ID   FOXE3_RAT               Reviewed;         286 AA.
AC   Q63250; G3V6Y8;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   24-JUN-2015, sequence version 2.
DT   03-AUG-2022, entry version 145.
DE   RecName: Full=Forkhead box protein E3;
DE   AltName: Full=Forkhead-related protein FKHL12;
DE   AltName: Full=Forkhead-related transcription factor 8;
DE            Short=FREAC-8;
DE   AltName: Full=Hepatocyte nuclear factor 3 forkhead homolog 7;
DE            Short=HFH-7;
GN   Name=Foxe3; Synonyms=Fkhl12, Freac8, Hfh7;
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 [MRNA].
RC   STRAIN=Sprague-Dawley;
RX   PubMed=7683413; DOI=10.1073/pnas.90.9.3948;
RA   Clevidence D.E., Overdier D.G., Tao W., Qian X., Pani L., Lai E.,
RA   Costa R.H.;
RT   "Identification of nine tissue-specific transcription factors of the
RT   hepatocyte nuclear factor 3/forkhead DNA-binding-domain family.";
RL   Proc. Natl. Acad. Sci. U.S.A. 90:3948-3952(1993).
RN   [2]
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Brown Norway;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Transcription factor that controls lens epithelial cell
CC       growth through regulation of proliferation, apoptosis and cell cycle
CC       (By similarity). During lens development, controls the ratio of the
CC       lens fiber cells to the cells of the anterior lens epithelium by
CC       regulating the rate of proliferation and differentiation (By
CC       similarity). Controls lens vesicle closure and subsequent separation of
CC       the lens vesicle from ectoderm (By similarity). Controls the expression
CC       of DNAJB1 in a pathway that is crucial for the development of the
CC       anterior segment of the eye (By similarity).
CC       {ECO:0000250|UniProtKB:Q13461, ECO:0000250|UniProtKB:Q9QY14}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9QY14}.
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DR   EMBL; L13207; AAA41323.1; -; mRNA.
DR   EMBL; AABR06039461; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH474008; EDL90326.1; -; Genomic_DNA.
DR   PIR; I60921; I60921.
DR   RefSeq; NP_599166.1; NM_134339.1.
DR   AlphaFoldDB; Q63250; -.
DR   SMR; Q63250; -.
DR   STRING; 10116.ENSRNOP00000010208; -.
DR   PhosphoSitePlus; Q63250; -.
DR   PaxDb; Q63250; -.
DR   Ensembl; ENSRNOT00000010208; ENSRNOP00000010208; ENSRNOG00000007770.
DR   GeneID; 171302; -.
DR   KEGG; rno:171302; -.
DR   UCSC; RGD:621727; rat.
DR   CTD; 2301; -.
DR   RGD; 621727; Foxe3.
DR   eggNOG; KOG2294; Eukaryota.
DR   GeneTree; ENSGT00940000163987; -.
DR   InParanoid; Q63250; -.
DR   OMA; MAGRSDM; -.
DR   OrthoDB; 1270467at2759; -.
DR   TreeFam; TF316127; -.
DR   PRO; PR:Q63250; -.
DR   Proteomes; UP000002494; Chromosome 5.
DR   Proteomes; UP000234681; Chromosome 5.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0005667; C:transcription regulator complex; ISO:RGD.
DR   GO; GO:0003677; F:DNA binding; ISS:UniProtKB.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; ISS:UniProtKB.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR   GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR   GO; GO:0043565; F:sequence-specific DNA binding; ISS:UniProtKB.
DR   GO; GO:0009653; P:anatomical structure morphogenesis; IBA:GO_Central.
DR   GO; GO:0043010; P:camera-type eye development; ISO:RGD.
DR   GO; GO:0048468; P:cell development; ISO:RGD.
DR   GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR   GO; GO:0061073; P:ciliary body morphogenesis; ISS:UniProtKB.
DR   GO; GO:0061303; P:cornea development in camera-type eye; ISS:UniProtKB.
DR   GO; GO:0050673; P:epithelial cell proliferation; IEA:Ensembl.
DR   GO; GO:0001654; P:eye development; ISS:UniProtKB.
DR   GO; GO:0061072; P:iris morphogenesis; ISS:UniProtKB.
DR   GO; GO:0002088; P:lens development in camera-type eye; ISS:UniProtKB.
DR   GO; GO:0042789; P:mRNA transcription by RNA polymerase II; ISS:UniProtKB.
DR   GO; GO:0043066; P:negative regulation of apoptotic process; ISS:UniProtKB.
DR   GO; GO:1902747; P:negative regulation of lens fiber cell differentiation; ISS:UniProtKB.
DR   GO; GO:0050679; P:positive regulation of epithelial cell proliferation; ISO:RGD.
DR   GO; GO:2001111; P:positive regulation of lens epithelial cell proliferation; ISS:UniProtKB.
DR   GO; GO:0051726; P:regulation of cell cycle; ISS:UniProtKB.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   GO; GO:0002930; P:trabecular meshwork development; ISS:UniProtKB.
DR   GO; GO:0006366; P:transcription by RNA polymerase II; ISO:RGD.
DR   CDD; cd00059; FH; 1.
DR   Gene3D; 1.10.10.10; -; 1.
DR   InterPro; IPR001766; Fork_head_dom.
DR   InterPro; IPR018122; TF_fork_head_CS_1.
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   PRINTS; PR00053; FORKHEAD.
DR   SMART; SM00339; FH; 1.
DR   SUPFAM; SSF46785; SSF46785; 1.
DR   PROSITE; PS00657; FORK_HEAD_1; 1.
DR   PROSITE; PS00658; FORK_HEAD_2; 1.
DR   PROSITE; PS50039; FORK_HEAD_3; 1.
PE   2: Evidence at transcript level;
KW   DNA-binding; Nucleus; Reference proteome; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..286
FT                   /note="Forkhead box protein E3"
FT                   /id="PRO_0000433236"
FT   DNA_BIND        64..158
FT                   /note="Fork-head"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00089"
FT   REGION          1..62
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   286 AA;  30469 MW;  4238A421281D4141 CRC64;
     MDAHVAFSGF PTLPSVSPSG PQPPSLAGDE PGREPEEVVG GGDSEPPAAP GPGRRRRRPL
     QRGKPPYSYI ALIAMALAHA PGRRLTLAAI YRFITERFAF YRDSPRKWQN SIRHNLTLND
     CFVKVPREPG NPGKGNYWTL DPAAADMFDN GSFLRRRKRF KRTELPAPPP PPFPYAPFPP
     APAPAPAPPA RLFRLDSLLG LQTEPPGPLA PEPPCCAAPD ASFPPCAAAA SPPLYSPAPE
     RLGLPAPLPA EPLLALAGSA GALGPLGAGE AYLRQPGFPP GLERYL