MYH2_HUMAN
ID MYH2_HUMAN Reviewed; 1941 AA.
AC Q9UKX2; A0AVL4; Q14322; Q16229; Q567P6; Q86T56;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 201.
DE RecName: Full=Myosin-2;
DE AltName: Full=Myosin heavy chain 2;
DE AltName: Full=Myosin heavy chain 2a;
DE Short=MyHC-2a;
DE AltName: Full=Myosin heavy chain IIa;
DE Short=MyHC-IIa;
DE AltName: Full=Myosin heavy chain, skeletal muscle, adult 2;
GN Name=MYH2; Synonyms=MYHSA2;
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 [MRNA] (ISOFORM 1).
RC TISSUE=Skeletal muscle;
RX PubMed=10388558; DOI=10.1006/jmbi.1999.2865;
RA Weiss A., Schiaffino S., Leinwand L.A.;
RT "Comparative sequence analysis of the complete human sarcomeric myosin
RT heavy chain family: implications for functional diversity.";
RL J. Mol. Biol. 290:61-75(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Skeletal muscle;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT human lineage.";
RL Nature 440:1045-1049(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Cerebellum;
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 1711-1941 (ISOFORM 1).
RC TISSUE=Skeletal muscle;
RX PubMed=7545970; DOI=10.1152/ajpcell.1994.267.6.c1723;
RA Smerdu V., Karsch-Mizrachi I., Campione M., Leinwand L., Schiaffino S.;
RT "Type IIx myosin heavy chain transcripts are expressed in type IIb fibers
RT of human skeletal muscle.";
RL Am. J. Physiol. 267:C1723-C1728(1994).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1823-1941 (ISOFORM 1).
RC TISSUE=Skeletal muscle;
RX PubMed=7751403; DOI=10.1007/bf00125308;
RA Ennion S., Sant'ana Pereira J., Sargeant T., Young A., Goldspink G.;
RT "Characterization of human skeletal muscle fibres according to the myosin
RT heavy chains they express.";
RL J. Muscle Res. Cell Motil. 16:35-43(1995).
RN [7]
RP INTERACTION WITH GCSAM.
RX PubMed=17823310; DOI=10.1182/blood-2007-04-087775;
RA Lu X., Chen J., Malumbres R., Cubedo Gil E., Helfman D.M., Lossos I.S.;
RT "HGAL, a lymphoma prognostic biomarker, interacts with the cytoskeleton and
RT mediates the effects of IL-6 on cell migration.";
RL Blood 110:4268-4277(2007).
RN [8]
RP VARIANT MYPOP LYS-706.
RX PubMed=11114175; DOI=10.1073/pnas.250289597;
RA Martinsson T., Oldfors A., Darin N., Berg K., Tajsharghi H., Kyllerman M.,
RA Wahlstroem J.;
RT "Autosomal dominant myopathy: missense mutation (Glu-706 --> Lys) in the
RT myosin heavy chain IIa gene.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:14614-14619(2000).
RN [9]
RP VARIANTS ILE-970 AND VAL-1061.
RX PubMed=15741996; DOI=10.1038/sj.ejhg.5201375;
RA Tajsharghi H., Darin N., Rekabdar E., Kyllerman M., Wahlstroem J.,
RA Martinsson T., Oldfors A.;
RT "Mutations and sequence variation in the human myosin heavy chain IIa gene
RT (MYH2).";
RL Eur. J. Hum. Genet. 13:617-622(2005).
CC -!- FUNCTION: Muscle contraction. Required for cytoskeleton organization
CC (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Muscle myosin is a hexameric protein that consists of 2 heavy
CC chain subunits (MHC), 2 alkali light chain subunits (MLC) and 2
CC regulatory light chain subunits (MLC-2). Interacts with GCSAM.
CC {ECO:0000269|PubMed:17823310}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, myofibril. Note=Thick filaments of the
CC myofibrils.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9UKX2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9UKX2-2; Sequence=VSP_056291;
CC -!- DOMAIN: The rodlike tail sequence is highly repetitive, showing cycles
CC of a 28-residue repeat pattern composed of 4 heptapeptides,
CC characteristic for alpha-helical coiled coils.
CC -!- DOMAIN: Limited proteolysis of myosin heavy chain produces 1 light
CC meromyosin (LMM) and 1 heavy meromyosin (HMM). HMM can be further
CC cleaved into 2 globular subfragments (S1) and 1 rod-shaped subfragment
CC (S2). {ECO:0000305}.
CC -!- DISEASE: Myopathy, proximal, with ophthalmoplegia (MYPOP) [MIM:605637]:
CC A muscular disorder characterized by mild-to-moderate muscle weakness,
CC ophthalmoplegia, and contractures at birth in some patients. Muscle
CC biopsies from patients show predominance of type 1 fibers and small or
CC absent type 2A fibers. The disease is non-progressive or it progresses
CC very slowly. Inheritance is autosomal dominant or recessive.
CC {ECO:0000269|PubMed:11114175}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Myosin family. {ECO:0000305}.
CC -!- CAUTION: Represents a conventional myosin. This protein should not be
CC confused with the unconventional myosin-2 (MYO2). {ECO:0000305}.
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DR EMBL; AF111784; AAD29950.1; -; mRNA.
DR EMBL; BX510904; CAD91136.1; -; mRNA.
DR EMBL; AC005323; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC093082; AAH93082.1; -; mRNA.
DR EMBL; BC126409; AAI26410.1; -; mRNA.
DR EMBL; S73840; AAC13916.1; -; mRNA.
DR EMBL; Z32858; CAA83687.1; -; mRNA.
DR CCDS; CCDS11156.1; -. [Q9UKX2-1]
DR PIR; I51912; I51912.
DR RefSeq; NP_001093582.1; NM_001100112.1. [Q9UKX2-1]
DR RefSeq; NP_060004.3; NM_017534.5. [Q9UKX2-1]
DR AlphaFoldDB; Q9UKX2; -.
DR SMR; Q9UKX2; -.
DR BioGRID; 110705; 42.
DR IntAct; Q9UKX2; 18.
DR MINT; Q9UKX2; -.
DR STRING; 9606.ENSP00000245503; -.
DR BindingDB; Q9UKX2; -.
DR ChEMBL; CHEMBL4295980; -.
DR iPTMnet; Q9UKX2; -.
DR PhosphoSitePlus; Q9UKX2; -.
DR BioMuta; MYH2; -.
DR DMDM; 13431716; -.
DR UCD-2DPAGE; Q9UKX2; -.
DR EPD; Q9UKX2; -.
DR jPOST; Q9UKX2; -.
DR MassIVE; Q9UKX2; -.
DR MaxQB; Q9UKX2; -.
DR PaxDb; Q9UKX2; -.
DR PeptideAtlas; Q9UKX2; -.
DR PRIDE; Q9UKX2; -.
DR ProteomicsDB; 62563; -.
DR ProteomicsDB; 84903; -. [Q9UKX2-1]
DR ABCD; Q9UKX2; 2 sequenced antibodies.
DR Antibodypedia; 4384; 146 antibodies from 25 providers.
DR DNASU; 4620; -.
DR Ensembl; ENST00000245503.10; ENSP00000245503.5; ENSG00000125414.19. [Q9UKX2-1]
DR Ensembl; ENST00000397183.6; ENSP00000380367.2; ENSG00000125414.19. [Q9UKX2-1]
DR Ensembl; ENST00000532183.6; ENSP00000433944.1; ENSG00000125414.19. [Q9UKX2-2]
DR Ensembl; ENST00000622564.4; ENSP00000482463.1; ENSG00000125414.19. [Q9UKX2-2]
DR GeneID; 4620; -.
DR KEGG; hsa:4620; -.
DR MANE-Select; ENST00000245503.10; ENSP00000245503.5; NM_017534.6; NP_060004.3.
DR UCSC; uc002gmp.5; human. [Q9UKX2-1]
DR CTD; 4620; -.
DR DisGeNET; 4620; -.
DR GeneCards; MYH2; -.
DR HGNC; HGNC:7572; MYH2.
DR HPA; ENSG00000125414; Group enriched (skeletal muscle, tongue).
DR MalaCards; MYH2; -.
DR MIM; 160740; gene.
DR MIM; 605637; phenotype.
DR neXtProt; NX_Q9UKX2; -.
DR OpenTargets; ENSG00000125414; -.
DR Orphanet; 363677; Childhood-onset autosomal recessive myopathy with external ophthalmoplegia.
DR Orphanet; 79091; Hereditary inclusion body myopathy-joint contractures-ophthalmoplegia syndrome.
DR PharmGKB; PA31369; -.
DR VEuPathDB; HostDB:ENSG00000125414; -.
DR eggNOG; KOG0161; Eukaryota.
DR GeneTree; ENSGT00940000161336; -.
DR HOGENOM; CLU_000192_7_5_1; -.
DR InParanoid; Q9UKX2; -.
DR OMA; KVHNETK; -.
DR OrthoDB; 47111at2759; -.
DR PhylomeDB; Q9UKX2; -.
DR TreeFam; TF314375; -.
DR PathwayCommons; Q9UKX2; -.
DR Reactome; R-HSA-2029482; Regulation of actin dynamics for phagocytic cup formation.
DR Reactome; R-HSA-9664422; FCGR3A-mediated phagocytosis.
DR SignaLink; Q9UKX2; -.
DR SIGNOR; Q9UKX2; -.
DR BioGRID-ORCS; 4620; 12 hits in 1068 CRISPR screens.
DR ChiTaRS; MYH2; human.
DR GeneWiki; MYH2; -.
DR GenomeRNAi; 4620; -.
DR Pharos; Q9UKX2; Tbio.
DR PRO; PR:Q9UKX2; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q9UKX2; protein.
DR Bgee; ENSG00000125414; Expressed in skeletal muscle tissue of rectus abdominis and 104 other tissues.
DR ExpressionAtlas; Q9UKX2; baseline and differential.
DR Genevisible; Q9UKX2; HS.
DR GO; GO:0005911; C:cell-cell junction; IMP:ARUK-UCL.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005859; C:muscle myosin complex; TAS:UniProtKB.
DR GO; GO:0030016; C:myofibril; IDA:BHF-UCL.
DR GO; GO:0032982; C:myosin filament; IBA:GO_Central.
DR GO; GO:0016460; C:myosin II complex; IBA:GO_Central.
DR GO; GO:0032991; C:protein-containing complex; IDA:LIFEdb.
DR GO; GO:0030017; C:sarcomere; NAS:BHF-UCL.
DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0000146; F:microfilament motor activity; IBA:GO_Central.
DR GO; GO:0006936; P:muscle contraction; IDA:BHF-UCL.
DR GO; GO:0030049; P:muscle filament sliding; NAS:BHF-UCL.
DR Gene3D; 1.20.5.370; -; 4.
DR Gene3D; 2.30.30.360; -; 1.
DR Gene3D; 3.40.850.10; -; 1.
DR InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR InterPro; IPR036961; Kinesin_motor_dom_sf.
DR InterPro; IPR001609; Myosin_head_motor_dom.
DR InterPro; IPR004009; Myosin_N.
DR InterPro; IPR008989; Myosin_S1_N.
DR InterPro; IPR002928; Myosin_tail.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR014751; XRCC4-like_C.
DR Pfam; PF00063; Myosin_head; 1.
DR Pfam; PF02736; Myosin_N; 1.
DR Pfam; PF01576; Myosin_tail_1; 1.
DR PRINTS; PR00193; MYOSINHEAVY.
DR SMART; SM00015; IQ; 1.
DR SMART; SM00242; MYSc; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS50096; IQ; 1.
DR PROSITE; PS51456; MYOSIN_MOTOR; 1.
DR PROSITE; PS51844; SH3_LIKE; 1.
PE 1: Evidence at protein level;
KW Actin-binding; Alternative splicing; ATP-binding; Calmodulin-binding;
KW Coiled coil; Cytoplasm; Disease variant; Methylation; Motor protein;
KW Muscle protein; Myosin; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Thick filament.
FT CHAIN 1..1941
FT /note="Myosin-2"
FT /id="PRO_0000123393"
FT DOMAIN 33..82
FT /note="Myosin N-terminal SH3-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01190"
FT DOMAIN 86..784
FT /note="Myosin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT DOMAIN 787..816
FT /note="IQ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT REGION 661..683
FT /note="Actin-binding"
FT /evidence="ECO:0000250"
FT REGION 763..777
FT /note="Actin-binding"
FT /evidence="ECO:0000250"
FT REGION 1128..1149
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1155..1174
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 845..1941
FT /evidence="ECO:0000255"
FT BINDING 179..186
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MOD_RES 64
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 69
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 130
FT /note="N6,N6,N6-trimethyllysine"
FT /evidence="ECO:0000255"
FT MOD_RES 389
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 392
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 419
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 625
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 759
FT /note="Pros-methylhistidine"
FT /evidence="ECO:0000250|UniProtKB:Q28641"
FT MOD_RES 1094
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1098
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1164
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1239
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1243
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1245
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1257
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1263
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1288
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1290
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1294
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1305
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1308
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1469
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1476
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1494
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1497
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1503
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1516
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1519
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1556
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1576
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1602
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1605
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1716
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1728
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1732
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1738
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1741
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT VAR_SEQ 659..1891
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_056291"
FT VARIANT 706
FT /note="E -> K (in MYPOP; dbSNP:rs121434589)"
FT /evidence="ECO:0000269|PubMed:11114175"
FT /id="VAR_032630"
FT VARIANT 970
FT /note="V -> I (in one patient with familial myopathy;
FT unknown pathological significance; dbSNP:rs143872329)"
FT /evidence="ECO:0000269|PubMed:15741996"
FT /id="VAR_032631"
FT VARIANT 1061
FT /note="L -> V (in dbSNP:rs142586585)"
FT /evidence="ECO:0000269|PubMed:15741996"
FT /id="VAR_032632"
FT VARIANT 1927
FT /note="R -> Q (in dbSNP:rs34161789)"
FT /id="VAR_032633"
FT CONFLICT 150
FT /note="E -> G (in Ref. 2; CAD91136)"
FT /evidence="ECO:0000305"
FT CONFLICT 1844
FT /note="K -> R (in Ref. 6; CAA83687)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1941 AA; 223044 MW; 681E866F83AEA83F CRC64;
MSSDSELAVF GEAAPFLRKS ERERIEAQNR PFDAKTSVFV AEPKESFVKG TIQSREGGKV
TVKTEGGATL TVKDDQVFPM NPPKYDKIED MAMMTHLHEP AVLYNLKERY AAWMIYTYSG
LFCVTVNPYK WLPVYKPEVV TAYRGKKRQE APPHIFSISD NAYQFMLTDR ENQSILITGE
SGAGKTVNTK RVIQYFATIA VTGEKKKEEI TSGKIQGTLE DQIISANPLL EAFGNAKTVR
NDNSSRFGKF IRIHFGTTGK LASADIETYL LEKSRVVFQL KAERSYHIFY QITSNKKPEL
IEMLLITTNP YDYPFVSQGE ISVASIDDQE ELMATDSAID ILGFTNEEKV SIYKLTGAVM
HYGNLKFKQK QREEQAEPDG TEVADKAAYL QSLNSADLLK ALCYPRVKVG NEYVTKGQTV
EQVSNAVGAL AKAVYEKMFL WMVARINQQL DTKQPRQYFI GVLDIAGFEI FDFNSLEQLC
INFTNEKLQQ FFNHHMFVLE QEEYKKEGIE WTFIDFGMDL AACIELIEKP MGIFSILEEE
CMFPKATDTS FKNKLYDQHL GKSANFQKPK VVKGKAEAHF ALIHYAGVVD YNITGWLEKN
KDPLNETVVG LYQKSAMKTL AQLFSGAQTA EGEGAGGGAK KGGKKKGSSF QTVSALFREN
LNKLMTNLRS THPHFVRCII PNETKTPGAM EHELVLHQLR CNGVLEGIRI CRKGFPSRIL
YADFKQRYKV LNASAIPEGQ FIDSKKASEK LLASIDIDHT QYKFGHTKVF FKAGLLGLLE
EMRDDKLAQL ITRTQARCRG FLARVEYQRM VERREAIFCI QYNIRSFMNV KHWPWMKLFF
KIKPLLKSAE TEKEMATMKE EFQKIKDELA KSEAKRKELE EKMVTLLKEK NDLQLQVQAE
AEGLADAEER CDQLIKTKIQ LEAKIKEVTE RAEDEEEINA ELTAKKRKLE DECSELKKDI
DDLELTLAKV EKEKHATENK VKNLTEEMAG LDETIAKLTK EKKALQEAHQ QTLDDLQAEE
DKVNTLTKAK IKLEQQVDDL EGSLEQEKKL RMDLERAKRK LEGDLKLAQE SIMDIENEKQ
QLDEKLKKKE FEISNLQSKI EDEQALGIQL QKKIKELQAR IEELEEEIEA ERASRAKAEK
QRSDLSRELE EISERLEEAG GATSAQIEMN KKREAEFQKM RRDLEEATLQ HEATAATLRK
KHADSVAELG EQIDNLQRVK QKLEKEKSEM KMEIDDLASN VETVSKAKGN LEKMCRTLED
QLSELKSKEE EQQRLINDLT AQRGRLQTES GEFSRQLDEK EALVSQLSRG KQAFTQQIEE
LKRQLEEEIK AKNALAHALQ SSRHDCDLLR EQYEEEQESK AELQRALSKA NTEVAQWRTK
YETDAIQRTE ELEEAKKKLA QRLQAAEEHV EAVNAKCASL EKTKQRLQNE VEDLMLDVER
TNAACAALDK KQRNFDKILA EWKQKCEETH AELEASQKEA RSLGTELFKI KNAYEESLDQ
LETLKRENKN LQQEISDLTE QIAEGGKRIH ELEKIKKQVE QEKCELQAAL EEAEASLEHE
EGKILRIQLE LNQVKSEVDR KIAEKDEEID QLKRNHIRIV ESMQSTLDAE IRSRNDAIRL
KKKMEGDLNE MEIQLNHANR MAAEALRNYR NTQGILKDTQ IHLDDALRSQ EDLKEQLAMV
ERRANLLQAE IEELRATLEQ TERSRKIAEQ ELLDASERVQ LLHTQNTSLI NTKKKLETDI
SQMQGEMEDI LQEARNAEEK AKKAITDAAM MAEELKKEQD TSAHLERMKK NMEQTVKDLQ
LRLDEAEQLA LKGGKKQIQK LEARVRELEG EVESEQKRNA EAVKGLRKHE RRVKELTYQT
EEDRKNILRL QDLVDKLQAK VKSYKRQAEE AEEQSNTNLA KFRKLQHELE EAEERADIAE
SQVNKLRVKS REVHTKVISE E
