TEAD4_MOUSE
ID TEAD4_MOUSE Reviewed; 427 AA.
AC Q62296; A2BDD5; P70282; Q61174; Q61175; Q62298;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=Transcriptional enhancer factor TEF-3;
DE AltName: Full=ETF-related factor 2;
DE Short=ETFR-2;
DE AltName: Full=TEA domain family member 4;
DE Short=TEAD-4;
DE AltName: Full=TEF-1-related factor 1;
DE AltName: Full=TEF-1-related factor FR-19;
DE Short=RTEF-1;
GN Name=Tead4; Synonyms=Tcf13r1, Tef3, Tefr1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
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 [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS LONG AND SHORT).
RX PubMed=8920920; DOI=10.1006/bbrc.1996.1667;
RA Yasunami M., Suzuki K., Ohkubo H.;
RT "A novel family of TEA domain-containing transcription factors with
RT distinct spatiotemporal expression patterns.";
RL Biochem. Biophys. Res. Commun. 228:365-370(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS LONG AND SHORT).
RC STRAIN=C3H/HeJ;
RX PubMed=8631987; DOI=10.1074/jbc.271.7.3727;
RA Yockey C.E., Smith G., Izumo S., Shimizu N.;
RT "cDNA cloning and characterization of murine transcriptional enhancer
RT factor-1-related protein 1, a transcription factor that binds to the M-CAT
RT motif.";
RL J. Biol. Chem. 271:3727-3736(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM SHORT).
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 7-427 (ISOFORMS LONG AND SHORT).
RC STRAIN=BALB/cJ;
RX PubMed=8662936; DOI=10.1074/jbc.271.23.13786;
RA Hsu D.K.W., Guo Y., Alberts G.F., Copeland N.G., Gilbert D.J.,
RA Jenkins N.A., Peifley K.A., Winkles J.A.;
RT "Identification of a murine TEF-1-related gene expressed after mitogenic
RT stimulation of quiescent fibroblasts and during myogenic differentiation.";
RL J. Biol. Chem. 271:13786-13795(1996).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 210-427 IN COMPLEX WITH YAP1.
RX PubMed=20123908; DOI=10.1101/gad.1865310;
RA Chen L., Chan S.W., Zhang X., Walsh M., Lim C.J., Hong W., Song H.;
RT "Structural basis of YAP recognition by TEAD4 in the hippo pathway.";
RL Genes Dev. 24:290-300(2010).
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 specifically and non-cooperatively to
CC the Sph and GT-IIC 'enhansons' (5'-GTGGAATGT-3') and activates
CC transcription. Binds to the M-CAT motif (By similarity). Might play a
CC role in the embryonic development of skeletal muscle. {ECO:0000250}.
CC -!- SUBUNIT: Interacts with WWTR1/TAZ (By similarity). Interacts with YAP1.
CC {ECO:0000250, ECO:0000269|PubMed:20123908}.
CC -!- INTERACTION:
CC Q62296; Q80V24: Vgll4; NbExp=3; IntAct=EBI-9253444, EBI-9253433;
CC Q62296-1; Q99NC0: Vgll1; NbExp=4; IntAct=EBI-15985676, EBI-15985690;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=Long; Synonyms=TEFR1A, ETFR-2A;
CC IsoId=Q62296-1; Sequence=Displayed;
CC Name=Short; Synonyms=TEFR1B, ETFR-2B;
CC IsoId=Q62296-2; Sequence=VSP_006390;
CC -!- TISSUE SPECIFICITY: Preferentially expressed in lung and in skeletal
CC muscle.
CC -!- INDUCTION: By FGF-1, FGF-2, calf serum, platelet-derived growth factor-
CC BB, and phorbol 12-myristate 13-acetate.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB12488.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAB12488.1; Type=Miscellaneous discrepancy; Note=Unusual initiator. The initiator methionine is coded by a non-canonical ATA isoleucine codon.; Evidence={ECO:0000305};
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DR EMBL; X94441; CAA64215.2; -; mRNA.
DR EMBL; D87966; BAA13519.1; -; mRNA.
DR EMBL; D87965; BAA13518.1; -; mRNA.
DR EMBL; L26343; AAB12488.1; ALT_SEQ; mRNA.
DR EMBL; L26344; AAC37680.1; -; mRNA.
DR EMBL; BC130257; AAI30258.1; -; mRNA.
DR EMBL; U51743; AAC52646.1; -; mRNA.
DR EMBL; U51745; AAC52647.1; -; mRNA.
DR CCDS; CCDS39645.1; -. [Q62296-2]
DR CCDS; CCDS39646.1; -. [Q62296-1]
DR PIR; JC5254; JC5254.
DR PIR; JC5255; JC5255.
DR RefSeq; NP_001074448.2; NM_001080979.1. [Q62296-2]
DR RefSeq; NP_035697.3; NM_011567.2. [Q62296-1]
DR PDB; 3JUA; X-ray; 3.00 A; A/C/E/G=210-427.
DR PDB; 4LN0; X-ray; 2.90 A; A/B=209-427.
DR PDB; 5GN0; X-ray; 2.90 A; A/B/C/D=210-427.
DR PDB; 5XJD; X-ray; 2.22 A; A/B=210-427.
DR PDB; 5Z2Q; X-ray; 2.74 A; A/B=210-427.
DR PDB; 6L9F; X-ray; 2.56 A; A/B=209-427.
DR PDB; 6SBA; X-ray; 1.30 A; A=209-427.
DR PDBsum; 3JUA; -.
DR PDBsum; 4LN0; -.
DR PDBsum; 5GN0; -.
DR PDBsum; 5XJD; -.
DR PDBsum; 5Z2Q; -.
DR PDBsum; 6L9F; -.
DR PDBsum; 6SBA; -.
DR AlphaFoldDB; Q62296; -.
DR SMR; Q62296; -.
DR BioGRID; 204101; 4.
DR CORUM; Q62296; -.
DR DIP; DIP-59847N; -.
DR IntAct; Q62296; 5.
DR STRING; 10090.ENSMUSP00000006311; -.
DR ChEMBL; CHEMBL4680035; -.
DR PhosphoSitePlus; Q62296; -.
DR SwissPalm; Q62296; -.
DR MaxQB; Q62296; -.
DR PaxDb; Q62296; -.
DR PeptideAtlas; Q62296; -.
DR PRIDE; Q62296; -.
DR ProteomicsDB; 262851; -. [Q62296-1]
DR ProteomicsDB; 262852; -. [Q62296-2]
DR Antibodypedia; 22199; 283 antibodies from 30 providers.
DR DNASU; 21679; -.
DR Ensembl; ENSMUST00000006311; ENSMUSP00000006311; ENSMUSG00000030353. [Q62296-1]
DR Ensembl; ENSMUST00000112157; ENSMUSP00000107784; ENSMUSG00000030353. [Q62296-2]
DR Ensembl; ENSMUST00000130454; ENSMUSP00000118083; ENSMUSG00000030353. [Q62296-2]
DR GeneID; 21679; -.
DR KEGG; mmu:21679; -.
DR UCSC; uc009ede.1; mouse. [Q62296-1]
DR UCSC; uc009edf.2; mouse. [Q62296-2]
DR CTD; 7004; -.
DR MGI; MGI:106907; Tead4.
DR eggNOG; KOG3841; Eukaryota.
DR GeneTree; ENSGT00950000182956; -.
DR InParanoid; Q62296; -.
DR OMA; AISGFWQ; -.
DR OrthoDB; 823827at2759; -.
DR PhylomeDB; Q62296; -.
DR TreeFam; TF313443; -.
DR Reactome; R-MMU-2032785; YAP1- and WWTR1 (TAZ)-stimulated gene expression.
DR Reactome; R-MMU-8951671; RUNX3 regulates YAP1-mediated transcription.
DR BioGRID-ORCS; 21679; 3 hits in 77 CRISPR screens.
DR ChiTaRS; Tead4; mouse.
DR EvolutionaryTrace; Q62296; -.
DR PRO; PR:Q62296; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q62296; protein.
DR Bgee; ENSMUSG00000030353; Expressed in ectoplacental cone and 117 other tissues.
DR ExpressionAtlas; Q62296; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0032993; C:protein-DNA complex; IDA:MGI.
DR GO; GO:0005667; C:transcription regulator complex; IDA:MGI.
DR GO; GO:0003677; F:DNA binding; IDA:MGI.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:NTNU_SB.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:MGI.
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; IDA:NTNU_SB.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:MGI.
DR GO; GO:0001825; P:blastocyst formation; IMP:MGI.
DR GO; GO:0045165; P:cell fate commitment; IDA:MGI.
DR GO; GO:0001708; P:cell fate specification; IMP:MGI.
DR GO; GO:0007566; P:embryo implantation; IMP:MGI.
DR GO; GO:0048568; P:embryonic organ development; IBA:GO_Central.
DR GO; GO:0035329; P:hippo signaling; ISO:MGI.
DR GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR GO; GO:1902459; P:positive regulation of stem cell population maintenance; IGI:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:NTNU_SB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IMP:MGI.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
DR GO; GO:0001830; P:trophectodermal cell fate commitment; IMP:MGI.
DR Gene3D; 6.10.20.40; -; 1.
DR IDEAL; IID50291; -.
DR InterPro; IPR000818; TEA/ATTS_dom.
DR InterPro; IPR038096; TEA/ATTS_sf.
DR InterPro; IPR027255; TEF-3.
DR InterPro; IPR016361; TEF_metazoa.
DR InterPro; IPR041086; YBD.
DR Pfam; PF01285; TEA; 1.
DR Pfam; PF17725; YBD; 1.
DR PIRSF; PIRSF002603; TEF; 1.
DR PIRSF; PIRSF500722; TEF-3; 1.
DR PRINTS; PR00065; TEADOMAIN.
DR SMART; SM00426; TEA; 1.
DR PROSITE; PS00554; TEA_1; 1.
DR PROSITE; PS51088; TEA_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; Alternative splicing; DNA-binding; Nucleus;
KW Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..427
FT /note="Transcriptional enhancer factor TEF-3"
FT /id="PRO_0000205938"
FT DNA_BIND 29..105
FT /note="TEA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00505"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 163..206
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 78..94
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 1..23
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 178..204
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 112..154
FT /note="Missing (in isoform Short)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:8631987, ECO:0000303|PubMed:8662936,
FT ECO:0000303|PubMed:8920920"
FT /id="VSP_006390"
FT CONFLICT 142
FT /note="A -> L (in Ref. 3; AAB12488)"
FT /evidence="ECO:0000305"
FT STRAND 211..213
FT /evidence="ECO:0007829|PDB:5Z2Q"
FT STRAND 218..228
FT /evidence="ECO:0007829|PDB:6SBA"
FT STRAND 231..233
FT /evidence="ECO:0007829|PDB:5XJD"
FT STRAND 238..244
FT /evidence="ECO:0007829|PDB:6SBA"
FT STRAND 250..252
FT /evidence="ECO:0007829|PDB:4LN0"
FT STRAND 257..259
FT /evidence="ECO:0007829|PDB:6SBA"
FT HELIX 260..262
FT /evidence="ECO:0007829|PDB:6SBA"
FT HELIX 264..266
FT /evidence="ECO:0007829|PDB:6SBA"
FT STRAND 270..272
FT /evidence="ECO:0007829|PDB:6L9F"
FT HELIX 274..280
FT /evidence="ECO:0007829|PDB:6SBA"
FT HELIX 283..285
FT /evidence="ECO:0007829|PDB:6SBA"
FT STRAND 286..293
FT /evidence="ECO:0007829|PDB:6SBA"
FT HELIX 299..302
FT /evidence="ECO:0007829|PDB:6SBA"
FT STRAND 305..317
FT /evidence="ECO:0007829|PDB:6SBA"
FT STRAND 320..329
FT /evidence="ECO:0007829|PDB:6SBA"
FT STRAND 332..342
FT /evidence="ECO:0007829|PDB:6SBA"
FT STRAND 344..346
FT /evidence="ECO:0007829|PDB:6SBA"
FT STRAND 349..358
FT /evidence="ECO:0007829|PDB:6SBA"
FT HELIX 362..371
FT /evidence="ECO:0007829|PDB:6SBA"
FT STRAND 373..375
FT /evidence="ECO:0007829|PDB:6L9F"
FT HELIX 376..384
FT /evidence="ECO:0007829|PDB:6SBA"
FT STRAND 386..394
FT /evidence="ECO:0007829|PDB:6SBA"
FT TURN 395..397
FT /evidence="ECO:0007829|PDB:6SBA"
FT STRAND 400..410
FT /evidence="ECO:0007829|PDB:6SBA"
FT TURN 413..415
FT /evidence="ECO:0007829|PDB:5XJD"
FT STRAND 418..425
FT /evidence="ECO:0007829|PDB:6SBA"
SQ SEQUENCE 427 AA; 48028 MW; 8A0E9749840D88EC CRC64;
MTSNEWSSPD SPEGSSISGG SQALDKPIDN DAEGVWSPEI ERSFQEALAI YPPCGRRKII
LTEEGKMYGR NELIARHIKL RTGKTRTRKQ VSSHIQVLAR RKAREIQAKL KDQAAKNKAL
QSMAAMSSAQ IVSATAFHSK MALARGPGYP AISGFWQGAL PGQPGTSHDV KPFSQNTYPV
QPPLPLPGFE SPAGPTPSPS APLAPPWQGR SIASSKLWML EFSAFLERQQ DPDTYNKHLF
VHISQSSPSY SDPYLETVDI RQIYDKFPEK KGGLKELFER GPSNAFFLVK FWADLNTNID
DEGSAFYGVS SQYESPENMI ITCSTKVCSF GKQVVEKVET EYARYENGHY LYRIHRSPLC
EYMINFIHKL KHLPEKYMMN SVLENFTILQ VVTNRDTQET LLCIAYVFEV SASEHGAQHH
IYRLVKE
