ID   MYH4_HUMAN              Reviewed;        1939 AA.
AC   Q9Y623;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 2.
DT   27-MAR-2024, entry version 191.
DE   RecName: Full=Myosin-4;
DE   AltName: Full=Myosin heavy chain 2b;
DE            Short=MyHC-2b;
DE   AltName: Full=Myosin heavy chain 4;
DE   AltName: Full=Myosin heavy chain IIb;
DE            Short=MyHC-IIb;
DE   AltName: Full=Myosin heavy chain, skeletal muscle, fetal;
GN   Name=MYH4;
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 VARIANTS MET-1106; LYS-1209; GLY-1802 AND
RP   GLU-1911.
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 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).
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   -!- 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-4 (MYO4). {ECO:0000305}.
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DR   EMBL; AF111783; AAD29949.1; -; mRNA.
DR   EMBL; AC005323; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   CCDS; CCDS11154.1; -.
DR   RefSeq; NP_060003.2; NM_017533.2.
DR   RefSeq; XP_016880165.1; XM_017024676.1.
DR   AlphaFoldDB; Q9Y623; -.
DR   SMR; Q9Y623; -.
DR   BioGRID; 110707; 85.
DR   IntAct; Q9Y623; 21.
DR   MINT; Q9Y623; -.
DR   STRING; 9606.ENSP00000255381; -.
DR   iPTMnet; Q9Y623; -.
DR   PhosphoSitePlus; Q9Y623; -.
DR   BioMuta; MYH4; -.
DR   DMDM; 224471840; -.
DR   EPD; Q9Y623; -.
DR   jPOST; Q9Y623; -.
DR   MassIVE; Q9Y623; -.
DR   MaxQB; Q9Y623; -.
DR   PaxDb; 9606-ENSP00000255381; -.
DR   PeptideAtlas; Q9Y623; -.
DR   ProteomicsDB; 86589; -.
DR   Pumba; Q9Y623; -.
DR   Antibodypedia; 62478; 165 antibodies from 23 providers.
DR   DNASU; 4622; -.
DR   Ensembl; ENST00000255381.2; ENSP00000255381.2; ENSG00000264424.1.
DR   GeneID; 4622; -.
DR   KEGG; hsa:4622; -.
DR   MANE-Select; ENST00000255381.2; ENSP00000255381.2; NM_017533.2; NP_060003.2.
DR   UCSC; uc002gmn.4; human.
DR   AGR; HGNC:7574; -.
DR   CTD; 4622; -.
DR   DisGeNET; 4622; -.
DR   GeneCards; MYH4; -.
DR   HGNC; HGNC:7574; MYH4.
DR   HPA; ENSG00000264424; Tissue enriched (skeletal).
DR   MIM; 160742; gene.
DR   neXtProt; NX_Q9Y623; -.
DR   OpenTargets; ENSG00000264424; -.
DR   PharmGKB; PA31371; -.
DR   VEuPathDB; HostDB:ENSG00000264424; -.
DR   eggNOG; KOG0161; Eukaryota.
DR   GeneTree; ENSGT00940000163211; -.
DR   HOGENOM; CLU_000192_8_0_1; -.
DR   InParanoid; Q9Y623; -.
DR   OMA; PGEVNQP; -.
DR   OrthoDB; 2877572at2759; -.
DR   PhylomeDB; Q9Y623; -.
DR   TreeFam; TF314375; -.
DR   PathwayCommons; Q9Y623; -.
DR   SignaLink; Q9Y623; -.
DR   BioGRID-ORCS; 4622; 23 hits in 1147 CRISPR screens.
DR   GeneWiki; MYH4; -.
DR   GenomeRNAi; 4622; -.
DR   Pharos; Q9Y623; Tbio.
DR   PRO; PR:Q9Y623; -.
DR   Proteomes; UP000005640; Chromosome 17.
DR   RNAct; Q9Y623; Protein.
DR   Bgee; ENSG00000264424; Expressed in skeletal muscle tissue of rectus abdominis and 22 other cell types or tissues.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005859; C:muscle myosin complex; NAS:BHF-UCL.
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: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:0016887; F:ATP hydrolysis activity; NAS:BHF-UCL.
DR   GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR   GO; GO:0003725; F:double-stranded RNA binding; IDA:MGI.
DR   GO; GO:0000146; F:microfilament motor activity; IBA:GO_Central.
DR   GO; GO:0030048; P:actin filament-based movement; NAS:UniProtKB.
DR   GO; GO:0046034; P:ATP metabolic process; NAS:BHF-UCL.
DR   GO; GO:0006936; P:muscle contraction; IDA:BHF-UCL.
DR   GO; GO:0030049; P:muscle filament sliding; NAS:BHF-UCL.
DR   CDD; cd14915; MYSc_Myh4; 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:SF78; MYOSIN-4; 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; 5.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS50096; IQ; 1.
DR   PROSITE; PS51456; MYOSIN_MOTOR; 1.
DR   PROSITE; PS51844; SH3_LIKE; 1.
DR   UCD-2DPAGE; Q9Y623; -.
DR   Genevisible; Q9Y623; HS.
PE   2: Evidence at transcript level;
KW   Actin-binding; ATP-binding; Calmodulin-binding; Coiled coil; Cytoplasm;
KW   Methylation; Motor protein; Muscle protein; Myosin; Nucleotide-binding;
KW   Phosphoprotein; Reference proteome; Thick filament.
FT   CHAIN           1..1939
FT                   /note="Myosin-4"
FT                   /id="PRO_0000123398"
FT   DOMAIN          33..82
FT                   /note="Myosin N-terminal SH3-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01190"
FT   DOMAIN          86..782
FT                   /note="Myosin motor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT   DOMAIN          785..814
FT                   /note="IQ"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT   REGION          659..681
FT                   /note="Actin-binding"
FT                   /evidence="ECO:0000250"
FT   REGION          761..775
FT                   /note="Actin-binding"
FT                   /evidence="ECO:0000250"
FT   COILED          843..1939
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         79
FT                   /note="Phosphoserine"
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         391
FT                   /note="Phosphothreonine"
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         757
FT                   /note="Pros-methylhistidine"
FT                   /evidence="ECO:0000250|UniProtKB:Q28641"
FT   MOD_RES         776
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT   MOD_RES         1092
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT   MOD_RES         1162
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT   MOD_RES         1237
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT   MOD_RES         1241
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT   MOD_RES         1243
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT   MOD_RES         1255
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT   MOD_RES         1261
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT   MOD_RES         1265
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT   MOD_RES         1278
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT   MOD_RES         1286
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT   MOD_RES         1288
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT   MOD_RES         1292
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT   MOD_RES         1303
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT   MOD_RES         1306
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT   MOD_RES         1413
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT   MOD_RES         1464
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT   MOD_RES         1467
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT   MOD_RES         1474
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT   MOD_RES         1492
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT   MOD_RES         1495
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT   MOD_RES         1501
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT   MOD_RES         1514
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT   MOD_RES         1517
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT   MOD_RES         1542
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT   MOD_RES         1547
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT   MOD_RES         1554
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT   MOD_RES         1574
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT   MOD_RES         1600
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT   MOD_RES         1603
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT   MOD_RES         1714
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT   MOD_RES         1726
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT   MOD_RES         1730
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT   MOD_RES         1736
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT   MOD_RES         1739
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT   VARIANT         594
FT                   /note="A -> T (in dbSNP:rs12949680)"
FT                   /id="VAR_030198"
FT   VARIANT         883
FT                   /note="T -> M (in dbSNP:rs3744558)"
FT                   /id="VAR_022110"
FT   VARIANT         1106
FT                   /note="I -> M (in dbSNP:rs917361)"
FT                   /evidence="ECO:0000269|PubMed:10388558"
FT                   /id="VAR_030199"
FT   VARIANT         1117
FT                   /note="A -> D (in dbSNP:rs16943441)"
FT                   /id="VAR_030200"
FT   VARIANT         1209
FT                   /note="E -> K (in dbSNP:rs11651295)"
FT                   /evidence="ECO:0000269|PubMed:10388558"
FT                   /id="VAR_030201"
FT   VARIANT         1802
FT                   /note="D -> G (in dbSNP:rs2277649)"
FT                   /evidence="ECO:0000269|PubMed:10388558"
FT                   /id="VAR_030202"
FT   VARIANT         1862
FT                   /note="R -> C (in dbSNP:rs34260986)"
FT                   /id="VAR_056175"
FT   VARIANT         1911
FT                   /note="K -> E (in dbSNP:rs3744554)"
FT                   /evidence="ECO:0000269|PubMed:10388558"
FT                   /id="VAR_024542"
FT   CONFLICT        1167
FT                   /note="M -> L (in Ref. 1; AAD29949)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1939 AA;  223071 MW;  023D6F73C476B19B CRC64;
     MSSDSEMAIF GEAAPFLRKS EKERIEAQNK PFDAKTSVFV VDPKESYVKA IVQSREGGKV
     TAKTEAGATV TVKEDQVFSM NPPKYDKIED MAMMTHLHEP AVLYNLKERY AAWMIYTYSG
     LFCVTVNPYK WLPVYNPEVV TAYRGKKRQE APPHIFSISD NAYQFMLTDR ENQSILITGE
     SGAGKTVNTK RVIQYFATIA VTGEKKKEEP ASGKMQGTLE DQIISANPLL EAFGNAKTVR
     NDNSSRFGKF IRIHFGATGK LASADIETYL LEKSRVTFQL KAERSYHIFY QILSNKKPEL
     IEMLLITTNP YDFAFVSQGE ITVPSIDDQE ELMATDSAVD ILGFTADEKV AIYKLTGAVM
     HYGNMKFKQK QREEQAEPDG TEVADKAAYL TSLNSADLLK SLCYPRVKVG NEFVTKGQTV
     QQVYNAVGAL AKAIYEKMFL WMVTRINQQL DTKQPRQYFI GVLDIAGFEI FDFNSLEQLC
     INFTNEKLQQ FFNHHMFVLE QEEYKKEGIE WEFIDFGMDL AACIELIEKP MGIFSILEEE
     CMFPKATDTS FKNKLYEQHL GKSNNFQKPK PAKGKPEAHF SLVHYAGTVD YNIAGWLDKN
     KDPLNETVVG LYQKSAMKTL AFLFSGAQTA EAEGGGGKKG GKKKGSSFQT VSALFRENLN
     KLMTNLRSTH PHFVRCIIPN ETKTPGAMEH ELVLHQLRCN GVLEGIRICR KGFPSRILYA
     DFKQRYKVLN ASAIPEGQFI DSKKASEKLL GSIEIDHTQY KFGHTKVFFK AGLLGTLEEM
     RDEKLAQLIT RTQAICRGFL MRVEFRKMME RRESIFCIQY NIRAFMNVKH WPWMKLYFKI
     KPLLKSAETE KEMANMKEEF EKTKEELAKT EAKRKELEEK MVTLMQEKND LQLQVQAEAD
     ALADAEERCD QLIKTKIQLE AKIKEVTERA EDEEEINAEL TAKKRKLEDE CSELKKDIDD
     LELTLAKVEK EKHATENKVK NLTEEMAGLD ETIAKLTKEK KALQEAHQQT LDDLQMEEDK
     VNTLTKAKTK LEQQVDDLEG SLEQEKKLCM DLERAKRKLE GDLKLAQEST MDTENDKQQL
     NEKLKKKEFE MSNLQGKIED EQALAIQLQK KIKELQARIE ELEEEIEAER ASRAKAEKQR
     SDLSRELEEI SERLEEAGGA TSAQIEMNKK REAEFQKMRR DLEESTLQHE ATAAALRKKH
     ADSVAELGEQ IDSLQRVKQK LEKEKSELKM EINDLASNME TVSKAKANFE KMCRTLEDQL
     SEIKTKEEEQ QRLINELSAQ KARLHTESGE FSRQLDEKDA MVSQLSRGKQ AFTQQIEELK
     RQLEEETKAK STLAHALQSA RHDCDLLREQ YEEEQEAKAE LQRGMSKANS EVAQWRTKYE
     TDAIQRTEEL EEAKKKLAQR LQDAEEHVEA VNSKCASLEK TKQRLQNEVE DLMIDVERSN
     AACIALDKKQ RNFDKVLAEW KQKYEETQAE LEASQKESRS LSTELFKVKN AYEESLDHLE
     TLKRENKNLQ QEISDLTEQI AEGGKHIHEL EKVKKQLDHE KSELQTSLEE AEASLEHEEG
     KILRIQLELN QVKSEIDRKI AEKDEELDQL KRNHLRVVES MQSTLDAEIR SRNDALRIKK
     KMEGDLNEME IQLNHANRQA AEALRNLRNT QGILKDTQLH LDDAIRGQDD LKEQLAMVER
     RANLMQAEVE ELRASLERTE RGRKMAEQEL LDASERVQLL HTQNTSLINT KKKLETDISQ
     IQGEMEDIVQ EARNAEEKAK KAITDAAMMA EELKKEQDTS AHLERMKKNM EQTVKDLQLR
     LDEAEQLALK GGKKQIQKLE ARVRELESEV ESEQKHNVEA VKGLRKHERR VKELTYQTEE
     DRKNILRLQD LVDKLQTKVK AYKRQAEEAE EQSNVNLAKF RKLQHELEEA KERADIAESQ
     VNKLRVKSRE VHTKVISEE
//