FOXP2_PANTR
ID FOXP2_PANTR Reviewed; 716 AA.
AC Q8MJA0; Q8MHX3;
DT 21-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Forkhead box protein P2;
GN Name=FOXP2;
OS Pan troglodytes (Chimpanzee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9598;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RX PubMed=12192408; DOI=10.1038/nature01025;
RA Enard W., Przeworski M., Fisher S.E., Lai C.S.L., Wiebe V., Kitano T.,
RA Monaco A.P., Paeaebo S.;
RT "Molecular evolution of FOXP2, a gene involved in speech and language.";
RL Nature 418:869-872(2002).
RN [2]
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).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC TISSUE=Blood;
RA Walter N.A.R., Thompson J., McGoldrick D.J., Messier W.;
RT "The FOXP2 gene, implicated in language development, is conserved in
RT mammalian evolution.";
RL Submitted (NOV-2001) to the EMBL/GenBank/DDBJ databases.
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; AF512947; AAN03385.1; -; mRNA.
DR EMBL; AF515051; AAN03409.1; -; Genomic_DNA.
DR EMBL; AF515052; AAN03410.1; -; Genomic_DNA.
DR EMBL; AY143178; AAN60056.1; -; mRNA.
DR EMBL; AY064549; AAL57735.1; -; mRNA.
DR EMBL; AY064565; AAL57731.1; -; Genomic_DNA.
DR EMBL; AY064551; AAL57731.1; JOINED; Genomic_DNA.
DR EMBL; AY064552; AAL57731.1; JOINED; Genomic_DNA.
DR EMBL; AY064553; AAL57731.1; JOINED; Genomic_DNA.
DR EMBL; AY064554; AAL57731.1; JOINED; Genomic_DNA.
DR EMBL; AY064555; AAL57731.1; JOINED; Genomic_DNA.
DR EMBL; AY064556; AAL57731.1; JOINED; Genomic_DNA.
DR EMBL; AY064557; AAL57731.1; JOINED; Genomic_DNA.
DR EMBL; AY064558; AAL57731.1; JOINED; Genomic_DNA.
DR EMBL; AY064559; AAL57731.1; JOINED; Genomic_DNA.
DR EMBL; AY064560; AAL57731.1; JOINED; Genomic_DNA.
DR EMBL; AY064561; AAL57731.1; JOINED; Genomic_DNA.
DR EMBL; AY064562; AAL57731.1; JOINED; Genomic_DNA.
DR EMBL; AY064563; AAL57731.1; JOINED; Genomic_DNA.
DR EMBL; AY064564; AAL57731.1; JOINED; Genomic_DNA.
DR RefSeq; NP_001009020.1; NM_001009020.3.
DR AlphaFoldDB; Q8MJA0; -.
DR SMR; Q8MJA0; -.
DR STRING; 9598.ENSPTRP00000033573; -.
DR PaxDb; Q8MJA0; -.
DR GeneID; 449627; -.
DR KEGG; ptr:449627; -.
DR CTD; 93986; -.
DR eggNOG; KOG4385; Eukaryota.
DR HOGENOM; CLU_019502_3_1_1; -.
DR InParanoid; Q8MJA0; -.
DR TreeFam; TF326978; -.
DR Proteomes; UP000002277; Unplaced.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; ISS:UniProtKB.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0021757; P:caudate nucleus development; ISS:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0021758; P:putamen development; ISS:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
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_0000091884"
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
