NR1I2_MACMU
ID NR1I2_MACMU Reviewed; 434 AA.
AC Q8SQ01;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Nuclear receptor subfamily 1 group I member 2;
DE AltName: Full=Orphan nuclear receptor PXR;
DE AltName: Full=Pregnane X receptor;
GN Name=NR1I2; Synonyms=PXR;
OS Macaca mulatta (Rhesus macaque).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9544;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=11981033; DOI=10.1210/mend.16.5.0828;
RA Moore L.B., Maglich J.M., McKee D.D., Wisely B., Willson T.M.,
RA Kliewer S.A., Lambert M.H., Moore J.T.;
RT "Pregnane X receptor (PXR), constitutive androstane receptor (CAR), and
RT benzoate X receptor (BXR) define three pharmacologically distinct classes
RT of nuclear receptors.";
RL Mol. Endocrinol. 16:977-986(2002).
CC -!- FUNCTION: Nuclear receptor that binds and is activated by a variety of
CC endogenous and xenobiotic compounds. Transcription factor that
CC activates the transcription of multiple genes involved in the
CC metabolism and secretion of potentially harmful xenobiotics, endogenous
CC compounds and drugs. Response to specific ligands is species-specific,
CC due to differences in the ligand-binding domain. Activated by naturally
CC occurring steroids, such as pregnenolone and progesterone. Binds to a
CC response element in the promoters of the CYP3A4 and ABCB1/MDR1 genes
CC (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Heterodimer with RXRA (By similarity). Interacts with NCOA1
CC (By similarity). Interacts (via domain NR LBD) with CRY1 and CRY2 in a
CC ligand-dependent manner (By similarity). {ECO:0000250|UniProtKB:O54915,
CC ECO:0000250|UniProtKB:O75469}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00407}.
CC -!- SIMILARITY: Belongs to the nuclear hormone receptor family. NR1
CC subfamily. {ECO:0000305}.
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DR EMBL; AF454671; AAM10633.1; -; mRNA.
DR RefSeq; NP_001028054.3; NM_001032882.3.
DR AlphaFoldDB; Q8SQ01; -.
DR SMR; Q8SQ01; -.
DR STRING; 9544.ENSMMUP00000002638; -.
DR GeneID; 574226; -.
DR KEGG; mcc:574226; -.
DR CTD; 8856; -.
DR eggNOG; KOG3575; Eukaryota.
DR InParanoid; Q8SQ01; -.
DR OrthoDB; 297114at2759; -.
DR Proteomes; UP000006718; Unplaced.
DR GO; GO:0005654; C:nucleoplasm; IEA:UniProt.
DR GO; GO:0004879; F:nuclear receptor activity; ISS:UniProtKB.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0042178; P:xenobiotic catabolic process; ISS:UniProtKB.
DR GO; GO:0006805; P:xenobiotic metabolic process; ISS:UniProtKB.
DR GO; GO:0042908; P:xenobiotic transport; ISS:UniProtKB.
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; 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 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 2: Evidence at transcript level;
KW Activator; DNA-binding; Metal-binding; Nucleus; Receptor;
KW Reference proteome; Transcription; Transcription regulation; Zinc;
KW Zinc-finger.
FT CHAIN 1..434
FT /note="Nuclear receptor subfamily 1 group I member 2"
FT /id="PRO_0000053548"
FT DOMAIN 146..433
FT /note="NR LBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01189"
FT DNA_BIND 38..107
FT /note="Nuclear receptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT ZN_FING 41..61
FT /note="NR C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT ZN_FING 77..102
FT /note="NR C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT REGION 108..145
FT /note="Hinge"
FT /evidence="ECO:0000250"
FT MOTIF 66..92
FT /note="Bipartite nuclear localization signal"
FT /evidence="ECO:0000250"
FT BINDING 247
FT /ligand="hyperforin"
FT /ligand_id="ChEBI:CHEBI:5834"
FT /ligand_note="agonist"
FT /evidence="ECO:0000250|UniProtKB:O75469"
FT BINDING 285..288
FT /ligand="hyperforin"
FT /ligand_id="ChEBI:CHEBI:5834"
FT /ligand_note="agonist"
FT /evidence="ECO:0000250|UniProtKB:O75469"
FT BINDING 407
FT /ligand="hyperforin"
FT /ligand_id="ChEBI:CHEBI:5834"
FT /ligand_note="agonist"
FT /evidence="ECO:0000250|UniProtKB:O75469"
SQ SEQUENCE 434 AA; 49993 MW; F3BE3017815F3A59 CRC64;
MEVRPKEGWN HADFVYCEDT EFAPGKPTVN ADEEVGGPQI CRVCGDKATG YHFNVMTCEG
CKGFFRRAMK RNARLRCPFR KGACEITRKT RRQCQACRLR KCLESGMKKE MIMSDAAVEE
RRALIKRKKR ERIGTQPPGV QGLTEEQRMM IRELMDAQMK TFDTTFSHFK NFRLPGVLSS
GCEMPESLQA PSREEAAKWN QVRKDLWSVK VSVQLRGEDG SVWNYKPPAD NGGKEIFSLL
PHMADMSTYM FKGIINFAKV ISYFRDLPIE DQISLLKGAT FELCQLRFNT VFNAETGTWE
CGRLSYCLED PAGGFQQLLL EPMLKFHYML KKLQLHEEEY VLMQAISLFS PDRPGVVQHR
VVDQLQEQYA ITLKSYIECN RPQPAHRFLF LKIMAMLTEL RSINAQHTQR LLRIQDIHPF
ATPLMQELFG ITGS
