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Nuclear receptor subfamily 1 group I member 2 (Orphan nuclear receptor PAR1) (Orphan nuclear receptor PXR) (Pregnane X receptor) (Steroid and xenobiotic receptor) (SXR)

 NR1I2_HUMAN             Reviewed;         434 AA.
O75469; Q006P5; Q008C8; Q96AC7; Q9UJ22; Q9UJ23; Q9UJ24; Q9UJ25;
Q9UJ26; Q9UJ27; Q9UNW4;
15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
01-NOV-1998, sequence version 1.
22-NOV-2017, entry version 194.
RecName: Full=Nuclear receptor subfamily 1 group I member 2;
AltName: Full=Orphan nuclear receptor PAR1;
AltName: Full=Orphan nuclear receptor PXR;
AltName: Full=Pregnane X receptor;
AltName: Full=Steroid and xenobiotic receptor;
Short=SXR;
Name=NR1I2; Synonyms=PXR;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1A).
PubMed=9784494; DOI=10.1101/gad.12.20.3195;
Blumberg B., Sabbagh W. Jr., Juguilon H., Bolado J. Jr.,
van Meter C.M., Ong E.S., Evans R.M.;
"SXR, a novel steroid and xenobiotic-sensing nuclear receptor.";
Genes Dev. 12:3195-3205(1998).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1A), AND FUNCTION.
TISSUE=Liver;
PubMed=9727070; DOI=10.1172/JCI3703;
Lehmann J.M., McKee D.D., Watson M.A., Willson T.M., Moore J.T.,
Kliewer S.A.;
"The human orphan nuclear receptor PXR is activated by compounds that
regulate CYP3A4 gene expression and cause drug interactions.";
J. Clin. Invest. 102:1016-1023(1998).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1A AND 3).
TISSUE=Liver;
PubMed=9770465; DOI=10.1073/pnas.95.21.12208;
Bertilsson G., Heidrich J., Svensson K., Asman M., Jendeberg L.,
Sydow-Baeckman M., Ohlsson R., Postlind H., Blomquist P.,
Berkenstam A.;
"Identification of a human nuclear receptor defines a new signaling
pathway for CYP3A induction.";
Proc. Natl. Acad. Sci. U.S.A. 95:12208-12213(1998).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1A AND 3), FUNCTION, AND
VARIANTS SER-27; ARG-36 AND GLN-122.
PubMed=11668216; DOI=10.1097/00008571-200110000-00003;
Zhang J., Kuehl P., Green E.D., Touchman J.W., Watkins P.B., Daly A.,
Hall S.D., Maurel P., Relling M., Brimer C., Yasuda K., Wrighton S.A.,
Hancock M., Kim R.B., Strom S., Thummel K., Russell C.G.,
Hudson J.R. Jr., Schuetz E.G., Boguski M.S.;
"The human pregnane X receptor: genomic structure and identification
and functional characterization of natural allelic variants.";
Pharmacogenetics 11:555-572(2001).
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1A; 1B; 1C; 2A; 2B AND 2C), AND
VARIANT THR-12.
TISSUE=Liver;
Heard D.J., Holloway J., Hansen C., Tommerup N., Aagaard L.,
Vissing H.;
"Identification of a novel protein isoform of the human nuclear
hormone receptor PXR/SXR and localization to chromosome 3q12.1
-13.3.";
Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Wang X., Li J., Deng X., Chen J., Huang M.;
Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS LYS-18; SER-27 AND
THR-370.
SeattleSNPs variation discovery resource;
Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1A).
TISSUE=Hepatoma;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[9]
FUNCTION.
PubMed=11297522; DOI=10.1074/jbc.M010173200;
Geick A., Eichelbaum M., Burk O.;
"Nuclear receptor response elements mediate induction of intestinal
MDR1 by rifampin.";
J. Biol. Chem. 276:14581-14587(2001).
[10]
SUBCELLULAR LOCATION, MUTAGENESIS OF 66-ARG-ARG-67 AND 91-ARG-ARG-92,
AND NUCLEAR LOCALIZATION SIGNAL.
PubMed=12606758; DOI=10.1124/mol.63.3.524;
Kawana K., Ikuta T., Kobayashi Y., Gotoh O., Takeda K., Kawajiri K.;
"Molecular mechanism of nuclear translocation of an orphan nuclear
receptor, SXR.";
Mol. Pharmacol. 63:524-531(2003).
[11]
FUNCTION.
PubMed=19297428; DOI=10.3945/jn.108.103572;
Li Y., Ross-Viola J.S., Shay N.F., Moore D.D., Ricketts M.L.;
"Human CYP3A4 and murine Cyp3A11 are regulated by equol and genistein
via the pregnane X receptor in a species-specific manner.";
J. Nutr. 139:898-904(2009).
[12]
X-RAY CRYSTALLOGRAPHY (2.52 ANGSTROMS) OF 130-434.
PubMed=11408620; DOI=10.1126/science.1060762;
Watkins R.E., Wisely G.B., Moore L.B., Collins J.L., Lambert M.H.,
Williams S.P., Willson T.M., Kliewer S.A., Redinbo M.R.;
"The human nuclear xenobiotic receptor PXR: structural determinants of
directed promiscuity.";
Science 292:2329-2333(2001).
[13]
X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 130-434 IN COMPLEX WITH
HYPERFORIN, FUNCTION, AND INTERACTION WITH NCOA1.
PubMed=12578355; DOI=10.1021/bi0268753;
Watkins R.E., Maglich J.M., Moore L.B., Wisely G.B., Noble S.M.,
Davis-Searles P.R., Lambert M.H., Kliewer S.A., Redinbo M.R.;
"2.1 A crystal structure of human PXR in complex with the St. John's
wort compound hyperforin.";
Biochemistry 42:1430-1438(2003).
[14]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 130-434 IN COMPLEX WITH THE
CHOLESTEROL-LOWERING COMPOUND SR12813 AND NCOA1.
PubMed=12909012; DOI=10.1016/S0022-2836(03)00795-2;
Watkins R.E., Davis-Searles P.R., Lambert M.H., Redinbo M.R.;
"Coactivator binding promotes the specific interaction between ligand
and the pregnane X receptor.";
J. Mol. Biol. 331:815-828(2003).
[15]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 130-431 IN COMPLEX WITH
RIFAMPICIN.
PubMed=15705662; DOI=10.1210/me.2004-0346;
Chrencik J.E., Orans J., Moore L.B., Xue Y., Peng L., Collins J.L.,
Wisely G.B., Lambert M.H., Kliewer S.A., Redinbo M.R.;
"Structural disorder in the complex of human pregnane X receptor and
the macrolide antibiotic rifampicin.";
Mol. Endocrinol. 19:1125-1134(2005).
[16]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 142-434 IN COMPLEX WITH
T0901317 AND NCOA1, AND INTERACTION WITH NCOA1.
PubMed=17215127; DOI=10.1016/j.bmc.2006.12.026;
Xue Y., Chao E., Zuercher W.J., Willson T.M., Collins J.L.,
Redinbo M.R.;
"Crystal structure of the PXR-T1317 complex provides a scaffold to
examine the potential for receptor antagonism.";
Bioorg. Med. Chem. 15:2156-2166(2007).
[17]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 130-434 IN COMPLEX WITH
COLUPULONE, AND FUNCTION.
PubMed=18768384; DOI=10.1124/mol.108.050732;
Teotico D.G., Bischof J.J., Peng L., Kliewer S.A., Redinbo M.R.;
"Structural basis of human pregnane X receptor activation by the hops
constituent colupulone.";
Mol. Pharmacol. 74:1512-1520(2008).
[18]
VARIANTS CYS-98; GLN-148; TRP-381 AND VAL-403.
PubMed=15618712; DOI=10.2133/dmpk.17.561;
Koyano S., Kurose K., Ozawa S., Saeki M., Nakajima Y., Hasegawa R.,
Komamura K., Ueno K., Kamakura S., Nakajima T., Saito H., Kimura H.,
Goto Y., Saitoh O., Katoh M., Ohnuma T., Kawai M., Sugai K.,
Ohtsuki T., Suzuki C., Minami N., Saito Y., Sawada J.;
"Eleven novel single nucleotide polymorphisms in the NR1I2 (PXR) gene,
four of which induce non-synonymous amino acid alterations.";
Drug Metab. Pharmacokinet. 17:561-565(2002).
-!- FUNCTION: Nuclear receptor that binds and is activated by variety
of endogenous and xenobiotic compounds. Transcription factor that
activates the transcription of multiple genes involved in the
metabolism and secretion of potentially harmful xenobiotics, drugs
and endogenous compounds. Activated by the antibiotic rifampicin
and various plant metabolites, such as hyperforin, guggulipid,
colupulone, and isoflavones. Response to specific ligands is
species-specific. Activated by naturally occurring steroids, such
as pregnenolone and progesterone. Binds to a response element in
the promoters of the CYP3A4 and ABCB1/MDR1 genes.
{ECO:0000269|PubMed:11297522, ECO:0000269|PubMed:11668216,
ECO:0000269|PubMed:12578355, ECO:0000269|PubMed:18768384,
ECO:0000269|PubMed:19297428, ECO:0000269|PubMed:9727070}.
-!- SUBUNIT: Heterodimer with RXR. Interacts with NCOA1.
{ECO:0000269|PubMed:12578355, ECO:0000269|PubMed:12909012,
ECO:0000269|PubMed:15705662, ECO:0000269|PubMed:17215127,
ECO:0000269|PubMed:18768384}.
-!- INTERACTION:
P08238:HSP90AB1; NbExp=2; IntAct=EBI-3905991, EBI-352572;
Q15788:NCOA1; NbExp=5; IntAct=EBI-3905991, EBI-455189;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12606758,
ECO:0000270|PROSITE-ProRule:PRU00407}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=7;
Name=1A; Synonyms=1, PRR1-A;
IsoId=O75469-1; Sequence=Displayed;
Name=1B; Synonyms=PRR1-B;
IsoId=O75469-2; Sequence=VSP_003668;
Name=1C; Synonyms=PRR1-C;
IsoId=O75469-3; Sequence=VSP_003667;
Name=2A; Synonyms=2, PRR2-A;
IsoId=O75469-4; Sequence=VSP_003669;
Name=2B; Synonyms=PRR2-B;
IsoId=O75469-5; Sequence=VSP_003668, VSP_003669;
Name=2C; Synonyms=PRR2-C;
IsoId=O75469-6; Sequence=VSP_003667, VSP_003669;
Name=3;
IsoId=O75469-7; Sequence=VSP_026669;
-!- TISSUE SPECIFICITY: Expressed in liver, colon and small intestine.
-!- SIMILARITY: Belongs to the nuclear hormone receptor family. NR1
subfamily. {ECO:0000320}.
-!- WEB RESOURCE: Name=SeattleSNPs;
URL="http://pga.gs.washington.edu/data/nr1i2/";
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EMBL; AY091855; AAM26736.1; -; mRNA.
EMBL; AF061056; AAD05436.1; -; mRNA.
EMBL; AF084644; AAC64557.1; -; mRNA.
EMBL; AF084645; AAC64558.1; -; mRNA.
EMBL; AF364606; AAK38720.1; -; Genomic_DNA.
EMBL; AF364606; AAK38721.1; -; Genomic_DNA.
EMBL; AF364606; AAK38722.1; -; Genomic_DNA.
EMBL; AJ009936; CAB55489.1; -; mRNA.
EMBL; AJ009936; CAB55490.1; -; mRNA.
EMBL; AJ009936; CAB55491.1; -; mRNA.
EMBL; AJ009937; CAB55492.1; -; mRNA.
EMBL; AJ009937; CAB55493.1; -; mRNA.
EMBL; AJ009937; CAB55494.1; -; mRNA.
EMBL; DQ911122; ABJ52965.1; -; Genomic_DNA.
EMBL; DQ923326; ABJ52966.1; -; Genomic_DNA.
EMBL; EF614253; ABR09276.1; -; Genomic_DNA.
EMBL; BC017304; AAH17304.2; -; mRNA.
CCDS; CCDS2995.1; -. [O75469-7]
CCDS; CCDS43136.1; -. [O75469-1]
CCDS; CCDS54627.1; -. [O75469-4]
RefSeq; NP_003880.3; NM_003889.3. [O75469-1]
RefSeq; NP_071285.1; NM_022002.2. [O75469-7]
RefSeq; NP_148934.1; NM_033013.2. [O75469-4]
UniGene; Hs.7303; -.
PDB; 1ILG; X-ray; 2.52 A; A=130-434.
PDB; 1ILH; X-ray; 2.76 A; A=130-434.
PDB; 1M13; X-ray; 2.15 A; A=130-434.
PDB; 1NRL; X-ray; 2.00 A; A/B=130-434.
PDB; 1SKX; X-ray; 2.80 A; A=130-431.
PDB; 2O9I; X-ray; 2.80 A; A/B=142-434.
PDB; 2QNV; X-ray; 2.80 A; A=130-434.
PDB; 3CTB; X-ray; 2.00 A; A/B=130-434.
PDB; 3HVL; X-ray; 2.10 A; A/B=130-434.
PDB; 3R8D; X-ray; 2.80 A; A=130-434.
PDB; 4J5W; X-ray; 2.80 A; A/B=130-434.
PDB; 4J5X; X-ray; 2.80 A; A/B=130-434.
PDB; 4NY9; X-ray; 2.80 A; A=142-431.
PDB; 4S0S; X-ray; 2.80 A; A/B=130-434.
PDB; 4S0T; X-ray; 3.14 A; A/B=130-434.
PDB; 4X1F; X-ray; 2.00 A; A=130-434.
PDB; 4X1G; X-ray; 2.25 A; A=130-434.
PDB; 4XAO; X-ray; 2.58 A; A=130-434.
PDB; 4XHD; X-ray; 2.40 A; A=130-434.
PDB; 5A86; X-ray; 2.25 A; A/B=130-432.
PDB; 5X0R; X-ray; 2.67 A; A/B=130-434.
PDBsum; 1ILG; -.
PDBsum; 1ILH; -.
PDBsum; 1M13; -.
PDBsum; 1NRL; -.
PDBsum; 1SKX; -.
PDBsum; 2O9I; -.
PDBsum; 2QNV; -.
PDBsum; 3CTB; -.
PDBsum; 3HVL; -.
PDBsum; 3R8D; -.
PDBsum; 4J5W; -.
PDBsum; 4J5X; -.
PDBsum; 4NY9; -.
PDBsum; 4S0S; -.
PDBsum; 4S0T; -.
PDBsum; 4X1F; -.
PDBsum; 4X1G; -.
PDBsum; 4XAO; -.
PDBsum; 4XHD; -.
PDBsum; 5A86; -.
PDBsum; 5X0R; -.
DisProt; DP00323; -.
ProteinModelPortal; O75469; -.
SMR; O75469; -.
BioGrid; 114380; 39.
IntAct; O75469; 10.
STRING; 9606.ENSP00000336528; -.
BindingDB; O75469; -.
ChEMBL; CHEMBL3401; -.
DrugBank; DB01248; Docetaxel.
DrugBank; DB00530; Erlotinib.
DrugBank; DB00783; Estradiol.
DrugBank; DB00977; Ethinyl Estradiol.
DrugBank; DB01892; Hyperforin.
DrugBank; DB01229; Paclitaxel.
DrugBank; DB01708; Prasterone.
DrugBank; DB01045; Rifampicin.
DrugBank; DB01220; Rifaximin.
DrugBank; DB08864; Rilpivirine.
DrugBank; DB04466; SR12813.
DrugBank; DB00163; Vitamin E.
GuidetoPHARMACOLOGY; 606; -.
SwissLipids; SLP:000001583; -.
iPTMnet; O75469; -.
PhosphoSitePlus; O75469; -.
BioMuta; NR1I2; -.
PaxDb; O75469; -.
PeptideAtlas; O75469; -.
PRIDE; O75469; -.
Ensembl; ENST00000337940; ENSP00000336528; ENSG00000144852. [O75469-7]
Ensembl; ENST00000638727; ENSP00000492264; ENSG00000144852. [O75469-4]
Ensembl; ENST00000640105; ENSP00000492881; ENSG00000144852. [O75469-1]
GeneID; 8856; -.
KEGG; hsa:8856; -.
UCSC; uc003edk.3; human. [O75469-1]
CTD; 8856; -.
DisGeNET; 8856; -.
EuPathDB; HostDB:ENSG00000144852.16; -.
GeneCards; NR1I2; -.
HGNC; HGNC:7968; NR1I2.
HPA; HPA029309; -.
HPA; HPA055121; -.
HPA; HPA073926; -.
MIM; 603065; gene.
neXtProt; NX_O75469; -.
OpenTargets; ENSG00000144852; -.
PharmGKB; PA378; -.
eggNOG; KOG3575; Eukaryota.
eggNOG; ENOG410XRZC; LUCA.
GeneTree; ENSGT00870000136372; -.
HOVERGEN; HBG108655; -.
InParanoid; O75469; -.
KO; K08540; -.
OMA; YIECNRP; -.
OrthoDB; EOG091G05X3; -.
PhylomeDB; O75469; -.
TreeFam; TF316304; -.
Reactome; R-HSA-383280; Nuclear Receptor transcription pathway.
SignaLink; O75469; -.
SIGNOR; O75469; -.
ChiTaRS; NR1I2; human.
EvolutionaryTrace; O75469; -.
GeneWiki; Pregnane_X_receptor; -.
GenomeRNAi; 8856; -.
PRO; PR:O75469; -.
Proteomes; UP000005640; Chromosome 3.
Bgee; ENSG00000144852; -.
ExpressionAtlas; O75469; baseline and differential.
Genevisible; O75469; HS.
GO; GO:0045111; C:intermediate filament cytoskeleton; HTP:HPA.
GO; GO:0016604; C:nuclear body; HTP:HPA.
GO; GO:0005654; C:nucleoplasm; HTP:HPA.
GO; GO:0008144; F:drug binding; HTP:UniProtKB.
GO; GO:0004879; F:nuclear receptor activity; HTP:UniProtKB.
GO; GO:0000977; F:RNA polymerase II regulatory region sequence-specific DNA binding; HTP:NTNU_SB.
GO; GO:0003707; F:steroid hormone receptor activity; RCA:InterPro.
GO; GO:0003713; F:transcription coactivator activity; IBA:ProtInc.
GO; GO:0001228; F:transcriptional activator activity, RNA polymerase II transcription regulatory region sequence-specific binding; HTP:NTNU_SB.
GO; GO:0008270; F:zinc ion binding; RCA:InterPro.
GO; GO:0046618; P:drug export; HTP:UniProtKB.
GO; GO:0042738; P:exogenous drug catabolic process; HTP:UniProtKB.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; HTP:MGI.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; HTP:NTNU_SB.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; HTP:UniProtKB.
GO; GO:0007165; P:signal transduction; IBA:ProtInc.
GO; GO:0008202; P:steroid metabolic process; IBA:ProtInc.
GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; IBA:Reactome.
GO; GO:0006805; P:xenobiotic metabolic process; HTP:UniProtKB.
GO; GO:0042908; P:xenobiotic transport; HTP:UniProtKB.
Gene3D; 1.10.565.10; -; 1.
Gene3D; 3.30.50.10; -; 1.
InterPro; IPR035500; NHR_like_dom_sf.
InterPro; IPR000536; Nucl_hrmn_rcpt_lig-bd.
InterPro; IPR001723; Nuclear_hrmn_rcpt.
InterPro; IPR001628; Znf_hrmn_rcpt.
InterPro; IPR013088; Znf_NHR/GATA.
Pfam; PF00104; Hormone_recep; 1.
Pfam; PF00105; zf-C4; 1.
PRINTS; PR00398; STRDHORMONER.
PRINTS; PR00047; STROIDFINGER.
SMART; SM00430; HOLI; 1.
SMART; SM00399; ZnF_C4; 1.
SUPFAM; SSF48508; SSF48508; 1.
PROSITE; PS00031; NUCLEAR_REC_DBD_1; 1.
PROSITE; PS51030; NUCLEAR_REC_DBD_2; 1.
1: Evidence at protein level;
3D-structure; Activator; Alternative splicing; Complete proteome;
DNA-binding; Metal-binding; Nucleus; Polymorphism; Receptor;
Reference proteome; Transcription; Transcription regulation; Zinc;
Zinc-finger.
CHAIN 1 434 Nuclear receptor subfamily 1 group I
member 2.
/FTId=PRO_0000053547.
DNA_BIND 38 107 Nuclear receptor. {ECO:0000270|PROSITE-
ProRule:PRU00407}.
ZN_FING 41 61 NR C4-type. {ECO:0000270|PROSITE-
ProRule:PRU00407}.
ZN_FING 77 102 NR C4-type. {ECO:0000270|PROSITE-
ProRule:PRU00407}.
REGION 108 204 Hinge.
REGION 205 434 Ligand-binding.
MOTIF 66 92 Bipartite nuclear localization signal.
BINDING 247 247 Agonist.
BINDING 285 285 Agonist.
BINDING 288 288 Agonist.
BINDING 299 299 Agonist.
BINDING 407 407 Agonist.
VAR_SEQ 1 55 Missing (in isoform 1B and isoform 2B).
{ECO:0000319|Ref.5}.
/FTId=VSP_003668.
VAR_SEQ 1 1 M -> MDPRGEVGAKNLPPNSPRGPEANL (in isoform
1C and isoform 2C). {ECO:0000319|Ref.5}.
/FTId=VSP_003667.
VAR_SEQ 1 1 M -> MTVTRTHHFKEGSLRAPAIPLHSAAAELASNHPRGP
EANL (in isoform 3).
{ECO:0000319|PubMed:9770465}.
/FTId=VSP_026669.
VAR_SEQ 174 210 Missing (in isoform 2A, isoform 2B and
isoform 2C). {ECO:0000319|Ref.5}.
/FTId=VSP_003669.
VARIANT 12 12 A -> T (in dbSNP:rs1063955).
{ECO:0000269|Ref.5}.
/FTId=VAR_050581.
VARIANT 18 18 E -> K (in dbSNP:rs59371185).
{ECO:0000269|Ref.7}.
/FTId=VAR_033237.
VARIANT 27 27 P -> S (in allele PXR*2;
dbSNP:rs12721613).
{ECO:0000269|PubMed:11668216,
ECO:0000269|Ref.7}.
/FTId=VAR_012228.
VARIANT 36 36 G -> R (in allele PXR*3;
dbSNP:rs12721607).
{ECO:0000269|PubMed:11668216}.
/FTId=VAR_012229.
VARIANT 98 98 R -> C (in dbSNP:rs72551371).
{ECO:0000269|PubMed:15618712}.
/FTId=VAR_018340.
VARIANT 122 122 R -> Q (in allele PXR*4; rare
polymorphism; dbSNP:rs12721608).
{ECO:0000269|PubMed:11668216}.
/FTId=VAR_012230.
VARIANT 148 148 R -> Q (in dbSNP:rs72551373).
{ECO:0000269|PubMed:15618712}.
/FTId=VAR_018341.
VARIANT 370 370 A -> T (in dbSNP:rs35761343).
{ECO:0000269|Ref.7}.
/FTId=VAR_033238.
VARIANT 381 381 R -> W (in dbSNP:rs72551375).
{ECO:0000269|PubMed:15618712}.
/FTId=VAR_018342.
VARIANT 403 403 I -> V (in dbSNP:rs72551376).
{ECO:0000269|PubMed:15618712}.
/FTId=VAR_018343.
MUTAGEN 66 67 RR->AA: Abolishes nuclear localization;
when associated with 91-A-A-92.
{ECO:0000269|PubMed:12606758}.
MUTAGEN 91 92 RR->AA: Abolishes nuclear localization;
when associated with 66-A-A-67.
{ECO:0000269|PubMed:12606758}.
CONFLICT 109 109 K -> N (in Ref. 5; CAB55489/CAB55490/
CAB55491/CAB55492/CAB55493/CAB55494).
{ECO:0000320}.
CONFLICT 174 174 Missing (in Ref. 8; AAH17304).
{ECO:0000320}.
HELIX 145 161 {ECO:0000307|PDB:1NRL}.
HELIX 193 206 {ECO:0000307|PDB:1NRL}.
HELIX 207 209 {ECO:0000307|PDB:2O9I}.
STRAND 211 216 {ECO:0000307|PDB:1NRL}.
STRAND 218 220 {ECO:0000307|PDB:4S0S}.
STRAND 222 226 {ECO:0000307|PDB:1NRL}.
STRAND 231 233 {ECO:0000307|PDB:1M13}.
HELIX 234 237 {ECO:0000307|PDB:1NRL}.
HELIX 240 260 {ECO:0000307|PDB:1NRL}.
HELIX 262 265 {ECO:0000307|PDB:1NRL}.
HELIX 269 290 {ECO:0000307|PDB:1NRL}.
TURN 294 297 {ECO:0000307|PDB:1NRL}.
STRAND 298 301 {ECO:0000307|PDB:1NRL}.
STRAND 304 308 {ECO:0000307|PDB:1NRL}.
STRAND 311 313 {ECO:0000307|PDB:1ILG}.
HELIX 315 318 {ECO:0000307|PDB:1NRL}.
HELIX 322 332 {ECO:0000307|PDB:1NRL}.
HELIX 337 348 {ECO:0000307|PDB:1NRL}.
STRAND 351 353 {ECO:0000307|PDB:2QNV}.
HELIX 359 380 {ECO:0000307|PDB:1NRL}.
HELIX 384 386 {ECO:0000307|PDB:1NRL}.
HELIX 389 417 {ECO:0000307|PDB:1NRL}.
HELIX 423 428 {ECO:0000307|PDB:1NRL}.
SEQUENCE 434 AA; 49762 MW; 1DF6A2AE3109C4DA CRC64;
MEVRPKESWN HADFVHCEDT ESVPGKPSVN ADEEVGGPQI CRVCGDKATG YHFNVMTCEG
CKGFFRRAMK RNARLRCPFR KGACEITRKT RRQCQACRLR KCLESGMKKE MIMSDEAVEE
RRALIKRKKS ERTGTQPLGV QGLTEEQRMM IRELMDAQMK TFDTTFSHFK NFRLPGVLSS
GCELPESLQA PSREEAAKWS QVRKDLCSLK VSLQLRGEDG SVWNYKPPAD SGGKEIFSLL
PHMADMSTYM FKGIISFAKV ISYFRDLPIE DQISLLKGAA FELCQLRFNT VFNAETGTWE
CGRLSYCLED TAGGFQQLLL EPMLKFHYML KKLQLHEEEY VLMQAISLFS PDRPGVLQHR
VVDQLQEQFA ITLKSYIECN RPQPAHRFLF LKIMAMLTEL RSINAQHTQR LLRIQDIHPF
ATPLMQELFG ITGS


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