NR1I3_HUMAN
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 03-AUG-2022, entry version 209.
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}.
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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; 39.
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; DB00836; Loperamide.
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 PaxDb; Q14994; -.
DR PeptideAtlas; Q14994; -.
DR PRIDE; 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; 473 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 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; 297114at2759; -.
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 1094 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 99 other tissues.
DR ExpressionAtlas; Q14994; baseline and differential.
DR Genevisible; Q14994; HS.
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 Gene3D; 1.10.565.10; -; 1.
DR Gene3D; 3.30.50.10; -; 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 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; 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; 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 unknown pathological 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
