FOXP2_HYLLA
ID FOXP2_HYLLA Reviewed; 713 AA.
AC Q5QL03;
DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 1.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=Forkhead box protein P2;
GN Name=FOXP2;
OS Hylobates lar (Common gibbon) (White-handed gibbon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hylobatidae;
OC Hylobates.
OX NCBI_TaxID=9580;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
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; AY064581; AAL57732.1; -; Genomic_DNA.
DR EMBL; AY064567; AAL57732.1; JOINED; Genomic_DNA.
DR EMBL; AY064568; AAL57732.1; JOINED; Genomic_DNA.
DR EMBL; AY064570; AAL57732.1; JOINED; Genomic_DNA.
DR EMBL; AY064569; AAL57732.1; JOINED; Genomic_DNA.
DR EMBL; AY064572; AAL57732.1; JOINED; Genomic_DNA.
DR EMBL; AY064574; AAL57732.1; JOINED; Genomic_DNA.
DR EMBL; AY064576; AAL57732.1; JOINED; Genomic_DNA.
DR EMBL; AY064578; AAL57732.1; JOINED; Genomic_DNA.
DR EMBL; AY064580; AAL57732.1; JOINED; Genomic_DNA.
DR EMBL; AY064579; AAL57732.1; JOINED; Genomic_DNA.
DR EMBL; AY064577; AAL57732.1; JOINED; Genomic_DNA.
DR EMBL; AY064575; AAL57732.1; JOINED; Genomic_DNA.
DR EMBL; AY064573; AAL57732.1; JOINED; Genomic_DNA.
DR EMBL; AY064571; AAL57732.1; JOINED; Genomic_DNA.
DR AlphaFoldDB; Q5QL03; -.
DR SMR; Q5QL03; -.
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 3: Inferred from homology;
KW DNA-binding; Metal-binding; Nucleus; Repressor; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..713
FT /note="Forkhead box protein P2"
FT /id="PRO_0000091880"
FT ZN_FING 344..369
FT /note="C2H2-type"
FT DNA_BIND 502..592
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 279..337
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 386..407
FT /note="Leucine-zipper"
FT REGION 420..424
FT /note="CTBP1-binding"
FT /evidence="ECO:0000250"
FT REGION 436..463
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 647..666
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 676..713
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 286..325
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 648..663
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 699..713
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 713 AA; 79677 MW; 6E0CE0F898920D39 CRC64;
MMQESATETI SNSSMNQNGM STLSSQLDAG SRDGRSSGDT SSEVSTVELL HLQQQQALQA
ARQLLLQQQT SGLKSPKSSD KQRPLQVPVS VAMMTPQVIT PQQMQQILQQ QVLSPQQLQA
LLQQQQAVML QQQQLQEFYK KQQEQLHLQL LQQQQQQQQQ QQQQQQQQQQ QQQQQQQQQQ
QQQQQQQQQQ HPGKQAKEQQ QQQQQQQLAA QQLVFQQQLL QMQQLQQQQH LLSLQRQGLI
SIPPGQAALP VQSLPQAGLS PAEIQQLWKE VTGVHSMEDN GIKHGGLDLT TNNSSSTTSS
TTSKASPPIT HHSIVNGQSS VLNARRDSSS HEETGASHTL YGHGVCKWPG CESICEDFGQ
FLKHLNNEHA LDDRSTAQCR VQMQVVQQLE IQLSKERERL QAMMTHLHMR PSEPKPSPKP
LNLVSSVTMS KNMLETSPQS LPQTPTTPTA PVTPITQGPS VITPASVPNV GAIRRRHSDK
YNIPMSSEIA PNYEFYKNAD VRPPFTYATL IRQAIMESSD RQLTLNEIYS WFTRTFAYFR
RNAATWKNAV RHNLSLHKCF VRVENVKGAV WTVDEVEYQK RRSQKITGSP TLVKNIPTSL
GYGAALNASL QAALAESSLP LLSNPGLINN ASSGLLQAVH EDLNGSLDHI DSNGNSSPGC
SPQPHIHSIH VKEEPVIAED EDCPMSLVTT ANHSPELEDD REIEEEPLSE DLE
