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 27-MAR-2024, entry version 220. 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), ALTERNATIVE SPLICING, AND FUNCTION RP (MICROBIAL INFECTION). 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 (MICROBIAL INFECTION), AND INTERACTION WITH HNF1A. RX PubMed=14728801; DOI=10.1038/sj.cr.7290187; RA Cai Y.N., Zhou Q., Kong Y.Y., Li M., Viollet B., Xie Y.H., Wang Y.; RT "LRH-1/hB1F and HNF1 synergistically up-regulate hepatitis B virus gene RT transcription and DNA replication."; RL Cell Res. 13:451-458(2003). RN [11] 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 [12] 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 [13] 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 [14] 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 [15] {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). May be CC responsible for the liver-specific activity of enhancer II, probably in CC combination with other hepatocyte transcription factors. Key regulator CC of cholesterol 7-alpha-hydroxylase gene (CYP7A) expression in liver. CC May also contribute to the regulation of pancreas-specific genes and CC play important roles in embryonic development. Activates the CC 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 -!- FUNCTION: (Microbial infection) Plays a crucial role for hepatitis B CC virus gene transcription and DNA replication. Mechanistically, CC synergistically cooperates with HNF1A to up-regulate the activity of CC one of the critical cis-elements in the hepatitis B virus genome CC enhancer II (ENII). {ECO:0000269|PubMed:14728801, CC ECO:0000269|PubMed:9786908}. 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). Interacts with CC HNF1A (PubMed:14728801). {ECO:0000250, ECO:0000269|PubMed:14728801, 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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. 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 PDB; 7TT8; X-ray; 2.80 A; A=299-541. DR PDB; 8F8M; X-ray; 2.60 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 PDBsum; 7TT8; -. DR PDBsum; 8F8M; -. DR AlphaFoldDB; O00482; -. DR SASBDB; O00482; -. DR SMR; O00482; -. DR BioGRID; 108772; 32. 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; 9606-ENSP00000356331; -. DR PeptideAtlas; O00482; -. DR ProteomicsDB; 47928; -. [O00482-1] DR ProteomicsDB; 47929; -. [O00482-2] DR ProteomicsDB; 47930; -. [O00482-3] DR ProteomicsDB; 5842; -. DR Antibodypedia; 1690; 521 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 AGR; HGNC:7984; -. 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; DNMQVSQ; -. DR OrthoDB; 2968690at2759; -. 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; 19 hits in 1173 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 105 other cell types or tissues. DR ExpressionAtlas; O00482; baseline and differential. 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:0045893; P:positive regulation of DNA-templated transcription; IDA:BHF-UCL. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; 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:0006355; P:regulation of DNA-templated transcription; IDA:UniProtKB. DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central. DR GO; GO:0009888; P:tissue development; IBA:GO_Central. DR CDD; cd07167; NR_DBD_Lrh-1_like; 1. DR CDD; cd07069; NR_LBD_Lrh-1; 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 IDEAL; IID00001; -. DR InterPro; IPR035500; NHR-like_dom_sf. DR InterPro; IPR016355; NR5-like. 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; NUCLEAR RECEPTOR SUBFAMILY 5 GROUP A; 1. DR PANTHER; PTHR24086:SF18; NUCLEAR RECEPTOR SUBFAMILY 5 GROUP A MEMBER 2; 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; 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. DR Genevisible; O00482; HS. 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 FT anti-inflammatory role during the hepatic acute phase FT 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:7JYD" 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 //