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UniProtKB/Swiss-Prot entry O00482


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name NR5A2_HUMAN
Primary accession number O00482
Secondary accession number O95642
Integrated into Swiss-Prot on July 15, 1998
Sequence was last modified on May 30, 2000 (Sequence version 2)
Annotations were last modified on    June 16, 2009 (Entry version 94)
Name and origin of the protein
Protein name Nuclear receptor subfamily 5 group A member 2
Synonyms Alpha-1-fetoprotein transcription factor
Hepatocytic transcription factor
B1-binding factor
hB1F
CYP7A promoter-binding factor
Liver receptor homolog 1
LRH-1
Gene name
Name: NR5A2
Synonyms: B1F, CPF, FTF
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND ALTERNATIVE SPLICING.
TISSUE=Liver;
DOI=10.1074/jbc.273.44.29022; PubMed=9786908 [NCBI, ExPASy, EBI, Israel, Japan]
Li M., Xie Y.-H., Kong Y.-Y., Wu X., Zhu L., Wang Y.;
"Cloning and characterization of a novel human hepatocyte transcription factor, hB1F, which binds and activates enhancer II of hepatitis B virus.";
J. Biol. Chem. 273:29022-29031(1998).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
TISSUE=Hepatoma;
Li M., Xie Y.-H., Wang Y.;
Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3).
TISSUE=Liver;
DOI=10.1073/pnas.96.12.6660; PubMed=10359768 [NCBI, ExPASy, EBI, Israel, Japan]
Nitta M., Ku S., Brown C., Okamoto A.Y., Shan B.;
"CPF: an orphan nuclear receptor that regulates liver-specific expression of the human cholesterol 7alpha-hydroxylase gene.";
Proc. Natl. Acad. Sci. U.S.A. 96:6660-6665(1999).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING.
DOI=10.1016/S0378-1119(01)00586-8; PubMed=11595170 [NCBI, ExPASy, EBI, Israel, Japan]
Zhang C.K., Lin W., Cai Y.N., Xu P.L., Dong H., Li M., Kong Y.Y., Fu G., Xie Y.H., Huang G.M., Wang Y.;
"Characterization of the genomic structure and tissue-specific promoter of the human nuclear receptor NR5A2 (hB1F) gene.";
Gene 273:239-249(2001).
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 41-541.
PubMed=9858833 [NCBI, ExPASy, EBI, Israel, Japan]
Galarneau L., Drouin R., Belanger L.;
"Assignment of the fetoprotein transcription factor gene (FTF) to human chromosome band 1q32.11 by in situ hybridization.";
Cytogenet. Cell Genet. 82:269-270(1998).
[6]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 300-541 IN COMPLEX WITH NCOA2 AND PHOSPHOLIPIDS.
DOI=10.1016/j.cell.2005.01.024; PubMed=15707893 [NCBI, ExPASy, EBI, Israel, Japan]
Krylova I.N., Sablin E.P., Moore J., Xu R.X., Waitt G.M., MacKay J.A., Juzumiene D., Bynum J.M., Madauss K., Montana V., Lebedeva L., Suzawa M., Williams J.D., Williams S.P., Guy R.K., Thornton J.W., Fletterick R.J., Willson T.M., Ingraham H.A.;
"Structural analyses reveal phosphatidyl inositols as ligands for the NR5 orphan receptors SF-1 and LRH-1.";
Cell 120:343-355(2005).
[7]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 79-187 IN COMPLEX WITH DNA, AND MUTAGENESIS OF TYR-96; PHE-168; 169-GLY-PRO-170 AND TYR-172.
DOI=10.1016/j.jmb.2005.10.009; PubMed=16289203 [NCBI, ExPASy, EBI, Israel, Japan]
Solomon I.H., Hager J.M., Safi R., McDonnell D.P., Redinbo M.R., Ortlund E.A.;
"Crystal structure of the human LRH-1 DBD-DNA complex reveals Ftz-F1 domain positioning is required for receptor activity.";
J. Mol. Biol. 354:1091-1102(2005).
[8]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 290-541 IN COMPLEX WITH NR0B2 AND PHOSPHOLIPID, AND MUTAGENESIS OF PHE-342 AND ILE-416.
DOI=10.1038/nsmb910; PubMed=15723037 [NCBI, ExPASy, EBI, Israel, Japan]
Ortlund E.A., Lee Y., Solomon I.H., Hager J.M., Safi R., Choi Y., Guan Z., Tripathy A., Raetz C.R.H., McDonnell D.P., Moore D.D., Redinbo M.R.;
"Modulation of human nuclear receptor LRH-1 activity by phospholipids and SHP.";
Nat. Struct. Mol. Biol. 12:357-363(2005).
[9]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 297-541 IN COMPLEX WITH NCOA2 AND PHOSPHOLIPID.
DOI=10.1073/pnas.0409482102; PubMed=15897460 [NCBI, ExPASy, EBI, Israel, Japan]
Wang W., Zhang C., Marimuthu A., Krupka H.I., Tabrizizad M., Shelloe R., Mehra U., Eng K., Nguyen H., Settachatgul C., Powell B., Milburn M.V., West B.L.;
"The crystal structures of human steroidogenic factor-1 and liver receptor homologue-1.";
Proc. Natl. Acad. Sci. U.S.A. 102:7505-7510(2005).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
U80251; AAC78727.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF146343; AAD37378.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF124247; AAD26565.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF190464; AAG17124.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF190464; AAG17125.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U93553; AAD03155.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
IPI IPI00011769; -.
IPI00217284; -.
IPI00217285; -.
RefSeq NP_003813.1; -.
NP_995582.1; -.
UniGene Hs.33446
3D structure databases
PDB
1YOK; X-ray; 2.50 A; A=300-541.[ExPASy / RCSB / EBI]
1YUC; X-ray; 1.90 A; A/B=290-541.[ExPASy / RCSB / EBI]
1ZDU; X-ray; 2.50 A; A=297-541.[ExPASy / RCSB / EBI]
2A66; X-ray; 2.20 A; A=79-187.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1YOK; -.
1YUC; -.
1ZDU; -.
2A66; -.
ModBase O00482.
Protein-protein interaction databases
IntAct O00482; 1.
PTM databases
PhosphoSite O00482; -.
Enzyme and pathway databases
Reactome REACT_13698; Regulation of beta-cell development.
Organism-specific databases
GeneCards GC01P198263; -.
H-InvDB HIX0028494; -.
HGNC HGNC:7984; NR5A2.
GenAtlas NR5A2.
HPA HPA005455; -.
HPA017067; -.
MIM 604453; gene. [NCBI / EBI]
PharmGKB PA31765; -.
Gene expression databases
ArrayExpress O00482; -.
Bgee O00482; -.
CleanEx HS_NR5A2; -.
GermOnline ENSG00000116833; Homo sapiens.
Ontologies
GO
GO:0005634; Cellular component: nucleus (inferred from direct assay from HPA).
GO:0008289; Molecular function: lipid binding (inferred from electronic annotation from UniProtKB-KW).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from UniProtKB).
GO:0003705; Molecular function: RNA polymerase II transcription factor activity, enhancer binding (traceable author statement from ProtInc).
GO:0043565; Molecular function: sequence-specific DNA binding (inferred from direct assay from UniProtKB).
GO:0003707; Molecular function: steroid hormone receptor activity (inferred from electronic annotation from InterPro).
GO:0008270; Molecular function: zinc ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0009653; Biological process: anatomical structure morphogenesis (traceable author statement from ProtInc).
GO:0009790; Biological process: embryonic development (traceable author statement from UniProtKB).
GO:0042592; Biological process: homeostatic process (non-traceable author statement from UniProtKB).
GO:0006355; Biological process: regulation of transcription, DNA-dependent (inferred from electronic annotation from UniProtKB-KW).
GO:0006366; Biological process: transcription from RNA polymerase II promoter (traceable author statement from ProtInc).
QuickGo view.
Family and domain databases
InterPro IPR016355; Nuc_orph_rcpt_FTZ-F1.
IPR008946; Nucl_hormone_rcpt_ligand-bd.
IPR000536; Nucl_hrmn_rcpt_lig-bd_core.
IPR001723; Str_hrmn_rcpt.
IPR000324; VitD_rcpt.
IPR001628; Znf_hrmn_rcpt.
IPR013088; Znf_NHR/GATA.
Graphical view of domain structure.
Gene3D G3DSA:1.10.565.10; Nucl_hrmn_rcpt_lig_bd; 1.
G3DSA:3.30.50.10; Znf_NHR/GATA; 1.
Pfam PF00104; Hormone_recep; 1.
PF00105; zf-C4; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF002530; Nuc_orph_FTZ-F1; 1.
PRINTS PR00398; STRDHORMONER.
PR00047; STROIDFINGER.
PR00350; VITAMINDR.
ProDom PD000035; Znf_C4steroid; 1.
[Domain structure / List of seq. sharing at least 1 domain]
SMART SM00430; HOLI; 1.
SM00399; ZnF_C4; 1.
SMART graphical view of domain structure.
PROSITE PS00031; NUCLEAR_REC_DBD_1; 1.
PS51030; NUCLEAR_REC_DBD_2; 1.
PROSITE graphical view of domain structure (profiles).
Proteomic databases
PRIDE O00482; -.
Genome annotation databases
Ensembl ENSG00000116833; Homo sapiens. [Contig view]
GeneID 2494; -.
KEGG hsa:2494; -.
Phylogenomic databases
HOGENOM O00482; -.
HOVERGEN O00482; -.
OMA O00482; YSYMDGY.
Other
BindingDB O00482; -.
NextBio 9851; -.
SOURCE NR5A2; Homo sapiens.
ProtoNet O00482.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Alternative splicing; DNA-binding; Lipid-binding; Metal-binding; Nucleus; Receptor; Transcription; Transcription regulation; Zinc; Zinc-finger.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   541  541     Nuclear receptor subfamily 5 group A member 2. PRO_0000053735
DNA_BIND   83   154  72     Nuclear receptor. 
ZN_FING   86   106  21     NR C4-type. 
ZN_FING   122   146  25     NR C4-type. 
REGION   342   390  49     Ligand-binding. 
REGION   419   424  6     Lipid binding. 
MOTIF   155   184  30     FTZ-F1 box. 
BINDING   516   516        Lipid headgroup. 
BINDING   520   520        Lipid headgroup. 
VAR_SEQ   22    67        Missing (in isoform 1). VSP_003716
VAR_SEQ   199   370        Missing (in isoform 3). VSP_003717
MUTAGEN   96    96        Y->A: Slightly reduced DNA binding. Strongly reduced transactivation; when associated with A-168 and A-172. 
MUTAGEN   168   168        F->A: Slightly reduced DNA binding. Strongly reduced transactivation; when associated with A-96 and A-172. 
MUTAGEN   169   170        GP->VA: Reduced DNA binding. Loss of transactivation. 
MUTAGEN   172   172        Y->A: Slightly reduced DNA binding. Strongly reduced transactivation; when associated with A-96 and A-168. 
MUTAGEN   342   342        F->W: Reduced phospholipid binding. Strongly reduced transactivation; when associated with W-416. 
MUTAGEN   416   416        I->W: Reduced phospholipid binding. Strongly reduced transactivation; when associated with W-342. 
CONFLICT   250   251        PP -> L (in Ref. 5; AAD03155). 
CONFLICT   353   353        L -> V (in Ref. 5; AAD03155). 
TURN   87    89  3      
STRAND   92    97  6      
STRAND   100   103  4      
HELIX   104   115  12      
TURN   132   137  6      
HELIX   139   148  10      
HELIX   153   155  3      
HELIX   169   177  9      
HELIX   303   309  7      
HELIX   315   332  18      
HELIX   341   362  22      
HELIX   366   368  3      
HELIX   371   396  26      
STRAND   402   404  3      
STRAND   410   412  3      
HELIX   413   419  7      
HELIX   422   441  20      
HELIX   445   456  12      
HELIX   467   488  22      
HELIX   495   500  6      
HELIX   502   522  21      
HELIX   531   537  7      
Sequence information
Length: 541 AA [This is the length of the unprocessed precursor] Molecular weight: 61331 Da [This is the MW of the unprocessed precursor] CRC64: 7B07170C075490FE [This is a checksum on the sequence]
        10         20         30         40         50         60 
MSSNSDTGDL QESLKHGLTP IGAGLPDRHG SPIPARGRLV MLPKVETEAL GLARSHGEQG 

        70         80         90        100        110        120 
QMPENMQVSQ FKMVNYSYDE DLEELCPVCG DKVSGYHYGL LTCESCKGFF KRTVQNNKRY 

       130        140        150        160        170        180 
TCIENQNCQI DKTQRKRCPY CRFQKCLSVG MKLEAVRADR MRGGRNKFGP MYKRDRALKQ 

       190        200        210        220        230        240 
QKKALIRANG LKLEAMSQVI QAMPSDLTIS SAIQNIHSAS KGLPLNHAAL PPTDYDRSPF 

       250        260        270        280        290        300 
VTSPISMTMP PHGSLQGYQT YGHFPSRAIK SEYPDPYTSS PESIMGYSYM DSYQTSSPAS 

       310        320        330        340        350        360 
IPHLILELLK CEPDEPQVQA KIMAYLQQEQ ANRSKHEKLS TFGLMCKMAD QTLFSIVEWA 

       370        380        390        400        410        420 
RSSIFFRELK VDDQMKLLQN CWSELLILDH IYRQVVHGKE GSIFLVTGQQ VDYSIIASQA 

       430        440        450        460        470        480 
GATLNNLMSH AQELVAKLRS LQFDQREFVC LKFLVLFSLD VKNLENFQLV EGVQEQVNAA 

       490        500        510        520        530        540 
LLDYTMCNYP QQTEKFGQLL LRLPEIRAIS MQAEEYLYYK HLNGDVPYNN LLIEMLHAKR 


A 

O00482 in FASTA format

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