MYH8_HUMAN
ID MYH8_HUMAN Reviewed; 1937 AA.
AC P13535; Q14910;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 3.
DT 03-AUG-2022, entry version 207.
DE RecName: Full=Myosin-8;
DE AltName: Full=Myosin heavy chain 8;
DE AltName: Full=Myosin heavy chain, skeletal muscle, perinatal;
DE Short=MyHC-perinatal;
GN Name=MYH8;
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], AND VARIANT GLY-1261.
RC TISSUE=Skeletal muscle;
RX PubMed=2373371; DOI=10.1016/0378-1119(90)90020-r;
RA Karsch-Mizrachi I., Feghali R., Shows T.B. Jr., Leinwand L.A.;
RT "Generation of a full-length human perinatal myosin heavy-chain-encoding
RT cDNA.";
RL Gene 89:289-294(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Skeletal muscle;
RX PubMed=7601129; DOI=10.1111/j.1432-1033.1995.tb20648.x;
RA Jullian E.H., Kelly A.M., Pompidou A.J., Hoffman R., Schiaffino S.,
RA Stedman H.H., Rubinstein N.A.;
RT "Characterization of a human perinatal myosin heavy-chain transcript.";
RL Eur. J. Biochem. 230:1001-1006(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 502-1937.
RC TISSUE=Skeletal muscle;
RX PubMed=1691980; DOI=10.1111/j.1432-1033.1990.tb15459.x;
RA Bober E., Buchberger-Seidl A., Braun T., Singh S., Goedde H.W.,
RA Arnold H.H.;
RT "Identification of three developmentally controlled isoforms of human
RT myosin heavy chains.";
RL Eur. J. Biochem. 189:55-65(1990).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 860-1937, AND VARIANT GLY-1261.
RX PubMed=2715179; DOI=10.1083/jcb.108.5.1791;
RA Feghali R., Leinwand L.A.;
RT "Molecular genetic characterization of a developmentally regulated human
RT perinatal myosin heavy chain.";
RL J. Cell Biol. 108:1791-1797(1989).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-46.
RA Esser K., Tidhar A., Myszkowski M.;
RT "Isolation and characterization of the human perinatal MHC promoter.";
RL Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP VARIANT CACOV GLN-674, AND VARIANT DA7 GLN-674.
RX PubMed=15282353; DOI=10.1056/nejmoa040584;
RA Veugelers M., Bressan M., McDermott D.A., Weremowicz S., Morton C.C.,
RA Mabry C.C., Lefaivre J.-F., Zunamon A., Destree A., Chaudron J.-M.,
RA Basson C.T.;
RT "Mutation of perinatal myosin heavy chain associated with a Carney complex
RT variant.";
RL N. Engl. J. Med. 351:460-469(2004).
RN [7]
RP VARIANT DA7 GLN-674.
RX PubMed=20949528; DOI=10.1002/ajmg.a.33671;
RA Bonapace G., Ceravolo F., Piccirillo A., Duro G., Strisciuglio P.,
RA Concolino D.;
RT "Germline mosaicism for the c.2021G > A (p.Arg674Gln) mutation in siblings
RT with trismus pseudocamptodactyly.";
RL Am. J. Med. Genet. A 152:2898-2900(2010).
CC -!- FUNCTION: Muscle contraction.
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).
CC -!- SUBCELLULAR LOCATION: Cytoplasm, myofibril. Note=Thick filaments of the
CC myofibrils.
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: Carney complex variant (CACOV) [MIM:608837]: Carney complex is
CC a multiple neoplasia syndrome characterized by spotty skin
CC pigmentation, cardiac and other myxomas, endocrine tumors, and
CC psammomatous melanotic schwannomas. Familial cardiac myxomas are
CC associated with spotty pigmentation of the skin and other phenotypes,
CC including primary pigmented nodular adrenocortical dysplasia,
CC extracardiac (frequently cutaneous) myxomas, schwannomas, and
CC pituitary, thyroid, testicular, bone, ovarian, and breast tumors.
CC Cardiac myxomas do not develop in all patients with the Carney complex,
CC but affected patients have at least two features of the complex or one
CC feature and a clinically significant family history.
CC {ECO:0000269|PubMed:15282353}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Arthrogryposis, distal, 7 (DA7) [MIM:158300]: A form of distal
CC arthrogryposis, a disease characterized by congenital joint
CC contractures that mainly involve two or more distal parts of the limbs,
CC in the absence of a primary neurological or muscle disease. DA7 is
CC characterized by an inability to open the mouth fully (trismus) and
CC pseudocamptodactyly in which wrist dorsiflexion, but not volarflexion,
CC produces involuntary flexion contracture of distal and proximal
CC interphalangeal joints. Additional features include shortened hamstring
CC muscles and short stature. {ECO:0000269|PubMed:15282353,
CC ECO:0000269|PubMed:20949528}. 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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M36769; AAC17185.1; -; mRNA.
DR EMBL; Z38133; CAA86293.1; -; mRNA.
DR EMBL; X51592; CAA35941.1; -; mRNA.
DR EMBL; AF067143; AAC21557.1; -; Genomic_DNA.
DR CCDS; CCDS11153.1; -.
DR PIR; I38055; I38055.
DR RefSeq; NP_002463.2; NM_002472.2.
DR AlphaFoldDB; P13535; -.
DR SMR; P13535; -.
DR BioGRID; 110711; 42.
DR IntAct; P13535; 9.
DR STRING; 9606.ENSP00000384330; -.
DR iPTMnet; P13535; -.
DR PhosphoSitePlus; P13535; -.
DR BioMuta; MYH8; -.
DR DMDM; 3041707; -.
DR EPD; P13535; -.
DR jPOST; P13535; -.
DR MassIVE; P13535; -.
DR MaxQB; P13535; -.
DR PaxDb; P13535; -.
DR PeptideAtlas; P13535; -.
DR PRIDE; P13535; -.
DR ProteomicsDB; 52925; -.
DR Antibodypedia; 4295; 67 antibodies from 20 providers.
DR DNASU; 4626; -.
DR Ensembl; ENST00000403437.2; ENSP00000384330.2; ENSG00000133020.4.
DR GeneID; 4626; -.
DR KEGG; hsa:4626; -.
DR MANE-Select; ENST00000403437.2; ENSP00000384330.2; NM_002472.3; NP_002463.2.
DR UCSC; uc002gmm.3; human.
DR CTD; 4626; -.
DR DisGeNET; 4626; -.
DR GeneCards; MYH8; -.
DR HGNC; HGNC:7578; MYH8.
DR HPA; ENSG00000133020; Group enriched (esophagus, lymphoid tissue, skeletal muscle, tongue).
DR MalaCards; MYH8; -.
DR MIM; 158300; phenotype.
DR MIM; 160741; gene.
DR MIM; 608837; phenotype.
DR neXtProt; NX_P13535; -.
DR OpenTargets; ENSG00000133020; -.
DR Orphanet; 319340; Carney complex-trismus-pseudocamptodactyly syndrome.
DR Orphanet; 3377; Trismus-pseudocamptodactyly syndrome.
DR PharmGKB; PA31376; -.
DR VEuPathDB; HostDB:ENSG00000133020; -.
DR eggNOG; KOG0161; Eukaryota.
DR GeneTree; ENSGT00940000161785; -.
DR HOGENOM; CLU_000192_8_0_1; -.
DR InParanoid; P13535; -.
DR OMA; XPLGIFS; -.
DR OrthoDB; 47111at2759; -.
DR PhylomeDB; P13535; -.
DR TreeFam; TF314375; -.
DR PathwayCommons; P13535; -.
DR Reactome; R-HSA-390522; Striated Muscle Contraction.
DR SignaLink; P13535; -.
DR BioGRID-ORCS; 4626; 9 hits in 1072 CRISPR screens.
DR ChiTaRS; MYH8; human.
DR GeneWiki; MYH8; -.
DR GenomeRNAi; 4626; -.
DR Pharos; P13535; Tbio.
DR PRO; PR:P13535; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; P13535; protein.
DR Bgee; ENSG00000133020; Expressed in vastus lateralis and 48 other tissues.
DR Genevisible; P13535; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005859; C:muscle myosin complex; NAS:UniProtKB.
DR GO; GO:0032982; C:myosin filament; IBA:GO_Central.
DR GO; GO:0016460; C:myosin II complex; IBA:GO_Central.
DR GO; GO:0030017; C:sarcomere; IC:BHF-UCL.
DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IMP:BHF-UCL.
DR GO; GO:0016887; F:ATP hydrolysis activity; IMP:BHF-UCL.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0000146; F:microfilament motor activity; IMP:BHF-UCL.
DR GO; GO:0032027; F:myosin light chain binding; TAS:BHF-UCL.
DR GO; GO:0017018; F:myosin phosphatase activity; TAS:Reactome.
DR GO; GO:0008307; F:structural constituent of muscle; NAS:UniProtKB.
DR GO; GO:0046034; P:ATP metabolic process; IMP:BHF-UCL.
DR GO; GO:0006936; P:muscle contraction; IBA:GO_Central.
DR GO; GO:0030049; P:muscle filament sliding; IMP:BHF-UCL.
DR GO; GO:0003009; P:skeletal muscle contraction; IMP: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; 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; ATP-binding; Calmodulin-binding; Coiled coil; Cytoplasm;
KW Disease variant; Methylation; Motor protein; Muscle protein; Myosin;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Thick filament.
FT CHAIN 1..1937
FT /note="Myosin-8"
FT /id="PRO_0000123413"
FT DOMAIN 35..84
FT /note="Myosin N-terminal SH3-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01190"
FT DOMAIN 88..781
FT /note="Myosin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT DOMAIN 781..813
FT /note="IQ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT REGION 658..680
FT /note="Actin-binding"
FT REGION 760..774
FT /note="Actin-binding"
FT REGION 1126..1146
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 842..1937
FT /evidence="ECO:0000255"
FT BINDING 181..188
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT MOD_RES 66
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 71
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 132
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 424
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 625
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 756
FT /note="Pros-methylhistidine"
FT /evidence="ECO:0000250|UniProtKB:Q28641"
FT MOD_RES 1091
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1095
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1161
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1236
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1242
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1260
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1264
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1285
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1291
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1302
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 1463
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1466
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1473
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1491
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1494
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1500
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1513
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1516
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1553
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1573
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 1713
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1725
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1729
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1738
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT VARIANT 326
FT /note="I -> T (in dbSNP:rs34124921)"
FT /id="VAR_050202"
FT VARIANT 636
FT /note="A -> V (in dbSNP:rs34693726)"
FT /id="VAR_050203"
FT VARIANT 674
FT /note="R -> Q (in CACOV and DA7; dbSNP:rs121434590)"
FT /evidence="ECO:0000269|PubMed:15282353,
FT ECO:0000269|PubMed:20949528"
FT /id="VAR_019810"
FT VARIANT 924
FT /note="E -> G (in dbSNP:rs4372733)"
FT /id="VAR_030207"
FT VARIANT 1229
FT /note="M -> T (in dbSNP:rs35962914)"
FT /id="VAR_050204"
FT VARIANT 1261
FT /note="E -> G (in dbSNP:rs1063926)"
FT /evidence="ECO:0000269|PubMed:2373371,
FT ECO:0000269|PubMed:2715179"
FT /id="VAR_030208"
FT VARIANT 1692
FT /note="W -> R (in dbSNP:rs8069834)"
FT /id="VAR_030209"
FT CONFLICT 15
FT /note="A -> R (in Ref. 2; CAA86293)"
FT /evidence="ECO:0000305"
FT CONFLICT 970
FT /note="E -> Q (in Ref. 1 and 4)"
FT /evidence="ECO:0000305"
FT CONFLICT 1072
FT /note="M -> N (in Ref. 3; CAA35941)"
FT /evidence="ECO:0000305"
FT CONFLICT 1247
FT /note="N -> H (in Ref. 1 and 4)"
FT /evidence="ECO:0000305"
FT CONFLICT 1251..1252
FT /note="MC -> DGG (in Ref. 3; CAA35941)"
FT /evidence="ECO:0000305"
FT CONFLICT 1297
FT /note="K -> Q (in Ref. 1 and 4)"
FT /evidence="ECO:0000305"
FT CONFLICT 1377..1378
FT /note="KY -> NT (in Ref. 3; CAA35941)"
FT /evidence="ECO:0000305"
FT CONFLICT 1504..1505
FT /note="EN -> AH (in Ref. 1 and 4)"
FT /evidence="ECO:0000305"
FT CONFLICT 1847
FT /note="E -> D (in Ref. 1 and 4)"
FT /evidence="ECO:0000305"
FT CONFLICT 1914
FT /note="D -> H (in Ref. 2; CAA86293)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1937 AA; 222763 MW; A3EE2D151792E9E8 CRC64;
MSASSDAEMA VFGEAAPYLR KSEKERIEAQ NKPFDAKTSV FVAEPKESYV KSTIQSKEGG
KVTVKTEGGA TLTVREDQVF PMNPPKYDKI EDMAMMTHLH EPGVLYNLKE RYAAWMIYTY
SGLFCVTVNP YKWLPVYKPE VVAAYRGKKR QEAPPHIFSI SDNAYQFMLT DRENQSILIT
GESGAGKTVN TKRVIQYFAT IAVTGEKKKD ESGKMQGTLE DQIISANPLL EAFGNAKTVR
NDNSSRFGKF IRIHFGTTGK LASADIETYL LEKSRVTFQL KAERSYHIFY QITSNKKPDL
IEMLLITTNP YDYAFVSQGE ITVPSIDDQE ELMATDSAID ILGFTPEEKV SIYKLTGAVM
HYGNMKFKQK QREEQAEPDG TEVADKAAYL QSLNSADLLK ALCYPRVKVG NEYVTKGQTV
QQVYNAVGAL AKAVYEKMFL WMVTRINQQL DTKQPRQYFI GVLDIAGFEI FDFNSLEQLC
INFTNEKLQQ FFNHHMFVLE QEEYKKEGIE WTFIDFGMDL AACIELIEKP LGIFSILEEE
CMFPKATDTS FKNKLYDQHL GKSANFQKPK VVKGKAEAHF SLIHYAGTVD YNITGWLDKN
KDPLNDTVVG LYQKSAMKTL ASLFSTYASA EADSSAKKGA KKKGSSFQTV SALFRENLNK
LMTNLRSTHP HFVRCIIPNE TKTPGAMEHE LVLHQLRCNG VLEGIRICRK GFPSRILYGD
FKQRYKVLNA SAIPEGQFID SKKASEKLLA SIDIDHTQYK FGHTKVFFKA GLLGLLEEMR
DEKLAQIITR TQAVCRGFLM RVEYQKMLQR REALFCIQYN VRAFMNVKHW PWMKLFFKIK
PLLKSAETEK EMATMKEEFQ KTKDELAKSE AKRKELEEKM VTLLKEKNDL QLQVQSEADS
LADAEERCEQ LIKNKIQLEA KIKEVTERAE EEEEINAELT AKKRKLEDEC SELKKDIDDL
ELTLAKVEKE KHATENKVKN LTEEMAGLDE TIAKLSKEKK ALQETHQQTL DDLQAEEDKV
NILTKAKTKL EQQVDDLEGS LEQEKKLRMD LERAKRKLEG DLKLAQESTM DMENDKQQLD
EKLEKKEFEI SNLISKIEDE QAVEIQLQKK IKELQARIEE LGEEIEAERA SRAKAEKQRS
DLSRELEEIS ERLEEAGGAT SAQVELNKKR EAEFQKLRRD LEEATLQHEA MVAALRKKHA
DSMAELGEQI DNLQRVKQKL EKEKSELKME TDDLSSNAEA ISKAKGNLEK MCRSLEDQVS
ELKTKEEEQQ RLINDLTAQR ARLQTEAGEY SRQLDEKDAL VSQLSRSKQA STQQIEELKH
QLEEETKAKN ALAHALQSSR HDCDLLREQY EEEQEGKAEL QRALSKANSE VAQWRTKYET
DAIQRTEELE EAKKKLAQRL QEAEEHVEAV NAKCASLEKT KQRLQNEVED LMLDVERSNA
ACAALDKKQR NFDKVLSEWK QKYEETQAEL EASQKESRSL STELFKVKNV YEESLDQLET
LRRENKNLQQ EISDLTEQIA EGGKQIHELE KIKKQVEQEK CEIQAALEEA EASLEHEEGK
ILRIQLELNQ VKSEVDRKIA EKDEEIDQLK RNHTRVVETM QSTLDAEIRS RNDALRVKKK
MEGDLNEMEI QLNHANRLAA ESLRNYRNTQ GILKETQLHL DDALRGQEDL KEQLAIVERR
ANLLQAEIEE LWATLEQTER SRKIAEQELL DASERVQLLH TQNTSLINTK KKLENDVSQL
QSEVEEVIQE SRNAEEKAKK AITDAAMMAE ELKKEQDTSA HLERMKKNLE QTVKDLQHRL
DEAEQLALKG GKKQIQKLEA RVRELEGEVE NEQKRNAEAV KGLRKHERRV KELTYQTEED
RKNVLRLQDL VDKLQAKVKS YKRQAEEAEE QSNANLSKFR KLQHELEEAE ERADIAESQV
NKLRVKSREV HTKISAE
