ID   FOXD1_CHICK             Reviewed;         440 AA.
AC   Q98937;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   03-AUG-2022, entry version 134.
DE   RecName: Full=Forkhead box protein D1;
DE   AltName: Full=Brain factor 2;
DE            Short=BF-2;
DE            Short=cBF-2;
DE   AltName: Full=HFH-BF-2;
DE   AltName: Full=T-14-6;
GN   Name=FOXD1; Synonyms=HFHBF2;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP   STAGE.
RC   STRAIN=White leghorn; TISSUE=Retina;
RX   PubMed=8757134; DOI=10.1038/382632a0;
RA   Yuasa J., Hirano S., Yamagata M., Noda M.;
RT   "Visual projection map specified by topographic expression of transcription
RT   factors in the retina.";
RL   Nature 382:632-635(1996).
CC   -!- FUNCTION: May determine the nasotemporal axis of the retina, and
CC       consequently specify the topographical projection of the retinal
CC       ganglion-cell axons to the tectum by controlling expression of their
CC       target genes. {ECO:0000269|PubMed:8757134}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00089}.
CC   -!- TISSUE SPECIFICITY: Retina. {ECO:0000269|PubMed:8757134}.
CC   -!- DEVELOPMENTAL STAGE: Can be detected in regions including primordial
CC       retina and neuroepithelium by embryonic day 2 (E2). At E3, expressed in
CC       the temporal retina and associated pigment epithelium as well as in
CC       part of the diencephalon, and at E7 is expressed in retinal ganglion
CC       cells. Levels begin to decline from E4 and almost disappear by E10.
CC       {ECO:0000269|PubMed:8757134}.
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DR   EMBL; U47276; AAB08467.1; -; mRNA.
DR   PIR; S71795; S71795.
DR   AlphaFoldDB; Q98937; -.
DR   SMR; Q98937; -.
DR   STRING; 9031.ENSGALP00000035264; -.
DR   VEuPathDB; HostDB:geneid_396109; -.
DR   eggNOG; KOG2294; Eukaryota.
DR   HOGENOM; CLU_077699_5_1_1; -.
DR   InParanoid; Q98937; -.
DR   OrthoDB; 1270467at2759; -.
DR   Proteomes; UP000000539; Unplaced.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR   GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR   GO; GO:0009653; P:anatomical structure morphogenesis; IBA:GO_Central.
DR   GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
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   2: Evidence at transcript level;
KW   Developmental protein; DNA-binding; Nucleus; Reference proteome;
KW   Transcription; Transcription regulation.
FT   CHAIN           1..440
FT                   /note="Forkhead box protein D1"
FT                   /id="PRO_0000091814"
FT   DNA_BIND        143..237
FT                   /note="Fork-head"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00089"
FT   REGION          1..135
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          295..334
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          388..417
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        18..32
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        33..47
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        48..63
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        301..334
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   440 AA;  44670 MW;  82266C2E1E103A48 CRC64;
     MTLSSEMSEA SALAEETDID VVGEEDDEED EEEPQPRHRR RRRSYAEDEE EEEEEEEEDA
     GDLHDDALLP RSPVRAGGGG GGGGGGGGAG GGDGPGGSRP PSRGGPQKAA AAGGGGAGGG
     GGGGGGAGGG GGGGGGGKNS LVKPPYSYIA LITMAILQSP KKRLTLSEIC EFISGRFPYY
     REKFPAWQNS IRHNLSLNDC FVKIPREPGN PGKGNYWTLD PESADMFDNG SFLRRRKRFK
     RQQLPAPELL LRAVDPAAFL PQPPPQPPQQ PPCAYGPYGC GYGLQLQPYH PHSALFAFHH
     PSPPPRQPPA APAGAPAAAL PPPPPPPPPP RRRAPLLPAA ELARTPFGYP HPLGPALAAS
     LHAAKPGSGA AVARSPFSIE SIIGGGPGPG LGAGPAPGAG GSCASQSGAA TGLSRSLGSG
     LAPAAALPAA PGLAARISNC