq; NP_001070949.1; NM_001077481.2. [Q14994-3] DR RefSeq; NP_001070950.1; NM_001077482.2. [Q14994-8] DR RefSeq; NP_005113.1; NM_005122.4. [Q14994-2] DR PDB; 1XV9; X-ray; 2.70 A; B/D=103-352. DR PDB; 1XVP; X-ray; 2.60 A; B/D=103-352. DR PDBsum; 1XV9; -. DR PDBsum; 1XVP; -. DR AlphaFoldDB; Q14994; -. DR SASBDB; Q14994; -. DR SMR; Q14994; -. DR BioGRID; 115295; 40. DR IntAct; Q14994; 20. DR STRING; 9606.ENSP00000356959; -. DR BindingDB; Q14994; -. DR ChEMBL; CHEMBL5503; -. DR DrugBank; DB01889; 16,17-Androstene-3-Ol. DR DrugBank; DB07557; 3,20-Pregnanedione. DR DrugBank; DB01076; Atorvastatin. DR DrugBank; DB04540; Cholesterol. DR DrugBank; DB00366; Doxylamine. DR DrugBank; DB07931; Hexestrol. DR DrugBank; DB01026; Ketoconazole. DR DrugBank; DB00737; Meclizine. DR DrugBank; DB01620; Pheniramine. DR DrugBank; DB04824; Phenolphthalein. DR DrugBank; DB01708; Prasterone. DR DrugBank; DB02709; Resveratrol. DR DrugBank; DB08604; Triclosan. DR DrugCentral; Q14994; -. DR GuidetoPHARMACOLOGY; 607; -. DR SwissLipids; SLP:000001585; -. DR iPTMnet; Q14994; -. DR PhosphoSitePlus; Q14994; -. DR BioMuta; NR1I3; -. DR DMDM; 49066046; -. DR jPOST; Q14994; -. DR MassIVE; Q14994; -. DR PaxDb; 9606-ENSP00000356959; -. DR PeptideAtlas; Q14994; -. DR ProteomicsDB; 19747; -. DR ProteomicsDB; 20507; -. DR ProteomicsDB; 60278; -. [Q14994-1] DR ProteomicsDB; 60279; -. [Q14994-2] DR ProteomicsDB; 60280; -. [Q14994-3] DR ProteomicsDB; 60281; -. [Q14994-4] DR ProteomicsDB; 60282; -. [Q14994-5] DR ProteomicsDB; 60283; -. [Q14994-6] DR ProteomicsDB; 60284; -. [Q14994-7] DR ProteomicsDB; 62261; -. DR Antibodypedia; 20508; 531 antibodies from 32 providers. DR DNASU; 9970; -. DR Ensembl; ENST00000367979.6; ENSP00000356958.2; ENSG00000143257.12. [Q14994-8] DR Ensembl; ENST00000367980.6; ENSP00000356959.2; ENSG00000143257.12. [Q14994-8] DR Ensembl; ENST00000367981.7; ENSP00000356960.3; ENSG00000143257.12. [Q14994-6] DR Ensembl; ENST00000367982.8; ENSP00000356961.4; ENSG00000143257.12. [Q14994-1] DR Ensembl; ENST00000367983.9; ENSP00000356962.5; ENSG00000143257.12. [Q14994-2] DR Ensembl; ENST00000367984.8; ENSP00000356963.4; ENSG00000143257.12. [Q14994-7] DR Ensembl; ENST00000367985.7; ENSP00000356965.3; ENSG00000143257.12. [Q14994-3] DR Ensembl; ENST00000412844.6; ENSP00000399361.2; ENSG00000143257.12. [Q14994-11] DR Ensembl; ENST00000428574.6; ENSP00000412672.2; ENSG00000143257.12. [Q14994-13] DR Ensembl; ENST00000437437.6; ENSP00000407446.2; ENSG00000143257.12. [Q14994-9] DR Ensembl; ENST00000442691.6; ENSP00000406493.2; ENSG00000143257.12. [Q14994-12] DR Ensembl; ENST00000504010.5; ENSP00000424345.1; ENSG00000143257.12. [Q14994-4] DR Ensembl; ENST00000505005.5; ENSP00000424934.1; ENSG00000143257.12. [Q14994-15] DR Ensembl; ENST00000508740.5; ENSP00000423666.1; ENSG00000143257.12. [Q14994-10] DR Ensembl; ENST00000511676.5; ENSP00000427175.1; ENSG00000143257.12. [Q14994-5] DR Ensembl; ENST00000512372.5; ENSP00000425417.1; ENSG00000143257.12. [Q14994-16] DR GeneID; 9970; -. DR KEGG; hsa:9970; -. DR MANE-Select; ENST00000367983.9; ENSP00000356962.5; NM_005122.5; NP_005113.1. [Q14994-2] DR UCSC; uc001fzf.4; human. [Q14994-1] DR AGR; HGNC:7969; -. DR CTD; 9970; -. DR DisGeNET; 9970; -. DR GeneCards; NR1I3; -. DR HGNC; HGNC:7969; NR1I3. DR HPA; ENSG00000143257; Tissue enriched (liver). DR MIM; 603881; gene. DR neXtProt; NX_Q14994; -. DR OpenTargets; ENSG00000143257; -. DR PharmGKB; PA391; -. DR VEuPathDB; HostDB:ENSG00000143257; -. DR eggNOG; KOG3575; Eukaryota. DR GeneTree; ENSGT00940000160641; -. DR HOGENOM; CLU_007368_12_0_1; -. DR InParanoid; Q14994; -. DR OMA; VHAGFQE; -. DR OrthoDB; 5359733at2759; -. DR PhylomeDB; Q14994; -. DR TreeFam; TF316304; -. DR PathwayCommons; Q14994; -. DR Reactome; R-HSA-383280; Nuclear Receptor transcription pathway. DR SignaLink; Q14994; -. DR SIGNOR; Q14994; -. DR BioGRID-ORCS; 9970; 15 hits in 1174 CRISPR screens. DR ChiTaRS; NR1I3; human. DR EvolutionaryTrace; Q14994; -. DR GeneWiki; Constitutive_androstane_receptor; -. DR GenomeRNAi; 9970; -. DR Pharos; Q14994; Tchem. DR PRO; PR:Q14994; -. DR Proteomes; UP000005640; Chromosome 1. DR RNAct; Q14994; Protein. DR Bgee; ENSG00000143257; Expressed in right lobe of liver and 100 other cell types or tissues. DR ExpressionAtlas; Q14994; baseline and differential. DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB. DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB. DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell. DR GO; GO:0005829; C:cytosol; IEA:Ensembl. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; ISS:UniProtKB. DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:NTNU_SB. DR GO; GO:0003700; F:DNA-binding transcription factor activity; TAS:ProtInc. 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; IDA:GO_Central. DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central. DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IDA:NTNU_SB. 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:0030154; P:cell differentiation; IBA:GO_Central. DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IBA:GO_Central. DR GO; GO:0001649; P:osteoblast differentiation; IEA:Ensembl. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:NTNU_SB. DR GO; GO:0007165; P:signal transduction; TAS:ProtInc. DR CDD; cd07156; NR_DBD_VDR_like; 1. DR CDD; cd06934; NR_LBD_PXR_like; 1. DR Gene3D; 3.30.50.10; Erythroid Transcription Factor GATA-1, subunit A; 1. DR Gene3D; 1.10.565.10; Retinoid X Receptor; 1. DR IDEAL; IID00475; -. DR InterPro; IPR035500; NHR-like_dom_sf. DR InterPro; IPR000536; Nucl_hrmn_rcpt_lig-bd. DR InterPro; IPR001723; Nuclear_hrmn_rcpt. DR InterPro; IPR001728; ThyrH_rcpt. DR InterPro; IPR001628; Znf_hrmn_rcpt. DR InterPro; IPR013088; Znf_NHR/GATA. DR PANTHER; PTHR24082; NUCLEAR HORMONE RECEPTOR; 1. DR PANTHER; PTHR24082:SF231; NUCLEAR RECEPTOR SUBFAMILY 1 GROUP I MEMBER 3; 1. DR Pfam; PF00104; Hormone_recep; 1. DR Pfam; PF00105; zf-C4; 1. DR PRINTS; PR00398; STRDHORMONER. DR PRINTS; PR00047; STROIDFINGER. DR PRINTS; PR00546; THYROIDHORMR. DR SMART; SM00430; HOLI; 1. DR SMART; SM00399; ZnF_C4; 1. DR SUPFAM; SSF57716; Glucocorticoid receptor-like (DNA-binding domain); 1. DR SUPFAM; SSF48508; Nuclear receptor ligand-binding domain; 1. DR PROSITE; PS51843; NR_LBD; 1. DR PROSITE; PS00031; NUCLEAR_REC_DBD_1; 1. DR PROSITE; PS51030; NUCLEAR_REC_DBD_2; 1. DR Genevisible; Q14994; HS. PE 1: Evidence at protein level; KW 3D-structure; Activator; Alternative splicing; Cytoplasm; Cytoskeleton; KW DNA-binding; Metal-binding; Nucleus; Phosphoprotein; Receptor; KW Reference proteome; Transcription; Transcription regulation; Zinc; KW Zinc-finger. FT CHAIN 1..352 FT /note="Nuclear receptor subfamily 1 group I member 3" FT /id="PRO_0000053552" FT DOMAIN 109..352 FT /note="NR LBD" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01189" FT DNA_BIND 8..83 FT /note="Nuclear receptor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407" FT ZN_FING 11..31 FT /note="NR C4-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407" FT ZN_FING 47..71 FT /note="NR C4-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407" FT MOD_RES 38 FT /note="Phosphothreonine; by PKC" FT /evidence="ECO:0000269|PubMed:19858220" FT VAR_SEQ 1..35 FT /note="MASREDELRNCVVCGDQATGYHFNALTCEGCKGFF -> MLPKRS (in FT isoform 4, isoform 5, isoform 6, isoform 9, isoform 10, FT isoform 11 and isoform 15)" FT /evidence="ECO:0000303|PubMed:15194709" FT /id="VSP_043730" FT VAR_SEQ 232..274 FT /note="VSPTVGFQVEFLELLFHFHGTLRKLQLQEPEYVLLAAMALFSP -> APYLT FT (in isoform 3)" FT /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.4" FT /id="VSP_043144" FT VAR_SEQ 232..274 FT /note="Missing (in isoform 4, isoform 7, isoform 14 and FT isoform 15)" FT /evidence="ECO:0000303|PubMed:15194709, FT ECO:0000303|PubMed:15489334, ECO:0000303|Ref.4" FT /id="VSP_043731" FT VAR_SEQ 232..235 FT /note="Missing (in isoform 13)" FT /evidence="ECO:0000303|PubMed:15194709" FT /id="VSP_055180" FT VAR_SEQ 233..236 FT /note="Missing (in isoform 2, isoform 5, isoform 6, isoform FT 9 and isoform 10)" FT /evidence="ECO:0000303|PubMed:15194709, FT ECO:0000303|PubMed:8114692, ECO:0000303|Ref.4" FT /id="VSP_010634" FT VAR_SEQ 274 FT /note="P -> PAPYLT (in isoform 6, isoform 8, isoform 10, FT isoform 11 and isoform 13)" FT /evidence="ECO:0000303|PubMed:15194709, ECO:0000303|Ref.3" FT /id="VSP_043732" FT VAR_SEQ 311..352 FT /note="FLYAKLLGLLAELRSINEAYGYQIQHIQGLSAMMPLLQEICS -> SPGTPW FT IHWSGKMLGPKIGPGSKGAQWLQ (in isoform 9, isoform 10, isoform FT 11, isoform 12, isoform 13, isoform 14 and isoform 15)" FT /evidence="ECO:0000303|PubMed:15194709" FT /id="VSP_046144" FT VARIANT 133 FT /note="V -> G" FT /evidence="ECO:0000269|PubMed:15618763" FT /id="VAR_018344" FT VARIANT 247 FT /note="F -> S (found in a patient with Kleefstra syndrome; FT uncertain significance; dbSNP:rs398122411)" FT /evidence="ECO:0000269|PubMed:22726846" FT /id="VAR_080264" FT HELIX 108..122 FT /evidence="ECO:0007829|PDB:1XVP" FT STRAND 125..127 FT /evidence="ECO:0007829|PDB:1XVP" FT HELIX 128..135 FT /evidence="ECO:0007829|PDB:1XVP" FT HELIX 139..141 FT /evidence="ECO:0007829|PDB:1XVP" FT HELIX 155..176 FT /evidence="ECO:0007829|PDB:1XVP" FT HELIX 180..184 FT /evidence="ECO:0007829|PDB:1XVP" FT HELIX 187..206 FT /evidence="ECO:0007829|PDB:1XVP" FT HELIX 207..209 FT /evidence="ECO:0007829|PDB:1XVP" FT TURN 212..215 FT /evidence="ECO:0007829|PDB:1XVP" FT STRAND 216..218 FT /evidence="ECO:0007829|PDB:1XVP" FT STRAND 222..224 FT /evidence="ECO:0007829|PDB:1XV9" FT HELIX 226..232 FT /evidence="ECO:0007829|PDB:1XVP" FT HELIX 240..255 FT /evidence="ECO:0007829|PDB:1XVP" FT HELIX 260..271 FT /evidence="ECO:0007829|PDB:1XVP" FT STRAND 274..276 FT /evidence="ECO:0007829|PDB:1XVP" FT HELIX 282..301 FT /evidence="ECO:0007829|PDB:1XVP" FT HELIX 312..336 FT /evidence="ECO:0007829|PDB:1XVP" FT HELIX 340..343 FT /evidence="ECO:0007829|PDB:1XVP" FT HELIX 345..350 FT /evidence="ECO:0007829|PDB:1XVP" SQ SEQUENCE 352 AA; 39942 MW; 73B060FE4950D519 CRC64; MASREDELRN CVVCGDQATG YHFNALTCEG CKGFFRRTVS KSIGPTCPFA GSCEVSKTQR RHCPACRLQK CLDAGMRKDM ILSAEALALR RAKQAQRRAQ QTPVQLSKEQ EELIRTLLGA HTRHMGTMFE QFVQFRPPAH LFIHHQPLPT LAPVLPLVTH FADINTFMVL QVIKFTKDLP VFRSLPIEDQ ISLLKGAAVE ICHIVLNTTF CLQTQNFLCG PLRYTIEDGA RVSPTVGFQV EFLELLFHFH GTLRKLQLQE PEYVLLAAMA LFSPDRPGVT QRDEIDQLQE EMALTLQSYI KGQQRRPRDR FLYAKLLGLL AELRSINEAY GYQIQHIQGL SAMMPLLQEI CS //