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Database: UniProt
Entry: A0A8U0UUK3_MUSPF
LinkDB: A0A8U0UUK3_MUSPF
Original site: A0A8U0UUK3_MUSPF 
ID   A0A8U0UUK3_MUSPF        Unreviewed;       673 AA.
AC   A0A8U0UUK3;
DT   12-OCT-2022, integrated into UniProtKB/TrEMBL.
DT   12-OCT-2022, sequence version 1.
DT   28-JAN-2026, entry version 16.
DE   SubName: Full=Forkhead box protein P4 isoform X3 {ECO:0000313|RefSeq:XP_044926951.1};
GN   Name=FOXP4 {ECO:0000313|RefSeq:XP_044926951.1};
OS   Mustela putorius furo (European domestic ferret) (Mustela furo).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC   Mustelinae; Mustela.
OX   NCBI_TaxID=9669 {ECO:0000313|Proteomes:UP000000715, ECO:0000313|RefSeq:XP_044926951.1};
RN   [1] {ECO:0000313|RefSeq:XP_044926951.1}
RP   IDENTIFICATION.
RC   TISSUE=Brain {ECO:0000313|RefSeq:XP_044926951.1};
RG   RefSeq;
RL   Submitted (AUG-2025) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC       ECO:0000256|PROSITE-ProRule:PRU00089}.
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DR   RefSeq; XP_044926951.1; XM_045071016.1.
DR   AlphaFoldDB; A0A8U0UUK3; -.
DR   GeneID; 101669952; -.
DR   CTD; 116113; -.
DR   Proteomes; UP000000715; Unplaced.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IEA:TreeGrafter.
DR   GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IEA:TreeGrafter.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR   CDD; cd20067; FH_FOXP4; 1.
DR   FunFam; 1.20.5.340:FF:000005; Forkhead box P1, isoform CRA_f; 1.
DR   FunFam; 1.10.10.10:FF:000010; Forkhead box P2 isoform B; 1.
DR   Gene3D; 1.20.5.340; -; 1.
DR   Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR   InterPro; IPR047414; FH_FOXP4.
DR   InterPro; IPR001766; Fork_head_dom.
DR   InterPro; IPR050998; FOXP.
DR   InterPro; IPR032354; FOXP-CC.
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; PTHR45796; FORKHEAD BOX P, ISOFORM C; 1.
DR   PANTHER; PTHR45796:SF7; FORKHEAD BOX PROTEIN P4; 1.
DR   Pfam; PF00250; Forkhead; 1.
DR   Pfam; PF16159; FOXP-CC; 1.
DR   PRINTS; PR00053; FORKHEAD.
DR   SMART; SM00339; FH; 1.
DR   SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR   PROSITE; PS00658; FORK_HEAD_2; 1.
DR   PROSITE; PS50039; FORK_HEAD_3; 1.
PE   4: Predicted;
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|PROSITE-
KW   ProRule:PRU00089}; Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PROSITE-
KW   ProRule:PRU00089}; Reference proteome {ECO:0000313|Proteomes:UP000000715};
KW   Repressor {ECO:0000256|ARBA:ARBA00022491};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT   DOMAIN          460..533
FT                   /note="Fork-head"
FT                   /evidence="ECO:0000259|PROSITE:PS50039"
FT   DNA_BIND        460..533
FT                   /note="Fork-head"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00089"
FT   REGION          1..64
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          265..309
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          382..438
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          595..673
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        18..50
FT                   /note="Gly residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        275..289
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        292..303
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        610..628
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        629..643
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        661..673
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   673 AA;  72385 MW;  1C7B6FBE29471E3D CRC64;
     MMVESASETI RSAPSGQNGV GGISGQADGG GGGGGGGGAG AAGAGGGGPG RDSAAGPDSN
     GELSPAELLH FQQQQALQVA RQFLLQQASG LSSPGNNDSK QSASSVQVPV SVAMMSPQML
     TPQQMQQILS PPQLQALLQQ QQALMLQQEY YKKQQEQLHL QLLTQQQAGK QQPKEALGNK
     QLAFQQQLLQ MQQLQQQHLL NLQRQGLVSL QPGQASGPLQ TLPQAAVCPT DLPQLWKGEG
     APGQPAEDSV KQEGLDLTGS ATTATSFAAP PKVSPSLSHH TLPNGQPTVL TPRRDSSSHE
     ETPGSHPLYG HGECKWPGCE TLCEDLGQFI KHLNTEHALD DRSTAQCRVQ MQVVQQLEIQ
     LAKESERLQA MMAHLHMRPS EPKPFNQPVT VSAADSFPDG LVHPPTSAAA PVTPLRPPGL
     SSASLHSGGP ARRRSSDKFC SPISSELAQN HEFYKNADVR PPFTYASLIR QAILETPDRQ
     LTLNEIYNWF TRMFAYFRRN TATWKNAVRH NLSLHKCFVR VENVKGAVWT VDEREYQKRR
     PPKMTGSPTL VKNMISGLSY GALNASYQAA LAESSFPLLN SPGMLNPGSA SSLLPLSHED
     VGAPVEPLPS NGSSSPPRLS PPQYSHQVQV KEEPQEAEED RRPGPPLGPP NPSTAAPPED
     RDLEEELPGE ELS
//
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