FOXP2_GORGO
ID FOXP2_GORGO Reviewed; 713 AA.
AC Q8MJ99; Q5QL02;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Forkhead box protein P2;
GN Name=FOXP2;
OS Gorilla gorilla gorilla (Western lowland gorilla).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Gorilla.
OX NCBI_TaxID=9595;
RN [1]
RP NUCLEOTIDE SEQUENCE [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].
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; AF512948; AAN03386.1; -; mRNA.
DR EMBL; AY143180; AAN60058.1; -; mRNA.
DR EMBL; AY064597; AAL57733.1; -; Genomic_DNA.
DR EMBL; AY064583; AAL57733.1; JOINED; Genomic_DNA.
DR EMBL; AY064584; AAL57733.1; JOINED; Genomic_DNA.
DR EMBL; AY064586; AAL57733.1; JOINED; Genomic_DNA.
DR EMBL; AY064585; AAL57733.1; JOINED; Genomic_DNA.
DR EMBL; AY064588; AAL57733.1; JOINED; Genomic_DNA.
DR EMBL; AY064590; AAL57733.1; JOINED; Genomic_DNA.
DR EMBL; AY064592; AAL57733.1; JOINED; Genomic_DNA.
DR EMBL; AY064594; AAL57733.1; JOINED; Genomic_DNA.
DR EMBL; AY064596; AAL57733.1; JOINED; Genomic_DNA.
DR EMBL; AY064595; AAL57733.1; JOINED; Genomic_DNA.
DR EMBL; AY064593; AAL57733.1; JOINED; Genomic_DNA.
DR EMBL; AY064591; AAL57733.1; JOINED; Genomic_DNA.
DR EMBL; AY064589; AAL57733.1; JOINED; Genomic_DNA.
DR EMBL; AY064587; AAL57733.1; JOINED; Genomic_DNA.
DR RefSeq; NP_001266466.1; NM_001279537.1.
DR AlphaFoldDB; Q8MJ99; -.
DR SMR; Q8MJ99; -.
DR GeneID; 101150977; -.
DR KEGG; ggo:101150977; -.
DR CTD; 93986; -.
DR InParanoid; Q8MJ99; -.
DR OrthoDB; 836427at2759; -.
DR Proteomes; UP000001519; 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..713
FT /note="Forkhead box protein P2"
FT /id="PRO_0000091878"
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..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 283..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; 1F326A13E8019CB5 CRC64;
MMQESATETI SNSSMNQNGM STLSSQLDAG SRDGRSSGDT SSEVSTVELL HLQQQQALQA
ARQLLLQQQT SGLKSPKSSD KQRPLQVPVS VAMMTPQVIT PQQMQQILQQ QVLSPQQLQA
LLQQQQAVML QQQQLQEFYK KQQEQLHLQL LQQQQQQQQQ QQQQQQQQQQ QQQQQQQQQQ
QQQQQQQQQH PGKQAKEQQQ 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
