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Database: UniProt
Entry: A0A7L3QQ83_9SYLV
LinkDB: A0A7L3QQ83_9SYLV
Original site: A0A7L3QQ83_9SYLV 
ID   A0A7L3QQ83_9SYLV        Unreviewed;       510 AA.
AC   A0A7L3QQ83;
DT   07-APR-2021, integrated into UniProtKB/TrEMBL.
DT   07-APR-2021, sequence version 1.
DT   08-OCT-2025, entry version 17.
DE   SubName: Full=FOXP1 protein {ECO:0000313|EMBL:NXV03399.1};
DE   Flags: Fragment;
GN   Name=Foxp1 {ECO:0000313|EMBL:NXV03399.1};
GN   ORFNames=CETCET_R01396 {ECO:0000313|EMBL:NXV03399.1};
OS   Cettia cetti.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Neoaves; Telluraves; Australaves;
OC   Passeriformes; Sylvioidea; Sylviidae; Acrocephalinae; Cettia.
OX   NCBI_TaxID=68486 {ECO:0000313|EMBL:NXV03399.1, ECO:0000313|Proteomes:UP000524451};
RN   [1] {ECO:0000313|EMBL:NXV03399.1, ECO:0000313|Proteomes:UP000524451}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OUT-0056 {ECO:0000313|EMBL:NXV03399.1};
RC   TISSUE=Blood {ECO:0000313|EMBL:NXV03399.1};
RA   Zhang G.;
RT   "Bird 10,000 Genomes (B10K) Project - Family phase.";
RL   Submitted (SEP-2019) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC       ECO:0000256|PROSITE-ProRule:PRU00089}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:NXV03399.1}.
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DR   EMBL; VZUI01047515; NXV03399.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A7L3QQ83; -.
DR   Proteomes; UP000524451; Unassembled WGS sequence.
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:UP000524451};
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          298..371
FT                   /note="Fork-head"
FT                   /evidence="ECO:0000259|PROSITE:PS50039"
FT   DNA_BIND        298..371
FT                   /note="Fork-head"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00089"
FT   REGION          104..130
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          227..264
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          443..510
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        104..116
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        119..130
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        227..236
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        237..251
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        252..263
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        445..456
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        500..510
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:NXV03399.1"
FT   NON_TER         510
FT                   /evidence="ECO:0000313|EMBL:NXV03399.1"
SQ   SEQUENCE   510 AA;  56817 MW;  995F6F7AC939A11E CRC64;
     QPQQQQVATQ QLAFQQQLLQ MQQLQQQHLL SLQRQGLLTI QPGQPTLPLQ PLAQGMIPTE
     LQQLWKEVTS SHTAEEAASN NHSSLDLSTT CVSSSAPSKT SLIINPHAST NGQLSVHTPK
     RESLSHEEHS HSHPLYGHGV CKWPGCEAVC EDFQSFLKHL NSEHALDDRS TAQCRVQMQV
     VQQLELQLAK DKERLQAMMT HLHVKSTEPK ATPQPLNLVS SVTLSKTASE ASPQSLPHTP
     TTPTAPITPV TQGPSVITTT SMHSVGPIRR RYSDKYNVPI SSADIAQNQE FYKNAEVRPP
     FTYASLIRQA ILESPEKQLT LNEIYNWFTR MFAYFRRNAA TWKNAVRHNL SLHKCFVRVE
     NVKGAVWTVD ELEFQKRRPQ KISGNPSLIK NIQTSHTYCT PLNAALQASM AENSIPLYTT
     ASMGNPTLGN LASAMREELN GAMEHTNSNG SDSSPGRSPM QAMHPVHVKE EPLDPDENEG
     PLSLVTTANH SPDFDHDRDY EDEPVNEDIE
//
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