NR5A2_HUMAN
ID NR5A2_HUMAN Reviewed; 541 AA.
AC O00482; B4E2P3; O95642; Q147U3;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 2.
DT 03-AUG-2022, entry version 211.
DE RecName: Full=Nuclear receptor subfamily 5 group A member 2;
DE AltName: Full=Alpha-1-fetoprotein transcription factor;
DE AltName: Full=B1-binding factor;
DE Short=hB1F;
DE AltName: Full=CYP7A promoter-binding factor;
DE AltName: Full=Hepatocytic transcription factor;
DE AltName: Full=Liver receptor homolog 1;
DE Short=LRH-1;
GN Name=NR5A2; Synonyms=B1F, CPF, FTF;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND ALTERNATIVE SPLICING.
RC TISSUE=Liver;
RX PubMed=9786908; DOI=10.1074/jbc.273.44.29022;
RA Li M., Xie Y.-H., Kong Y.-Y., Wu X., Zhu L., Wang Y.;
RT "Cloning and characterization of a novel human hepatocyte transcription
RT factor, hB1F, which binds and activates enhancer II of hepatitis B virus.";
RL J. Biol. Chem. 273:29022-29031(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC TISSUE=Hepatoma;
RA Li M., Xie Y.-H., Wang Y.;
RL Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3).
RC TISSUE=Liver;
RX PubMed=10359768; DOI=10.1073/pnas.96.12.6660;
RA Nitta M., Ku S., Brown C., Okamoto A.Y., Shan B.;
RT "CPF: an orphan nuclear receptor that regulates liver-specific expression
RT of the human cholesterol 7alpha-hydroxylase gene.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:6660-6665(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING.
RX PubMed=11595170; DOI=10.1016/s0378-1119(01)00586-8;
RA Zhang C.K., Lin W., Cai Y.N., Xu P.L., Dong H., Li M., Kong Y.Y., Fu G.,
RA Xie Y.H., Huang G.M., Wang Y.;
RT "Characterization of the genomic structure and tissue-specific promoter of
RT the human nuclear receptor NR5A2 (hB1F) gene.";
RL Gene 273:239-249(2001).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC TISSUE=Trachea;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [9]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 41-541.
RX PubMed=9858833; DOI=10.1159/000015116;
RA Galarneau L., Drouin R., Belanger L.;
RT "Assignment of the fetoprotein transcription factor gene (FTF) to human
RT chromosome band 1q32.11 by in situ hybridization.";
RL Cytogenet. Cell Genet. 82:269-270(1998).
RN [10]
RP FUNCTION, INTERACTION WITH GPS2, SUMOYLATION AT LYS-270, AND MUTAGENESIS OF
RP LYS-270.
RX PubMed=20159957; DOI=10.1101/gad.545110;
RA Venteclef N., Jakobsson T., Ehrlund A., Damdimopoulos A., Mikkonen L.,
RA Ellis E., Nilsson L.M., Parini P., Jaenne O.A., Gustafsson J.A.,
RA Steffensen K.R., Treuter E.;
RT "GPS2-dependent corepressor/SUMO pathways govern anti-inflammatory actions
RT of LRH-1 and LXRbeta in the hepatic acute phase response.";
RL Genes Dev. 24:381-395(2010).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 300-541 IN COMPLEX WITH NCOA2 AND
RP PHOSPHOLIPIDS, AND FUNCTION.
RX PubMed=15707893; DOI=10.1016/j.cell.2005.01.024;
RA Krylova I.N., Sablin E.P., Moore J., Xu R.X., Waitt G.M., MacKay J.A.,
RA Juzumiene D., Bynum J.M., Madauss K., Montana V., Lebedeva L., Suzawa M.,
RA Williams J.D., Williams S.P., Guy R.K., Thornton J.W., Fletterick R.J.,
RA Willson T.M., Ingraham H.A.;
RT "Structural analyses reveal phosphatidyl inositols as ligands for the NR5
RT orphan receptors SF-1 and LRH-1.";
RL Cell 120:343-355(2005).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 79-187 IN COMPLEX WITH DNA,
RP MUTAGENESIS OF TYR-96; PHE-168; 169-GLY-PRO-170 AND TYR-172, AND FUNCTION.
RX PubMed=16289203; DOI=10.1016/j.jmb.2005.10.009;
RA Solomon I.H., Hager J.M., Safi R., McDonnell D.P., Redinbo M.R.,
RA Ortlund E.A.;
RT "Crystal structure of the human LRH-1 DBD-DNA complex reveals Ftz-F1 domain
RT positioning is required for receptor activity.";
RL J. Mol. Biol. 354:1091-1102(2005).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 290-541 IN COMPLEX WITH NR0B2 AND
RP PHOSPHOLIPID, MUTAGENESIS OF PHE-342 AND ILE-416, AND FUNCTION.
RX PubMed=15723037; DOI=10.1038/nsmb910;
RA Ortlund E.A., Lee Y., Solomon I.H., Hager J.M., Safi R., Choi Y., Guan Z.,
RA Tripathy A., Raetz C.R.H., McDonnell D.P., Moore D.D., Redinbo M.R.;
RT "Modulation of human nuclear receptor LRH-1 activity by phospholipids and
RT SHP.";
RL Nat. Struct. Mol. Biol. 12:357-363(2005).
RN [14] {ECO:0007744|PDB:1ZDU}
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 297-541 IN COMPLEX WITH NCOA2 AND
RP PHOSPHATIDYLGLYCEROL-PHOSPHOGLYCEROL, AND FUNCTION.
RX PubMed=15897460; DOI=10.1073/pnas.0409482102;
RA Wang W., Zhang C., Marimuthu A., Krupka H.I., Tabrizizad M., Shelloe R.,
RA Mehra U., Eng K., Nguyen H., Settachatgul C., Powell B., Milburn M.V.,
RA West B.L.;
RT "The crystal structures of human steroidogenic factor-1 and liver receptor
RT homologue-1.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:7505-7510(2005).
CC -!- FUNCTION: Nuclear receptor that acts as a key metabolic sensor by
CC regulating the expression of genes involved in bile acid synthesis,
CC cholesterol homeostasis and triglyceride synthesis. Together with the
CC oxysterol receptors NR1H3/LXR-alpha and NR1H2/LXR-beta, acts as an
CC essential transcriptional regulator of lipid metabolism. Plays an anti-
CC inflammatory role during the hepatic acute phase response by acting as
CC a corepressor: inhibits the hepatic acute phase response by preventing
CC dissociation of the N-Cor corepressor complex (PubMed:20159957). Binds
CC to the sequence element 5'-AACGACCGACCTTGAG-3' of the enhancer II of
CC hepatitis B virus genes, a critical cis-element of their expression and
CC regulation. May be responsible for the liver-specific activity of
CC enhancer II, probably in combination with other hepatocyte
CC transcription factors. Key regulator of cholesterol 7-alpha-hydroxylase
CC gene (CYP7A) expression in liver. May also contribute to the regulation
CC of pancreas-specific genes and play important roles in embryonic
CC development. Activates the transcription of CYP2C38 (By similarity).
CC {ECO:0000250|UniProtKB:P45448, ECO:0000269|PubMed:15707893,
CC ECO:0000269|PubMed:15723037, ECO:0000269|PubMed:15897460,
CC ECO:0000269|PubMed:16289203, ECO:0000269|PubMed:20159957}.
CC -!- SUBUNIT: Binds DNA as a monomer (By similarity). Interacts with GRIP1,
CC NCOA2 and NR0B2 (PubMed:15707893, PubMed:15723037, PubMed:15897460,
CC PubMed:16289203). Interacts (when sumoylated) with GPS2; interaction
CC with GPS2 onto hepatic acute phase protein promoters prevents N-Cor
CC corepressor complex dissociation (PubMed:20159957). {ECO:0000250,
CC ECO:0000269|PubMed:15707893, ECO:0000269|PubMed:15723037,
CC ECO:0000269|PubMed:15897460, ECO:0000269|PubMed:16289203,
CC ECO:0000269|PubMed:20159957}.
CC -!- INTERACTION:
CC O00482; O60869: EDF1; NbExp=2; IntAct=EBI-781320, EBI-781301;
CC O00482-1; P35222: CTNNB1; NbExp=5; IntAct=EBI-15960777, EBI-491549;
CC O00482-1; Q15596: NCOA2; NbExp=2; IntAct=EBI-15960777, EBI-81236;
CC O00482-1; Q15466: NR0B2; NbExp=2; IntAct=EBI-15960777, EBI-3910729;
CC O00482-2; Q6P1K8: GTF2H2C_2; NbExp=3; IntAct=EBI-9257474, EBI-8469755;
CC O00482-2; Q92786: PROX1; NbExp=9; IntAct=EBI-9257474, EBI-3912635;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=2; Synonyms=B1F2;
CC IsoId=O00482-1; Sequence=Displayed;
CC Name=1;
CC IsoId=O00482-2; Sequence=VSP_003716;
CC Name=3;
CC IsoId=O00482-3; Sequence=VSP_003717;
CC Name=4;
CC IsoId=O00482-4; Sequence=VSP_054548;
CC -!- TISSUE SPECIFICITY: Abundantly expressed in pancreas, less in liver,
CC very low levels in heart and lung. Expressed in the Hep-G2 cell line.
CC Isoform 1 and isoform 2 seem to be present in fetal and adult liver and
CC Hep-G2 cells.
CC -!- PTM: Sumoylated by SUMO1 at Lys-270 during the hepatic acute phase
CC response, leading to promote interaction with GPS2 and prevent N-Cor
CC corepressor complex dissociation. {ECO:0000269|PubMed:20159957}.
CC -!- MISCELLANEOUS: [Isoform 3]: Does not induce CYP7A promoter activity.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the nuclear hormone receptor family. NR5
CC subfamily. {ECO:0000305}.
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DR EMBL; U80251; AAC78727.1; -; mRNA.
DR EMBL; AF146343; AAD37378.1; -; mRNA.
DR EMBL; AF124247; AAD26565.1; -; mRNA.
DR EMBL; AF190464; AAG17124.1; -; Genomic_DNA.
DR EMBL; AF190464; AAG17125.1; -; Genomic_DNA.
DR EMBL; AK304365; BAG65205.1; -; mRNA.
DR EMBL; AK316513; BAH14884.1; -; mRNA.
DR EMBL; AC096633; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471067; EAW91306.1; -; Genomic_DNA.
DR EMBL; BC118571; AAI18572.1; -; mRNA.
DR EMBL; BC118652; AAI18653.1; -; mRNA.
DR EMBL; U93553; AAD03155.1; -; mRNA.
DR CCDS; CCDS1400.1; -. [O00482-2]
DR CCDS; CCDS1401.1; -. [O00482-1]
DR CCDS; CCDS60383.1; -. [O00482-4]
DR RefSeq; NP_001263393.1; NM_001276464.1. [O00482-4]
DR RefSeq; NP_003813.1; NM_003822.4. [O00482-2]
DR RefSeq; NP_995582.1; NM_205860.2. [O00482-1]
DR RefSeq; XP_005245119.1; XM_005245062.3. [O00482-4]
DR RefSeq; XP_011507684.1; XM_011509382.1. [O00482-4]
DR PDB; 1YOK; X-ray; 2.50 A; A=300-541.
DR PDB; 1YUC; X-ray; 1.90 A; A/B=290-541.
DR PDB; 1ZDU; X-ray; 2.50 A; A=297-541.
DR PDB; 2A66; X-ray; 2.20 A; A=79-187.
DR PDB; 3PLZ; X-ray; 1.75 A; A/B=300-541.
DR PDB; 3TX7; X-ray; 2.76 A; B=191-541.
DR PDB; 4DOR; X-ray; 1.90 A; A/B=290-541.
DR PDB; 4DOS; X-ray; 2.00 A; A=299-538.
DR PDB; 4IS8; X-ray; 2.78 A; A/B=300-538.
DR PDB; 4ONI; X-ray; 1.80 A; A/B=291-541.
DR PDB; 4PLD; X-ray; 1.75 A; A=301-541.
DR PDB; 4PLE; X-ray; 1.75 A; A/C/E/G=301-541.
DR PDB; 4RWV; X-ray; 1.86 A; A=294-541.
DR PDB; 5L0M; X-ray; 2.20 A; A=79-187.
DR PDB; 5L11; X-ray; 1.85 A; A=299-541.
DR PDB; 5SYZ; X-ray; 1.93 A; A=297-538.
DR PDB; 5UNJ; X-ray; 1.96 A; A=299-541.
DR PDB; 6OQX; X-ray; 2.00 A; A=299-541.
DR PDB; 6OQY; X-ray; 2.23 A; A=299-541.
DR PDB; 6OR1; X-ray; 2.17 A; A=299-541.
DR PDB; 6VC2; X-ray; 1.70 A; A=299-541.
DR PDB; 6VIF; X-ray; 2.26 A; A=299-541.
DR PDB; 7JYD; X-ray; 2.30 A; A=299-541.
DR PDB; 7JYE; X-ray; 2.55 A; A=299-541.
DR PDBsum; 1YOK; -.
DR PDBsum; 1YUC; -.
DR PDBsum; 1ZDU; -.
DR PDBsum; 2A66; -.
DR PDBsum; 3PLZ; -.
DR PDBsum; 3TX7; -.
DR PDBsum; 4DOR; -.
DR PDBsum; 4DOS; -.
DR PDBsum; 4IS8; -.
DR PDBsum; 4ONI; -.
DR PDBsum; 4PLD; -.
DR PDBsum; 4PLE; -.
DR PDBsum; 4RWV; -.
DR PDBsum; 5L0M; -.
DR PDBsum; 5L11; -.
DR PDBsum; 5SYZ; -.
DR PDBsum; 5UNJ; -.
DR PDBsum; 6OQX; -.
DR PDBsum; 6OQY; -.
DR PDBsum; 6OR1; -.
DR PDBsum; 6VC2; -.
DR PDBsum; 6VIF; -.
DR PDBsum; 7JYD; -.
DR PDBsum; 7JYE; -.
DR AlphaFoldDB; O00482; -.
DR SASBDB; O00482; -.
DR SMR; O00482; -.
DR BioGRID; 108772; 31.
DR CORUM; O00482; -.
DR DIP; DIP-37952N; -.
DR IntAct; O00482; 11.
DR MINT; O00482; -.
DR STRING; 9606.ENSP00000356331; -.
DR BindingDB; O00482; -.
DR ChEMBL; CHEMBL3544; -.
DR GuidetoPHARMACOLOGY; 633; -.
DR SwissLipids; SLP:000001542; -.
DR TCDB; 9.B.208.1.4; the vitamin d3 receptor (vdr) family.
DR iPTMnet; O00482; -.
DR PhosphoSitePlus; O00482; -.
DR BioMuta; NR5A2; -.
DR jPOST; O00482; -.
DR MassIVE; O00482; -.
DR PaxDb; O00482; -.
DR PeptideAtlas; O00482; -.
DR PRIDE; O00482; -.
DR ProteomicsDB; 47928; -. [O00482-1]
DR ProteomicsDB; 47929; -. [O00482-2]
DR ProteomicsDB; 47930; -. [O00482-3]
DR ProteomicsDB; 5842; -.
DR Antibodypedia; 1690; 491 antibodies from 40 providers.
DR DNASU; 2494; -.
DR Ensembl; ENST00000236914.7; ENSP00000236914.3; ENSG00000116833.14. [O00482-2]
DR Ensembl; ENST00000367362.8; ENSP00000356331.3; ENSG00000116833.14. [O00482-1]
DR Ensembl; ENST00000544748.5; ENSP00000439116.1; ENSG00000116833.14. [O00482-4]
DR GeneID; 2494; -.
DR KEGG; hsa:2494; -.
DR MANE-Select; ENST00000367362.8; ENSP00000356331.3; NM_205860.3; NP_995582.1.
DR UCSC; uc001gvb.5; human. [O00482-1]
DR CTD; 2494; -.
DR DisGeNET; 2494; -.
DR GeneCards; NR5A2; -.
DR HGNC; HGNC:7984; NR5A2.
DR HPA; ENSG00000116833; Group enriched (intestine, liver, pancreas).
DR MIM; 604453; gene.
DR neXtProt; NX_O00482; -.
DR OpenTargets; ENSG00000116833; -.
DR PharmGKB; PA31765; -.
DR VEuPathDB; HostDB:ENSG00000116833; -.
DR eggNOG; KOG4218; Eukaryota.
DR GeneTree; ENSGT00940000153391; -.
DR HOGENOM; CLU_011437_0_0_1; -.
DR InParanoid; O00482; -.
DR OMA; FLMVEWA; -.
DR OrthoDB; 619653at2759; -.
DR PhylomeDB; O00482; -.
DR TreeFam; TF350737; -.
DR PathwayCommons; O00482; -.
DR Reactome; R-HSA-210747; Regulation of gene expression in early pancreatic precursor cells. [O00482-1]
DR Reactome; R-HSA-383280; Nuclear Receptor transcription pathway.
DR Reactome; R-HSA-4090294; SUMOylation of intracellular receptors. [O00482-2]
DR Reactome; R-HSA-9018519; Estrogen-dependent gene expression.
DR SignaLink; O00482; -.
DR SIGNOR; O00482; -.
DR BioGRID-ORCS; 2494; 17 hits in 1090 CRISPR screens.
DR ChiTaRS; NR5A2; human.
DR EvolutionaryTrace; O00482; -.
DR GeneWiki; Liver_receptor_homolog-1; -.
DR GenomeRNAi; 2494; -.
DR Pharos; O00482; Tchem.
DR PRO; PR:O00482; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; O00482; protein.
DR Bgee; ENSG00000116833; Expressed in body of pancreas and 104 other tissues.
DR ExpressionAtlas; O00482; baseline and differential.
DR Genevisible; O00482; HS.
DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
DR GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:BHF-UCL.
DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; ISS:BHF-UCL.
DR GO; GO:0003682; F:chromatin binding; ISS:BHF-UCL.
DR GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IEA:Ensembl.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:UniProtKB.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB.
DR GO; GO:0004879; F:nuclear receptor activity; IDA:BHF-UCL.
DR GO; GO:0005543; F:phospholipid binding; IDA:UniProtKB.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; ISS:BHF-UCL.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:UniProtKB.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IDA:ARUK-UCL.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IDA:BHF-UCL.
DR GO; GO:0001221; F:transcription coregulator binding; IPI:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0090425; P:acinar cell differentiation; IEA:Ensembl.
DR GO; GO:0008206; P:bile acid metabolic process; IEA:Ensembl.
DR GO; GO:0097720; P:calcineurin-mediated signaling; IEA:Ensembl.
DR GO; GO:1990830; P:cellular response to leukemia inhibitory factor; IEA:Ensembl.
DR GO; GO:0042632; P:cholesterol homeostasis; IEA:Ensembl.
DR GO; GO:0009792; P:embryo development ending in birth or egg hatching; TAS:UniProtKB.
DR GO; GO:0042592; P:homeostatic process; NAS:UniProtKB.
DR GO; GO:0009755; P:hormone-mediated signaling pathway; IBA:GO_Central.
DR GO; GO:0061113; P:pancreas morphogenesis; IEA:Ensembl.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:BHF-UCL.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:BHF-UCL.
DR GO; GO:0045070; P:positive regulation of viral genome replication; IDA:BHF-UCL.
DR GO; GO:0042127; P:regulation of cell population proliferation; IEA:Ensembl.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0009888; P:tissue development; IBA:GO_Central.
DR Gene3D; 1.10.565.10; -; 1.
DR Gene3D; 3.30.50.10; -; 1.
DR IDEAL; IID00001; -.
DR InterPro; IPR035500; NHR-like_dom_sf.
DR InterPro; IPR016355; NR5_fam.
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 PANTHER; PTHR24086; PTHR24086; 1.
DR Pfam; PF00104; Hormone_recep; 1.
DR Pfam; PF00105; zf-C4; 1.
DR PIRSF; PIRSF002530; Nuc_orph_FTZ-F1; 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 1: Evidence at protein level;
KW 3D-structure; Activator; Alternative splicing; DNA-binding;
KW Isopeptide bond; Lipid-binding; Metal-binding; Nucleus; Receptor;
KW Reference proteome; Transcription; Transcription regulation;
KW Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..541
FT /note="Nuclear receptor subfamily 5 group A member 2"
FT /id="PRO_0000053735"
FT DOMAIN 300..539
FT /note="NR LBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01189"
FT DNA_BIND 83..154
FT /note="Nuclear receptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT ZN_FING 86..106
FT /note="NR C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT ZN_FING 122..146
FT /note="NR C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT REGION 1..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 155..184
FT /note="FTZ-F1 box"
FT BINDING 421..424
FT /ligand="a phosphatidylglycerol phosphate"
FT /ligand_id="ChEBI:CHEBI:60522"
FT /evidence="ECO:0000269|PubMed:15897460"
FT BINDING 516
FT /ligand="a phosphatidylglycerol phosphate"
FT /ligand_id="ChEBI:CHEBI:60522"
FT /evidence="ECO:0000269|PubMed:15897460"
FT BINDING 520
FT /ligand="a phosphatidylglycerol phosphate"
FT /ligand_id="ChEBI:CHEBI:60522"
FT /evidence="ECO:0000269|PubMed:15897460"
FT CROSSLNK 270
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1)"
FT /evidence="ECO:0000269|PubMed:20159957"
FT VAR_SEQ 1..72
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_054548"
FT VAR_SEQ 22..67
FT /note="Missing (in isoform 1)"
FT /evidence="ECO:0000303|PubMed:10359768,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:9786908"
FT /id="VSP_003716"
FT VAR_SEQ 199..370
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:10359768"
FT /id="VSP_003717"
FT MUTAGEN 96
FT /note="Y->A: Slightly reduced DNA binding. Strongly reduced
FT transactivation; when associated with A-168 and A-172."
FT /evidence="ECO:0000269|PubMed:16289203"
FT MUTAGEN 168
FT /note="F->A: Slightly reduced DNA binding. Strongly reduced
FT transactivation; when associated with A-96 and A-172."
FT /evidence="ECO:0000269|PubMed:16289203"
FT MUTAGEN 169..170
FT /note="GP->VA: Reduced DNA binding. Loss of
FT transactivation."
FT /evidence="ECO:0000269|PubMed:16289203"
FT MUTAGEN 172
FT /note="Y->A: Slightly reduced DNA binding. Strongly reduced
FT transactivation; when associated with A-96 and A-168."
FT /evidence="ECO:0000269|PubMed:16289203"
FT MUTAGEN 270
FT /note="K->R: Impaired ability to act as an anti-
FT inflammatory role during the hepatic acute phase response."
FT /evidence="ECO:0000269|PubMed:20159957"
FT MUTAGEN 342
FT /note="F->W: Reduced phospholipid binding. Strongly reduced
FT transactivation; when associated with W-416."
FT /evidence="ECO:0000269|PubMed:15723037"
FT MUTAGEN 416
FT /note="I->W: Reduced phospholipid binding. Strongly reduced
FT transactivation; when associated with W-342."
FT /evidence="ECO:0000269|PubMed:15723037"
FT CONFLICT 250..251
FT /note="PP -> L (in Ref. 9; AAD03155)"
FT /evidence="ECO:0000305"
FT CONFLICT 353
FT /note="L -> V (in Ref. 9; AAD03155)"
FT /evidence="ECO:0000305"
FT TURN 87..89
FT /evidence="ECO:0007829|PDB:5L0M"
FT STRAND 95..97
FT /evidence="ECO:0007829|PDB:5L0M"
FT STRAND 100..102
FT /evidence="ECO:0007829|PDB:5L0M"
FT HELIX 104..115
FT /evidence="ECO:0007829|PDB:5L0M"
FT TURN 132..137
FT /evidence="ECO:0007829|PDB:5L0M"
FT HELIX 139..148
FT /evidence="ECO:0007829|PDB:5L0M"
FT HELIX 153..155
FT /evidence="ECO:0007829|PDB:5L0M"
FT TURN 167..170
FT /evidence="ECO:0007829|PDB:5L0M"
FT HELIX 171..175
FT /evidence="ECO:0007829|PDB:5L0M"
FT HELIX 303..310
FT /evidence="ECO:0007829|PDB:6VC2"
FT HELIX 315..332
FT /evidence="ECO:0007829|PDB:6VC2"
FT HELIX 335..337
FT /evidence="ECO:0007829|PDB:4PLD"
FT HELIX 341..361
FT /evidence="ECO:0007829|PDB:6VC2"
FT HELIX 366..368
FT /evidence="ECO:0007829|PDB:6VC2"
FT HELIX 371..397
FT /evidence="ECO:0007829|PDB:6VC2"
FT STRAND 402..404
FT /evidence="ECO:0007829|PDB:6VC2"
FT STRAND 410..412
FT /evidence="ECO:0007829|PDB:6VC2"
FT HELIX 413..440
FT /evidence="ECO:0007829|PDB:6VC2"
FT HELIX 445..456
FT /evidence="ECO:0007829|PDB:6VC2"
FT HELIX 467..488
FT /evidence="ECO:0007829|PDB:6VC2"
FT STRAND 490..492
FT /evidence="ECO:0007829|PDB:4IS8"
FT HELIX 495..522
FT /evidence="ECO:0007829|PDB:6VC2"
FT STRAND 528..530
FT /evidence="ECO:0007829|PDB:6OQX"
FT HELIX 531..537
FT /evidence="ECO:0007829|PDB:6VC2"
SQ SEQUENCE 541 AA; 61331 MW; 7B07170C075490FE CRC64;
MSSNSDTGDL QESLKHGLTP IGAGLPDRHG SPIPARGRLV MLPKVETEAL GLARSHGEQG
QMPENMQVSQ FKMVNYSYDE DLEELCPVCG DKVSGYHYGL LTCESCKGFF KRTVQNNKRY
TCIENQNCQI DKTQRKRCPY CRFQKCLSVG MKLEAVRADR MRGGRNKFGP MYKRDRALKQ
QKKALIRANG LKLEAMSQVI QAMPSDLTIS SAIQNIHSAS KGLPLNHAAL PPTDYDRSPF
VTSPISMTMP PHGSLQGYQT YGHFPSRAIK SEYPDPYTSS PESIMGYSYM DSYQTSSPAS
IPHLILELLK CEPDEPQVQA KIMAYLQQEQ ANRSKHEKLS TFGLMCKMAD QTLFSIVEWA
RSSIFFRELK VDDQMKLLQN CWSELLILDH IYRQVVHGKE GSIFLVTGQQ VDYSIIASQA
GATLNNLMSH AQELVAKLRS LQFDQREFVC LKFLVLFSLD VKNLENFQLV EGVQEQVNAA
LLDYTMCNYP QQTEKFGQLL LRLPEIRAIS MQAEEYLYYK HLNGDVPYNN LLIEMLHAKR
A
