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Calpain-type cysteine protease DEK1 (EC 3.4.22.-) (Phytocalpain DEK1) (Protein DEFECTIVE KERNEL 1) (AtDEK1) (Protein EMBRYO DEFECTIVE 1275) (Protein EMBRYO DEFECTIVE 80)

 DEK1_ARATH              Reviewed;        2151 AA.
Q8RVL2; Q8VXW6; Q949X8; Q9C8A6;
18-SEP-2013, integrated into UniProtKB/Swiss-Prot.
01-JUN-2002, sequence version 1.
30-AUG-2017, entry version 108.
RecName: Full=Calpain-type cysteine protease DEK1;
EC=3.4.22.-;
AltName: Full=Phytocalpain DEK1;
AltName: Full=Protein DEFECTIVE KERNEL 1;
Short=AtDEK1;
AltName: Full=Protein EMBRYO DEFECTIVE 1275;
AltName: Full=Protein EMBRYO DEFECTIVE 80;
Flags: Precursor;
Name=DEK1; Synonyms=EMB1275, EMB80; OrderedLocusNames=At1g55350;
ORFNames=F7A10.23;
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
STRAIN=cv. Columbia; TISSUE=Seed;
PubMed=11929961; DOI=10.1073/pnas.042098799;
Lid S.E., Gruis D., Jung R., Lorentzen J.A., Ananiev E.,
Chamberlin M., Niu X., Meeley R., Nichols S., Olsen O.-A.;
"The defective kernel 1 (dek1) gene required for aleurone cell
development in the endosperm of maize grains encodes a membrane
protein of the calpain gene superfamily.";
Proc. Natl. Acad. Sci. U.S.A. 99:5460-5465(2002).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=11130712; DOI=10.1038/35048500;
Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S.,
White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y.,
Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W.,
Chung M.K., Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K.,
Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y.,
Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L.,
Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E.,
Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B.,
Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P.,
Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A.,
Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I.,
Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D.,
Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M.,
Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M.,
Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.;
"Sequence and analysis of chromosome 1 of the plant Arabidopsis
thaliana.";
Nature 408:816-820(2000).
[3]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
The Arabidopsis Information Portal (Araport);
Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-543 AND 1603-2151.
STRAIN=cv. Columbia;
PubMed=14593172; DOI=10.1126/science.1088305;
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
"Empirical analysis of transcriptional activity in the Arabidopsis
genome.";
Science 302:842-846(2003).
[5]
SUBCELLULAR LOCATION.
STRAIN=cv. La-0;
PubMed=14506206; DOI=10.1074/mcp.T300006-MCP200;
Nuehse T.S., Stensballe A., Jensen O.N., Peck S.C.;
"Large-scale analysis of in vivo phosphorylated membrane proteins by
immobilized metal ion affinity chromatography and mass spectrometry.";
Mol. Cell. Proteomics 2:1234-1243(2003).
[6]
SUBCELLULAR LOCATION.
PubMed=15308754; DOI=10.1105/tpc.104.023150;
Nuehse T.S., Stensballe A., Jensen O.N., Peck S.C.;
"Phosphoproteomics of the Arabidopsis plasma membrane and a new
phosphorylation site database.";
Plant Cell 16:2394-2405(2004).
[7]
IDENTIFICATION [LARGE SCALE ANALYSIS], AND DISRUPTION PHENOTYPE [LARGE
SCALE ANALYSIS].
PubMed=15266054; DOI=10.1104/pp.104.045179;
Tzafrir I., Pena-Muralla R., Dickerman A., Berg M., Rogers R.,
Hutchens S., Sweeney T.C., McElver J., Aux G., Patton D., Meinke D.;
"Identification of genes required for embryo development in
Arabidopsis.";
Plant Physiol. 135:1206-1220(2004).
[8]
FUNCTION, DISRUPTION PHENOTYPE, AND DEVELOPMENTAL STAGE.
STRAIN=cv. Columbia;
PubMed=15647902; DOI=10.1007/s00425-004-1448-6;
Lid S.E., Olsen L., Nestestog R., Aukerman M., Brown R.C., Lemmon B.,
Mucha M., Opsahl-Sorteberg H.-G., Olsen O.-A.;
"Mutation in the Arabidopisis thaliana DEK1 calpain gene perturbs
endosperm and embryo development while over-expression affects organ
development globally.";
Planta 221:339-351(2005).
[9]
FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, AND DEVELOPMENTAL
STAGE.
STRAIN=cv. Columbia;
PubMed=16167900; DOI=10.1111/j.1365-313X.2005.02514.x;
Johnson K.L., Degnan K.A., Ross Walker J., Ingram G.C.;
"AtDEK1 is essential for specification of embryonic epidermal cell
fate.";
Plant J. 44:114-127(2005).
[10]
FUNCTION, DISRUPTION PHENOTYPE, AND SUBCELLULAR LOCATION.
PubMed=17933905; DOI=10.1105/tpc.106.048868;
Tian Q., Olsen L., Sun B., Lid S.E., Brown R.C., Lemmon B.E.,
Fosnes K., Gruis D.F., Opsahl-Sorteberg H.-G., Otegui M.S.,
Olsen O.-A.;
"Subcellular localization and functional domain studies of DEFECTIVE
KERNEL1 in maize and Arabidopsis suggest a model for aleurone cell
fate specification involving CRINKLY4 and SUPERNUMERARY ALEURONE
LAYER1.";
Plant Cell 19:3127-3145(2007).
[11]
FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, PROTEOLYSIS,
MUTAGENESIS OF CYS-1761, AND DOMAIN.
PubMed=18952779; DOI=10.1105/tpc.108.059964;
Johnson K.L., Faulkner C., Jeffree C.E., Ingram G.C.;
"The phytocalpain defective kernel 1 is a novel Arabidopsis growth
regulator whose activity is regulated by proteolytic processing.";
Plant Cell 20:2619-2630(2008).
[12]
IDENTIFICATION [LARGE SCALE ANALYSIS], AND DISRUPTION PHENOTYPE [LARGE
SCALE ANALYSIS].
PubMed=19812694; DOI=10.1371/journal.pone.0007386;
Meinke D., Sweeney C., Muralla R.;
"Integrating the genetic and physical maps of Arabidopsis thaliana:
identification of mapped alleles of cloned essential (EMB) genes.";
PLoS ONE 4:E7386-E7386(2009).
[13]
FUNCTION, AND MUTAGENESIS OF ARG-2106.
PubMed=23095885; DOI=10.1242/dev.082925;
Roeder A.H.K., Cunha A., Ohno C.K., Meyerowitz E.M.;
"Cell cycle regulates cell type in the Arabidopsis sepal.";
Development 139:4416-4427(2012).
-!- FUNCTION: Essential protein involved in epiderm development.
Required for aleurone cell development in the endosperm probably
by maintaining and restricting the aleurone and embryonic
epidermal L1 cell-layer fates as well as meristems organization.
Involved in the maintenance of adaxial/abaxial axis information in
developing leaves, probably by regulating cell proliferation and
expansion. Does not need calcium ions to be active. Required for
the formation of giant cells in sepals by determining cell fate
and promoting endoreplication. {ECO:0000269|PubMed:15647902,
ECO:0000269|PubMed:16167900, ECO:0000269|PubMed:17933905,
ECO:0000269|PubMed:18952779, ECO:0000269|PubMed:23095885}.
-!- CATALYTIC ACTIVITY: Broad endopeptidase specificity.
-!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
Endosome membrane; Multi-pass membrane protein. Endoplasmic
reticulum membrane; Multi-pass membrane protein. Cytoplasm.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=1;
Comment=Additional isoforms may exist.;
Name=1;
IsoId=Q8RVL2-1; Sequence=Displayed;
-!- TISSUE SPECIFICITY: Mostly expressed in meristems and organ
primordia. Expressed at low levels in young and germinating seeds
at 10 ppm and in seedling roots at 67 ppm. Present in most tissues
at a low level. {ECO:0000269|PubMed:11929961,
ECO:0000269|PubMed:16167900}.
-!- DEVELOPMENTAL STAGE: Mostly observed in vegetative, inflorescence
and floral meristems as well as in young leaf and floral organ
primordia. Strongly expressed in developing ovules and during
early embryogenesis. Expressed evenly throughout the endosperm and
the embryo in developing seed. Present in the embryo proper, but
excluded from the suspensor, until the late heart stage, and fades
out later, especially in the hypocotyl region, to be present at
low levels throughout walking-stick embryos. Accumulates at the
margins and in the tips of cotyledons and lateral organs, in the
apical meristem, in a subset of cells at the root pole and in a
restricted number of cells within the presumptive vasculature of
the hypocotyls. Also detected during early endosperm development,
prior to cellularization. {ECO:0000269|PubMed:15647902,
ECO:0000269|PubMed:16167900}.
-!- DOMAIN: The transmembrane regions are not required for calpain
activity but may play regulatory roles.
{ECO:0000269|PubMed:18952779}.
-!- PTM: Autocatalytic proteolytic cleavage leading to the production
of mainly cytoplasmic localized subproducts of about 85 and 120
kDa.
-!- DISRUPTION PHENOTYPE: Defective embryo arrested at
preglobular/globular stage. Disturbed endosperm lacking the
aleurone-like peripheral cell layer and unorganized embryo
development displaying irregular mitotic divisions in the embryo
proper and suspensor. In a partially disrupted phenotype, impaired
meristems organization characterized by vacuolated cells, abnormal
cotyledon epiderm made of chloroplast-containing cells, and
radialized leaves. {ECO:0000269|PubMed:15266054,
ECO:0000269|PubMed:15647902, ECO:0000269|PubMed:16167900,
ECO:0000269|PubMed:17933905, ECO:0000269|PubMed:18952779,
ECO:0000269|PubMed:19812694}.
-!- MISCELLANEOUS: Although homology to other calpains is high within
the protease domain, the lack of calcium-binding sites suggests
that this protein is a protease that may not be activated by
calcium ions.
-!- SIMILARITY: Belongs to the peptidase C2 family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAG51565.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Seed defective Arabidopsis mutants;
URL="http://www.seedgenes.org/MutantList";
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EMBL; AY061803; AAL38186.1; -; mRNA.
EMBL; AC027034; AAG51565.1; ALT_SEQ; Genomic_DNA.
EMBL; CP002684; AEE33232.1; -; Genomic_DNA.
EMBL; CP002684; AEE33233.1; -; Genomic_DNA.
EMBL; CP002684; AEE33234.1; -; Genomic_DNA.
EMBL; CP002684; AEE33235.1; -; Genomic_DNA.
EMBL; CP002684; ANM58867.1; -; Genomic_DNA.
EMBL; AY050822; AAK92757.1; -; mRNA.
EMBL; AY074514; AAL67128.1; -; mRNA.
PIR; G96595; G96595.
RefSeq; NP_001319240.1; NM_001333706.1. [Q8RVL2-1]
RefSeq; NP_001321273.1; NM_001333707.1. [Q8RVL2-1]
RefSeq; NP_175932.2; NM_104411.4. [Q8RVL2-1]
RefSeq; NP_850966.1; NM_180635.1. [Q8RVL2-1]
RefSeq; NP_850967.1; NM_180636.1. [Q8RVL2-1]
UniGene; At.17726; -.
ProteinModelPortal; Q8RVL2; -.
SMR; Q8RVL2; -.
BioGrid; 27206; 2.
IntAct; Q8RVL2; 1.
STRING; 3702.AT1G55350.5; -.
MEROPS; C02.019; -.
iPTMnet; Q8RVL2; -.
PaxDb; Q8RVL2; -.
EnsemblPlants; AT1G55350.1; AT1G55350.1; AT1G55350. [Q8RVL2-1]
EnsemblPlants; AT1G55350.2; AT1G55350.2; AT1G55350. [Q8RVL2-1]
EnsemblPlants; AT1G55350.3; AT1G55350.3; AT1G55350. [Q8RVL2-1]
EnsemblPlants; AT1G55350.4; AT1G55350.4; AT1G55350. [Q8RVL2-1]
EnsemblPlants; AT1G55350.6; AT1G55350.6; AT1G55350. [Q8RVL2-1]
GeneID; 841981; -.
Gramene; AT1G55350.1; AT1G55350.1; AT1G55350.
Gramene; AT1G55350.2; AT1G55350.2; AT1G55350.
Gramene; AT1G55350.3; AT1G55350.3; AT1G55350.
Gramene; AT1G55350.4; AT1G55350.4; AT1G55350.
Gramene; AT1G55350.6; AT1G55350.6; AT1G55350.
KEGG; ath:AT1G55350; -.
Araport; AT1G55350; -.
eggNOG; KOG0045; Eukaryota.
eggNOG; ENOG410XP0B; LUCA.
HOGENOM; HOG000030613; -.
PhylomeDB; Q8RVL2; -.
Reactome; R-ATH-1474228; Degradation of the extracellular matrix.
Reactome; R-ATH-6798695; Neutrophil degranulation.
PRO; PR:Q8RVL2; -.
Proteomes; UP000006548; Chromosome 1.
ExpressionAtlas; Q8RVL2; baseline and differential.
Genevisible; Q8RVL2; AT.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB.
GO; GO:0010008; C:endosome membrane; IDA:UniProtKB.
GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
GO; GO:0004198; F:calcium-dependent cysteine-type endopeptidase activity; IBA:GO_Central.
GO; GO:0008234; F:cysteine-type peptidase activity; IMP:UniProtKB.
GO; GO:0009793; P:embryo development ending in seed dormancy; IMP:UniProtKB.
GO; GO:0090628; P:plant epidermal cell fate specification; IMP:UniProtKB.
GO; GO:0032877; P:positive regulation of DNA endoreduplication; IMP:UniProtKB.
GO; GO:2000011; P:regulation of adaxial/abaxial pattern formation; ISS:UniProtKB.
GO; GO:0001558; P:regulation of cell growth; IMP:UniProtKB.
GO; GO:0042127; P:regulation of cell proliferation; IMP:UniProtKB.
GO; GO:2000014; P:regulation of endosperm development; IMP:UniProtKB.
GO; GO:2000024; P:regulation of leaf development; IMP:UniProtKB.
GO; GO:0009934; P:regulation of meristem structural organization; IMP:UniProtKB.
GO; GO:0097264; P:self proteolysis; IDA:UniProtKB.
GO; GO:0090392; P:sepal giant cell differentiation; IMP:UniProtKB.
CDD; cd00214; Calpain_III; 1.
CDD; cd00044; CysPc; 1.
InterPro; IPR033883; C2_III.
InterPro; IPR022684; Calpain_cysteine_protease.
InterPro; IPR022682; Calpain_domain_III.
InterPro; IPR022683; Calpain_III.
InterPro; IPR013320; ConA-like_dom.
InterPro; IPR000169; Pept_cys_AS.
InterPro; IPR001300; Peptidase_C2_calpain_cat.
Pfam; PF01067; Calpain_III; 1.
Pfam; PF00648; Peptidase_C2; 1.
PRINTS; PR00704; CALPAIN.
SMART; SM00720; calpain_III; 1.
SMART; SM00230; CysPc; 1.
SUPFAM; SSF49758; SSF49758; 1.
SUPFAM; SSF49899; SSF49899; 1.
PROSITE; PS50203; CALPAIN_CAT; 1.
PROSITE; PS00139; THIOL_PROTEASE_CYS; 1.
1: Evidence at protein level;
Alternative splicing; Cell membrane; Complete proteome; Cytoplasm;
Developmental protein; Endoplasmic reticulum; Endosome; Hydrolase;
Membrane; Protease; Reference proteome; Repeat; Signal;
Thiol protease; Transmembrane; Transmembrane helix.
SIGNAL 1 32 {ECO:0000255}.
CHAIN 33 2151 Calpain-type cysteine protease DEK1.
/FTId=PRO_0000423437.
PROPEP 33 ?
/FTId=PRO_0000423438.
TOPO_DOM 33 69 Extracellular. {ECO:0000255}.
TRANSMEM 70 90 Helical; Name=1. {ECO:0000255}.
TOPO_DOM 91 94 Cytoplasmic. {ECO:0000255}.
TRANSMEM 95 115 Helical; Name=2. {ECO:0000255}.
TOPO_DOM 116 126 Extracellular. {ECO:0000255}.
TRANSMEM 127 147 Helical; Name=3. {ECO:0000255}.
TOPO_DOM 148 163 Cytoplasmic. {ECO:0000255}.
TRANSMEM 164 184 Helical; Name=4. {ECO:0000255}.
TOPO_DOM 185 235 Extracellular. {ECO:0000255}.
TRANSMEM 236 256 Helical; Name=5. {ECO:0000255}.
TOPO_DOM 257 263 Cytoplasmic. {ECO:0000255}.
TRANSMEM 264 284 Helical; Name=6. {ECO:0000255}.
TOPO_DOM 285 293 Extracellular. {ECO:0000255}.
TRANSMEM 294 314 Helical; Name=7. {ECO:0000255}.
TOPO_DOM 315 319 Cytoplasmic. {ECO:0000255}.
TRANSMEM 320 340 Helical; Name=8. {ECO:0000255}.
TOPO_DOM 341 615 Extracellular. {ECO:0000255}.
TRANSMEM 616 636 Helical; Name=9. {ECO:0000255}.
TOPO_DOM 637 652 Cytoplasmic. {ECO:0000255}.
TRANSMEM 653 673 Helical; Name=10. {ECO:0000255}.
TOPO_DOM 674 686 Extracellular. {ECO:0000255}.
TRANSMEM 687 707 Helical; Name=11. {ECO:0000255}.
TOPO_DOM 708 711 Cytoplasmic. {ECO:0000255}.
TRANSMEM 712 732 Helical; Name=12. {ECO:0000255}.
TOPO_DOM 733 760 Extracellular. {ECO:0000255}.
TRANSMEM 761 782 Helical; Name=13. {ECO:0000255}.
TOPO_DOM 783 813 Cytoplasmic. {ECO:0000255}.
TRANSMEM 814 834 Helical; Name=14. {ECO:0000255}.
TOPO_DOM 835 844 Extracellular. {ECO:0000255}.
TRANSMEM 845 865 Helical; Name=15. {ECO:0000255}.
TOPO_DOM 866 878 Cytoplasmic. {ECO:0000255}.
TRANSMEM 879 899 Helical; Name=16. {ECO:0000255}.
TOPO_DOM 900 912 Extracellular. {ECO:0000255}.
TRANSMEM 913 933 Helical; Name=17. {ECO:0000255}.
TOPO_DOM 934 936 Cytoplasmic. {ECO:0000255}.
TRANSMEM 937 957 Helical; Name=18. {ECO:0000255}.
TOPO_DOM 958 971 Extracellular. {ECO:0000255}.
TRANSMEM 972 992 Helical; Name=19. {ECO:0000255}.
TOPO_DOM 993 1006 Cytoplasmic. {ECO:0000255}.
TRANSMEM 1007 1027 Helical; Name=20. {ECO:0000255}.
TOPO_DOM 1028 1050 Extracellular. {ECO:0000255}.
TRANSMEM 1051 1071 Helical; Name=21. {ECO:0000255}.
TOPO_DOM 1072 2151 Cytoplasmic. {ECO:0000255}.
DOMAIN 1407 1600 Calpain catalytic 1.
{ECO:0000255|PROSITE-ProRule:PRU00239}.
DOMAIN 1695 1997 Calpain catalytic 2.
{ECO:0000255|PROSITE-ProRule:PRU00239}.
COMPBIAS 369 485 Ser-rich.
COMPBIAS 1595 1636 Asp-rich.
ACT_SITE 1761 1761 {ECO:0000250}.
ACT_SITE 1919 1919 {ECO:0000250}.
ACT_SITE 1939 1939 {ECO:0000250}.
MUTAGEN 1761 1761 C->S: Loss of activity.
{ECO:0000269|PubMed:18952779}.
MUTAGEN 2106 2106 R->C: In dek1-4; near absence of giant
cells in sepals due to a reduced
endoreduplication.
{ECO:0000269|PubMed:23095885}.
SEQUENCE 2151 AA; 238264 MW; 50D571D7446A5609 CRC64;
MEGDERGVLL ACVISGTLFT VFGSGSFWIL WAVNWRPWRL YSWIFARKWP KVLQGPQLDI
LCGVLSLFAW IVVVSPIAIL IGWGSWLIVI LDRHIIGLAI IMAGTALLLA FYSIMLWWRT
QWQSSRAVAL LLLLGVALLC AYELCAVYVT AGAHASQQYS PSGFFFGVSA IALAINMLFI
CRMVFNGNGL DVDEYVRRAY KFAYSDCIEV GPVACLPEPP DPNELYPRQT SRASHLGLLY
LGSLVVLLAY SVLYGLTARE SRWLGGITSA AVIVLDWNIG ACLYGFKLLQ NRVLALFVAG
ISRLFLICFG IHYWYLGHCI SYIFVASVLS GAAVSRHLSI TDPSAARRDA LQSTVIRLRE
GFRRKEQNSS SSSSDGCGSS IKRSSSIDAG HTGCTNEANR TAESCTADNL TRTGSSQEGI
NSDKSEESGR PSLGLRSSSC RSVVQEPEAG TSYFMDKVSD QNNTLVVCSS SGLDSQGYES
STSNSANQQL LDMNLALAFQ DQLNNPRIAS ILKKKAKEGD LELTNLLQDK GLDPNFAVML
KEKNLDPTIL ALLQRSSLDA DRDHRDNTDI TIIDSNSVDN TLPNQISLSE ELRLRGLEKW
LKLSRLLLHH VAGTPERAWG LFSLVFILET IIVAIFRPKT ITIINSSHQQ FEFGFSVLLL
SPVVCSIMAF LRSLQVEEMA LTSKSRKYGF VAWLLSTSVG LSLSFLSKSS VLLGISLTVP
LMAACLSIAV PIWMHNGYQF WVPQLSCGDQ ARDLRSPRIK GFILWICVVL FAGSVISLGA
IISAKPLDDL KYKLFSAREN NVTSPYTSSV YLGWAMSSGI ALVVTAILPI VSWFATYRFS
HSSAVCLMIF SVVLVAFCGT SYLEVVKSRD DQLPTKGDFL AALLPLACIP ALLSLCCGMV
KWKDDCWILS RGVYVFFSIG LLLLFGAIAA VIAVKPWTIG VSFLLVLFLM VVTIGVIHLW
ASNNFYLTRK QTSFVCFLAL LLGLAAFLLG WHQDKAFAGA SVGYFTFLSL LAGRALAVLL
SPPIVVYSPR VLPVYVYDAH ADCGKNVSAA FLVLYGIALA TEGWGVVASL IIYPPFAGAA
VSAITLVVAF GFAVSRPCLT LEMMEVAVRF LSKDTIVQAI SRSATKTRNA LSGTYSAPQR
SASSAALLVG DPSAMRDKAG NFVLPRDDVM KLRDRLRNEE RVAGSIFYKM QCRKGFRHEP
PTNVDYRRDM CAHARVLALE EAIDTEWVYM WDKFGGYLLL LLGLTAKAER VQDEVRLRLF
LDSIGFSDLS ARKISKWKPE DRRQFEIIQE SYLREKEMEE ESLMQRREEE GRGKERRKAL
LEKEERKWKE IEASLIPSIP NAGSREAAAM AAAIRAVGGD SVLEDSFARE RVSGIARRIR
TAQLERRAQQ TGISGAVCVL DDEPMISGKH CGQMDSSVCQ SQKISFSVTA MIQSDSGPVC
LFGTEFQKKV CWEILVAGSE QGIEAGQVGL RLITKGERQT TVAREWYIGA TSITDGRWHT
VTITIDADAG EATCYIDGGF DGYQNGLPLS IGSAIWEQGA EVWLGVRPPI DVDAFGRSDS
DGVESKMHIM DVFLWGKCLS EEEAASLHAA IGMADLDMID LSDDNWQWTD SPPRVDGWDS
DPADVDLYDR DDVDWDGQYS SGRKRRSGRD FVMSVDSFAR RHRKPRMETQ EDINQRMRSV
ELAVKEALSA RGDKQFTDQE FPPNDRSLFV DTQNPPSKLQ VVSEWMRPDS IVKENGSDSR
PCLFSGDANP SDVCQGRLGD CWFLSAVAVL TEVSRISEVI ITPEYNEEGI YTVRFCIQGE
WVPVVIDDWI PCESPGKPAF ATSRKLNELW VSMVEKAYAK LHGSYEALEG GLVQDALVDL
TGGAGEEIDL RSAQAQIDLA SGRLWSQLLR FKQEGFLLGA GSPSGSDVHV SSSGIVQGHA
YSVLQVREVD GHRLVQIRNP WANEVEWNGP WSDSSPEWTD RMKHKLKHVP QSKEGIFWMS
WQDFQIHFRS IYVCRVYPRE MRYSVNGQWR GYSAGGCQDY SSWHQNPQFR LRATGSDASL
PIHVFITLTQ GVGFSRTTPG FRNYQSSHDS QLFYIGLRIL KTRGRRAAYN IFLHESVGGT
DYVNSREISC EMVLDPDPKG YTIVPTTIHP GEEAPFVLSV FTKASIVLEA L


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