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Hepatocyte nuclear factor 4-alpha (HNF-4-alpha) (Nuclear receptor subfamily 2 group A member 1) (Transcription factor 14) (TCF-14) (Transcription factor HNF-4)

 HNF4A_MOUSE             Reviewed;         474 AA.
P49698; A2A5I5; A2ICH0; Q3UNX3; Q8CFY1;
01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
29-MAY-2007, sequence version 2.
22-NOV-2017, entry version 167.
RecName: Full=Hepatocyte nuclear factor 4-alpha;
Short=HNF-4-alpha;
AltName: Full=Nuclear receptor subfamily 2 group A member 1;
AltName: Full=Transcription factor 14;
Short=TCF-14;
AltName: Full=Transcription factor HNF-4;
Name=Hnf4a; Synonyms=Hnf-4, Hnf4, Nr2a1, Tcf14;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS LONG AND SHORT).
STRAIN=C57BL/6 X CBA; TISSUE=Liver;
PubMed=7999795; DOI=10.1016/0167-4781(94)00177-5;
Hata S., Inoue T., Kosuga K., Nakashima T., Tsukamoto T., Osumi T.;
"Identification of two splice isoforms of mRNA for mouse hepatocyte
nuclear factor 4 (HNF-4).";
Biochim. Biophys. Acta 1260:55-61(1995).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=CAST/EiJ; TISSUE=Liver;
PubMed=16670015; DOI=10.1186/1471-2164-7-102;
Farber C.R., Corva P.M., Medrano J.F.;
"Genome-wide isolation of growth and obesity QTL using mouse speed
congenic strains.";
BMC Genomics 7:102-102(2006).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Kidney;
PubMed=16141072; DOI=10.1126/science.1112014;
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., 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.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=FVB/N; TISSUE=Kidney;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 21-378.
STRAIN=C57BL/6J; TISSUE=Liver;
Huang J., Karakucuk V., Levitsky L.L., Rhoads D.B.;
"Expression of HNF4 alpha 3 in pancreatic islets and Ins-1 beta
cells.";
Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
[7]
DISRUPTION PHENOTYPE.
PubMed=17407387; DOI=10.1371/journal.pmed.0040118;
Pearson E.R., Boj S.F., Steele A.M., Barrett T., Stals K.,
Shield J.P., Ellard S., Ferrer J., Hattersley A.T.;
"Macrosomia and hyperinsulinaemic hypoglycaemia in patients with
heterozygous mutations in the HNF4A gene.";
PLoS Med. 4:E118-E118(2007).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-429 AND THR-432, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=17242355; DOI=10.1073/pnas.0609836104;
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
"Large-scale phosphorylation analysis of mouse liver.";
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-429 AND SER-436, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Kidney;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[10]
INTERACTION WITH PER2.
PubMed=20159955; DOI=10.1101/gad.564110;
Schmutz I., Ripperger J.A., Baeriswyl-Aebischer S., Albrecht U.;
"The mammalian clock component PERIOD2 coordinates circadian output by
interaction with nuclear receptors.";
Genes Dev. 24:345-357(2010).
-!- FUNCTION: Transcriptionally controlled transcription factor. Binds
to DNA sites required for the transcription of alpha 1-
antitrypsin, apolipoprotein CIII, transthyretin genes and HNF1-
alpha. May be essential for development of the liver, kidney and
intestine.
-!- SUBUNIT: Homodimerization is required for HNF4-alpha to bind to
its recognition site. Interacts with PER2.
{ECO:0000269|PubMed:20159955}.
-!- SUBCELLULAR LOCATION: Nucleus.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=Long;
IsoId=P49698-1; Sequence=Displayed;
Name=Short;
IsoId=P49698-2; Sequence=VSP_003676;
-!- PTM: Phosphorylated on tyrosine residue(s); phosphorylation is
important for its DNA-binding activity. Phosphorylation may
directly or indirectly play a regulatory role in the subnuclear
distribution. Phosphorylation at Ser-313 by AMPK reduces the
ability to form homodimers and bind DNA (By similarity).
{ECO:0000250}.
-!- PTM: Acetylation at Lys-458 lowers transcriptional activation by
about two-fold. {ECO:0000250}.
-!- DISRUPTION PHENOTYPE: Pancreatic beta-cells-specific knockout
results in hyperinsulinemia and hypoglycemia.
{ECO:0000269|PubMed:17407387}.
-!- MISCELLANEOUS: Binds fatty acids. {ECO:0000250}.
-!- SIMILARITY: Belongs to the nuclear hormone receptor family. NR2
subfamily. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAA06101.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
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EMBL; D29015; BAA06101.1; ALT_INIT; mRNA.
EMBL; AY902317; AAX90602.1; -; Genomic_DNA.
EMBL; AK143948; BAE25624.1; -; mRNA.
EMBL; AL591488; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC039220; AAH39220.1; -; mRNA.
EMBL; EF193393; ABM69091.1; -; mRNA.
CCDS; CCDS17012.1; -. [P49698-1]
PIR; S52074; S52074.
RefSeq; NP_032287.2; NM_008261.3. [P49698-1]
RefSeq; XP_006498850.1; XM_006498787.1. [P49698-2]
UniGene; Mm.202383; -.
ProteinModelPortal; P49698; -.
SMR; P49698; -.
BioGrid; 200354; 4.
CORUM; P49698; -.
IntAct; P49698; 3.
MINT; MINT-5027670; -.
STRING; 10090.ENSMUSP00000018094; -.
iPTMnet; P49698; -.
PhosphoSitePlus; P49698; -.
MaxQB; P49698; -.
PaxDb; P49698; -.
PeptideAtlas; P49698; -.
PRIDE; P49698; -.
Ensembl; ENSMUST00000018094; ENSMUSP00000018094; ENSMUSG00000017950. [P49698-1]
GeneID; 15378; -.
KEGG; mmu:15378; -.
UCSC; uc008nta.2; mouse. [P49698-1]
UCSC; uc012cit.1; mouse. [P49698-2]
CTD; 3172; -.
MGI; MGI:109128; Hnf4a.
eggNOG; KOG4215; Eukaryota.
eggNOG; ENOG410XQT8; LUCA.
GeneTree; ENSGT00760000118948; -.
HOGENOM; HOG000260822; -.
HOVERGEN; HBG005606; -.
InParanoid; P49698; -.
KO; K07292; -.
OMA; KRMRYQV; -.
OrthoDB; EOG091G0A89; -.
PhylomeDB; P49698; -.
TreeFam; TF352097; -.
Reactome; R-MMU-383280; Nuclear Receptor transcription pathway.
ChiTaRS; Hnf4a; mouse.
PRO; PR:P49698; -.
Proteomes; UP000000589; Chromosome 2.
Bgee; ENSMUSG00000017950; -.
CleanEx; MM_HNF4A; -.
ExpressionAtlas; P49698; baseline and differential.
Genevisible; P49698; MM.
GO; GO:0005737; C:cytoplasm; ISO:MGI.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
GO; GO:0005634; C:nucleus; IDA:MGI.
GO; GO:0003677; F:DNA binding; IDA:MGI.
GO; GO:0005504; F:fatty acid binding; ISO:MGI.
GO; GO:0004879; F:nuclear receptor activity; IEA:InterPro.
GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
GO; GO:0005102; F:receptor binding; ISO:MGI.
GO; GO:0001102; F:RNA polymerase II activating transcription factor binding; IPI:BHF-UCL.
GO; GO:0000979; F:RNA polymerase II core promoter sequence-specific DNA binding; IDA:MGI.
GO; GO:0043565; F:sequence-specific DNA binding; IDA:MGI.
GO; GO:0003707; F:steroid hormone receptor activity; IEA:InterPro.
GO; GO:0003705; F:transcription factor activity, RNA polymerase II distal enhancer sequence-specific binding; IDA:MGI.
GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IDA:BHF-UCL.
GO; GO:0044212; F:transcription regulatory region DNA binding; IDA:BHF-UCL.
GO; GO:0001228; F:transcriptional activator activity, RNA polymerase II transcription regulatory region sequence-specific binding; IDA:MGI.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0007596; P:blood coagulation; ISO:MGI.
GO; GO:0031018; P:endocrine pancreas development; TAS:Reactome.
GO; GO:0042593; P:glucose homeostasis; IMP:BHF-UCL.
GO; GO:0055088; P:lipid homeostasis; ISO:MGI.
GO; GO:0006629; P:lipid metabolic process; IMP:MGI.
GO; GO:0030308; P:negative regulation of cell growth; ISO:MGI.
GO; GO:0008285; P:negative regulation of cell proliferation; ISO:MGI.
GO; GO:0006591; P:ornithine metabolic process; ISO:MGI.
GO; GO:0055091; P:phospholipid homeostasis; IMP:BHF-UCL.
GO; GO:2000189; P:positive regulation of cholesterol homeostasis; IMP:BHF-UCL.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:BHF-UCL.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:MGI.
GO; GO:0010470; P:regulation of gastrulation; IMP:MGI.
GO; GO:0050796; P:regulation of insulin secretion; IMP:BHF-UCL.
GO; GO:0019216; P:regulation of lipid metabolic process; ISO:MGI.
GO; GO:0006357; P:regulation of transcription from RNA polymerase II promoter; IMP:MGI.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IMP:MGI.
GO; GO:0009749; P:response to glucose; IMP:BHF-UCL.
GO; GO:0007548; P:sex differentiation; IMP:MGI.
GO; GO:0023019; P:signal transduction involved in regulation of gene expression; IDA:MGI.
GO; GO:0060395; P:SMAD protein signal transduction; IDA:MGI.
GO; GO:0070328; P:triglyceride homeostasis; IMP:BHF-UCL.
GO; GO:0006805; P:xenobiotic metabolic process; ISO:MGI.
Gene3D; 1.10.565.10; -; 1.
Gene3D; 3.30.50.10; -; 1.
InterPro; IPR003068; COUP_TF.
InterPro; IPR035500; NHR_like_dom_sf.
InterPro; IPR000536; Nucl_hrmn_rcpt_lig-bd.
InterPro; IPR001723; Nuclear_hrmn_rcpt.
InterPro; IPR001628; Znf_hrmn_rcpt.
InterPro; IPR013088; Znf_NHR/GATA.
Pfam; PF00104; Hormone_recep; 1.
Pfam; PF00105; zf-C4; 1.
PRINTS; PR01282; COUPTNFACTOR.
PRINTS; PR00398; STRDHORMONER.
PRINTS; PR00047; STROIDFINGER.
SMART; SM00430; HOLI; 1.
SMART; SM00399; ZnF_C4; 1.
SUPFAM; SSF48508; SSF48508; 1.
PROSITE; PS00031; NUCLEAR_REC_DBD_1; 1.
PROSITE; PS51030; NUCLEAR_REC_DBD_2; 1.
1: Evidence at protein level;
Acetylation; Alternative splicing; Complete proteome; DNA-binding;
Isopeptide bond; Metal-binding; Nucleus; Phosphoprotein; Receptor;
Reference proteome; Transcription; Transcription regulation;
Ubl conjugation; Zinc; Zinc-finger.
CHAIN 1 474 Hepatocyte nuclear factor 4-alpha.
/FTId=PRO_0000053559.
DNA_BIND 57 132 Nuclear receptor. {ECO:0000255|PROSITE-
ProRule:PRU00407}.
ZN_FING 60 80 NR C4-type. {ECO:0000255|PROSITE-
ProRule:PRU00407}.
ZN_FING 96 120 NR C4-type. {ECO:0000255|PROSITE-
ProRule:PRU00407}.
MOD_RES 142 142 Phosphoserine.
{ECO:0000250|UniProtKB:P41235}.
MOD_RES 144 144 Phosphotyrosine.
{ECO:0000250|UniProtKB:P41235}.
MOD_RES 166 166 Phosphothreonine.
{ECO:0000250|UniProtKB:P41235}.
MOD_RES 167 167 Phosphoserine.
{ECO:0000250|UniProtKB:P41235}.
MOD_RES 313 313 Phosphoserine; by AMPK.
{ECO:0000250|UniProtKB:P41235}.
MOD_RES 429 429 Phosphothreonine.
{ECO:0000244|PubMed:17242355,
ECO:0000244|PubMed:21183079}.
MOD_RES 432 432 Phosphothreonine.
{ECO:0000244|PubMed:17242355}.
MOD_RES 436 436 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 458 458 N6-acetyllysine.
{ECO:0000250|UniProtKB:P41235}.
CROSSLNK 234 234 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000250|UniProtKB:P41235}.
CROSSLNK 307 307 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000250|UniProtKB:P41235}.
VAR_SEQ 418 428 CEWPRPRGQAA -> S (in isoform Short).
{ECO:0000303|PubMed:7999795}.
/FTId=VSP_003676.
CONFLICT 55 55 G -> S (in Ref. 1; BAA06101).
{ECO:0000305}.
CONFLICT 365 365 K -> R (in Ref. 3; BAE25624).
{ECO:0000305}.
CONFLICT 378 378 S -> L (in Ref. 6; ABM69091).
{ECO:0000305}.
SEQUENCE 474 AA; 52684 MW; 10843D528EAE87EE CRC64;
MRLSKTLAGM DMADYSAALD PAYTTLEFEN VQVLTMGNDT SPSEGANLNS SNSLGVSALC
AICGDRATGK HYGASSCDGC KGFFRRSVRK NHMYSCRFSR QCVVDKDKRN QCRYCRLKKC
FRAGMKKEAV QNERDRISTR RSSYEDSSLP SINALLQAEV LSQQITSPIS GINGDIRAKK
IANITDVCES MKEQLLVLVE WAKYIPAFCE LLLDDQVALL RAHAGEHLLL GATKRSMVFK
DVLLLGNDYI VPRHCPELAE MSRVSIRILD ELVLPFQELQ IDDNEYACLK AIIFFDPDAK
GLSDPGKIKR LRSQVQVSLE DYINDRQYDS RGRFGELLLL LPTLQSITWQ MIEQIQFIKL
FGMAKIDNLL QEMLLGGSAS DAPHTHHPLH PHLMQEHMGT NVIVANTMPS HLSNGQMCEW
PRPRGQAATP ETPQPSPPSG SGSESYKLLP GAITTIVKPP SAIPQPTITK QEAI


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