ID   TEAD2_HUMAN             Reviewed;         447 AA.
AC   Q15562; B4DTJ6; M0R1T9; Q8NA25; Q96IG3;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   27-MAY-2002, sequence version 2.
DT   27-MAR-2024, entry version 200.
DE   RecName: Full=Transcriptional enhancer factor TEF-4;
DE   AltName: Full=TEA domain family member 2;
DE            Short=TEAD-2;
GN   Name=TEAD2; Synonyms=TEF4;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC   TISSUE=Placenta, and Testis;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15057824; DOI=10.1038/nature02399;
RA   Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA   Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA   Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA   Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA   Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA   Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA   Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA   Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA   Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA   McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA   Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA   Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA   She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA   Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA   Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA   Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA   Rubin E.M., Lucas S.M.;
RT   "The DNA sequence and biology of human chromosome 19.";
RL   Nature 428:529-535(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
RC   TISSUE=Eye, and Skin;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 32-367.
RC   TISSUE=Brain;
RX   PubMed=8702974; DOI=10.1074/jbc.271.36.21775;
RA   Jacquemin P., Hwang J.-J., Martial J.A., Dolle P., Davidson I.;
RT   "A novel family of developmentally regulated mammalian transcription
RT   factors containing the TEA/ATTS DNA binding domain.";
RL   J. Biol. Chem. 271:21775-21785(1996).
RN   [6]
RP   FUNCTION, AND INTERACTION WITH YAP1.
RX   PubMed=18579750; DOI=10.1101/gad.1664408;
RA   Zhao B., Ye X., Yu J., Li L., Li W., Li S., Yu J., Lin J.D., Wang C.Y.,
RA   Chinnaiyan A.M., Lai Z.C., Guan K.L.;
RT   "TEAD mediates YAP-dependent gene induction and growth control.";
RL   Genes Dev. 22:1962-1971(2008).
RN   [7]
RP   IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, AND INTERACTION WITH WWTR1.
RX   PubMed=19324877; DOI=10.1074/jbc.m900843200;
RA   Zhang H., Liu C.Y., Zha Z.Y., Zhao B., Yao J., Zhao S., Xiong Y., Lei Q.Y.,
RA   Guan K.L.;
RT   "TEAD transcription factors mediate the function of TAZ in cell growth and
RT   epithelial-mesenchymal transition.";
RL   J. Biol. Chem. 284:13355-13362(2009).
CC   -!- FUNCTION: Transcription factor which plays a key role in the Hippo
CC       signaling pathway, a pathway involved in organ size control and tumor
CC       suppression by restricting proliferation and promoting apoptosis. The
CC       core of this pathway is composed of a kinase cascade wherein MST1/MST2,
CC       in complex with its regulatory protein SAV1, phosphorylates and
CC       activates LATS1/2 in complex with its regulatory protein MOB1, which in
CC       turn phosphorylates and inactivates YAP1 oncoprotein and WWTR1/TAZ.
CC       Acts by mediating gene expression of YAP1 and WWTR1/TAZ, thereby
CC       regulating cell proliferation, migration and epithelial mesenchymal
CC       transition (EMT) induction. Binds to the SPH and GT-IIC 'enhansons'
CC       (5'-GTGGAATGT-3'). May be involved in the gene regulation of neural
CC       development. Binds to the M-CAT motif. {ECO:0000269|PubMed:18579750,
CC       ECO:0000269|PubMed:19324877}.
CC   -!- SUBUNIT: Interacts with YAP1 and WWTR1/TAZ.
CC       {ECO:0000269|PubMed:18579750, ECO:0000269|PubMed:19324877}.
CC   -!- INTERACTION:
CC       Q15562; Q5TBC7: BCL2L15; NbExp=4; IntAct=EBI-6427252, EBI-10247136;
CC       Q15562; Q15853: USF2; NbExp=3; IntAct=EBI-6427252, EBI-1055994;
CC       Q15562; P46937: YAP1; NbExp=6; IntAct=EBI-6427252, EBI-1044059;
CC       Q15562-2; Q9P2W3: GNG13; NbExp=3; IntAct=EBI-9370956, EBI-11427343;
CC       Q15562-2; Q14642: INPP5A; NbExp=3; IntAct=EBI-9370956, EBI-8670520;
CC       Q15562-2; Q01196-8: RUNX1; NbExp=3; IntAct=EBI-9370956, EBI-12001422;
CC       Q15562-2; Q8N1H7: SIX6OS1; NbExp=3; IntAct=EBI-9370956, EBI-12182077;
CC       Q15562-2; O75382: TRIM3; NbExp=3; IntAct=EBI-9370956, EBI-2129889;
CC       Q15562-2; Q99990: VGLL1; NbExp=3; IntAct=EBI-9370956, EBI-11983165;
CC       Q15562-2; A8MV65-2: VGLL3; NbExp=3; IntAct=EBI-9370956, EBI-11957216;
CC       Q15562-2; Q14135: VGLL4; NbExp=3; IntAct=EBI-9370956, EBI-5278589;
CC       Q15562-2; Q9GZV5: WWTR1; NbExp=3; IntAct=EBI-9370956, EBI-747743;
CC       Q15562-2; P46937: YAP1; NbExp=3; IntAct=EBI-9370956, EBI-1044059;
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1;
CC         IsoId=Q15562-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q15562-2; Sequence=VSP_045127;
CC       Name=3;
CC         IsoId=Q15562-3; Sequence=VSP_045126, VSP_045127;
CC       Name=4;
CC         IsoId=Q15562-4; Sequence=VSP_055673;
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DR   EMBL; AK093236; BAC04104.1; -; mRNA.
DR   EMBL; AK290736; BAF83425.1; -; mRNA.
DR   EMBL; AK300241; BAG62008.1; -; mRNA.
DR   EMBL; AC010524; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471177; EAW52469.1; -; Genomic_DNA.
DR   EMBL; BC051301; AAH51301.1; -; mRNA.
DR   EMBL; BC007556; AAH07556.1; -; mRNA.
DR   EMBL; BC018803; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; X94440; CAA64214.1; -; mRNA.
DR   CCDS; CCDS12761.1; -. [Q15562-1]
DR   CCDS; CCDS58670.1; -. [Q15562-3]
DR   CCDS; CCDS58671.1; -. [Q15562-2]
DR   CCDS; CCDS59406.1; -. [Q15562-4]
DR   PIR; G01116; G01116.
DR   RefSeq; NP_001243587.1; NM_001256658.1. [Q15562-2]
DR   RefSeq; NP_001243588.1; NM_001256659.1. [Q15562-2]
DR   RefSeq; NP_001243589.1; NM_001256660.1. [Q15562-4]
DR   RefSeq; NP_001243590.1; NM_001256661.1. [Q15562-4]
DR   RefSeq; NP_001243591.1; NM_001256662.1. [Q15562-3]
DR   RefSeq; NP_003589.1; NM_003598.1. [Q15562-1]
DR   RefSeq; XP_006723487.1; XM_006723424.1.
DR   RefSeq; XP_011525705.1; XM_011527403.1. [Q15562-2]
DR   PDB; 3L15; X-ray; 2.00 A; A/B=217-447.
DR   PDB; 5DQ8; X-ray; 2.31 A; A/B=217-447.
DR   PDB; 5DQE; X-ray; 2.18 A; A/B=217-447.
DR   PDB; 5EMV; X-ray; 2.00 A; A/B=218-446.
DR   PDB; 5HGU; X-ray; 2.05 A; A/B=217-447.
DR   PDB; 6CDY; X-ray; 2.32 A; A/B=217-447.
DR   PDB; 6E5G; X-ray; 2.43 A; A/B=217-447.
DR   PDB; 6S60; X-ray; 2.00 A; A/B=217-447.
DR   PDB; 6S64; X-ray; 2.22 A; A/B=217-447.
DR   PDB; 6S66; X-ray; 2.20 A; A/B=217-447.
DR   PDB; 6S69; X-ray; 2.15 A; A/B=217-447.
DR   PDB; 6S6J; X-ray; 2.10 A; A/B=217-447.
DR   PDB; 6UYB; X-ray; 1.54 A; A/B=217-447.
DR   PDB; 6UYC; X-ray; 1.66 A; A/B=217-447.
DR   PDB; 6VAH; X-ray; 2.11 A; A/B=217-447.
DR   PDB; 7OYJ; X-ray; 1.91 A; A/B=217-447.
DR   PDB; 7T2J; X-ray; 2.70 A; A/B=217-447.
DR   PDB; 7T2K; X-ray; 2.34 A; A/B=217-447.
DR   PDB; 7T2L; X-ray; 2.15 A; A/B=217-447.
DR   PDB; 7T2M; X-ray; 2.81 A; A/B=217-447.
DR   PDB; 7TYP; X-ray; 1.60 A; A/B=217-447.
DR   PDB; 7TYQ; X-ray; 1.88 A; A/B=217-447.
DR   PDB; 7TYU; X-ray; 1.78 A; A/B=217-447.
DR   PDB; 8CUH; X-ray; 2.40 A; A/B=217-447.
DR   PDB; 8E1O; X-ray; 2.25 A; A/B=217-447.
DR   PDB; 8P29; X-ray; 2.06 A; A/B=217-447.
DR   PDB; 8POJ; X-ray; 2.45 A; A/B=217-447.
DR   PDB; 8POM; X-ray; 1.95 A; A/B=217-447.
DR   PDB; 8PON; X-ray; 2.20 A; A/B=217-447.
DR   PDBsum; 3L15; -.
DR   PDBsum; 5DQ8; -.
DR   PDBsum; 5DQE; -.
DR   PDBsum; 5EMV; -.
DR   PDBsum; 5HGU; -.
DR   PDBsum; 6CDY; -.
DR   PDBsum; 6E5G; -.
DR   PDBsum; 6S60; -.
DR   PDBsum; 6S64; -.
DR   PDBsum; 6S66; -.
DR   PDBsum; 6S69; -.
DR   PDBsum; 6S6J; -.
DR   PDBsum; 6UYB; -.
DR   PDBsum; 6UYC; -.
DR   PDBsum; 6VAH; -.
DR   PDBsum; 7OYJ; -.
DR   PDBsum; 7T2J; -.
DR   PDBsum; 7T2K; -.
DR   PDBsum; 7T2L; -.
DR   PDBsum; 7T2M; -.
DR   PDBsum; 7TYP; -.
DR   PDBsum; 7TYQ; -.
DR   PDBsum; 7TYU; -.
DR   PDBsum; 8CUH; -.
DR   PDBsum; 8E1O; -.
DR   PDBsum; 8P29; -.
DR   PDBsum; 8POJ; -.
DR   PDBsum; 8POM; -.
DR   PDBsum; 8PON; -.
DR   AlphaFoldDB; Q15562; -.
DR   SMR; Q15562; -.
DR   BioGRID; 114041; 132.
DR   DIP; DIP-59318N; -.
DR   IntAct; Q15562; 85.
DR   MINT; Q15562; -.
DR   STRING; 9606.ENSP00000472109; -.
DR   BindingDB; Q15562; -.
DR   ChEMBL; CHEMBL4523301; -.
DR   GuidetoPHARMACOLOGY; 3241; -.
DR   iPTMnet; Q15562; -.
DR   PhosphoSitePlus; Q15562; -.
DR   SwissPalm; Q15562; -.
DR   BioMuta; TEAD2; -.
DR   DMDM; 21264529; -.
DR   EPD; Q15562; -.
DR   jPOST; Q15562; -.
DR   MassIVE; Q15562; -.
DR   MaxQB; Q15562; -.
DR   PaxDb; 9606-ENSP00000472109; -.
DR   PeptideAtlas; Q15562; -.
DR   ProteomicsDB; 5111; -.
DR   ProteomicsDB; 60636; -. [Q15562-1]
DR   Pumba; Q15562; -.
DR   Antibodypedia; 31984; 299 antibodies from 33 providers.
DR   DNASU; 8463; -.
DR   Ensembl; ENST00000311227.6; ENSP00000310701.1; ENSG00000074219.14. [Q15562-1]
DR   Ensembl; ENST00000377214.8; ENSP00000366419.4; ENSG00000074219.14. [Q15562-2]
DR   Ensembl; ENST00000539846.5; ENSP00000437928.1; ENSG00000074219.14. [Q15562-3]
DR   Ensembl; ENST00000593945.6; ENSP00000469640.2; ENSG00000074219.14. [Q15562-4]
DR   Ensembl; ENST00000598810.5; ENSP00000472109.1; ENSG00000074219.14. [Q15562-4]
DR   Ensembl; ENST00000601519.5; ENSP00000469672.1; ENSG00000074219.14. [Q15562-2]
DR   GeneID; 8463; -.
DR   KEGG; hsa:8463; -.
DR   MANE-Select; ENST00000593945.6; ENSP00000469640.2; NM_001256660.2; NP_001243589.1. [Q15562-4]
DR   UCSC; uc002png.5; human. [Q15562-1]
DR   AGR; HGNC:11715; -.
DR   CTD; 8463; -.
DR   DisGeNET; 8463; -.
DR   GeneCards; TEAD2; -.
DR   HGNC; HGNC:11715; TEAD2.
DR   HPA; ENSG00000074219; Low tissue specificity.
DR   MIM; 601729; gene.
DR   neXtProt; NX_Q15562; -.
DR   OpenTargets; ENSG00000074219; -.
DR   PharmGKB; PA36433; -.
DR   VEuPathDB; HostDB:ENSG00000074219; -.
DR   eggNOG; KOG3841; Eukaryota.
DR   GeneTree; ENSGT00950000182956; -.
DR   HOGENOM; CLU_012515_2_0_1; -.
DR   InParanoid; Q15562; -.
DR   OMA; WQTRALG; -.
DR   OrthoDB; 1408493at2759; -.
DR   PhylomeDB; Q15562; -.
DR   TreeFam; TF313443; -.
DR   PathwayCommons; Q15562; -.
DR   Reactome; R-HSA-2032785; YAP1- and WWTR1 (TAZ)-stimulated gene expression.
DR   Reactome; R-HSA-8951671; RUNX3 regulates YAP1-mediated transcription.
DR   Reactome; R-HSA-9796292; Formation of axial mesoderm.
DR   SignaLink; Q15562; -.
DR   SIGNOR; Q15562; -.
DR   BioGRID-ORCS; 8463; 14 hits in 1183 CRISPR screens.
DR   ChiTaRS; TEAD2; human.
DR   EvolutionaryTrace; Q15562; -.
DR   GeneWiki; TEAD2; -.
DR   GenomeRNAi; 8463; -.
DR   Pharos; Q15562; Tbio.
DR   PRO; PR:Q15562; -.
DR   Proteomes; UP000005640; Chromosome 19.
DR   RNAct; Q15562; Protein.
DR   Bgee; ENSG00000074219; Expressed in vena cava and 149 other cell types or tissues.
DR   ExpressionAtlas; Q15562; baseline and differential.
DR   GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
DR   GO; GO:0005829; C:cytosol; IDA:HPA.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0005634; C:nucleus; NAS:UniProtKB.
DR   GO; GO:0140552; C:TEAD-YAP complex; IDA:CAFA.
DR   GO; GO:0005667; C:transcription regulator complex; IBA:GO_Central.
DR   GO; GO:0097718; F:disordered domain specific binding; IMP:CAFA.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:UniProtKB.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB.
DR   GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR   GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IDA:ARUK-UCL.
DR   GO; GO:0001223; F:transcription coactivator binding; IPI:CAFA.
DR   GO; GO:0071300; P:cellular response to retinoic acid; IEA:Ensembl.
DR   GO; GO:0003143; P:embryonic heart tube morphogenesis; IEA:Ensembl.
DR   GO; GO:0048568; P:embryonic organ development; IBA:GO_Central.
DR   GO; GO:0035329; P:hippo signaling; IDA:UniProtKB.
DR   GO; GO:0048368; P:lateral mesoderm development; IEA:Ensembl.
DR   GO; GO:0001843; P:neural tube closure; IEA:Ensembl.
DR   GO; GO:0030903; P:notochord development; IEA:Ensembl.
DR   GO; GO:0048339; P:paraxial mesoderm development; IEA:Ensembl.
DR   GO; GO:0045893; P:positive regulation of DNA-templated transcription; IMP:CAFA.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR   GO; GO:0065003; P:protein-containing complex assembly; IMP:CAFA.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; NAS:UniProtKB.
DR   GO; GO:2000736; P:regulation of stem cell differentiation; IEA:Ensembl.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   GO; GO:0006366; P:transcription by RNA polymerase II; IEA:Ensembl.
DR   GO; GO:0001570; P:vasculogenesis; IEA:Ensembl.
DR   Gene3D; 2.70.50.80; -; 1.
DR   Gene3D; 6.10.20.40; TEA/ATTS domain; 1.
DR   InterPro; IPR000818; TEA/ATTS_dom.
DR   InterPro; IPR038096; TEA/ATTS_sf.
DR   InterPro; IPR016361; TEF_metazoa.
DR   InterPro; IPR041086; YBD.
DR   PANTHER; PTHR11834; TRANSCRIPTIONAL ENHANCER FACTOR TEF RELATED; 1.
DR   PANTHER; PTHR11834:SF5; TRANSCRIPTIONAL ENHANCER FACTOR TEF-4; 1.
DR   Pfam; PF01285; TEA; 1.
DR   Pfam; PF17725; YBD; 1.
DR   PIRSF; PIRSF002603; TEF; 1.
DR   PRINTS; PR00065; TEADOMAIN.
DR   SMART; SM00426; TEA; 1.
DR   PROSITE; PS00554; TEA_1; 1.
DR   PROSITE; PS51088; TEA_2; 1.
DR   Genevisible; Q15562; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Activator; Alternative splicing; DNA-binding; Nucleus;
KW   Reference proteome; Transcription; Transcription regulation.
FT   CHAIN           1..447
FT                   /note="Transcriptional enhancer factor TEF-4"
FT                   /id="PRO_0000205932"
FT   DNA_BIND        38..114
FT                   /note="TEA"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00505"
FT   REGION          1..46
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          172..447
FT                   /note="Transcriptional activation"
FT                   /evidence="ECO:0000255"
FT   REGION          183..218
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        195..217
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VAR_SEQ         1..131
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:14702039,
FT                   ECO:0000303|PubMed:15489334"
FT                   /id="VSP_045126"
FT   VAR_SEQ         120
FT                   /note="K -> KALNV (in isoform 4)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_055673"
FT   VAR_SEQ         155
FT                   /note="P -> PQVV (in isoform 2 and isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:14702039,
FT                   ECO:0000303|PubMed:15489334"
FT                   /id="VSP_045127"
FT   CONFLICT        144
FT                   /note="P -> L (in Ref. 5; CAA64214)"
FT                   /evidence="ECO:0000305"
FT   STRAND          221..224
FT                   /evidence="ECO:0007829|PDB:7TYP"
FT   STRAND          229..238
FT                   /evidence="ECO:0007829|PDB:6UYB"
FT   HELIX           240..243
FT                   /evidence="ECO:0007829|PDB:6UYB"
FT   STRAND          249..254
FT                   /evidence="ECO:0007829|PDB:6UYB"
FT   STRAND          267..270
FT                   /evidence="ECO:0007829|PDB:6UYB"
FT   HELIX           271..277
FT                   /evidence="ECO:0007829|PDB:6UYB"
FT   STRAND          281..283
FT                   /evidence="ECO:0007829|PDB:7TYP"
FT   HELIX           285..291
FT                   /evidence="ECO:0007829|PDB:6UYB"
FT   HELIX           294..296
FT                   /evidence="ECO:0007829|PDB:6UYB"
FT   STRAND          297..304
FT                   /evidence="ECO:0007829|PDB:6UYB"
FT   STRAND          326..337
FT                   /evidence="ECO:0007829|PDB:6UYB"
FT   STRAND          340..349
FT                   /evidence="ECO:0007829|PDB:6UYB"
FT   STRAND          352..362
FT                   /evidence="ECO:0007829|PDB:6UYB"
FT   STRAND          364..366
FT                   /evidence="ECO:0007829|PDB:6UYB"
FT   STRAND          369..378
FT                   /evidence="ECO:0007829|PDB:6UYB"
FT   HELIX           381..390
FT                   /evidence="ECO:0007829|PDB:6UYB"
FT   HELIX           396..403
FT                   /evidence="ECO:0007829|PDB:6UYB"
FT   STRAND          406..414
FT                   /evidence="ECO:0007829|PDB:6UYB"
FT   TURN            415..417
FT                   /evidence="ECO:0007829|PDB:6UYB"
FT   STRAND          420..430
FT                   /evidence="ECO:0007829|PDB:6UYB"
FT   TURN            433..435
FT                   /evidence="ECO:0007829|PDB:6UYB"
FT   STRAND          438..445
FT                   /evidence="ECO:0007829|PDB:6UYB"
SQ   SEQUENCE   447 AA;  49243 MW;  A9077F55638A3AC7 CRC64;
     MGEPRAGAAL DDGSGWTGSE EGSEEGTGGS EGAGGDGGPD AEGVWSPDIE QSFQEALAIY
     PPCGRRKIIL SDEGKMYGRN ELIARYIKLR TGKTRTRKQV SSHIQVLARR KSREIQSKLK
     DQVSKDKAFQ TMATMSSAQL ISAPSLQAKL GPTGPQASEL FQFWSGGSGP PWNVPDVKPF
     SQTPFTLSLT PPSTDLPGYE PPQALSPLPP PTPSPPAWQA RGLGTARLQL VEFSAFVEPP
     DAVDSYQRHL FVHISQHCPS PGAPPLESVD VRQIYDKFPE KKGGLRELYD RGPPHAFFLV
     KFWADLNWGP SGEEAGAGGS ISSGGFYGVS SQYESLEHMT LTCSSKVCSF GKQVVEKVET
     ERAQLEDGRF VYRLLRSPMC EYLVNFLHKL RQLPERYMMN SVLENFTILQ VVTNRDTQEL
     LLCTAYVFEV STSERGAQHH IYRLVRD
//