FOXD3_RAT
ID FOXD3_RAT Reviewed; 101 AA.
AC Q63245;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 156.
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;
DE Flags: Fragment;
GN Name=Foxd3; Synonyms=Hfh2;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley;
RX PubMed=7683413; DOI=10.1073/pnas.90.9.3948;
RA Clevidence D.E., Overdier D.G., Tao W., Qian X., Pani L., Lai E.,
RA Costa R.H.;
RT "Identification of nine tissue-specific transcription factors of the
RT hepatocyte nuclear factor 3/forkhead DNA-binding-domain family.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:3948-3952(1993).
RN [2]
RP STRUCTURE BY NMR OF 3-97.
RX PubMed=9571051; DOI=10.1006/jmbi.1998.1703;
RA Marsden I., Jin C., Liao X.;
RT "Structural changes in the region directly adjacent to the DNA-binding
RT helix highlight a possible mechanism to explain the observed changes in the
RT sequence-specific binding of winged helix proteins.";
RL J. Mol. Biol. 278:293-299(1998).
CC -!- FUNCTION: Binds to the consensus sequence 5'-A[AT]T[AG]TTTGTTT-3' and
CC acts as a transcriptional repressor. Also acts as a transcriptional
CC activator. Promotes development of neural crest cells from neural tube
CC progenitors. Restricts neural progenitor cells to the neural crest
CC lineage while suppressing interneuron differentiation. Required for
CC maintenance of pluripotent cells in the pre-implantation and peri-
CC implantation stages of embryogenesis (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with POU5F1. {ECO:0000250|UniProtKB:Q9UJU5}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00089}.
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DR EMBL; L13202; AAA41319.1; -; mRNA.
DR PIR; I60917; I60917.
DR PDB; 2HDC; NMR; -; A=2-98.
DR PDB; 2HFH; NMR; -; A=2-101.
DR PDBsum; 2HDC; -.
DR PDBsum; 2HFH; -.
DR AlphaFoldDB; Q63245; -.
DR SMR; Q63245; -.
DR STRING; 10116.ENSRNOP00000054694; -.
DR PhosphoSitePlus; Q63245; -.
DR PaxDb; Q63245; -.
DR UCSC; RGD:621715; rat.
DR RGD; 621715; Foxd3.
DR eggNOG; KOG2294; Eukaryota.
DR InParanoid; Q63245; -.
DR PhylomeDB; Q63245; -.
DR EvolutionaryTrace; Q63245; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0000785; C:chromatin; ISO:RGD.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IDA:RGD.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISS: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:RGD.
DR GO; GO:0003690; F:double-stranded DNA binding; IMP:RGD.
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:RGD.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:RGD.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; ISO:RGD.
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; ISO:RGD.
DR GO; GO:0001892; P:embryonic placenta development; ISO:RGD.
DR GO; GO:0001701; P:in utero embryonic development; ISS:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISS: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:0006355; P:regulation of transcription, DNA-templated; TAS:RGD.
DR GO; GO:0001829; P:trophectodermal cell differentiation; ISO:RGD.
DR CDD; cd00059; FH; 1.
DR Gene3D; 1.10.10.10; -; 1.
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 Pfam; PF00250; Forkhead; 1.
DR PRINTS; PR00053; FORKHEAD.
DR SMART; SM00339; FH; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR PROSITE; PS00657; FORK_HEAD_1; 1.
DR PROSITE; PS00658; FORK_HEAD_2; 1.
DR PROSITE; PS50039; FORK_HEAD_3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; Developmental protein; DNA-binding; Nucleus;
KW Reference proteome; Repressor; Transcription; Transcription regulation.
FT CHAIN <1..>101
FT /note="Forkhead box protein D3"
FT /id="PRO_0000091819"
FT DNA_BIND 3..97
FT /note="Fork-head"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00089"
FT NON_TER 1
FT NON_TER 101
FT HELIX 8..17
FT /evidence="ECO:0007829|PDB:2HDC"
FT TURN 20..22
FT /evidence="ECO:0007829|PDB:2HDC"
FT HELIX 26..36
FT /evidence="ECO:0007829|PDB:2HDC"
FT HELIX 38..43
FT /evidence="ECO:0007829|PDB:2HDC"
FT HELIX 47..59
FT /evidence="ECO:0007829|PDB:2HDC"
FT STRAND 62..64
FT /evidence="ECO:0007829|PDB:2HDC"
FT STRAND 71..73
FT /evidence="ECO:0007829|PDB:2HDC"
FT STRAND 76..78
FT /evidence="ECO:0007829|PDB:2HDC"
FT HELIX 83..89
FT /evidence="ECO:0007829|PDB:2HDC"
FT STRAND 94..96
FT /evidence="ECO:0007829|PDB:2HDC"
SQ SEQUENCE 101 AA; 11943 MW; DC0ADEC15A1DD143 CRC64;
LVKPPYSYIA LITMAILQSP QKKLTLSGIC EFISNRFPYY REKFPAWQNS IRHNLSLNDC
FVKIPREPGN PGKGNYWTLD PQSEDMFDNG SFLRRRKRFK R
