DESP_MOUSE
ID DESP_MOUSE Reviewed; 2883 AA.
AC E9Q557;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 05-APR-2011, sequence version 1.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=Desmoplakin;
DE Short=DP;
GN Name=Dsp;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2836, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-22; THR-59; SER-65; TYR-68;
RP THR-73; SER-2221; SER-2832 AND SER-2836, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC and 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 [4]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-2837 AND ARG-2858, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
RN [5]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH TMEM65.
RX PubMed=26403541; DOI=10.1038/ncomms9391;
RA Sharma P., Abbasi C., Lazic S., Teng A.C., Wang D., Dubois N.,
RA Ignatchenko V., Wong V., Liu J., Araki T., Tiburcy M., Ackerley C.,
RA Zimmermann W.H., Hamilton R., Sun Y., Liu P.P., Keller G., Stagljar I.,
RA Scott I.C., Kislinger T., Gramolini A.O.;
RT "Evolutionarily conserved intercalated disc protein Tmem65 regulates
RT cardiac conduction and connexin 43 function.";
RL Nat. Commun. 6:8391-8391(2015).
CC -!- FUNCTION: Major high molecular weight protein of desmosomes. Involved
CC in the organization of the desmosomal cadherin-plakoglobin complexes
CC into discrete plasma membrane domains and in the anchoring of
CC intermediate filaments to the desmosomes.
CC -!- SUBUNIT: Homodimer. Interacts with COL17A1 (via cytoplasmic region).
CC Associates (via C-terminal) with KRT5-KRT14 (via rod region), KRT8-
CC KRT18 and VIM intermediate filaments. Interacts with PKP2 (By
CC similarity). Interacts weakly with TMEM65 (PubMed:26403541).
CC {ECO:0000250|UniProtKB:P15924, ECO:0000269|PubMed:26403541}.
CC -!- SUBCELLULAR LOCATION: Cell junction, desmosome
CC {ECO:0000250|UniProtKB:P15924}. Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:P15924}. Cell membrane
CC {ECO:0000269|PubMed:26403541}. Note=Innermost portion of the desmosomal
CC plaque. Colocalizes with epidermal KRT5-KRT14 and simple KRT8-KRT18
CC keratins and VIM intermediate filaments network (By similarity).
CC Localizes at the intercalated disk in cardiomyocytes (PubMed:26403541).
CC {ECO:0000250|UniProtKB:P15924, ECO:0000269|PubMed:26403541}.
CC -!- DOMAIN: Its association with epidermal and simple keratins is dependent
CC on the tertiary structure induced by heterodimerization of these
CC intermediate filaments proteins and most likely involves recognition
CC sites located in the rod domain of these keratins. {ECO:0000250}.
CC -!- DOMAIN: The N-terminal region is required for localization to the
CC desmosomal plaque and interacts with the N-terminal region of
CC plakophilin 1. {ECO:0000250}.
CC -!- DOMAIN: The three tandem plakin repeat regions in the C-terminus
CC mediate binding to intermediate filaments. {ECO:0000250}.
CC -!- PTM: Ser-2860 is probably phosphorylated by a cAMP-dependent protein
CC kinase. Phosphorylation on Ser-2860 probably affects its association
CC with epidermal, simple cytokeratins and VIM intermediate filaments (By
CC similarity). {ECO:0000250}.
CC -!- PTM: Substrate of transglutaminase. Some glutamines and lysines are
CC cross-linked to other desmoplakin molecules, to other proteins such as
CC keratin, envoplakin, periplakin and involucrin, and to lipids like
CC omega-hydroxyceramide (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the plakin or cytolinker family. {ECO:0000305}.
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DR EMBL; AC140331; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS49239.1; -.
DR RefSeq; NP_076331.2; NM_023842.2.
DR SMR; E9Q557; -.
DR BioGRID; 224908; 21.
DR IntAct; E9Q557; 35.
DR MINT; E9Q557; -.
DR STRING; 10090.ENSMUSP00000115062; -.
DR iPTMnet; E9Q557; -.
DR PhosphoSitePlus; E9Q557; -.
DR SwissPalm; E9Q557; -.
DR CPTAC; non-CPTAC-3703; -.
DR EPD; E9Q557; -.
DR jPOST; E9Q557; -.
DR MaxQB; E9Q557; -.
DR PaxDb; E9Q557; -.
DR PeptideAtlas; E9Q557; -.
DR PRIDE; E9Q557; -.
DR ProteomicsDB; 279376; -.
DR Antibodypedia; 24671; 335 antibodies from 39 providers.
DR DNASU; 109620; -.
DR Ensembl; ENSMUST00000124830; ENSMUSP00000115062; ENSMUSG00000054889.
DR GeneID; 109620; -.
DR KEGG; mmu:109620; -.
DR UCSC; uc007qdk.2; mouse.
DR CTD; 1832; -.
DR MGI; MGI:109611; Dsp.
DR VEuPathDB; HostDB:ENSMUSG00000054889; -.
DR eggNOG; KOG0516; Eukaryota.
DR GeneTree; ENSGT00940000154843; -.
DR InParanoid; E9Q557; -.
DR OMA; ALCKWIC; -.
DR OrthoDB; 7016at2759; -.
DR PhylomeDB; E9Q557; -.
DR TreeFam; TF106435; -.
DR Reactome; R-MMU-351906; Apoptotic cleavage of cell adhesion proteins.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR Reactome; R-MMU-6805567; Keratinization.
DR Reactome; R-MMU-6809371; Formation of the cornified envelope.
DR Reactome; R-MMU-9696264; RND3 GTPase cycle.
DR Reactome; R-MMU-9696273; RND1 GTPase cycle.
DR BioGRID-ORCS; 109620; 0 hits in 73 CRISPR screens.
DR ChiTaRS; Dsp; mouse.
DR PRO; PR:E9Q557; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; E9Q557; protein.
DR Bgee; ENSMUSG00000054889; Expressed in tail skin and 251 other tissues.
DR ExpressionAtlas; E9Q557; baseline and differential.
DR Genevisible; E9Q557; MM.
DR GO; GO:0016323; C:basolateral plasma membrane; IDA:MGI.
DR GO; GO:0005911; C:cell-cell junction; IDA:MGI.
DR GO; GO:0001533; C:cornified envelope; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0030057; C:desmosome; IDA:UniProtKB.
DR GO; GO:0005916; C:fascia adherens; ISO:MGI.
DR GO; GO:0014704; C:intercalated disc; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0050839; F:cell adhesion molecule binding; IEA:InterPro.
DR GO; GO:0005080; F:protein kinase C binding; ISO:MGI.
DR GO; GO:0097110; F:scaffold protein binding; ISO:MGI.
DR GO; GO:0005198; F:structural molecule activity; IBA:GO_Central.
DR GO; GO:0034332; P:adherens junction organization; IMP:MGI.
DR GO; GO:0086073; P:bundle of His cell-Purkinje myocyte adhesion involved in cell communication; ISO:MGI.
DR GO; GO:0098609; P:cell-cell adhesion; IMP:MGI.
DR GO; GO:0002934; P:desmosome organization; IMP:BHF-UCL.
DR GO; GO:0090136; P:epithelial cell-cell adhesion; ISO:MGI.
DR GO; GO:0045104; P:intermediate filament cytoskeleton organization; IMP:MGI.
DR GO; GO:0045109; P:intermediate filament organization; IMP:BHF-UCL.
DR GO; GO:0030216; P:keratinocyte differentiation; ISO:MGI.
DR GO; GO:0018149; P:peptide cross-linking; ISO:MGI.
DR GO; GO:0150105; P:protein localization to cell-cell junction; IMP:BHF-UCL.
DR GO; GO:0086091; P:regulation of heart rate by cardiac conduction; ISO:MGI.
DR GO; GO:0098911; P:regulation of ventricular cardiac muscle cell action potential; ISO:MGI.
DR GO; GO:0043588; P:skin development; IMP:MGI.
DR GO; GO:0003223; P:ventricular compact myocardium morphogenesis; IMP:BHF-UCL.
DR GO; GO:0042060; P:wound healing; IBA:GO_Central.
DR CDD; cd00176; SPEC; 1.
DR Gene3D; 3.90.1290.10; -; 3.
DR InterPro; IPR028462; Desmoplakin.
DR InterPro; IPR041615; Desmoplakin_SH3.
DR InterPro; IPR041573; Desmoplakin_Spectrin-like.
DR InterPro; IPR043197; Plakin.
DR InterPro; IPR035915; Plakin_repeat_sf.
DR InterPro; IPR001101; Plectin_repeat.
DR InterPro; IPR001452; SH3_domain.
DR InterPro; IPR018159; Spectrin/alpha-actinin.
DR PANTHER; PTHR23169; PTHR23169; 1.
DR PANTHER; PTHR23169:SF26; PTHR23169:SF26; 1.
DR Pfam; PF00681; Plectin; 8.
DR Pfam; PF17902; SH3_10; 1.
DR Pfam; PF18373; Spectrin_like; 1.
DR SMART; SM00250; PLEC; 18.
DR SMART; SM00150; SPEC; 2.
DR SUPFAM; SSF75399; SSF75399; 4.
DR PROSITE; PS50002; SH3; 1.
PE 1: Evidence at protein level;
KW Cardiomyopathy; Cell junction; Cell membrane; Coiled coil; Cytoplasm;
KW Cytoskeleton; Lipoprotein; Membrane; Methylation; Phosphoprotein;
KW Reference proteome; Repeat; SH3 domain.
FT CHAIN 1..2883
FT /note="Desmoplakin"
FT /id="PRO_0000410831"
FT REPEAT 190..283
FT /note="Spectrin 1"
FT REPEAT 284..387
FT /note="Spectrin 2"
FT REPEAT 388..458
FT /note="Spectrin 3a"
FT DOMAIN 470..527
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REPEAT 528..557
FT /note="Spectrin 3b"
FT REPEAT 558..639
FT /note="Spectrin 4"
FT REPEAT 666..781
FT /note="Spectrin 5"
FT REPEAT 782..895
FT /note="Spectrin 6"
FT REPEAT 2021..2057
FT /note="Plectin 1"
FT REPEAT 2058..2095
FT /note="Plectin 2"
FT REPEAT 2096..2133
FT /note="Plectin 3"
FT REPEAT 2134..2171
FT /note="Plectin 4"
FT REPEAT 2175..2209
FT /note="Plectin 5"
FT REPEAT 2210..2245
FT /note="Plectin 6"
FT REPEAT 2263..2300
FT /note="Plectin 7"
FT REPEAT 2301..2338
FT /note="Plectin 8"
FT REPEAT 2339..2376
FT /note="Plectin 9"
FT REPEAT 2377..2414
FT /note="Plectin 10"
FT REPEAT 2418..2452
FT /note="Plectin 11"
FT REPEAT 2468..2505
FT /note="Plectin 12"
FT REPEAT 2519..2556
FT /note="Plectin 13"
FT REPEAT 2622..2659
FT /note="Plectin 14"
FT REPEAT 2660..2697
FT /note="Plectin 15"
FT REPEAT 2736..2773
FT /note="Plectin 16"
FT REPEAT 2774..2811
FT /note="Plectin 17"
FT REGION 1..1068
FT /note="Globular 1"
FT REGION 1..596
FT /note="Interaction with plakophilin 1 and junction
FT plakoglobin"
FT /evidence="ECO:0000250"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1069..1957
FT /note="Central fibrous rod domain"
FT REGION 1958..2882
FT /note="Globular 2"
FT REGION 1972..2220
FT /note="4.5 X 38 AA tandem repeats (Domain A)"
FT REGION 2256..2458
FT /note="4.5 X 38 AA tandem repeats (Domain B)"
FT REGION 2621..2833
FT /note="4.5 X 38 AA tandem repeats (Domain C)"
FT REGION 2822..2883
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2835..2858
FT /note="6 X 4 AA tandem repeats of G-S-R-[SR]"
FT COILED 1034..1956
FT /evidence="ECO:0000255"
FT COMPBIAS 2823..2883
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 22
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 59
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 65
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 68
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 73
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 177
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P15924"
FT MOD_RES 178
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P15924"
FT MOD_RES 188
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P15924"
FT MOD_RES 1670
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P15924"
FT MOD_RES 1720
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P15924"
FT MOD_RES 2036
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P15924"
FT MOD_RES 2219
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P15924"
FT MOD_RES 2221
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 2237
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P15924"
FT MOD_RES 2822
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P15924"
FT MOD_RES 2827
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P15924"
FT MOD_RES 2829
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P15924"
FT MOD_RES 2832
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 2836
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 2837
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 2858
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 2860
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P15924"
FT MOD_RES 2864
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P15924"
FT MOD_RES 2879
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P15924"
FT LIPID 2492
FT /note="Omega-hydroxyceramide glutamate ester"
FT /evidence="ECO:0000250"
SQ SEQUENCE 2883 AA; 332912 MW; 1D8B68788D519940 CRC64;
MSCNGGSHPR INTLGRMTRA ESGPDLRYEM TYSGGGGGGG GGGGGGTSRT FYSHSRRCTV
NDQNSDGYCQ TGTMSRHQNQ NTIQEMLQNC SDCLMRAELI AQPELKFGEG MQLAWNRELD
EYFTQANDQM EIIDGLIREM RQMGQPCDAY QKRLLQLQEQ MRALYKAISV PRVRRASSKG
AGGYTCQSGS GWDEFTKRLT GECLGWMRQQ REEMDLMAWG VDAGSVEQHI NSHRSIHNTI
GDYRWQLDKI KADLREKSAI YQLEEEYENL LKASFERMDH LRQLQNIIQA TSREIMWIND
CEEEELLYDW SDKNTNIAQK QEAFSIRMSQ LEVKEKELNK LKQESDQLVL NQHPASDKIE
AYMDTLQTQW SWILQITKCI DVHLKENAAY FQFFEEAQST EAYLKGLQDS IRKKYPCDKN
MPLQHLLEQI KELEKEREKI IEYKRQVQNL VNKSKKIVQL KPRNPDYRSN KPIILRALCD
YKQDQKIVHK GDECILKDNN ERSKWYVTGP GGVDMLVPSV GLIIPPPNPL AVDLSCKIEQ
YYEAILALWN QLYINMKSLV SWHYCMIDIE KIRAMTIAKL KTMRQEDYMK TIEDLELHYQ
DFIKNSQGSE MFGDDDKRRM QSQFTDAQKH YQTLVIQLPG HPQHQTVTKT EITHLGTCQD
VNHNKVIETN RENDKQETWL LMELQKIRRQ MEHCEARMTL KNLLLAEQGS THHITVKINE
LKSVQNDSQA LAEVLNQLKD MLANFRGSEK YCYLQNEIFG LFQKLENING VSDGYLNSLC
SVRALLQAIL QTEDMLKVYE ARLTEEETVC LDLDKVEAYR CGLKKIKNDL NLKKSLLATM
KTELQKAQQI HSQSSQQYPL YDLDLGKFTE KVTQLTDRWQ KIDKQIDFRL WDLEKQIKQL
RNYRDNYQSF CKWLYDAKRR QDSLESMKFG DSNTVMRFLN EQKNLHSEIS GKRDKSEEVH
KIAELCANSI KDYELQLASY TSGLETLLNI PIKRTMVQSP SGVILQEAAD IHARYIELLT
RSGDYYRFLS EMLKSLEDLK LKNTKIEVLE EELRLARDAN SENCNKNKFL DQNLQKYQAE
CSQFKAKLVS LEELKRQAEL DGKSAKQNLD KCYGQIKELN EKITRLTYEI EDEKRRRKTV
EDRFDQQKND YDQLQKARQC EKENLSWQKL ESEKAIKEKE YEIERLRVLL QEEGARKREY
ENELAKVRNH YNEEMSNLRN KYETEINITK TTIKEISMQK EDDSKNLRNQ MDRLSRENRD
LKDEIVRLND SILQATEQRR RAEENALQQK ACGSETMQKK QRLEIELKQV IQQRSEDNAR
HKQSLEEAAK TIQDKNKEIE RLKAEYQEEA KRRWEYENEL SKVRNSYDEE IISLKNQFET
EINITKTTIH QLTMQKEEDT SGYRAQIDNL TRENRSLCEE VKRLKNTLAQ TTENLRRVEE
NAQQQKATGS EMSQRKQQLE IELRQVTQMR TEESMRYKQS LDDAAKTIQD KNKEIERLKQ
LVDKETNERK CLEDENSKLQ RVQYDLQKAN NSATEAMSKL KVQEQELTRL RIDYERVSQE
RTVKDQDITR IQSSLKDLQL QKQKAEEELS RLKRTASDES SKRKMLEEEL EAMRRSLKEQ
AVKITNLTQQ LEQASIVKKR SEDDLRQQRD VLDGHVREKQ RTQEELRRLS LDVEALRRQL
VQEQENVKQA HLRNEHFQKA IEDKSRSLNE SKIEIERLQS LTENLTKEHL MLEEELRNLR
LEYDDLRRGR SEADSDKNST ISELRSQLQI SNNRTLELQG LINDLQRERE NLRQEIEKFQ
KQALEASNRI QESKSQCTQV VQERESLLVK IKVLEQDKAR LQRLEDELNR AKATLEAESR
VKQRLECEKQ QIQNDLNQWK TQYSRKEETI RKIESEREKS EREKNSLRSE IERLQAEIKR
IEERCRRKLE DSSRETQSQL ESERCRLQKE IEKLRQRPYG SHRETQTEYE WTVDSSKLVF
DGLRKKVTAM QLYECQLIDK TTLDKLLKGK KSVEEVASEI QPFLRGAGAI AGASASPKEK
YSLVEAKRKK FITPESTVML LEAQAATGGI IDPHRNEKLT VDNAVARDLI DFDDRQQIYT
AEKAITGFDD PFSGKTVSVS EAIKKNLIDR ETGMRLLEAQ LASGGVVDPV NSVFLPKDVA
LARGLIDRDL YRSLNDPRDS QKNFVDPITK KKVSYMQLRE RCRIEPHTGL LLLSVQKRSM
SFQGIRQPVT VTELVDSGIL RPSTVNELES GQISYDEVGE RIKDFLQGSS CIAGIYNETT
KQKLGIYEAM KIGLVRPGTA LELLEAQAAT GFIVDPVSNL RLPVEEAYKR GLVGIEFKEK
LLSAERAVTG YNDPETGNII SLFQAMNKEL IEKGHGIRLL EAQIATGGII DPKESHRLPV
DMAYKRGYFN EELSEILSDP SDDTKGFFDP NTEENLTYLQ LKERCIKDEE TGLCLLPLKE
KKKQVQTSQK NTLRKRRVVI VDPETNKEMS VQEAYKKGLI DYDTFKELCE QECEWEEITI
TGSDGSTRVV LVDRKTGSQY DIQDAIDKGL VDRKFFDQYR SGSLSLTQFA DMISLKNGVG
NSSGLGGSVN DDVFSSSRHD SVSKISTISS VRNLTIRSSS LSDPLEESSP IAAIFDTENL
EKISIAEGIE RGIVDSITGQ RLLEAQACTG GIIHPTTGQK LSLQDAVNQG LIDQDMATRL
KPAQKAFIGF EGVKGKKKMS AAEAVKEKWL PYEAGQRFLE FQFLTGGLVD PEVHGRISTE
EAIRKGFIDG RAAQRLQDIS SYAKILTCPK TKLKISYKDA MNRSMVEDIT GLRLLEAASV
SSKGLPSPYN MSAPGSRSGS RSGSRSGSRS GSRSGSRRGS FDATGNSSYS YSYSFSSSSI
GGY
