TEAD1_HUMAN
ID TEAD1_HUMAN Reviewed; 426 AA.
AC P28347; A4FUP2; E7EV65;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 2.
DT 03-AUG-2022, entry version 211.
DE RecName: Full=Transcriptional enhancer factor TEF-1;
DE AltName: Full=NTEF-1;
DE AltName: Full=Protein GT-IIC;
DE AltName: Full=TEA domain family member 1;
DE Short=TEAD-1;
DE AltName: Full=Transcription factor 13;
DE Short=TCF-13;
GN Name=TEAD1; Synonyms=TCF13, TEF1;
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 [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=1851669; DOI=10.1016/0092-8674(91)90088-g;
RA Xiao J.H., Davidson I., Matthes H., Garnier J.-M., Chambon P.;
RT "Cloning, expression, and transcriptional properties of the human enhancer
RT factor TEF-1.";
RL Cell 65:551-568(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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 [4]
RP DOMAIN TEA.
RX PubMed=2070413; DOI=10.1016/0092-8674(91)90132-i;
RA Buerglin T.R.;
RT "The TEA domain: a novel, highly conserved DNA-binding motif.";
RL Cell 66:11-12(1991).
RN [5]
RP FUNCTION, INTERACTION WITH YAP1, AND CHARACTERIZATION OF VARIANT SCRA
RP HIS-421.
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 [6]
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).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [10]
RP STRUCTURE BY NMR OF 28-104.
RX PubMed=17085591; DOI=10.1073/pnas.0607171103;
RA Anbanandam A., Albarado D.C., Nguyen C.T., Halder G., Gao X.,
RA Veeraraghavan S.;
RT "Insights into transcription enhancer factor 1 (TEF-1) activity from the
RT solution structure of the TEA domain.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:17225-17230(2006).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 209-426 IN COMPLEX WITH YAP1,
RP CHARACTERIZATION OF VARIANT SCRA HIS-421, AND MUTAGENESIS OF TYR-421.
RX PubMed=20123905; DOI=10.1101/gad.1865810;
RA Li Z., Zhao B., Wang P., Chen F., Dong Z., Yang H., Guan K.L., Xu Y.;
RT "Structural insights into the YAP and TEAD complex.";
RL Genes Dev. 24:235-240(2010).
RN [12]
RP VARIANT SCRA HIS-421.
RX PubMed=15016762; DOI=10.1093/hmg/ddh106;
RA Fossdal R., Jonasson F., Kristjansdottir G.T., Kong A., Stefansson H.,
RA Gosh S., Gulcher J.R., Stefansson K.;
RT "A novel TEAD1 mutation is the causative allele in Sveinsson's
RT chorioretinal atrophy (helicoid peripapillary chorioretinal
RT degeneration).";
RL Hum. Mol. Genet. 13:975-981(2004).
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 cooperatively to the
CC SPH and GT-IIC 'enhansons' (5'-GTGGAATGT-3') and activates
CC transcription in vivo in a cell-specific manner. The activation
CC function appears to be mediated by a limiting cell-specific
CC transcriptional intermediary factor (TIF). Involved in cardiac
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 ECO:0000269|PubMed:20123905}.
CC -!- INTERACTION:
CC P28347; P46937: YAP1; NbExp=11; IntAct=EBI-529156, EBI-1044059;
CC P28347; Q26366: vg; Xeno; NbExp=3; IntAct=EBI-529156, EBI-162687;
CC P28347-2; P01023: A2M; NbExp=3; IntAct=EBI-12151837, EBI-640741;
CC P28347-2; P54253: ATXN1; NbExp=3; IntAct=EBI-12151837, EBI-930964;
CC P28347-2; P07339: CTSD; NbExp=3; IntAct=EBI-12151837, EBI-2115097;
CC P28347-2; P50570-2: DNM2; NbExp=3; IntAct=EBI-12151837, EBI-10968534;
CC P28347-2; P28799: GRN; NbExp=3; IntAct=EBI-12151837, EBI-747754;
CC P28347-2; P42858: HTT; NbExp=18; IntAct=EBI-12151837, EBI-466029;
CC P28347-2; Q96CV9: OPTN; NbExp=3; IntAct=EBI-12151837, EBI-748974;
CC P28347-2; Q9BXM7: PINK1; NbExp=3; IntAct=EBI-12151837, EBI-2846068;
CC P28347-2; Q9Y3C5: RNF11; NbExp=3; IntAct=EBI-12151837, EBI-396669;
CC P28347-2; P37840: SNCA; NbExp=3; IntAct=EBI-12151837, EBI-985879;
CC P28347-2; O75382: TRIM3; NbExp=3; IntAct=EBI-12151837, EBI-2129889;
CC P28347-2; A8MV65-2: VGLL3; NbExp=3; IntAct=EBI-12151837, EBI-11957216;
CC P28347-2; O76024: WFS1; NbExp=3; IntAct=EBI-12151837, EBI-720609;
CC P28347-2; Q9GZV5: WWTR1; NbExp=3; IntAct=EBI-12151837, EBI-747743;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P28347-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P28347-2; Sequence=VSP_056275, VSP_056276, VSP_056277;
CC -!- TISSUE SPECIFICITY: Preferentially expressed in skeletal muscle. Lower
CC levels in pancreas, placenta, and heart.
CC -!- DISEASE: Sveinsson chorioretinal atrophy (SCRA) [MIM:108985]:
CC Characterized by symmetrical lesions radiating from the optic disk
CC involving the retina and the choroid. {ECO:0000269|PubMed:15016762,
CC ECO:0000269|PubMed:18579750, ECO:0000269|PubMed:20123905}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-16 is the initiator.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB00791.1; Type=Miscellaneous discrepancy; Note=Unusual initiator. The initiator methionine is coded by a non-canonical ATT isoleucine codon.; Evidence={ECO:0000305};
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DR EMBL; M63896; AAB00791.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC013549; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC084859; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC107881; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC115398; AAI15399.1; -; mRNA.
DR CCDS; CCDS7810.2; -. [P28347-1]
DR PIR; A40032; A40032.
DR RefSeq; NP_068780.2; NM_021961.5. [P28347-1]
DR PDB; 2HZD; NMR; -; A=28-104.
DR PDB; 3KYS; X-ray; 2.80 A; A/C=209-426.
DR PDB; 4RE1; X-ray; 2.20 A; A/B=209-426.
DR PDB; 4Z8E; X-ray; 2.09 A; A/B/C=28-104.
DR PDB; 5NNX; X-ray; 3.29 A; A=31-104.
DR PDB; 6HIL; X-ray; 2.30 A; A/B/C/D=208-425.
DR PDB; 6IM5; X-ray; 1.70 A; A/B=210-426.
DR PDB; 7CMM; X-ray; 3.50 A; A/B/C/D=207-426.
DR PDBsum; 2HZD; -.
DR PDBsum; 3KYS; -.
DR PDBsum; 4RE1; -.
DR PDBsum; 4Z8E; -.
DR PDBsum; 5NNX; -.
DR PDBsum; 6HIL; -.
DR PDBsum; 6IM5; -.
DR PDBsum; 7CMM; -.
DR AlphaFoldDB; P28347; -.
DR SMR; P28347; -.
DR BioGRID; 112862; 151.
DR ComplexPortal; CPX-256; YAP1-TEAD1 complex.
DR DIP; DIP-34360N; -.
DR IntAct; P28347; 141.
DR MINT; P28347; -.
DR STRING; 9606.ENSP00000435233; -.
DR BindingDB; P28347; -.
DR ChEMBL; CHEMBL3334416; -.
DR GlyGen; P28347; 3 sites, 1 O-linked glycan (3 sites).
DR iPTMnet; P28347; -.
DR PhosphoSitePlus; P28347; -.
DR SwissPalm; P28347; -.
DR BioMuta; TEAD1; -.
DR DMDM; 3041733; -.
DR EPD; P28347; -.
DR jPOST; P28347; -.
DR MassIVE; P28347; -.
DR MaxQB; P28347; -.
DR PaxDb; P28347; -.
DR PeptideAtlas; P28347; -.
DR PRIDE; P28347; -.
DR ProteomicsDB; 54479; -. [P28347-1]
DR ProteomicsDB; 674; -.
DR Antibodypedia; 11848; 259 antibodies from 33 providers.
DR DNASU; 7003; -.
DR Ensembl; ENST00000334310.10; ENSP00000334754.6; ENSG00000187079.20. [P28347-2]
DR Ensembl; ENST00000527636.7; ENSP00000435233.2; ENSG00000187079.20. [P28347-1]
DR GeneID; 7003; -.
DR KEGG; hsa:7003; -.
DR MANE-Select; ENST00000527636.7; ENSP00000435233.2; NM_021961.6; NP_068780.2.
DR UCSC; uc057zfn.1; human. [P28347-1]
DR CTD; 7003; -.
DR DisGeNET; 7003; -.
DR GeneCards; TEAD1; -.
DR HGNC; HGNC:11714; TEAD1.
DR HPA; ENSG00000187079; Low tissue specificity.
DR MalaCards; TEAD1; -.
DR MIM; 108985; phenotype.
DR MIM; 189967; gene.
DR neXtProt; NX_P28347; -.
DR OpenTargets; ENSG00000187079; -.
DR Orphanet; 86813; Helicoid peripapillary chorioretinal degeneration.
DR PharmGKB; PA36432; -.
DR VEuPathDB; HostDB:ENSG00000187079; -.
DR eggNOG; KOG3841; Eukaryota.
DR GeneTree; ENSGT00950000182956; -.
DR InParanoid; P28347; -.
DR OMA; IATHKLC; -.
DR PhylomeDB; P28347; -.
DR PathwayCommons; P28347; -.
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-9619665; EGR2 and SOX10-mediated initiation of Schwann cell myelination.
DR SignaLink; P28347; -.
DR SIGNOR; P28347; -.
DR BioGRID-ORCS; 7003; 122 hits in 1073 CRISPR screens.
DR ChiTaRS; TEAD1; human.
DR EvolutionaryTrace; P28347; -.
DR GeneWiki; TEAD1; -.
DR GenomeRNAi; 7003; -.
DR Pharos; P28347; Tchem.
DR PRO; PR:P28347; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; P28347; protein.
DR Bgee; ENSG00000187079; Expressed in skeletal muscle tissue of rectus abdominis and 187 other tissues.
DR ExpressionAtlas; P28347; baseline and differential.
DR Genevisible; P28347; HS.
DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0140552; C:TEAD-YAP complex; IDA:CAFA.
DR GO; GO:0005667; C:transcription regulator complex; IBA:GO_Central.
DR GO; GO:0000987; F:cis-regulatory region sequence-specific DNA binding; IMP:BHF-UCL.
DR GO; GO:0003677; F:DNA binding; TAS:ProtInc.
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; IMP:BHF-UCL.
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:0048568; P:embryonic organ development; IBA:GO_Central.
DR GO; GO:0035329; P:hippo signaling; IDA:UniProtKB.
DR GO; GO:0030307; P:positive regulation of cell growth; IDA:ComplexPortal.
DR GO; GO:1902895; P:positive regulation of miRNA transcription; IMP:BHF-UCL.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:ComplexPortal.
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:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR Gene3D; 6.10.20.40; -; 1.
DR IDEAL; IID00547; -.
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; Acetylation; Activator; Alternative splicing;
KW Direct protein sequencing; Disease variant; DNA-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..426
FT /note="Transcriptional enhancer factor TEF-1"
FT /id="PRO_0000205930"
FT DNA_BIND 28..104
FT /note="TEA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00505"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 167..426
FT /note="Transcriptional activation"
FT /evidence="ECO:0000255"
FT COMPBIAS 1..16
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 11
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..15
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_056275"
FT VAR_SEQ 110
FT /note="K -> KVTSM (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_056276"
FT VAR_SEQ 234..291
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_056277"
FT VARIANT 421
FT /note="Y -> H (in SCRA; loss of interaction with YAP1 and
FT also activation by YAP1; dbSNP:rs11567847)"
FT /evidence="ECO:0000269|PubMed:15016762,
FT ECO:0000269|PubMed:18579750, ECO:0000269|PubMed:20123905"
FT /id="VAR_031530"
FT MUTAGEN 421
FT /note="Y->A: Important loss of interaction with YAP1."
FT /evidence="ECO:0000269|PubMed:20123905"
FT HELIX 29..31
FT /evidence="ECO:0007829|PDB:2HZD"
FT TURN 32..35
FT /evidence="ECO:0007829|PDB:4Z8E"
FT HELIX 37..49
FT /evidence="ECO:0007829|PDB:4Z8E"
FT STRAND 52..54
FT /evidence="ECO:0007829|PDB:2HZD"
FT STRAND 62..64
FT /evidence="ECO:0007829|PDB:5NNX"
FT HELIX 69..81
FT /evidence="ECO:0007829|PDB:4Z8E"
FT HELIX 87..98
FT /evidence="ECO:0007829|PDB:4Z8E"
FT STRAND 217..230
FT /evidence="ECO:0007829|PDB:6IM5"
FT STRAND 233..242
FT /evidence="ECO:0007829|PDB:6IM5"
FT STRAND 256..258
FT /evidence="ECO:0007829|PDB:6IM5"
FT HELIX 259..261
FT /evidence="ECO:0007829|PDB:6IM5"
FT HELIX 263..265
FT /evidence="ECO:0007829|PDB:6IM5"
FT HELIX 273..279
FT /evidence="ECO:0007829|PDB:6IM5"
FT HELIX 282..284
FT /evidence="ECO:0007829|PDB:6IM5"
FT STRAND 285..292
FT /evidence="ECO:0007829|PDB:6IM5"
FT STRAND 304..316
FT /evidence="ECO:0007829|PDB:6IM5"
FT STRAND 319..328
FT /evidence="ECO:0007829|PDB:6IM5"
FT STRAND 331..341
FT /evidence="ECO:0007829|PDB:6IM5"
FT STRAND 343..345
FT /evidence="ECO:0007829|PDB:6IM5"
FT STRAND 348..357
FT /evidence="ECO:0007829|PDB:6IM5"
FT HELIX 360..370
FT /evidence="ECO:0007829|PDB:6IM5"
FT STRAND 372..374
FT /evidence="ECO:0007829|PDB:6IM5"
FT HELIX 375..382
FT /evidence="ECO:0007829|PDB:6IM5"
FT STRAND 385..393
FT /evidence="ECO:0007829|PDB:6IM5"
FT TURN 394..396
FT /evidence="ECO:0007829|PDB:6IM5"
FT STRAND 399..409
FT /evidence="ECO:0007829|PDB:6IM5"
FT STRAND 411..414
FT /evidence="ECO:0007829|PDB:6IM5"
FT STRAND 417..424
FT /evidence="ECO:0007829|PDB:6IM5"
SQ SEQUENCE 426 AA; 47946 MW; EFD8067F2770B3C7 CRC64;
MEPSSWSGSE SPAENMERMS DSADKPIDND AEGVWSPDIE QSFQEALAIY PPCGRRKIIL
SDEGKMYGRN ELIARYIKLR TGKTRTRKQV SSHIQVLARR KSRDFHSKLK DQTAKDKALQ
HMAAMSSAQI VSATAIHNKL GLPGIPRPTF PGAPGFWPGM IQTGQPGSSQ DVKPFVQQAY
PIQPAVTAPI PGFEPASAPA PSVPAWQGRS IGTTKLRLVE FSAFLEQQRD PDSYNKHLFV
HIGHANHSYS DPLLESVDIR QIYDKFPEKK GGLKELFGKG PQNAFFLVKF WADLNCNIQD
DAGAFYGVTS QYESSENMTV TCSTKVCSFG KQVVEKVETE YARFENGRFV YRINRSPMCE
YMINFIHKLK HLPEKYMMNS VLENFTILLV VTNRDTQETL LCMACVFEVS NSEHGAQHHI
YRLVKD
