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FOXP2_RAT
ID   FOXP2_RAT               Reviewed;         710 AA.
AC   P0CF24;
DT   20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT   20-APR-2010, sequence version 1.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=Forkhead box protein P2;
GN   Name=Foxp2;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Brown Norway;
RX   PubMed=15057822; DOI=10.1038/nature02426;
RA   Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA   Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA   Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA   Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA   Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA   Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA   Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA   Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA   Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA   Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA   Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA   Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA   Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA   Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA   Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA   Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA   Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA   Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA   Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA   Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA   Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA   Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA   Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA   Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA   Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA   Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA   Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA   Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA   Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA   Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA   Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA   Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA   Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA   Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA   Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA   Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA   Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA   Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA   Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA   Mockrin S., Collins F.S.;
RT   "Genome sequence of the Brown Norway rat yields insights into mammalian
RT   evolution.";
RL   Nature 428:493-521(2004).
RN   [2]
RP   FUNCTION.
RX   PubMed=24179158; DOI=10.1126/science.1245079;
RA   Sia G.M., Clem R.L., Huganir R.L.;
RT   "The human language-associated gene SRPX2 regulates synapse formation and
RT   vocalization in mice.";
RL   Science 342:987-991(2013).
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 (By similarity). Plays a role in synapse formation by
CC       regulating SRPX2 levels. {ECO:0000250, ECO:0000269|PubMed:24179158}.
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; AC111321; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC128862; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC115440; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC122630; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; NP_001258033.1; NM_001271104.1.
DR   AlphaFoldDB; P0CF24; -.
DR   SMR; P0CF24; -.
DR   IntAct; P0CF24; 1.
DR   STRING; 10116.ENSRNOP00000007759; -.
DR   PaxDb; P0CF24; -.
DR   GeneID; 500037; -.
DR   KEGG; rno:500037; -.
DR   UCSC; RGD:1559697; rat.
DR   CTD; 93986; -.
DR   RGD; 1559697; Foxp2.
DR   VEuPathDB; HostDB:ENSRNOG00000054508; -.
DR   eggNOG; KOG4385; Eukaryota.
DR   HOGENOM; CLU_019502_3_1_1; -.
DR   InParanoid; P0CF24; -.
DR   OMA; REYPESH; -.
DR   OrthoDB; 836427at2759; -.
DR   PhylomeDB; P0CF24; -.
DR   PRO; PR:P0CF24; -.
DR   Proteomes; UP000002494; Chromosome 4.
DR   Bgee; ENSRNOG00000054508; Expressed in pancreas and 16 other tissues.
DR   Genevisible; P0CF24; RN.
DR   GO; GO:0005634; C:nucleus; ISO:RGD.
DR   GO; GO:0003677; F:DNA binding; ISO:RGD.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; ISO:RGD.
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; ISO:RGD.
DR   GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0050681; F:nuclear androgen receptor binding; IPI:RGD.
DR   GO; GO:0042803; F:protein homodimerization activity; ISO:RGD.
DR   GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; ISO:RGD.
DR   GO; GO:0043565; F:sequence-specific DNA binding; ISO:RGD.
DR   GO; GO:0001221; F:transcription coregulator binding; ISO:RGD.
DR   GO; GO:0043010; P:camera-type eye development; ISO:RGD.
DR   GO; GO:0021757; P:caudate nucleus development; ISO:RGD.
DR   GO; GO:0021702; P:cerebellar Purkinje cell differentiation; ISO:RGD.
DR   GO; GO:0021549; P:cerebellum development; ISO:RGD.
DR   GO; GO:0021987; P:cerebral cortex development; ISO:RGD.
DR   GO; GO:0030900; P:forebrain development; IEP:RGD.
DR   GO; GO:0010467; P:gene expression; ISO:RGD.
DR   GO; GO:0098582; P:innate vocalization behavior; IMP:RGD.
DR   GO; GO:0048286; P:lung alveolus development; ISO:RGD.
DR   GO; GO:0030324; P:lung development; ISO:RGD.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:RGD.
DR   GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISO:RGD.
DR   GO; GO:0050679; P:positive regulation of epithelial cell proliferation; ISO:RGD.
DR   GO; GO:0060501; P:positive regulation of epithelial cell proliferation involved in lung morphogenesis; ISO:RGD.
DR   GO; GO:0002053; P:positive regulation of mesenchymal cell proliferation; ISO:RGD.
DR   GO; GO:0009791; P:post-embryonic development; ISO:RGD.
DR   GO; GO:0021758; P:putamen development; ISO:RGD.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   GO; GO:0033574; P:response to testosterone; IEP:RGD.
DR   GO; GO:0060013; P:righting reflex; ISO:RGD.
DR   GO; GO:0007519; P:skeletal muscle tissue development; ISO:RGD.
DR   GO; GO:0048745; P:smooth muscle tissue development; ISO:RGD.
DR   GO; GO:0042297; P:vocal learning; ISO:RGD.
DR   GO; GO:0071625; P:vocalization behavior; ISO:RGD.
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   Coiled coil; DNA-binding; Metal-binding; Nucleus; Reference proteome;
KW   Repressor; Transcription; Transcription regulation; Zinc; Zinc-finger.
FT   CHAIN           1..710
FT                   /note="Forkhead box protein P2"
FT                   /id="PRO_0000393401"
FT   ZN_FING         343..366
FT                   /note="C2H2-type"
FT   DNA_BIND        499..589
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          272..334
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          383..404
FT                   /note="Leucine-zipper"
FT   REGION          417..421
FT                   /note="CTBP1-binding"
FT                   /evidence="ECO:0000250"
FT   REGION          433..460
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          644..663
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          673..710
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        283..322
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        645..660
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        696..710
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   710 AA;  79236 MW;  CB77B7D405C4B6AD CRC64;
     MMQESATETI SNSSMNQNGM STLSSQLDAG SRDGRSSGDT SSEVSTVELL HLQQQQALQA
     ARQLLLQQQT SGLKSPKSSD KQRPLQVPVS VAMMTPQVIT PQQMQQILQQ QVLSPQQLQA
     LLQQQQAVML QQQQLQEFYK KQQEQLHLQL LQQQQQQQQQ QQQQQQQQQQ QQQQQQQQQQ
     QQQQQQQHPG KQAKEQQQQQ QQQQLAAQQL VFQQQLLQMQ QLQQQQHLLS LQCQGLISIP
     PGQAALPVQS LPQAGLSPAE IQQLWKEVTG VHSQEDNGIK HGGLDLTTNN SSSTTSSTTS
     KASPPITHHS IVNGQSSVLN ARRDSSSHEE TGASHTLYGH GVCKWPGCES ICEDFGQFLK
     HLNNEHALDD RSTAQCRVQM QVVQQLEIQL SKERERLQAM MTHLHMRPSE PKPSPKPLNL
     VSSVTMSKNM LETSPQSLPQ TPTTPTAPVT PITQGPSVIT PASVPNVGAI RRRHSDKYNI
     PMSSEIAPNY EFYKNADVRP PFTYATLIRQ AIMESSDRQL TLNEIYSWFT RTFAYFRRNA
     ATWKNAVRHN LSLHKCFVRV ENVKGAVWTV DEVEYQKRRS QKITGSPTLV KNIPTSLGYG
     AALNASLQAA LAESSLPLLS NPGLINNASS GLLQAVHEDL NGSLDHIDSN GNSSPGCSPQ
     PHIHSIHVKE EPVIAEDEDC PMSLVTTANH SPELEDDREI EEEPLSEDLE
 
 
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