ID A9UCL7_ASEST Unreviewed; 716 AA. AC A9UCL7; DT 05-FEB-2008, integrated into UniProtKB/TrEMBL. DT 05-FEB-2008, sequence version 1. DT 27-NOV-2024, entry version 76. DE RecName: Full=Forkhead box protein P2 {ECO:0000256|ARBA:ARBA00040052}; OS Aselliscus stoliczkanus (Stoliczka's Asian trident bat) (Asellia OS stoliczkana). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Laurasiatheria; Chiroptera; Yinpterochiroptera; Rhinolophoidea; OC Hipposideridae; Aselliscus. OX NCBI_TaxID=188568 {ECO:0000313|EMBL:ABW72040.1}; RN [1] {ECO:0000313|EMBL:ABW72040.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=17878935; DOI=10.1371/journal.pone.0000900; RA Li G., Wang J., Rossiter S.J., Jones G., Zhang S.; RT "Accelerated FoxP2 evolution in echolocating bats."; RL PLoS ONE 2:e900-e900(2007). CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123, CC ECO:0000256|PROSITE-ProRule:PRU00089}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; EU076392; ABW72040.1; -; mRNA. DR AlphaFoldDB; A9UCL7; -. 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:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IEA:TreeGrafter. 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: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 Repressor {ECO:0000256|ARBA:ARBA00022491}; KW Transcription {ECO:0000256|ARBA:ARBA00023015}; KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015}; KW Zinc {ECO:0000256|ARBA:ARBA00022833}; KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}. FT DOMAIN 505..578 FT /note="Fork-head" FT /evidence="ECO:0000259|PROSITE:PS50039" FT DNA_BIND 505..578 FT /note="Fork-head" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00089" FT REGION 1..46 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 159..193 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 281..340 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 649..669 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 683..716 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 166..180 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 289..328 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 651..666 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 702..716 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 716 AA; 79788 MW; B25B9A53BB3B7063 CRC64; MMQESATETI TNSSMNQNGM STLSSQLDAG SRDGRSSGDT SSEVSTVELL HLQQQQALQA ARQLLLQQQT SGLKSPKSSD KQRPLQVPVS VAMMTPQVIT PQQMQQILQQ QVLSPQQLQA LLQQQQAVML QQQQLQEFYK KQQEQLHLQL LQQQQQQQQQ QQQQPQPQPQ PQPPQPQPQH PGKQAKEQQQ QQQQQQQQQQ QQQQQQQQQQ LAAQQLVFQQ QLLQMQQLQQ QQHLLSLQRQ GLISIPPGQA ALPVQSLPQA GLSPAEIQQL WKEVTGVHSM EDNGIKHGGL DLTTNNSSST TSSTTSKASP PIPHHSMVNG QSSVLSARRD SSSHEETGAS HTLYGHGVCK WPGCESICED FGQFLKHLNN EHALDDRSTA QCRVQMQVVQ QLEIQLSKER ERLQAMMTHL HMRPSEPKPS PKPLNLVSSV TMSKNMLETS PQSLPQTPTT PTAPVTPLTQ GASVITPASV PNVGAIRRRH SDKYNIPMSS EIAPNYEFYK NADVRPPFTY ATLIRQAIME SSDRQLTLNE IYSWFTRTFA YFRRNAATWK NAVRHNLSLH KCFVRVENVK GAVWTVDEVE YQKRRSQKIT GSPTLVKNIP TSLGYGAALN ASLQAALAES SLPLLSNPGL INNASSGLLQ AVHEDLNGSL DHMDSNGNSS PGCSPQPHIH SIHVKEEPVI AEDEDCPISL VTTANHSPEL EDDREIEDEP LSEELE //