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Database: UniProt
Entry: HNF6_MOUSE
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ID   HNF6_MOUSE              Reviewed;         465 AA.
AC   O08755;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   24-JAN-2024, entry version 190.
DE   RecName: Full=Hepatocyte nuclear factor 6;
DE            Short=HNF-6;
DE   AltName: Full=One cut domain family member 1;
DE   AltName: Full=One cut homeobox 1;
GN   Name=Onecut1; Synonyms=Hnf6, Hnf6a;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Liver;
RX   PubMed=9441664; DOI=10.1006/dbio.1997.8744;
RA   Rausa F., Samadani U., Ye H., Lim L., Fletcher C.F., Jenkins N.A.,
RA   Copeland N.G., Costa R.H.;
RT   "The cut-homeodomain transcriptional activator HNF-6 is coexpressed with
RT   its target gene HNF-3 beta in the developing murine liver and pancreas.";
RL   Dev. Biol. 192:228-246(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Liver;
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   [3]
RP   FUNCTION.
RX   PubMed=15381696; DOI=10.1074/jbc.m409038200;
RA   Pierreux C.E., Vanhorenbeeck V., Jacquemin P., Lemaigre F.P.,
RA   Rousseau G.G.;
RT   "The transcription factor hepatocyte nuclear factor-6/Onecut-1 controls the
RT   expression of its paralog Onecut-3 in developing mouse endoderm.";
RL   J. Biol. Chem. 279:51298-51304(2004).
RN   [4]
RP   STRUCTURE BY NMR OF 291-437, AND SUBUNIT.
RX   PubMed=15169783; DOI=10.1074/jbc.m403805200;
RA   Sheng W., Yan H., Rausa F.M. III, Costa R.H., Liao X.;
RT   "Structure of the hepatocyte nuclear factor 6alpha and its interaction with
RT   DNA.";
RL   J. Biol. Chem. 279:33928-33936(2004).
CC   -!- FUNCTION: Transcriptional activator. Binds the consensus sequence 5'-
CC       DHWATTGAYTWWD-3' on a variety of gene promoters such as those of HNF3B
CC       and TTR. Important for liver genes transcription. Stimulates the
CC       expression of Onecut3 in the developing endoderm.
CC       {ECO:0000269|PubMed:15381696}.
CC   -!- SUBUNIT: Binds DNA as a monomer. {ECO:0000269|PubMed:15169783}.
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- SIMILARITY: Belongs to the CUT homeobox family. {ECO:0000305}.
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DR   EMBL; U95945; AAB53863.1; -; mRNA.
DR   EMBL; BC024053; AAH24053.1; -; mRNA.
DR   CCDS; CCDS23339.1; -.
DR   RefSeq; NP_032288.1; NM_008262.3.
DR   PDB; 1S7E; NMR; -; A=291-437.
DR   PDBsum; 1S7E; -.
DR   AlphaFoldDB; O08755; -.
DR   BMRB; O08755; -.
DR   SMR; O08755; -.
DR   STRING; 10090.ENSMUSP00000058020; -.
DR   ChEMBL; CHEMBL2176818; -.
DR   PhosphoSitePlus; O08755; -.
DR   MaxQB; O08755; -.
DR   PaxDb; 10090-ENSMUSP00000058020; -.
DR   PeptideAtlas; O08755; -.
DR   ProteomicsDB; 273371; -.
DR   Antibodypedia; 930; 272 antibodies from 30 providers.
DR   DNASU; 15379; -.
DR   Ensembl; ENSMUST00000056006.11; ENSMUSP00000058020.9; ENSMUSG00000043013.11.
DR   GeneID; 15379; -.
DR   KEGG; mmu:15379; -.
DR   UCSC; uc009qrh.1; mouse.
DR   AGR; MGI:1196423; -.
DR   CTD; 3175; -.
DR   MGI; MGI:1196423; Onecut1.
DR   VEuPathDB; HostDB:ENSMUSG00000043013; -.
DR   eggNOG; KOG2252; Eukaryota.
DR   GeneTree; ENSGT00950000183103; -.
DR   HOGENOM; CLU_018642_0_0_1; -.
DR   InParanoid; O08755; -.
DR   OMA; HPRSLGM; -.
DR   OrthoDB; 5396912at2759; -.
DR   PhylomeDB; O08755; -.
DR   TreeFam; TF318206; -.
DR   BioGRID-ORCS; 15379; 5 hits in 78 CRISPR screens.
DR   EvolutionaryTrace; O08755; -.
DR   PRO; PR:O08755; -.
DR   Proteomes; UP000000589; Chromosome 9.
DR   RNAct; O08755; Protein.
DR   Bgee; ENSMUSG00000043013; Expressed in foregut-midgut junction and 77 other cell types or tissues.
DR   Genevisible; O08755; MM.
DR   GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0003682; F:chromatin binding; IDA:MGI.
DR   GO; GO:0003677; F:DNA binding; IDA:MGI.
DR   GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; ISO:MGI.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:MGI.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISO:MGI.
DR   GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:MGI.
DR   GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:MGI.
DR   GO; GO:0009653; P:anatomical structure morphogenesis; IMP:MGI.
DR   GO; GO:0030183; P:B cell differentiation; IMP:MGI.
DR   GO; GO:0045165; P:cell fate commitment; IGI:MGI.
DR   GO; GO:0016477; P:cell migration; IGI:MGI.
DR   GO; GO:0060271; P:cilium assembly; IMP:MGI.
DR   GO; GO:0031018; P:endocrine pancreas development; IGI:MGI.
DR   GO; GO:0007492; P:endoderm development; IMP:MGI.
DR   GO; GO:0035883; P:enteroendocrine cell differentiation; IMP:MGI.
DR   GO; GO:0002064; P:epithelial cell development; IMP:MGI.
DR   GO; GO:0006006; P:glucose metabolic process; IMP:MGI.
DR   GO; GO:0001889; P:liver development; IGI:MGI.
DR   GO; GO:0030512; P:negative regulation of transforming growth factor beta receptor signaling pathway; IGI:MGI.
DR   GO; GO:0007219; P:Notch signaling pathway; IDA:MGI.
DR   GO; GO:0031016; P:pancreas development; IMP:MGI.
DR   GO; GO:0003310; P:pancreatic A cell differentiation; IMP:MGI.
DR   GO; GO:0003311; P:pancreatic D cell differentiation; IMP:MGI.
DR   GO; GO:0030335; P:positive regulation of cell migration; IGI:MGI.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:MGI.
DR   GO; GO:0001952; P:regulation of cell-matrix adhesion; IGI:MGI.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IMP:MGI.
DR   GO; GO:0048536; P:spleen development; IMP:MGI.
DR   GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; IGI:MGI.
DR   GO; GO:0003309; P:type B pancreatic cell differentiation; IMP:MGI.
DR   CDD; cd00086; homeodomain; 1.
DR   Gene3D; 1.10.10.60; Homeodomain-like; 1.
DR   Gene3D; 1.10.260.40; lambda repressor-like DNA-binding domains; 1.
DR   InterPro; IPR003350; CUT_dom.
DR   InterPro; IPR009057; Homeobox-like_sf.
DR   InterPro; IPR001356; Homeobox_dom.
DR   InterPro; IPR010982; Lambda_DNA-bd_dom_sf.
DR   PANTHER; PTHR14057:SF9; HEPATOCYTE NUCLEAR FACTOR 6; 1.
DR   PANTHER; PTHR14057; TRANSCRIPTION FACTOR ONECUT; 1.
DR   Pfam; PF02376; CUT; 1.
DR   Pfam; PF00046; Homeodomain; 1.
DR   SMART; SM01109; CUT; 1.
DR   SMART; SM00389; HOX; 1.
DR   SUPFAM; SSF46689; Homeodomain-like; 1.
DR   SUPFAM; SSF47413; lambda repressor-like DNA-binding domains; 1.
DR   PROSITE; PS51042; CUT; 1.
DR   PROSITE; PS50071; HOMEOBOX_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Activator; DNA-binding; Homeobox; Nucleus;
KW   Reference proteome; Transcription; Transcription regulation.
FT   CHAIN           1..465
FT                   /note="Hepatocyte nuclear factor 6"
FT                   /id="PRO_0000202403"
FT   DNA_BIND        283..369
FT                   /note="CUT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00374"
FT   DNA_BIND        385..444
FT                   /note="Homeobox"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00108"
FT   REGION          15..84
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          119..141
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          443..465
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        122..140
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        446..465
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   HELIX           295..305
FT                   /evidence="ECO:0007829|PDB:1S7E"
FT   HELIX           312..318
FT                   /evidence="ECO:0007829|PDB:1S7E"
FT   STRAND          320..322
FT                   /evidence="ECO:0007829|PDB:1S7E"
FT   HELIX           326..330
FT                   /evidence="ECO:0007829|PDB:1S7E"
FT   HELIX           344..355
FT                   /evidence="ECO:0007829|PDB:1S7E"
FT   STRAND          378..380
FT                   /evidence="ECO:0007829|PDB:1S7E"
FT   HELIX           394..403
FT                   /evidence="ECO:0007829|PDB:1S7E"
FT   HELIX           412..419
FT                   /evidence="ECO:0007829|PDB:1S7E"
FT   STRAND          424..426
FT                   /evidence="ECO:0007829|PDB:1S7E"
FT   HELIX           427..435
FT                   /evidence="ECO:0007829|PDB:1S7E"
SQ   SEQUENCE   465 AA;  50952 MW;  A770D27DD5AAC896 CRC64;
     MNAQLTMEAI GELHGVSHEP VPAPADLLGG SPHARSSVGH RGSHLPPAHP RSMGMASLLD
     GGSGGSDYHH HHRAPEHSLA GPLHPTMTMA CETPPGMSMP TTYTTLTPLQ PLPPISTVSD
     KFPHHHHHHH HHHHPHHHQR LAGNVSGSFT LMRDERGLAS MNNLYTPYHK DVAGMGQSLS
     PLSGSGLGSI HNSQQGLPHY AHPGAAMPTD KMLTPNGFEA HHPAMLGRHG EQHLTPTSAG
     MVPINGLPPH HPHAHLNAQG HGQLLGTARE PNPSVTGAQV SNGSNSGQME EINTKEVAQR
     ITTELKRYSI PQAIFAQRVL CRSQGTLSDL LRNPKPWSKL KSGRETFRRM WKWLQEPEFQ
     RMSALRLAAC KRKEQEHGKD RGNTPKKPRL VFTDVQRRTL HAIFKENKRP SKELQITISQ
     QLGLELSTVS NFFMNARRRS LDKWQDEGGS NSGSSSSSSS TCTKA
//
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