NR1I2_RAT
ID NR1I2_RAT Reviewed; 431 AA.
AC Q9R1A7;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 153.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley;
RX PubMed=10415106; DOI=10.1006/abbi.1999.1307;
RA Zhang H., LeCulyse E., Liu L., Hu M., Matoney L., Zhu W., Yan B.;
RT "Rat pregnane X receptor: molecular cloning, tissue distribution, and
RT xenobiotic regulation.";
RL Arch. Biochem. Biophys. 368:14-22(1999).
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; AF151377; AAD47214.1; -; mRNA.
DR RefSeq; NP_443212.1; NM_052980.2.
DR AlphaFoldDB; Q9R1A7; -.
DR SMR; Q9R1A7; -.
DR STRING; 10116.ENSRNOP00000003934; -.
DR BindingDB; Q9R1A7; -.
DR ChEMBL; CHEMBL2146315; -.
DR PhosphoSitePlus; Q9R1A7; -.
DR PaxDb; Q9R1A7; -.
DR PRIDE; Q9R1A7; -.
DR Ensembl; ENSRNOT00000003934; ENSRNOP00000003934; ENSRNOG00000002906.
DR GeneID; 84385; -.
DR KEGG; rno:84385; -.
DR UCSC; RGD:69057; rat.
DR CTD; 8856; -.
DR RGD; 69057; Nr1i2.
DR eggNOG; KOG3575; Eukaryota.
DR GeneTree; ENSGT00940000161118; -.
DR HOGENOM; CLU_007368_12_0_1; -.
DR InParanoid; Q9R1A7; -.
DR OMA; DEEPKAC; -.
DR OrthoDB; 297114at2759; -.
DR PhylomeDB; Q9R1A7; -.
DR TreeFam; TF316304; -.
DR Reactome; R-RNO-383280; Nuclear Receptor transcription pathway.
DR Reactome; R-RNO-4090294; SUMOylation of intracellular receptors.
DR PRO; PR:Q9R1A7; -.
DR Proteomes; UP000002494; Chromosome 11.
DR Bgee; ENSRNOG00000002906; Expressed in liver and 11 other tissues.
DR Genevisible; Q9R1A7; RN.
DR GO; GO:0045111; C:intermediate filament cytoskeleton; IEA:Ensembl.
DR GO; GO:0016604; C:nuclear body; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0005667; C:transcription regulator complex; ISO:RGD.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; ISO:RGD.
DR GO; GO:0004879; F:nuclear receptor activity; IDA:RGD.
DR GO; GO:0016922; F:nuclear receptor binding; ISO:RGD.
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; ISO:RGD.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:RGD.
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:0045892; P:negative regulation of transcription, DNA-templated; ISO:RGD.
DR GO; GO:0010628; P:positive regulation of gene expression; ISO:RGD.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; ISO:RGD.
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..431
FT /note="Nuclear receptor subfamily 1 group I member 2"
FT /id="PRO_0000053550"
FT DOMAIN 143..430
FT /note="NR LBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01189"
FT DNA_BIND 38..104
FT /note="Nuclear receptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT ZN_FING 38..58
FT /note="NR C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT ZN_FING 74..99
FT /note="NR C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT REGION 105..142
FT /note="Hinge"
FT MOTIF 63..89
FT /note="Bipartite nuclear localization signal"
FT /evidence="ECO:0000250"
FT BINDING 244
FT /ligand="hyperforin"
FT /ligand_id="ChEBI:CHEBI:5834"
FT /ligand_note="agonist"
FT /evidence="ECO:0000250|UniProtKB:O75469"
FT BINDING 282..285
FT /ligand="hyperforin"
FT /ligand_id="ChEBI:CHEBI:5834"
FT /ligand_note="agonist"
FT /evidence="ECO:0000250|UniProtKB:O75469"
SQ SEQUENCE 431 AA; 49660 MW; 4B545F21F9439697 CRC64;
MRPEERWNHV GLVQREEADS VLEEPINVDE EDGGLQICRV CGDKANGYHF NVMTCEGCKG
FFRRAMKRNV RLRCPFRKGT CEITRKTRRQ CQACRLRKCL ESGMKKEMIM SDAAVEQRRA
LIKRKKREKI EAPPPGGQGL TEEQQALIQE LMDAQMQTFD TTFSHFKDFR LPAVFHSDCE
LPEVLQASLL EDPATWSQIM KDSVPMKISV QLRGEDGSIW NYQPPSKSDG KEIIPLLPHL
ADVSTYMFKG VINFAKVISH FRELPIEDQI SLLKGATFEM CILRFNTMFD TETGTWECGR
LAYCFEDPNG GFQKLLLDPL MKFHCMLKKL QLREEEYVLM QAISLFSPDR PGVVQRSVVD
QLQERFALTL KAYIECSRPY PAHRFLFLKI MAVLTELRSI NAQQTQQLLR IQDTHPFATP
LMQELFSSTD G
