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 27-MAR-2024, entry version 92.
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.ENSRNOP00000069190; -.
DR PhosphoSitePlus; P0CF24; -.
DR PaxDb; 10116-ENSRNOP00000007759; -.
DR GeneID; 500037; -.
DR KEGG; rno:500037; -.
DR UCSC; RGD:1559697; rat.
DR AGR; RGD:1559697; -.
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 OrthoDB; 5385885at2759; -.
DR PhylomeDB; P0CF24; -.
DR PRO; PR:P0CF24; -.
DR Proteomes; UP000002494; Chromosome 4.
DR Bgee; ENSRNOG00000054508; Expressed in pancreas and 16 other cell types or 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: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:0060502; P:epithelial cell proliferation involved in lung morphogenesis; 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:0045892; P:negative regulation of DNA-templated transcription; ISO:RGD.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; 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; cd20065; FH_FOXP2; 1.
DR Gene3D; 1.20.5.340; -; 1.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR InterPro; IPR047412; FH_FOXP1_P2.
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 PANTHER; PTHR45796; FORKHEAD BOX P, ISOFORM C; 1.
DR PANTHER; PTHR45796:SF1; FORKHEAD BOX PROTEIN P2; 1.
DR Pfam; PF00250; Forkhead; 1.
DR Pfam; PF16159; FOXP-CC; 1.
DR PRINTS; PR00053; FORKHEAD.
DR SMART; SM00339; FH; 1.
DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 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
//
