ID A0A2K5P0T8_CERAT Unreviewed; 613 AA.
AC A0A2K5P0T8;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 28-JAN-2026, entry version 37.
DE SubName: Full=Forkhead box P1 {ECO:0000313|Ensembl:ENSCATP00000043270.1};
GN Name=FOXP1 {ECO:0000313|Ensembl:ENSCATP00000043270.1};
OS Cercocebus atys (Sooty mangabey) (Cercocebus torquatus atys).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Cercocebus.
OX NCBI_TaxID=9531 {ECO:0000313|Ensembl:ENSCATP00000043270.1, ECO:0000313|Proteomes:UP000233060};
RN [1] {ECO:0000313|Ensembl:ENSCATP00000043270.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [2] {ECO:0000313|Ensembl:ENSCATP00000043270.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2025) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC ECO:0000256|PROSITE-ProRule:PRU00089}.
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DR AlphaFoldDB; A0A2K5P0T8; -.
DR Ensembl; ENSCATT00000067707.1; ENSCATP00000043270.1; ENSCATG00000044155.1.
DR GeneTree; ENSGT00940000159892; -.
DR Proteomes; UP000233060; Unassembled WGS sequence.
DR Bgee; ENSCATG00000044155; Expressed in skeletal muscle tissue and 12 other cell types or tissues.
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 FunFam; 1.20.5.340:FF:000005; Forkhead box P1, isoform CRA_f; 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; IPR001766; Fork_head_dom.
DR InterPro; IPR050998; FOXP.
DR InterPro; IPR032354; FOXP-CC.
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; PS50039; FORK_HEAD_3; 1.
PE 4: Predicted;
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|PROSITE-
KW ProRule:PRU00089};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PROSITE-
KW ProRule:PRU00089}; Reference proteome {ECO:0000313|Proteomes:UP000233060};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
FT DOMAIN 465..516
FT /note="Fork-head"
FT /evidence="ECO:0000259|PROSITE:PS50039"
FT DNA_BIND 465..516
FT /note="Fork-head"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00089"
FT REGION 1..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 270..298
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 390..422
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 547..613
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 270..283
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 286..298
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 390..403
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 404..418
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 548..559
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 603..613
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 613 AA; 68104 MW; 270A46D1A63C1A28 CRC64;
MMQESGTETK SNGSAIQNGS GGSNHLLECS GLREGRSNGE TPAVDIGAAD LAHAQQQQQQ
ALQVARQLLL QQQQQQQVSG LKSPKRNDKQ PALQVPVSVA MMTPQVITPQ QMQQILQQQV
LSPQQLQVLL QQQQALMLQQ QQLQEFYKKQ QEQLQLQLLQ QQHAGKQPKE QQQVATQQLA
FQQQLLQMQQ LQQQHLLSLQ RQGLLTIQPG QPALPLQPLA QGMIPTELQQ LWKEVTSAHT
AEETTGNNHS SLDLTTTCVS SSAPSKTSLI MNPHASTNGQ LSVHTPKRES LSHEEHPHSH
PLYGHGVCKW PGCEAVCEDF QSFLKHLNSE HALDDRSTAQ CRVQMQVVQQ LELQLAKDKE
RLQAMMTHLH VKSTEPKAAP QPLNLVSSVT LSKSASEASP QSLPHTPTTP TAPLTPVTQG
PSVITTTSMH TVGPIRRRYS DKYNVPISSA DIAQNQEFYK NAEVRPPFTY ASLIRQAILE
SPEKQLTLNE IYNWFTRMFA YFRRNAATWK ASMAENSIPL YTTASMGNPT LGNLASAIRE
ELNGAMEHTN SNESDSSPGR SPMQAVHPVH VKEEPLDPEE AEGPLSLVTT ANHSPDFDHD
RDYEDEPVNE DME
//
