ID   FOXP2_PANPA             Reviewed;         716 AA.
AC   Q8HZ00;
DT   31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=Forkhead box protein P2;
GN   Name=FOXP2;
OS   Pan paniscus (Pygmy chimpanzee) (Bonobo).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pan.
OX   NCBI_TaxID=9597;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=12524352; DOI=10.1093/genetics/162.4.1825;
RA   Zhang J., Webb D.M., Podlaha O.;
RT   "Accelerated protein evolution and origins of human-specific features:
RT   Foxp2 as an example.";
RL   Genetics 162:1825-1835(2002).
CC   -!- FUNCTION: Transcriptional repressor that may play a role in the
CC       specification and differentiation of lung epithelium. May also play a
CC       role in developing neural, gastrointestinal and cardiovascular tissues.
CC       Can act with CTBP1 to synergistically repress transcription but CTPBP1
CC       is not essential. Plays a role in synapse formation by regulating SRPX2
CC       levels (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Forms homodimers and heterodimers with FOXP1 and FOXP4.
CC       Dimerization is required for DNA-binding. Interacts with CTBP1 (By
CC       similarity). Interacts with FOXP1 (By similarity). Interacts with TBR1
CC       (By similarity). Interacts with ZMYM2 (By similarity).
CC       {ECO:0000250|UniProtKB:O15409, ECO:0000250|UniProtKB:P58463}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC   -!- DOMAIN: The leucine-zipper is required for dimerization and
CC       transcriptional repression. {ECO:0000250}.
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DR   EMBL; AY143179; AAN60057.1; -; mRNA.
DR   RefSeq; NP_001266127.1; NM_001279198.1.
DR   AlphaFoldDB; Q8HZ00; -.
DR   SMR; Q8HZ00; -.
DR   STRING; 9597.NP_001266127.1; -.
DR   GeneID; 100990292; -.
DR   KEGG; pps:100990292; -.
DR   CTD; 93986; -.
DR   eggNOG; KOG4385; Eukaryota.
DR   OrthoDB; 836427at2759; -.
DR   Proteomes; UP000240080; Unplaced.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; ISS:UniProtKB.
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:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR   GO; GO:0021757; P:caudate nucleus development; ISS:UniProtKB.
DR   GO; GO:0021758; P:putamen development; ISS:UniProtKB.
DR   CDD; cd00059; FH; 1.
DR   Gene3D; 1.10.10.10; -; 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   Pfam; PF00250; Forkhead; 1.
DR   Pfam; PF16159; FOXP-CC; 1.
DR   PRINTS; PR00053; FORKHEAD.
DR   SMART; SM00339; FH; 1.
DR   SUPFAM; SSF46785; SSF46785; 1.
DR   PROSITE; PS00658; FORK_HEAD_2; 1.
DR   PROSITE; PS50039; FORK_HEAD_3; 1.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
PE   2: Evidence at transcript level;
KW   DNA-binding; Metal-binding; Nucleus; Reference proteome; Repressor;
KW   Transcription; Transcription regulation; Zinc; Zinc-finger.
FT   CHAIN           1..716
FT                   /note="Forkhead box protein P2"
FT                   /id="PRO_0000091883"
FT   ZN_FING         347..372
FT                   /note="C2H2-type"
FT   DNA_BIND        505..595
FT                   /note="Fork-head"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00089"
FT   REGION          1..45
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          286..340
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          389..410
FT                   /note="Leucine-zipper"
FT   REGION          423..427
FT                   /note="CTBP1-binding"
FT                   /evidence="ECO:0000250"
FT   REGION          439..466
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          650..669
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          679..716
FT                   /note="Disordered"
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;  80061 MW;  3169A2786B42F79F CRC64;
     MMQESATETI SNSSMNQNGM STLSSQLDAG SRDGRSSGDT SSEVSTVELL HLQQQQALQA
     ARQLLLQQQT SGLKSPKSSD KQRPLQVPVS VAMMTPQVIT PQQMQQILQQ QVLSPQQLQA
     LLQQQQAVML QQQQLQEFYK KQQEQLHLQL LQQQQQQQQQ QQQQQQQQQQ QQQQQQQQQQ
     QQQQQQQQQQ QQHPGKQAKE QQQQQQQQQQ LAAQQLVFQQ QLLQMQQLQQ QQHLLSLQRQ
     GLISIPPGQA ALPVQSLPQA GLSPAEIQQL WKEVTGVHSM EDNGIKHGGL DLTTNNSSST
     TSSTTSKASP PITHHSIVNG QSSVLNARRD SSSHEETGAS HTLYGHGVCK WPGCESICED
     FGQFLKHLNN EHALDDRSTA QCRVQMQVVQ QLEIQLSKER ERLQAMMTHL HMRPSEPKPS
     PKPLNLVSSV TMSKNMLETS PQSLPQTPTT PTAPVTPITQ GPSVITPASV PNVGAIRRRH
     SDKYNIPMSS EIAPNYEFYK NADVRPPFTY ATLIRQAIME SSDRQLTLNE IYSWFTRTFA
     YFRRNAATWK NAVRHNLSLH KCFVRVENVK GAVWTVDEVE YQKRRSQKIT GSPTLVKNIP
     TSLGYGAALN ASLQAALAES SLPLLSNPGL INNASSGLLQ AVHEDLNGSL DHIDSNGNSS
     PGCSPQPHIH SIHVKEEPVI AEDEDCPMSL VTTANHSPEL EDDREIEEEP LSEDLE