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   27-MAR-2024, entry version 216.
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; 48.
DR   IntAct; P13535; 10.
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; 9606-ENSP00000384330; -.
DR   PeptideAtlas; P13535; -.
DR   ProteomicsDB; 52925; -.
DR   Pumba; P13535; -.
DR   Antibodypedia; 4295; 75 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   AGR; HGNC:7578; -.
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; TMDMEND; -.
DR   OrthoDB; 2877572at2759; -.
DR   PhylomeDB; P13535; -.
DR   TreeFam; TF314375; -.
DR   PathwayCommons; P13535; -.
DR   Reactome; R-HSA-390522; Striated Muscle Contraction.
DR   SignaLink; P13535; -.
DR   BioGRID-ORCS; 4626; 10 hits in 1150 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 cell types or tissues.
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   CDD; cd14918; MYSc_Myh8; 1.
DR   Gene3D; 1.10.10.820; -; 1.
DR   Gene3D; 1.20.5.340; -; 5.
DR   Gene3D; 1.20.5.370; -; 4.
DR   Gene3D; 1.20.5.4820; -; 1.
DR   Gene3D; 1.20.58.530; -; 1.
DR   Gene3D; 6.10.250.2420; -; 1.
DR   Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR   Gene3D; 2.30.30.360; Myosin S1 fragment, N-terminal; 1.
DR   Gene3D; 1.20.120.720; Myosin VI head, motor domain, U50 subdomain; 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   PANTHER; PTHR45615; MYOSIN HEAVY CHAIN, NON-MUSCLE; 1.
DR   PANTHER; PTHR45615:SF35; MYOSIN-8; 1.
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; SSF90257; Myosin rod fragments; 4.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF57997; Tropomyosin; 1.
DR   PROSITE; PS50096; IQ; 1.
DR   PROSITE; PS51456; MYOSIN_MOTOR; 1.
DR   PROSITE; PS51844; SH3_LIKE; 1.
DR   Genevisible; P13535; HS.
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
//