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Hepatocyte nuclear factor 1-alpha (HNF-1-alpha) (HNF-1A) (Liver-specific transcription factor LF-B1) (LFB1) (Transcription factor 1) (TCF-1)

 HNF1A_MOUSE             Reviewed;         628 AA.
P22361; E9QP86;
01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
27-JUL-2011, sequence version 2.
22-NOV-2017, entry version 177.
RecName: Full=Hepatocyte nuclear factor 1-alpha;
Short=HNF-1-alpha;
Short=HNF-1A;
AltName: Full=Liver-specific transcription factor LF-B1;
Short=LFB1;
AltName: Full=Transcription factor 1;
Short=TCF-1;
Name=Hnf1a; Synonyms=Hnf-1, Hnf-1a, Tcf1;
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].
PubMed=2263635; DOI=10.1073/pnas.87.24.9838;
Kuo C.J., Conley P.B., Hsieh C.L., Francke U., Crabtree G.R.;
"Molecular cloning, functional expression, and chromosomal
localization of mouse hepatocyte nuclear factor 1.";
Proc. Natl. Acad. Sci. U.S.A. 87:9838-9842(1990).
[2]
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).
[3]
GENE STRUCTURE.
PubMed=1354855; DOI=10.1093/nar/20.16.4199;
Bach I., Pontoglio M., Yaniv M.;
"Structure of the gene encoding hepatocyte nuclear factor 1 (HNF1).";
Nucleic Acids Res. 20:4199-4204(1992).
[4]
DISRUPTION PHENOTYPE.
PubMed=9566924; DOI=10.1128/MCB.18.5.3059;
Lee Y.H., Sauer B., Gonzalez F.J.;
"Laron dwarfism and non-insulin-dependent diabetes mellitus in the
Hnf-1alpha knockout mouse.";
Mol. Cell. Biol. 18:3059-3068(1998).
[5]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=18630941; DOI=10.1021/pr800223m;
Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
"Specific phosphopeptide enrichment with immobilized titanium ion
affinity chromatography adsorbent for phosphoproteome analysis.";
J. Proteome Res. 7:3957-3967(2008).
[6]
FUNCTION.
PubMed=19289501; DOI=10.1128/MCB.01389-08;
Servitja J.M., Pignatelli M., Maestro M.A., Cardalda C., Boj S.F.,
Lozano J., Blanco E., Lafuente A., McCarthy M.I., Sumoy L., Guigo R.,
Ferrer J.;
"Hnf1alpha (MODY3) controls tissue-specific transcriptional programs
and exerts opposed effects on cell growth in pancreatic islets and
liver.";
Mol. Cell. Biol. 29:2945-2959(2009).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-70; THR-74; SER-247 AND
SER-313, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Kidney, Liver, and Pancreas;
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).
[8]
X-RAY CRYSTALLOGRAPHY (1.0 ANGSTROMS) OF 1-32, AND SUBUNIT.
PubMed=11106484; DOI=10.1021/bi001996t;
Rose R.B., Endrizzi J.A., Cronk J.D., Holton J., Alber T.;
"High-resolution structure of the HNF-1alpha dimerization domain.";
Biochemistry 39:15062-15070(2000).
[9]
X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 1-32 IN COMPLEX WITH PCBD1,
SUBUNIT, AND FUNCTION.
PubMed=10966642; DOI=10.1038/78966;
Rose R.B., Bayle J.H., Endrizzi J.A., Cronk J.D., Crabtree G.R.,
Alber T.;
"Structural basis of dimerization, coactivator recognition and MODY3
mutations in HNF-1alpha.";
Nat. Struct. Biol. 7:744-748(2000).
[10]
X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 2-32, AND SUBUNIT.
PubMed=11439029; DOI=10.1006/jmbi.2001.4780;
Narayana N., Hua Q., Weiss M.A.;
"The dimerization domain of HNF-1alpha: structure and plasticity of an
intertwined four-helix bundle with application to diabetes mellitus.";
J. Mol. Biol. 310:635-658(2001).
-!- FUNCTION: Transcriptional activator that regulates the tissue
specific expression of multiple genes, especially in pancreatic
islet cells and in liver. Required for the expression of several
liver specific genes. Binds to the inverted palindrome 5'-
GTTAATNATTAAC-3'. {ECO:0000269|PubMed:10966642,
ECO:0000269|PubMed:19289501}.
-!- SUBUNIT: Binds DNA as a dimer. Interacts with PCBD1.
Heterotetramer with PCBD1; formed by a dimer of dimers.
{ECO:0000269|PubMed:10966642, ECO:0000269|PubMed:11106484,
ECO:0000269|PubMed:11439029}.
-!- INTERACTION:
Q923E4:Sirt1; NbExp=5; IntAct=EBI-5272860, EBI-1802585;
-!- SUBCELLULAR LOCATION: Nucleus.
-!- TISSUE SPECIFICITY: Liver.
-!- DISRUPTION PHENOTYPE: Mice are born at less than half of the
expected frequency. Neonates are slightly smaller than normal and
do not grow normally. After 5 weeks mice weigh only 50 to 60% as
much as their littermates. Mice develop non-insulin-dependent
diabetes mellitus (NIDDM) 2 weeks after birth. Mice exhibit
elevated levels of blood glucose, combined with reduced blood
levels of insulin and insulin-like growth factor I (IGFI). Males
and females are sterile. {ECO:0000269|PubMed:9566924}.
-!- SIMILARITY: Belongs to the HNF1 homeobox family. {ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; M57966; AAA37821.1; -; mRNA.
EMBL; AC116500; -; NOT_ANNOTATED_CDS; Genomic_DNA.
CCDS; CCDS19577.1; -.
PIR; A39262; A39262.
RefSeq; NP_033353.2; NM_009327.3.
UniGene; Mm.332607; -.
PDB; 1F93; X-ray; 2.60 A; E/F/G/H=1-32.
PDB; 1G2Y; X-ray; 1.00 A; A/B/C/D=1-32.
PDB; 1G2Z; X-ray; 1.15 A; A/B=1-32.
PDB; 1G39; X-ray; 1.22 A; A/B/C/D=1-32.
PDB; 1JB6; X-ray; 1.70 A; A/B=1-33.
PDBsum; 1F93; -.
PDBsum; 1G2Y; -.
PDBsum; 1G2Z; -.
PDBsum; 1G39; -.
PDBsum; 1JB6; -.
ProteinModelPortal; P22361; -.
SMR; P22361; -.
BioGrid; 203999; 8.
CORUM; P22361; -.
IntAct; P22361; 2.
MINT; MINT-4097610; -.
STRING; 10090.ENSMUSP00000031535; -.
iPTMnet; P22361; -.
PhosphoSitePlus; P22361; -.
MaxQB; P22361; -.
PaxDb; P22361; -.
PeptideAtlas; P22361; -.
PRIDE; P22361; -.
Ensembl; ENSMUST00000031535; ENSMUSP00000031535; ENSMUSG00000029556.
GeneID; 21405; -.
KEGG; mmu:21405; -.
UCSC; uc008zcz.2; mouse.
CTD; 6927; -.
MGI; MGI:98504; Hnf1a.
eggNOG; ENOG410IFA0; Eukaryota.
eggNOG; ENOG410ZZZ0; LUCA.
GeneTree; ENSGT00900000141012; -.
HOGENOM; HOG000015305; -.
HOVERGEN; HBG005980; -.
InParanoid; P22361; -.
KO; K08036; -.
OMA; QSHVAQS; -.
OrthoDB; EOG091G052F; -.
TreeFam; TF320327; -.
EvolutionaryTrace; P22361; -.
PRO; PR:P22361; -.
Proteomes; UP000000589; Chromosome 5.
Bgee; ENSMUSG00000029556; -.
CleanEx; MM_HNF1A; -.
ExpressionAtlas; P22361; baseline and differential.
Genevisible; P22361; MM.
GO; GO:0005737; C:cytoplasm; IDA:MGI.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0001750; C:photoreceptor outer segment; IGI:MGI.
GO; GO:0045120; C:pronucleus; IDA:MGI.
GO; GO:0043234; C:protein complex; ISO:MGI.
GO; GO:0005667; C:transcription factor complex; IPI:MGI.
GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
GO; GO:0046983; F:protein dimerization activity; IPI:UniProtKB.
GO; GO:0046982; F:protein heterodimerization activity; IPI:MGI.
GO; GO:0042803; F:protein homodimerization activity; IPI:MGI.
GO; GO:0000978; F:RNA polymerase II core promoter proximal region sequence-specific DNA binding; IDA:MGI.
GO; GO:0001221; F:transcription cofactor binding; IEA:Ensembl.
GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IDA:UniProtKB.
GO; GO:0044212; F:transcription regulatory region DNA binding; ISS:UniProtKB.
GO; GO:0001077; F:transcriptional activator activity, RNA polymerase II core promoter proximal region sequence-specific binding; IEA:Ensembl.
GO; GO:0001228; F:transcriptional activator activity, RNA polymerase II transcription regulatory region sequence-specific binding; IDA:MGI.
GO; GO:0015721; P:bile acid and bile salt transport; IMP:MGI.
GO; GO:0006699; P:bile acid biosynthetic process; IMP:MGI.
GO; GO:0001824; P:blastocyst development; IMP:MGI.
GO; GO:0045453; P:bone resorption; IGI:MGI.
GO; GO:0008203; P:cholesterol metabolic process; IMP:MGI.
GO; GO:0006338; P:chromatin remodeling; IMP:UniProtKB.
GO; GO:0030326; P:embryonic limb morphogenesis; IGI:MGI.
GO; GO:0031018; P:endocrine pancreas development; IMP:MGI.
GO; GO:0006633; P:fatty acid biosynthetic process; IMP:MGI.
GO; GO:0015908; P:fatty acid transport; IMP:MGI.
GO; GO:0042593; P:glucose homeostasis; IDA:UniProtKB.
GO; GO:0046323; P:glucose import; IDA:UniProtKB.
GO; GO:0006783; P:heme biosynthetic process; IMP:MGI.
GO; GO:0016573; P:histone acetylation; IMP:MGI.
GO; GO:0030073; P:insulin secretion; IMP:MGI.
GO; GO:0001889; P:liver development; IMP:MGI.
GO; GO:0001779; P:natural killer cell differentiation; ISO:MGI.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IEA:Ensembl.
GO; GO:0048341; P:paraxial mesoderm formation; IGI:MGI.
GO; GO:0001890; P:placenta development; IGI:MGI.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:MGI.
GO; GO:0060261; P:positive regulation of transcription initiation from RNA polymerase II promoter; ISO:MGI.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0008104; P:protein localization; IMP:MGI.
GO; GO:0046883; P:regulation of hormone secretion; IMP:MGI.
GO; GO:0050796; P:regulation of insulin secretion; IMP:MGI.
GO; GO:0006357; P:regulation of transcription from RNA polymerase II promoter; IDA:MGI.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IMP:MGI.
GO; GO:0030111; P:regulation of Wnt signaling pathway; IGI:MGI.
GO; GO:0035623; P:renal glucose absorption; IDA:UniProtKB.
GO; GO:0048608; P:reproductive structure development; IMP:MGI.
GO; GO:0009749; P:response to glucose; IMP:MGI.
GO; GO:0006979; P:response to oxidative stress; IMP:MGI.
GO; GO:0043691; P:reverse cholesterol transport; IMP:MGI.
GO; GO:0060395; P:SMAD protein signal transduction; IDA:MGI.
CDD; cd00086; homeodomain; 1.
InterPro; IPR006899; HNF-1_N.
InterPro; IPR023219; HNF1_dimer_N_dom_sf.
InterPro; IPR006898; HNF1a_C.
InterPro; IPR006897; HNF1b_C.
InterPro; IPR009057; Homeobox-like_sf.
InterPro; IPR001356; Homeobox_dom.
InterPro; IPR010982; Lambda_DNA-bd_dom_sf.
Pfam; PF04814; HNF-1_N; 1.
Pfam; PF04813; HNF-1A_C; 1.
Pfam; PF04812; HNF-1B_C; 1.
Pfam; PF00046; Homeobox; 1.
SMART; SM00389; HOX; 1.
SUPFAM; SSF100957; SSF100957; 1.
SUPFAM; SSF46689; SSF46689; 1.
SUPFAM; SSF47413; SSF47413; 1.
PROSITE; PS00027; HOMEOBOX_1; 1.
PROSITE; PS50071; HOMEOBOX_2; 1.
1: Evidence at protein level;
3D-structure; Activator; Complete proteome; DNA-binding; Homeobox;
Nucleus; Phosphoprotein; Reference proteome; Transcription;
Transcription regulation.
CHAIN 1 628 Hepatocyte nuclear factor 1-alpha.
/FTId=PRO_0000049116.
DNA_BIND 199 279 Homeobox; HNF1-type.
{ECO:0000255|PROSITE-ProRule:PRU00108}.
REGION 1 31 Dimerization.
REGION 130 132 Interaction with DNA. {ECO:0000250}.
REGION 143 149 Interaction with DNA. {ECO:0000250}.
REGION 155 158 Interaction with DNA. {ECO:0000250}.
REGION 203 206 Interaction with DNA. {ECO:0000250}.
REGION 263 265 Interaction with DNA. {ECO:0000250}.
REGION 270 273 Interaction with DNA. {ECO:0000250}.
MOTIF 197 205 Nuclear localization signal.
{ECO:0000255}.
COMPBIAS 71 80 Asp/Glu-rich (acidic; potential
involvement with transcription).
MOD_RES 70 70 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 74 74 Phosphothreonine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 93 93 Phosphoserine.
{ECO:0000250|UniProtKB:P20823}.
MOD_RES 247 247 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 313 313 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
CONFLICT 89 89 L -> P (in Ref. 1; AAA37821).
{ECO:0000305}.
HELIX 4 18 {ECO:0000244|PDB:1G2Y}.
HELIX 23 30 {ECO:0000244|PDB:1G2Y}.
SEQUENCE 628 AA; 67253 MW; 737920D47BA1F081 CRC64;
MVSKLSQLQT ELLAALLESG LSKEALIQAL GEPGPYLMVG EGPLDKGESC GGSRGDLTEL
PNGLGETRGS EDDTDDDGED FAPPILKELE NLSPEEAAHQ KAVVESLLQE DPWRVAKMVK
SYLQQHNIPQ REVVDTTGLN QSHLSQHLNK GTPMKTQKRA ALYTWYVRKQ REVAQQFTHA
GQGGLIEEPT GDELPTKKGR RNRFKWGPAS QQILFQAYER QKNPSKEERE TLVEECNRAE
CIQRGVSPSQ AQGLGSNLVT EVRVYNWFAN RRKEEAFRHK LAMDTYNGPP PGPGPGPALP
AHSSPGLPTT TLSPSKVHGV RYGQSATSEA AEVPSSSGGP LVTVSAALHQ VSPTGLEPSS
LLSTEAKLVS ATGGPLPPVS TLTALHSLEQ TSPGLNQQPQ NLIMASLPGV MTIGPGEPAS
LGPTFTNTGA STLVIGLAST QAQSVPVINS MGSSLTTLQP VQFSQPLHPS YQQPLMPPVQ
SHVAQSPFMA TMAQLQSPHA LYSHKPEVAQ YTHTSLLPQT MLITDTNLST LASLTPTKQV
FTSDTEASSE PGLHEPPSPA TTIHIPSQDP SNIQHLQPAH RLSTSPTVSS SSLVLYQSSD
SNGHSHLLPS NHSVIETFIS TQMASSSQ


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