Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

O54915 (NR1I2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 123. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Nuclear receptor subfamily 1 group I member 2
Alternative name(s):
Orphan nuclear receptor PXR
Pregnane X receptor
Gene names
Name:Nr1i2
Synonyms:Pxr
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length431 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Nuclear receptor that binds and is activated by a 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, endogenous compounds and drugs. Response to specific ligands is species-specific, due to differences in the ligand-binding domain. Binds to a response element in the promoters of the CYP3A4 and ABCB1/MDR1 genes By similarity. Activated by naturally occurring steroids such as pregnenolone and progesterone, the cholesterol metabolite 5-beta-cholestane-3-alpha,7-alpha,12-alpha-triol, synthetic glucocorticoids and antiglucocorticoids and 16-alpha-carbonitrile (PCN). Ref.4 Ref.5

Subunit structure

Heterodimer with RXRA. Interacts with NCOA1 By similarity.

Subcellular location

Nucleus By similarity Ref.3.

Sequence similarities

Belongs to the nuclear hormone receptor family. NR1 subfamily.

Contains 1 nuclear receptor DNA-binding domain.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
   DomainZinc-finger
   LigandDNA-binding
Metal-binding
Zinc
   Molecular functionActivator
Receptor
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processdrug export

Inferred from sequence or structural similarity. Source: UniProtKB

exogenous drug catabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of transcription, DNA-templated

Inferred from sequence orthology PubMed 11891224. Source: MGI

positive regulation of gene expression

Inferred from mutant phenotype PubMed 18794335. Source: MGI

positive regulation of transcription, DNA-templated

Inferred from sequence or structural similarity. Source: UniProtKB

xenobiotic metabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

xenobiotic transport

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentnucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functiondrug binding

Inferred from sequence or structural similarity. Source: UniProtKB

ligand-activated sequence-specific DNA binding RNA polymerase II transcription factor activity

Inferred from sequence or structural similarity. Source: UniProtKB

protein binding

Inferred from physical interaction PubMed 11891224. Source: MGI

sequence-specific DNA binding

Inferred from electronic annotation. Source: InterPro

steroid hormone receptor activity

Inferred from electronic annotation. Source: InterPro

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: O54915-1)

Also known as: PXR.1;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: O54915-2)

Also known as: PXR.2;

The sequence of this isoform differs from the canonical sequence as follows:
     171-211: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 431431Nuclear receptor subfamily 1 group I member 2
PRO_0000053549

Regions

DNA binding35 – 10470Nuclear receptor
Zinc finger38 – 5821NR C4-type
Zinc finger74 – 9926NR C4-type
Region105 – 20197Hinge
Region202 – 431230Ligand-binding
Motif63 – 8927Bipartite nuclear localization signal By similarity

Sites

Binding site2441Agonist By similarity
Binding site2851Agonist By similarity
Binding site2961Agonist By similarity

Natural variations

Alternative sequence171 – 21141Missing in isoform 2.
VSP_003670

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (PXR.1) [UniParc].

Last modified June 1, 1998. Version 1.
Checksum: F592AF91F689329E

FASTA43149,567
        10         20         30         40         50         60 
MRPEESWSRV GLVQCEEADS ALEEPINVEE EDGGLQICRV CGDKANGYHF NVMTCEGCKG 

        70         80         90        100        110        120 
FFRRAMKRNV RLRCPFRKGT CEITRKTRRQ CQACRLRKCL ESGMKKEMIM SDAAVEQRRA 

       130        140        150        160        170        180 
LIKRKKREKI EAPPPGGQGL TEEQQALIQE LMDAQMQTFD TTFSHFKDFR LPAVFHSGCE 

       190        200        210        220        230        240 
LPEFLQASLL EDPATWSQIM KDRVPMKISL QLRGEDGSIW NYQPPSKSDG KEIIPLLPHL 

       250        260        270        280        290        300 
ADVSTYMFKG VINFAKVISY FRDLPIEDQI SLLKGATFEM CILRFNTMFD TETGTWECGR 

       310        320        330        340        350        360 
LAYCFEDPNG GFQKLLLDPL MKFHCMLKKL QLHKEEYVLM QAISLFSPDR PGVVQRSVVD 

       370        380        390        400        410        420 
QLQERFALTL KAYIECSRPY PAHRFLFLKI MAVLTELRSI NAQQTQQLLR IQDSHPFATP 

       430 
LMQELFSSTD G 

« Hide

Isoform 2 (PXR.2) [UniParc].

Checksum: 9425A40F980F08ED
Show »

FASTA39044,958

References

« Hide 'large scale' references
[1]"An orphan nuclear receptor activated by pregnanes defines a novel steroid signaling pathway."
Kliewer S.A., Moore J.T., Wade L., Staudinger J.L., Watson M.A., Jones S.A., McKee D.D., Oliver B.B., Willson T.M., Zetterstrom R.H., Perlmann T., Lehmann J.M.
Cell 92:73-82(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], ALTERNATIVE SPLICING.
Tissue: Liver.
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Strain: C57BL/6J.
Tissue: Cecum.
[3]"Molecular mechanism of nuclear translocation of an orphan nuclear receptor, SXR."
Kawana K., Ikuta T., Kobayashi Y., Gotoh O., Takeda K., Kawajiri K.
Mol. Pharmacol. 63:524-531(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[4]"Identification of an endogenous ligand that activates pregnane X receptor-mediated sterol clearance."
Dussault I., Yoo H.-D., Lin M., Wang E., Fan M., Batta A.K., Salen G., Erickson S.K., Forman B.M.
Proc. Natl. Acad. Sci. U.S.A. 100:833-838(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[5]"Human CYP3A4 and murine Cyp3A11 are regulated by equol and genistein via the pregnane X receptor in a species-specific manner."
Li Y., Ross-Viola J.S., Shay N.F., Moore D.D., Ricketts M.L.
J. Nutr. 139:898-904(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF031814 mRNA. Translation: AAC39964.1.
AK018630 mRNA. Translation: BAB31316.1.
CCDSCCDS28164.1. [O54915-1]
RefSeqNP_001091874.1. NM_001098404.1. [O54915-2]
NP_035066.1. NM_010936.3. [O54915-1]
XP_006521909.1. XM_006521846.1. [O54915-1]
XP_006521911.1. XM_006521848.1. [O54915-1]
UniGeneMm.8509.

3D structure databases

ProteinModelPortalO54915.
SMRO54915. Positions 34-426.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid201839. 5 interactions.

Chemistry

ChEMBLCHEMBL1743244.
GuidetoPHARMACOLOGY606.

PTM databases

PhosphoSiteO54915.

Proteomic databases

PRIDEO54915.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000023504; ENSMUSP00000023504; ENSMUSG00000022809. [O54915-1]
GeneID18171.
KEGGmmu:18171.
UCSCuc007zep.1. mouse. [O54915-2]
uc007zeq.1. mouse. [O54915-1]

Organism-specific databases

CTD8856.
MGIMGI:1337040. Nr1i2.

Phylogenomic databases

eggNOGNOG238483.
HOGENOMHOG000220844.
HOVERGENHBG108655.
InParanoidO54915.
KOK08540.
OMAHFKNFRL.
OrthoDBEOG7GBFXG.
PhylomeDBO54915.
TreeFamTF316304.

Gene expression databases

ArrayExpressO54915.
BgeeO54915.
CleanExMM_NR1I2.
GenevestigatorO54915.

Family and domain databases

Gene3D1.10.565.10. 2 hits.
3.30.50.10. 1 hit.
InterProIPR008946. Nucl_hormone_rcpt_ligand-bd.
IPR000536. Nucl_hrmn_rcpt_lig-bd_core.
IPR001723. Str_hrmn_rcpt.
IPR001628. Znf_hrmn_rcpt.
IPR013088. Znf_NHR/GATA.
[Graphical view]
PfamPF00104. Hormone_recep. 1 hit.
PF00105. zf-C4. 1 hit.
[Graphical view]
PRINTSPR00398. STRDHORMONER.
PR00047. STROIDFINGER.
SMARTSM00430. HOLI. 1 hit.
SM00399. ZnF_C4. 1 hit.
[Graphical view]
SUPFAMSSF48508. SSF48508. 1 hit.
PROSITEPS00031. NUCLEAR_REC_DBD_1. 1 hit.
PS51030. NUCLEAR_REC_DBD_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio293468.
PROO54915.
SOURCESearch...

Entry information

Entry nameNR1I2_MOUSE
AccessionPrimary (citable) accession number: O54915
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: June 1, 1998
Last modified: July 9, 2014
This is version 123 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot