ZEB1_MOUSE
ID ZEB1_MOUSE Reviewed; 1117 AA.
AC Q64318; A4QPD2; Q62519;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 185.
DE RecName: Full=Zinc finger E-box-binding homeobox 1;
DE AltName: Full=Delta EF1;
DE AltName: Full=Transcription factor 8;
DE Short=TCF-8;
DE AltName: Full=Zinc finger homeobox protein 1a;
DE Short=MEB1;
GN Name=Zeb1; Synonyms=Tcf8, Zfhx1a, Zfx1a, Zfx1ha;
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].
RC STRAIN=C57BL/6J; TISSUE=Embryo;
RX PubMed=8964504; DOI=10.1016/0378-1119(96)00185-0;
RA Sekido R., Takagi T., Okanami M., Moribe H., Yamamura M., Higashi Y.,
RA Kondoh H.;
RT "Organization of the gene encoding transcriptional repressor deltaEF1 and
RT cross-species conservation of its domains.";
RL Gene 173:227-232(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Spleen;
RA Wu Y., Montoya G.D., Rubin S.E., Brodie S.G., Jenkins N., Williams T.M.;
RL Submitted (MAY-1995) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Brain;
RX PubMed=8647466; DOI=10.1016/0378-1119(95)00824-1;
RA Genetta T., Kadesch T.;
RT "Cloning of a cDNA encoding a mouse transcriptional repressor displaying
RT striking sequence conservation across vertebrates.";
RL Gene 169:289-290(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 FUNCTION.
RX PubMed=19935649; DOI=10.1038/ncb1998;
RA Wellner U., Schubert J., Burk U.C., Schmalhofer O., Zhu F., Sonntag A.,
RA Waldvogel B., Vannier C., Darling D., zur Hausen A., Brunton V.G.,
RA Morton J., Sansom O., Schuler J., Stemmler M.P., Herzberger C., Hopt U.,
RA Keck T., Brabletz S., Brabletz T.;
RT "The EMT-activator ZEB1 promotes tumorigenicity by repressing stemness-
RT inhibiting microRNAs.";
RL Nat. Cell Biol. 11:1487-1495(2009).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-293; SER-302; SER-657;
RP SER-664; SER-671; SER-678 AND SER-682, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Spleen, and
RC Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [7]
RP FUNCTION, DNA-BINDING, INDUCTION, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=20346398; DOI=10.1016/j.mcn.2010.03.006;
RA Ravanpay A.C., Hansen S.J., Olson J.M.;
RT "Transcriptional inhibition of REST by NeuroD2 during neuronal
RT differentiation.";
RL Mol. Cell. Neurosci. 44:178-189(2010).
CC -!- FUNCTION: Acts as a transcriptional repressor. Binds to E-box sequences
CC in the immunoglobulin heavy chain enhancer as well as in the regulatory
CC regions of many other tissue-specific genes. Represses E-cadherin
CC promoter and induces an epithelial-mesenchymal transition (EMT) by
CC recruiting SMARCA4/BRG1. Represses BCL6 transcription in the presence
CC of the corepressor CTBP1 (By similarity). Positively regulates neuronal
CC differentiation. Represses RCOR1 transcription activation during
CC neurogenesis. Represses transcription by binding to the E box (5'-
CC CANNTG-3'). Promotes tumorigenicity by repressing stemness-inhibiting
CC microRNAs. {ECO:0000250, ECO:0000269|PubMed:19935649,
CC ECO:0000269|PubMed:20346398}.
CC -!- SUBUNIT: Interacts (via N-terminus) with SMARCA4/BRG1. {ECO:0000250}.
CC -!- INTERACTION:
CC Q64318; O88712: Ctbp1; NbExp=5; IntAct=EBI-8560245, EBI-604547;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20346398}.
CC -!- TISSUE SPECIFICITY: Expressed in the external germinal layer (EGL) and
CC internal granular layer (IGL) of the cerebellum (at protein level).
CC {ECO:0000269|PubMed:20346398}.
CC -!- INDUCTION: Up-regulated during NEUROD2-induced neurogenesis.
CC {ECO:0000269|PubMed:20346398}.
CC -!- SIMILARITY: Belongs to the delta-EF1/ZFH-1 C2H2-type zinc-finger
CC family. {ECO:0000305}.
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DR EMBL; U26259; AAA67564.1; -; mRNA.
DR EMBL; D76432; BAA11177.1; -; mRNA.
DR EMBL; L48363; AAB08442.1; -; Genomic_DNA.
DR EMBL; BC139769; AAI39770.1; -; mRNA.
DR CCDS; CCDS29039.1; -.
DR PIR; JC4934; JC4934.
DR RefSeq; NP_035676.1; NM_011546.3.
DR AlphaFoldDB; Q64318; -.
DR BioGRID; 204010; 20.
DR DIP; DIP-60280N; -.
DR IntAct; Q64318; 4.
DR MINT; Q64318; -.
DR STRING; 10090.ENSMUSP00000025081; -.
DR iPTMnet; Q64318; -.
DR PhosphoSitePlus; Q64318; -.
DR EPD; Q64318; -.
DR jPOST; Q64318; -.
DR MaxQB; Q64318; -.
DR PaxDb; Q64318; -.
DR PRIDE; Q64318; -.
DR ProteomicsDB; 302055; -.
DR Antibodypedia; 12930; 754 antibodies from 45 providers.
DR DNASU; 21417; -.
DR Ensembl; ENSMUST00000025081; ENSMUSP00000025081; ENSMUSG00000024238.
DR GeneID; 21417; -.
DR KEGG; mmu:21417; -.
DR UCSC; uc008dyy.2; mouse.
DR CTD; 6935; -.
DR MGI; MGI:1344313; Zeb1.
DR VEuPathDB; HostDB:ENSMUSG00000024238; -.
DR eggNOG; KOG3623; Eukaryota.
DR GeneTree; ENSGT00950000183208; -.
DR HOGENOM; CLU_005890_0_1_1; -.
DR InParanoid; Q64318; -.
DR OMA; IKTSQCS; -.
DR OrthoDB; 890458at2759; -.
DR PhylomeDB; Q64318; -.
DR TreeFam; TF331759; -.
DR BioGRID-ORCS; 21417; 4 hits in 72 CRISPR screens.
DR ChiTaRS; Zeb1; mouse.
DR PRO; PR:Q64318; -.
DR Proteomes; UP000000589; Chromosome 18.
DR RNAct; Q64318; protein.
DR Bgee; ENSMUSG00000024238; Expressed in meninx of diencephalon and 271 other tissues.
DR ExpressionAtlas; Q64318; baseline and differential.
DR Genevisible; Q64318; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; IDA:MGI.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IDA:MGI.
DR GO; GO:0003690; F:double-stranded DNA binding; ISO:MGI.
DR GO; GO:0070888; F:E-box binding; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; ISO:MGI.
DR GO; GO:0048856; P:anatomical structure development; IBA:GO_Central.
DR GO; GO:0048513; P:animal organ development; IMP:MGI.
DR GO; GO:0051216; P:cartilage development; IMP:MGI.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0008283; P:cell population proliferation; IMP:MGI.
DR GO; GO:0071230; P:cellular response to amino acid stimulus; IDA:MGI.
DR GO; GO:0071560; P:cellular response to transforming growth factor beta stimulus; IEA:Ensembl.
DR GO; GO:0007417; P:central nervous system development; IGI:MGI.
DR GO; GO:0090103; P:cochlea morphogenesis; IMP:MGI.
DR GO; GO:0048596; P:embryonic camera-type eye morphogenesis; IMP:MGI.
DR GO; GO:0048598; P:embryonic morphogenesis; IGI:MGI.
DR GO; GO:0048704; P:embryonic skeletal system morphogenesis; IMP:MGI.
DR GO; GO:0050673; P:epithelial cell proliferation; IMP:MGI.
DR GO; GO:0030900; P:forebrain development; IEA:Ensembl.
DR GO; GO:0043616; P:keratinocyte proliferation; IMP:MGI.
DR GO; GO:0045602; P:negative regulation of endothelial cell differentiation; ISO:MGI.
DR GO; GO:0030857; P:negative regulation of epithelial cell differentiation; IMP:MGI.
DR GO; GO:0050680; P:negative regulation of epithelial cell proliferation; IMP:MGI.
DR GO; GO:0010839; P:negative regulation of keratinocyte proliferation; IMP:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:MGI.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0007389; P:pattern specification process; IMP:MGI.
DR GO; GO:0045666; P:positive regulation of neuron differentiation; IDA:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:MGI.
DR GO; GO:0010464; P:regulation of mesenchymal cell proliferation; IMP:MGI.
DR GO; GO:0051150; P:regulation of smooth muscle cell differentiation; IMP:MGI.
DR GO; GO:0033081; P:regulation of T cell differentiation in thymus; IMP:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0017015; P:regulation of transforming growth factor beta receptor signaling pathway; IGI:MGI.
DR GO; GO:0014823; P:response to activity; IEA:Ensembl.
DR GO; GO:0031667; P:response to nutrient levels; IEA:Ensembl.
DR GO; GO:0048752; P:semicircular canal morphogenesis; IMP:MGI.
DR CDD; cd00086; homeodomain; 1.
DR InterPro; IPR008598; Di19_Zn-bd.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR001356; Homeobox_dom.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00096; zf-C2H2; 4.
DR Pfam; PF05605; zf-Di19; 1.
DR SMART; SM00355; ZnF_C2H2; 7.
DR SUPFAM; SSF46689; SSF46689; 1.
DR SUPFAM; SSF57667; SSF57667; 4.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 5.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 6.
PE 1: Evidence at protein level;
KW Activator; Differentiation; DNA-binding; Homeobox; Isopeptide bond;
KW Metal-binding; Neurogenesis; Nucleus; Phosphoprotein; Reference proteome;
KW Repeat; Repressor; Transcription; Transcription regulation;
KW Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..1117
FT /note="Zinc finger E-box-binding homeobox 1"
FT /id="PRO_0000047233"
FT ZN_FING 150..173
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 180..202
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 220..242
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 248..272
FT /note="C2H2-type 4; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT DNA_BIND 559..618
FT /note="Homeobox; atypical"
FT ZN_FING 882..904
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 910..932
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 938..959
FT /note="C2H2-type 7; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..103
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 122..143
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 278..307
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 476..501
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 528..566
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 613..687
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 834..876
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 991..1117
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 31..47
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 86..103
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 283..307
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 532..546
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 547..566
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 628..660
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 669..687
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 838..864
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1009..1032
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1040..1067
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1096..1117
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 31
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q62947"
FT MOD_RES 33
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q62947"
FT MOD_RES 293
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 302
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 657
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 664
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 671
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 678
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 680
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P37275"
FT MOD_RES 682
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CROSSLNK 166
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P37275"
FT CROSSLNK 175
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P37275"
FT CROSSLNK 287
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P37275"
FT CROSSLNK 311
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P37275"
FT CROSSLNK 315
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P37275"
FT CROSSLNK 327
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO); alternate"
FT /evidence="ECO:0000250"
FT CROSSLNK 327
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P37275"
FT CROSSLNK 419
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P37275"
FT CROSSLNK 473
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P37275"
FT CROSSLNK 484
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P37275"
FT CROSSLNK 495
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P37275"
FT CROSSLNK 528
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P37275"
FT CROSSLNK 752
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO); alternate"
FT /evidence="ECO:0000250"
FT CROSSLNK 752
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P37275"
FT CONFLICT 33
FT /note="S -> A (in Ref. 3; AAB08442)"
FT /evidence="ECO:0000305"
FT CONFLICT 57
FT /note="M -> K (in Ref. 3; AAB08442)"
FT /evidence="ECO:0000305"
FT CONFLICT 125
FT /note="Missing (in Ref. 3; AAB08442)"
FT /evidence="ECO:0000305"
FT CONFLICT 146
FT /note="F -> L (in Ref. 3; AAB08442)"
FT /evidence="ECO:0000305"
FT CONFLICT 313
FT /note="E -> EV (in Ref. 3; AAB08442)"
FT /evidence="ECO:0000305"
FT CONFLICT 353
FT /note="G -> A (in Ref. 3; AAB08442)"
FT /evidence="ECO:0000305"
FT CONFLICT 400
FT /note="V -> L (in Ref. 3; AAB08442)"
FT /evidence="ECO:0000305"
FT CONFLICT 461
FT /note="Q -> E (in Ref. 3; AAB08442)"
FT /evidence="ECO:0000305"
FT CONFLICT 528
FT /note="K -> KK (in Ref. 3; AAB08442)"
FT /evidence="ECO:0000305"
FT CONFLICT 664
FT /note="S -> T (in Ref. 3; AAB08442)"
FT /evidence="ECO:0000305"
FT CONFLICT 744
FT /note="E -> L (in Ref. 3; AAB08442)"
FT /evidence="ECO:0000305"
FT CONFLICT 822
FT /note="T -> A (in Ref. 3; AAB08442)"
FT /evidence="ECO:0000305"
FT CONFLICT 1062
FT /note="Missing (in Ref. 3; AAB08442)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1117 AA; 122465 MW; D1FAC2D048D34237 CRC64;
MADGPRCKRR KQANPRRNNV TNYNTVVEAN SDSDDEDKLH IVEEESITDA ADCEGGMPDD
ELPADQTVLP GGSDRGGGAK NCWQDNVKDN ECDSDAENEQ NHDPNVEEFL QQQDTAVIYP
EAPEEDQRQG TPEASSHDEN GTPDAFSQLL TCPYCDRGYK RFTSLKEHIK YRHEKNEDNF
SCSLCSYTFA YRTQLERHMT SHKSGREQRH VTQSGGNRKF KCTECGKAFK YKHHLKEHLR
IHSGEKPYEC PNCKKRFSHS GSYSSHISSK KCISLMPVNG RPRSGLKTSQ CSSPSLSTSP
GSPTRPQIRQ KIENKPLQEP LSVNQIKTEP VDYEFKPIVV ASGINCSTPL QNGVFSSGGQ
LQATSSPQGV VQAVVLPTVG LVSPISINLS DIQNVLKVAV DGNVIRQVLE TNQASLASKE
QEAVSASPIQ QGGHSVISAI SLPLVDQDGT TKIIINYSLE QPSQLQVVPQ NLKKEIPAPT
NSCKSEKLPE DLTVKSETDK SFEGARDDST CLLCEDCPGD LNALPELKHY DPECPAQPPP
PAPATEKPES SASSAGNGDL SPSQPPLKNL LSLLKAYYAL NAQPSTEELS KIADSVNLPL
DGVKKWFEKM QAGQIPGQSP DPPSPGTGSV NIPTKTDEQP QPADGNEPQE DSTRGQSPVK
IRSSPVLPVG SAMNGSRSCT SSPSPLNLCS ARNPQGYSCV AEGAQEEPQV EPLDLSLPKQ
QGELLERSTV SSVYQNSVYS VQEEPLNLSC AKKEPQKDSC VTDSEPVVNV VPPSANPINI
AIPTVTAQLP TIVAIADQNS VPCLRALAAN KQTILIPQVA YTYSATVSPA VQEPPVKVIQ
PNGNQDERQD TSSEGVSTVE DQNDSDSTPP KKKTRKTENG MYACDLCDKI FQKSSSLLRH
KYEHTGKRPH ECGICRKAFK HKHHLIEHMR LHSGEKPYQC DKCGKRFSHS GSYSQHMNHR
YSYCKRGAED RDAMEQEDAG PEVLPEVLAT EHVGARASPS QADSDERESL TREEDEDSEK
EEEEEDKEME ELQEGKECEN PQGEEEEEEE EEEEEEEEEE EEVEADEAEH EAAAKTDGTV
EVGAAQQAGS LEQKASESEM ESESESEQLS EEKTNEA
