ID FOXD3_MOUSE Reviewed; 465 AA. AC Q61060; DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot. DT 10-MAY-2005, sequence version 3. DT 08-NOV-2023, entry version 162. DE RecName: Full=Forkhead box protein D3; DE AltName: Full=HNF3/FH transcription factor genesis; DE AltName: Full=Hepatocyte nuclear factor 3 forkhead homolog 2; DE Short=HFH-2; GN Name=Foxd3; Synonyms=Hfh2; 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], AND FUNCTION. RC TISSUE=Embryonic carcinoma; RX PubMed=8798505; DOI=10.1074/jbc.271.38.23126; RA Sutton J., Costa R., Klug M., Field L., Xu D., Largaespada D.A., RA Fletcher C.F., Jenkins N.A., Copeland N.G., Klemsz M., Hromas R.; RT "Genesis, a winged helix transcriptional repressor with expression RT restricted to embryonic stem cells."; RL J. Biol. Chem. 271:23126-23133(1996). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY. RC TISSUE=Embryo; RX PubMed=9767163; DOI=10.1016/s0925-4773(98)00105-1; RA Labosky P.A., Kaestner K.H.; RT "The winged helix transcription factor Hfh2 is expressed in neural crest RT and spinal cord during mouse development."; RL Mech. Dev. 76:185-190(1998). RN [3] RP SEQUENCE REVISION. RA Kessler D.S., Labosky P.A., Kaestner K.H.; RL Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S., RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., RA Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of the RT mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [5] RP FUNCTION, AND DEVELOPMENTAL STAGE. RX PubMed=12381664; DOI=10.1101/gad.1020502; RA Hanna L.A., Foreman R.K., Tarasenko I.A., Kessler D.S., Labosky P.A.; RT "Requirement for Foxd3 in maintaining pluripotent cells of the early mouse RT embryo."; RL Genes Dev. 16:2650-2661(2002). RN [6] RP TISSUE SPECIFICITY. RX PubMed=11684651; DOI=10.1242/dev.128.21.4127; RA Dottori M., Gross M.K., Labosky P., Goulding M.; RT "The winged-helix transcription factor Foxd3 suppresses interneuron RT differentiation and promotes neural crest cell fate."; RL Development 128:4127-4138(2001). CC -!- FUNCTION: Binds to the consensus sequence 5'-A[AT]T[AG]TTTGTTT-3' and CC acts as a transcriptional repressor (PubMed:12381664, PubMed:8798505). CC Also acts as a transcriptional activator (PubMed:12381664, CC PubMed:8798505). Negatively regulates transcription of transcriptional CC repressor Rhit/Zfp13 (By similarity). Promotes development of neural CC crest cells from neural tube progenitors (PubMed:12381664, CC PubMed:8798505). Restricts neural progenitor cells to the neural crest CC lineage while suppressing interneuron differentiation (PubMed:12381664, CC PubMed:8798505). Required for maintenance of pluripotent cells in the CC pre-implantation and peri-implantation stages of embryogenesis CC (PubMed:12381664, PubMed:8798505). {ECO:0000250|UniProtKB:Q9UJU5, CC ECO:0000269|PubMed:12381664, ECO:0000269|PubMed:8798505}. CC -!- SUBUNIT: Interacts with POU5F1. {ECO:0000250|UniProtKB:Q9UJU5}. CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. CC -!- TISSUE SPECIFICITY: Expressed in premigratory and migrating neural CC crest cells in the early embryo and in motorneuron and interneuron CC progenitors in the developing spinal cord. CC {ECO:0000269|PubMed:11684651, ECO:0000269|PubMed:9767163}. CC -!- DEVELOPMENTAL STAGE: During early embryogenesis, not expressed in CC unfertilized oocytes or fertilized one-cell embryos but detected in CC blastocysts. {ECO:0000269|PubMed:12381664}. CC -!- SEQUENCE CAUTION: CC Sequence=AAA87569.1; Type=Frameshift; Evidence={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; U41047; AAA87569.1; ALT_FRAME; mRNA. DR EMBL; AF067421; AAC28352.2; -; mRNA. DR EMBL; BX005053; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR RefSeq; NP_034555.3; NM_010425.3. DR AlphaFoldDB; Q61060; -. DR SMR; Q61060; -. DR STRING; 10090.ENSMUSP00000084541; -. DR PhosphoSitePlus; Q61060; -. DR PaxDb; 10090-ENSMUSP00000084541; -. DR ProteomicsDB; 271592; -. DR DNASU; 15221; -. DR GeneID; 15221; -. DR KEGG; mmu:15221; -. DR AGR; MGI:1347473; -. DR CTD; 27022; -. DR MGI; MGI:1347473; Foxd3. DR eggNOG; KOG2294; Eukaryota. DR InParanoid; Q61060; -. DR OrthoDB; 5385885at2759; -. DR BioGRID-ORCS; 15221; 5 hits in 79 CRISPR screens. DR ChiTaRS; Foxd3; mouse. DR PRO; PR:Q61060; -. DR Proteomes; UP000000589; Unplaced. DR RNAct; Q61060; Protein. DR GO; GO:0000785; C:chromatin; ISO:MGI. DR GO; GO:0005634; C:nucleus; IC:UniProtKB. DR GO; GO:0005667; C:transcription regulator complex; TAS:MGI. DR GO; GO:0003677; F:DNA binding; ISO:MGI. 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; IBA:GO_Central. DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; ISO:MGI. DR GO; GO:0003690; F:double-stranded DNA binding; ISO:MGI. DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central. DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; ISO:MGI. DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:MGI. DR GO; GO:0000976; F:transcription cis-regulatory region binding; IDA:MGI. DR GO; GO:0009653; P:anatomical structure morphogenesis; IBA:GO_Central. DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central. DR GO; GO:1990830; P:cellular response to leukemia inhibitory factor; IEP:MGI. DR GO; GO:0006351; P:DNA-templated transcription; TAS:MGI. DR GO; GO:0001892; P:embryonic placenta development; IMP:MGI. DR GO; GO:0001701; P:in utero embryonic development; IDA:UniProtKB. DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:UniProtKB. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB. DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central. DR GO; GO:0001829; P:trophectodermal cell differentiation; IMP:MGI. DR CDD; cd20047; FH_FOXD3; 1. DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1. DR InterPro; IPR047392; FH_FOXD3. DR InterPro; IPR001766; Fork_head_dom. DR InterPro; IPR018122; TF_fork_head_CS_1. DR InterPro; IPR030456; TF_fork_head_CS_2. DR InterPro; IPR036388; WH-like_DNA-bd_sf. DR InterPro; IPR036390; WH_DNA-bd_sf. DR PANTHER; PTHR11829; FORKHEAD BOX PROTEIN; 1. DR PANTHER; PTHR11829:SF361; FORKHEAD BOX PROTEIN D3; 1. DR Pfam; PF00250; Forkhead; 1. DR PRINTS; PR00053; FORKHEAD. DR SMART; SM00339; FH; 1. DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1. DR PROSITE; PS00657; FORK_HEAD_1; 1. DR PROSITE; PS00658; FORK_HEAD_2; 1. DR PROSITE; PS50039; FORK_HEAD_3; 1. PE 2: Evidence at transcript level; KW Activator; Developmental protein; DNA-binding; Nucleus; Reference proteome; KW Repressor; Transcription; Transcription regulation. FT CHAIN 1..465 FT /note="Forkhead box protein D3" FT /id="PRO_0000091818" FT DNA_BIND 130..221 FT /note="Fork-head" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00089" FT REGION 1..127 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 375..405 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1..17 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 25..39 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 465 AA; 46345 MW; 7277EB2EE2C8E0C2 CRC64; MTLSGSGSAS DMSGQTVLTA EDVDIDVVGE GDDGLEEKDS DAGCDSPAGP PDLRLDEADE GPPVSAHHGQ SQPQALALPT EATGPGNDTG APEADGCKGG EDAVTGGGGP GAGSGATGGL TPNKPKNSLV KPPYSYIALI TMAILQSPQK KLTLSGICEF ISNRFPYYRE KFPAWQNSIR HNLSLNDCFV KIPREPGNPG KGNYWTLDPQ SEDMFDNGSF LRRRKRFKRH QQEHLREQTA LMMQSFGAYS LAAAAGAGPY GLHPAAAAGA YSHPAAAAAA AAAAALQYPY ALPPVAPVLP PAVPLLPSGE LGRKAAAFGS QLGPSLQLQL NTLGAAAAAA GTAGAAGTTS LIKSEPSARP SFSIENIIGA GSAAPGGSAG GGGSGGGAGG GGGSGGGGGA QSFLRPPGTV QSAALMATHQ PLSLSRTTAT IAPILSVPLS GQFLQPAASA AAAAAAAVQA KWPAQ //