ID   F1D8P9_HUMAN            Unreviewed;       473 AA.
AC   F1D8P9;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   03-MAY-2011, sequence version 1.
DT   02-SEP-2026, entry version 105.
DE   RecName: Full=Nuclear receptor subfamily 1 group I member 2 {ECO:0000256|ARBA:ARBA00074444};
DE   AltName: Full=Orphan nuclear receptor PXR {ECO:0000256|ARBA:ARBA00082649};
DE   AltName: Full=Pregnane X receptor {ECO:0000256|ARBA:ARBA00078912};
GN   Name=NR1i2 {ECO:0000313|EMBL:ADZ17348.1};
GN   Synonyms=NR1I2 {ECO:0000313|EMBL:EAW79538.1};
GN   ORFNames=hCG_21777 {ECO:0000313|EMBL:EAW79538.1};
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 {ECO:0000313|EMBL:ADZ17348.1};
RN   [1] {ECO:0000313|EMBL:EAW79538.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=11181995; DOI=10.1126/science.1058040;
RA   Venter J.C., Adams M.D., Myers E.W., Li P.W., Mural R.J., Sutton G.G.,
RA   Smith H.O., Yandell M., Evans C.A., Holt R.A., Gocayne J.D., Amanatides P.,
RA   Ballew R.M., Huson D.H., Wortman J.R., Zhang Q., Kodira C.D., Zheng X.H.,
RA   Chen L., Skupski M., Subramanian G., Thomas P.D., Zhang J.,
RA   Gabor Miklos G.L., Nelson C., Broder S., Clark A.G., Nadeau J.,
RA   McKusick V.A., Zinder N., Levine A.J., Roberts R.J., Simon M., Slayman C.,
RA   Hunkapiller M., Bolanos R., Delcher A., Dew I., Fasulo D., Flanigan M.,
RA   Florea L., Halpern A., Hannenhalli S., Kravitz S., Levy S., Mobarry C.,
RA   Reinert K., Remington K., Abu-Threideh J., Beasley E., Biddick K.,
RA   Bonazzi V., Brandon R., Cargill M., Chandramouliswaran I., Charlab R.,
RA   Chaturvedi K., Deng Z., Di Francesco V., Dunn P., Eilbeck K.,
RA   Evangelista C., Gabrielian A.E., Gan W., Ge W., Gong F., Gu Z., Guan P.,
RA   Heiman T.J., Higgins M.E., Ji R.R., Ke Z., Ketchum K.A., Lai Z., Lei Y.,
RA   Li Z., Li J., Liang Y., Lin X., Lu F., Merkulov G.V., Milshina N.,
RA   Moore H.M., Naik A.K., Narayan V.A., Neelam B., Nusskern D., Rusch D.B.,
RA   Salzberg S., Shao W., Shue B., Sun J., Wang Z., Wang A., Wang X., Wang J.,
RA   Wei M., Wides R., Xiao C., Yan C., Yao A., Ye J., Zhan M., Zhang W.,
RA   Zhang H., Zhao Q., Zheng L., Zhong F., Zhong W., Zhu S., Zhao S.,
RA   Gilbert D., Baumhueter S., Spier G., Carter C., Cravchik A., Woodage T.,
RA   Ali F., An H., Awe A., Baldwin D., Baden H., Barnstead M., Barrow I.,
RA   Beeson K., Busam D., Carver A., Center A., Cheng M.L., Curry L.,
RA   Danaher S., Davenport L., Desilets R., Dietz S., Dodson K., Doup L.,
RA   Ferriera S., Garg N., Gluecksmann A., Hart B., Haynes J., Haynes C.,
RA   Heiner C., Hladun S., Hostin D., Houck J., Howland T., Ibegwam C.,
RA   Johnson J., Kalush F., Kline L., Koduru S., Love A., Mann F., May D.,
RA   McCawley S., McIntosh T., McMullen I., Moy M., Moy L., Murphy B.,
RA   Nelson K., Pfannkoch C., Pratts E., Puri V., Qureshi H., Reardon M.,
RA   Rodriguez R., Rogers Y.H., Romblad D., Ruhfel B., Scott R., Sitter C.,
RA   Smallwood M., Stewart E., Strong R., Suh E., Thomas R., Tint N.N., Tse S.,
RA   Vech C., Wang G., Wetter J., Williams S., Williams M., Windsor S.,
RA   Winn-Deen E., Wolfe K., Zaveri J., Zaveri K., Abril J.F., Guigo R.,
RA   Campbell M.J., Sjolander K.V., Karlak B., Kejariwal A., Mi H., Lazareva B.,
RA   Hatton T., Narechania A., Diemer K., Muruganujan A., Guo N., Sato S.,
RA   Bafna V., Istrail S., Lippert R., Schwartz R., Walenz B., Yooseph S.,
RA   Allen D., Basu A., Baxendale J., Blick L., Caminha M., Carnes-Stine J.,
RA   Caulk P., Chiang Y.H., Coyne M., Dahlke C., Mays A., Dombroski M.,
RA   Donnelly M., Ely D., Esparham S., Fosler C., Gire H., Glanowski S.,
RA   Glasser K., Glodek A., Gorokhov M., Graham K., Gropman B., Harris M.,
RA   Heil J., Henderson S., Hoover J., Jennings D., Jordan C., Jordan J.,
RA   Kasha J., Kagan L., Kraft C., Levitsky A., Lewis M., Liu X., Lopez J.,
RA   Ma D., Majoros W., McDaniel J., Murphy S., Newman M., Nguyen T., Nguyen N.,
RA   Nodell M., Pan S., Peck J., Peterson M., Rowe W., Sanders R., Scott J.,
RA   Simpson M., Smith T., Sprague A., Stockwell T., Turner R., Venter E.,
RA   Wang M., Wen M., Wu D., Wu M., Xia A., Zandieh A., Zhu X.;
RT   "The sequence of the human genome.";
RL   Science 291:1304-1351(2001).
RN   [2] {ECO:0000313|EMBL:EAW79538.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Mural R.J., Istrail S., Sutton 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   [3] {ECO:0000313|EMBL:ADZ17348.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Liver {ECO:0000313|EMBL:ADZ17348.1};
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.
CC   -!- FUNCTION: Nuclear receptor that acts as a transcription factor
CC       regulating genes involved in the metabolism and excretion of
CC       xenobiotics, drugs, and endogenous compounds. Activated by a broad
CC       range of endogenous steroids (e.g. pregnenolone, progesterone) and
CC       xenobiotics, including the antibiotic rifampicin and certain plant-
CC       derived metabolites. Upon ligand binding, translocates to the nucleus,
CC       forms a heterodimer with the retinoid X receptor/RXR, and binds to
CC       response elements in target promoters, leading to transcriptional
CC       activation. Target genes include cytochrome P450 enzymes such as CYP3A4
CC       and ATP-binding cassette transporters including ABCB1/MDR1.
CC       {ECO:0000256|ARBA:ARBA00094202}.
CC   -!- SUBUNIT: Heterodimer with RXR. Interacts with NCOA1. Interacts (via
CC       domain NR LBD) with CRY1 and CRY2 in a ligand-dependent manner.
CC       Interacts with FBXO44; this interaction promotes NR1I2 ubiquitination
CC       and proteasomal degradation. {ECO:0000256|ARBA:ARBA00094815}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC       ECO:0000256|PROSITE-ProRule:PRU00407, ECO:0000256|RuleBase:RU004334}.
CC   -!- SIMILARITY: Belongs to the nuclear hormone receptor family. NR1
CC       subfamily. {ECO:0000256|ARBA:ARBA00008092}.
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DR   EMBL; HQ692837; ADZ17348.1; -; mRNA.
DR   EMBL; CH471052; EAW79538.1; -; Genomic_DNA.
DR   RefSeq; NP_071285.1; NM_022002.3.
DR   AlphaFoldDB; F1D8P9; -.
DR   SMR; F1D8P9; -.
DR   Antibodypedia; 16619; 425 antibodies from 43 providers.
DR   DNASU; 8856; -.
DR   GeneID; 8856; -.
DR   CTD; 8856; -.
DR   DisGeNET; 8856; -.
DR   VEuPathDB; HostDB:ENSG00000144852; -.
DR   OMA; GTCEITQ; -.
DR   OrthoDB; 6355676at2759; -.
DR   BioGRID-ORCS; 8856; 10 hits in 1183 CRISPR screens.
DR   ExpressionAtlas; F1D8P9; baseline and differential.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0004879; F:nuclear receptor activity; IEA:UniProtKB-ARBA.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   CDD; cd07162; NR_DBD_PXR; 1.
DR   CDD; cd06934; NR_LBD_PXR_like; 1.
DR   FunFam; 1.10.565.10:FF:000024; Nuclear receptor subfamily 1 group I member 2; 1.
DR   FunFam; 3.30.50.10:FF:000033; Nuclear receptor subfamily 1 group I member 2; 1.
DR   Gene3D; 3.30.50.10; Erythroid Transcription Factor GATA-1, subunit A; 1.
DR   Gene3D; 1.10.565.10; Retinoid X Receptor; 1.
DR   InterPro; IPR035500; NHR-like_dom_sf.
DR   InterPro; IPR000536; Nucl_hrmn_rcpt_lig-bd.
DR   InterPro; IPR050234; Nuclear_hormone_rcpt_NR1.
DR   InterPro; IPR001723; Nuclear_hrmn_rcpt.
DR   InterPro; IPR001628; Znf_hrmn_rcpt.
DR   InterPro; IPR013088; Znf_NHR/GATA.
DR   PANTHER; PTHR24082; NUCLEAR HORMONE RECEPTOR; 1.
DR   PANTHER; PTHR24082:SF39; NUCLEAR RECEPTOR SUBFAMILY 1 GROUP I MEMBER 2; 1.
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; SSF57716; Glucocorticoid receptor-like (DNA-binding domain); 1.
DR   SUPFAM; SSF48508; Nuclear receptor ligand-binding domain; 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 {ECO:0000256|ARBA:ARBA00023159};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|PROSITE-
KW   ProRule:PRU00407};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU004334};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PROSITE-
KW   ProRule:PRU00407}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000256|PROSITE-
KW   ProRule:PRU01189};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163, ECO:0000256|PROSITE-
KW   ProRule:PRU00407};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00023015,
KW   ECO:0000256|PROSITE-ProRule:PRU00407};
KW   Ubl conjugation {ECO:0000256|ARBA:ARBA00022843};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU004334};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00407}.
FT   DOMAIN          77..153
FT                   /note="Nuclear receptor"
FT                   /evidence="ECO:0000259|PROSITE:PS51030"
FT   DOMAIN          185..472
FT                   /note="NR LBD"
FT                   /evidence="ECO:0000259|PROSITE:PS51843"
FT   DNA_BIND        77..153
FT                   /note="Nuclear receptor"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00407"
FT   REGION          461..472
FT                   /note="AF-2"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01189"
SQ   SEQUENCE   473 AA;  53899 MW;  3049D23C9B903016 CRC64;
     MTVTRTHHFK EGSLRAPAIP LHSAAAELAS NHPRGPEANL EVRPKESWNH ADFVHCEDTE
     SVPGKPSVNA DEEVGGPQIC RVCGDKATGY HFNVMTCEGC KGFFRRAMKR NARLRCPFRK
     GACEITRKTR RQCQACRLRK CLESGMKKEM IMSDEAVEER RALIKRKKSE RTGTQPLGVQ
     GLTEEQRMMI RELMDAQMKT FDTTFSHFKN FRLPGVLSSG CELPESLQAP SREEAAKWSQ
     VRKDLCSLKV SLQLRGEDGS VWNYKPPADS GGKEIFSLLP HMADMSTYMF KGIISFAKVI
     SYFRDLPIED QISLLKGAAF ELCQLRFNTV FNAETGTWEC GRLSYCLEDT AGGFQQLLLE
     PMLKFHYMLK KLQLHEEEYV LMQAISLFSP DRPGVLQHRV VDQLQEQFAI TLKSYIECNR
     PQPAHRFLFL KIMAMLTELR SINAQHTQRL LRIQDIHPFA TPLMQELFGI TGS
//