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Database: UniProt
Entry: A0A7R5L3V0_9PASS
LinkDB: A0A7R5L3V0_9PASS
Original site: A0A7R5L3V0_9PASS 
ID   A0A7R5L3V0_9PASS        Unreviewed;       696 AA.
AC   A0A7R5L3V0;
DT   02-JUN-2021, integrated into UniProtKB/TrEMBL.
DT   02-JUN-2021, sequence version 1.
DT   28-JAN-2026, entry version 21.
DE   SubName: Full=Forkhead box protein P1 {ECO:0000313|RefSeq:XP_039244284.1};
GN   Name=FOXP1 {ECO:0000313|RefSeq:XP_039244284.1};
OS   Pipra filicauda (Wire-tailed manakin).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Neoaves; Telluraves; Australaves;
OC   Passeriformes; Pipridae; Pipra.
OX   NCBI_TaxID=649802 {ECO:0000313|Proteomes:UP000504627, ECO:0000313|RefSeq:XP_039244284.1};
RN   [1] {ECO:0000313|RefSeq:XP_039244284.1}
RP   IDENTIFICATION.
RC   TISSUE=Muscle {ECO:0000313|RefSeq:XP_039244284.1};
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_039244284.1; XM_039388350.1.
DR   AlphaFoldDB; A0A7R5L3V0; -.
DR   FunCoup; A0A7R5L3V0; 366.
DR   GeneID; 113982256; -.
DR   CTD; 27086; -.
DR   InParanoid; A0A7R5L3V0; -.
DR   Proteomes; UP000504627; 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; cd20065; FH_FOXP2; 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; IPR047412; FH_FOXP1_P2.
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:SF3; FORKHEAD BOX PROTEIN P1; 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:UP000504627};
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          471..544
FT                   /note="Fork-head"
FT                   /evidence="ECO:0000259|PROSITE:PS50039"
FT   DNA_BIND        471..544
FT                   /note="Fork-head"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00089"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          277..304
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          401..438
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          629..696
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..19
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        277..290
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        293..304
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        401..410
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        411..425
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        426..437
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        631..642
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        686..696
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   696 AA;  77783 MW;  09B820C6996BDEA3 CRC64;
     MMQESGTETK SNGSAIQNGA SGGNHLLECS LREVRSNGET PSVEIGAADL AHLQQQQALQ
     VARQLLLQQQ QQQQQQQQQQ QQVSGLKSPK RNDKQPALQV PVSVAMMTPQ VITPQQMQQI
     LQQQVLTPQQ LQVLLQQQQA LMLQQQQLQE FYKKQQEQLQ LQLLQQQHAG KQPKEPQQQQ
     VATQQLAFQQ QLLQMQQLQQ QHLLSLQRQG LLTIQPGQPT LPLQPLAQGM IPTELQQLWK
     EVTSSHTAEE AASNNHSSLD LSTTCVSSSA PSKTSLIINP HASTNGQLSV HTPKRESLSH
     EEHSHSHPLY GHGVCKWPGC EAVCEDFQSF LKHLNSEHAL DDRSTAQCRV QMQVVQQLEL
     QLAKDKERLQ AMMTHLHVKS TEPKATPQPL NLVSSVTLSK TASEASPQSL PHTPTTPTAP
     ITPVTQGPSV ITTTSMHNVG PIRRRYSDKY NVPISSDIAQ NQEFYKNAEV RPPFTYASLI
     RQAILESPEK QLTLNEIYNW FTRMFAYFRR NAATWKNAVR HNLSLHKCFV RVENVKGAVW
     TVDELEFQKR RPQKISGNPS LIKNIQTSHT YCTPLNAALQ GEEAALSPLC LWKASMAENS
     IPLYTTASMG NPTLGNLASA MREELNGAME HTNSNGSDSS PGRSPMQAMH PVHVKEEPLD
     PDENEGPLSL VTTANHSPDF DHDRDYEDEP VNEDIE
//
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