TEAD2_HUMAN
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 03-AUG-2022, entry version 191.
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 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 AlphaFoldDB; Q15562; -.
DR SMR; Q15562; -.
DR BioGRID; 114041; 129.
DR DIP; DIP-59318N; -.
DR IntAct; Q15562; 85.
DR MINT; Q15562; -.
DR STRING; 9606.ENSP00000472109; -.
DR BindingDB; Q15562; -.
DR ChEMBL; CHEMBL4523301; -.
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; Q15562; -.
DR PeptideAtlas; Q15562; -.
DR PRIDE; Q15562; -.
DR ProteomicsDB; 5111; -.
DR ProteomicsDB; 60636; -. [Q15562-1]
DR Antibodypedia; 31984; 263 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 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; 823827at2759; -.
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 SignaLink; Q15562; -.
DR SIGNOR; Q15562; -.
DR BioGRID-ORCS; 8463; 13 hits in 1105 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 147 other tissues.
DR ExpressionAtlas; Q15562; baseline and differential.
DR Genevisible; Q15562; HS.
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:0060548; P:negative regulation of cell death; 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:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IMP:CAFA.
DR GO; GO:0065003; P:protein-containing complex assembly; IMP:CAFA.
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:0006355; P:regulation of transcription, DNA-templated; NAS:UniProtKB.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0001570; P:vasculogenesis; IEA:Ensembl.
DR Gene3D; 6.10.20.40; -; 1.
DR InterPro; IPR000818; TEA/ATTS_dom.
DR InterPro; IPR038096; TEA/ATTS_sf.
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 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..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:6UYC"
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 280..284
FT /evidence="ECO:0007829|PDB:5EMV"
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
