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Database: UniProt
Entry: V6F874_HAPBU
LinkDB: V6F874_HAPBU
Original site: V6F874_HAPBU 
ID   V6F874_HAPBU            Unreviewed;       765 AA.
AC   V6F874;
DT   19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT   19-FEB-2014, sequence version 1.
DT   27-MAR-2024, entry version 54.
DE   RecName: Full=Forkhead box protein P2 {ECO:0000256|ARBA:ARBA00040052};
GN   Name=FoxP2 {ECO:0000313|EMBL:DAA64557.1};
OS   Haplochromis burtoni (Burton's mouthbrooder) (Chromis burtoni).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC   Pseudocrenilabrinae; Haplochromini; Haplochromis.
OX   NCBI_TaxID=8153 {ECO:0000313|EMBL:DAA64557.1};
RN   [1] {ECO:0000313|EMBL:DAA64557.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=24349554;
RA   Song X., Wang Y., Tang Y.;
RT   "Rapid Diversification of FoxP2 in Teleosts through Gene Duplication in the
RT   Teleost-Specific Whole Genome Duplication Event.";
RL   PLoS ONE 8:E83858-E83858(2013).
RN   [2] {ECO:0000313|Ensembl:ENSHBUP00000004249.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC       ECO:0000256|PROSITE-ProRule:PRU00089}.
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DR   EMBL; BK008620; DAA64557.1; -; mRNA.
DR   RefSeq; NP_001302467.1; NM_001315538.1.
DR   STRING; 8153.ENSHBUP00000004249; -.
DR   Ensembl; ENSHBUT00000009017.1; ENSHBUP00000004249.1; ENSHBUG00000005609.1.
DR   GeneID; 102293528; -.
DR   CTD; 93986; -.
DR   GeneTree; ENSGT00940000155480; -.
DR   OMA; XHLNNEH; -.
DR   OrthoDB; 5385885at2759; -.
DR   Proteomes; UP000264840; Unplaced.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR   GO; GO:0045471; P:response to ethanol; IEA:Ensembl.
DR   CDD; cd20065; FH_FOXP2; 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; 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:SF1; FORKHEAD BOX PROTEIN P2; 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   2: Evidence at transcript level;
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|PROSITE-
KW   ProRule:PRU00089}; Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleus {ECO:0000256|PROSITE-ProRule:PRU00089};
KW   Reference proteome {ECO:0000313|Proteomes:UP000264840};
KW   Repressor {ECO:0000256|ARBA:ARBA00022491};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT   DOMAIN          506..579
FT                   /note="Fork-head"
FT                   /evidence="ECO:0000259|PROSITE:PS50039"
FT   DNA_BIND        506..579
FT                   /note="Fork-head"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00089"
FT   REGION          1..44
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          204..330
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          422..450
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          649..671
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          696..765
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        267..302
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        304..325
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   765 AA;  83085 MW;  9B7808A2B1F9D3B7 CRC64;
     MMQESATETI SNSSMSQNGM STLSSSQLEA GSRDGRSSAG DTSSEVSTVE LLHLQQQQAL
     QAARQLLLQQ PGSGLKSPKS QDKQRPLQVP VSVAMMSPQV MTPQQMQQIL QQQVLSPQQL
     QALLQQQQAV MLQQQHLQEF YKKQQEQLHL QLLQQQHPGK QVKEQQQQQQ QLAAQQLVFQ
     QQLLQMQQLQ QQQHLLNMQR QGLLTLPGPA PGQAALPGQT LPPPAGLSPA ELQQLWKDVT
     GGGGHGMEDN GIKHSSGTGT GVGGGGGLDL STNNSSSTTS SSNPAKASPP ISHHSIANGQ
     SPALNHRRER ERERERERES SLHEESGGTH PLYGHGVCKW PGCENICEDF GQFLKHLNSE
     HALDDRSTAQ CRVQMQVVQQ LEIQLSKERE RLQAMMTHLH MRPSEPKSSP KPLNLVSSVT
     MSKNLPSASP PNLPQTPTTP TAPITPMAAM PHVPSVLGGA NVPSMGAMRR RHSDKYSMPL
     SSGGDTVFIF PEIAPNYEFY KNADVRPPFT YATLIRQAIM DSADMQLTLN EIYSWFTRTF
     AYFRRNAATW KNAVRHNLSL HKCFVRVENV KGAVWTVDEV EYQKRRSQKI TGSPSLVKNL
     PSSLGYGTAL NASLQAALAE TSLPLLGTPG LMGSGATGPM GGTCHGLLGG DPSGLTAGSP
     PGQLGGSPPG LLGVSPPVTL SGSPPMLLQS AHEDLNGSVD HLDTNGHSSP RYSPPVHMPP
     IHIKEEPLNM DDDDCPMSLV TTANHSPELE EDRELEEGNL SEDLE
//
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