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Database: UniProt
Entry: A0A2K6CDL0_MACNE
LinkDB: A0A2K6CDL0_MACNE
Original site: A0A2K6CDL0_MACNE 
ID   A0A2K6CDL0_MACNE        Unreviewed;       529 AA.
AC   A0A2K6CDL0;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   RecName: Full=Forkhead box protein P2 {ECO:0000256|ARBA:ARBA00040052};
GN   Name=FOXP2 {ECO:0000313|Ensembl:ENSMNEP00000021729.1};
OS   Macaca nemestrina (Pig-tailed macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9545 {ECO:0000313|Ensembl:ENSMNEP00000021729.1, ECO:0000313|Proteomes:UP000233120};
RN   [1] {ECO:0000313|Ensembl:ENSMNEP00000021729.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC       ECO:0000256|PROSITE-ProRule:PRU00089}.
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DR   AlphaFoldDB; A0A2K6CDL0; -.
DR   Ensembl; ENSMNET00000045981.1; ENSMNEP00000021729.1; ENSMNEG00000034461.1.
DR   GeneTree; ENSGT00940000155480; -.
DR   Proteomes; UP000233120; Unplaced.
DR   Bgee; ENSMNEG00000034461; Expressed in skeletal muscle tissue and 12 other cell types or tissues.
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   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; 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   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
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:UP000233120};
KW   Repressor {ECO:0000256|ARBA:ARBA00022491};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT   DOMAIN          330..391
FT                   /note="Fork-head"
FT                   /evidence="ECO:0000259|PROSITE:PS50039"
FT   DNA_BIND        330..391
FT                   /note="Fork-head"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00089"
FT   REGION          192..246
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          463..482
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          492..529
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          49..98
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        195..234
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        464..479
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        515..529
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   529 AA;  59808 MW;  14936EA094C9D227 CRC64;
     MMTPQVITPQ QMQQILQQQV LSPQQLQALL QQQQAVMLQQ QQLQEFYKKQ QEQLHLQLLQ
     QQQQQQQQQQ QQQQQQQQQQ QQQQQQQQQQ QQQQQQQQHP GKQAKEQQQQ QQQQQQLAAQ
     QLVFQQQLLQ MQQLQQQQHL LSLQRQGLIS IPPGQAALPV QSLPQAGLSP AEIQQLWKEV
     TGVHSMEDNG IKHGGLDLTT NNSSSTTSST TSKASPPITH HSIVNGQSSV LNARRDSSSH
     EETGASHTLY GHGVCKWPGC ESICEDFGQF LKHLNNEHAL DDRSTAQCRV QMQVVQQLEI
     QLSKERERLQ AMMTHLHMRP SEPKPSPKPA IMESSDRQLT LNEIYSWFTR TFAYFRRNAA
     TWKNAVRHNL SLHKCFVRVE NVKGAVWTVD EVEYQKRRSQ KITGSPTLVK NIPTSLGYGA
     ALNASLQAAL AESSLPLLSN PGLINNASSG LLQAVHEDLN GSLDHIDSNG NSSPGCSPQP
     HIHSIHVKEE PVIAEDEDCP MSLVTTANHS PELEDDREIE EEPLSEDLE
//
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