MYH1_HUMAN
ID MYH1_HUMAN Reviewed; 1939 AA.
AC P12882; Q14CA4; Q9Y622;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 14-APR-2009, sequence version 3.
DT 03-AUG-2022, entry version 208.
DE RecName: Full=Myosin-1;
DE AltName: Full=Myosin heavy chain 1;
DE AltName: Full=Myosin heavy chain 2x;
DE Short=MyHC-2x;
DE AltName: Full=Myosin heavy chain IIx/d;
DE Short=MyHC-IIx/d;
DE AltName: Full=Myosin heavy chain, skeletal muscle, adult 1;
GN Name=MYH1;
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].
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).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1064-1939.
RX PubMed=2421254; DOI=10.1093/nar/14.7.2951;
RA Saez L., Leinwand L.A.;
RT "Characterization of diverse forms of myosin heavy chain expressed in adult
RT human skeletal muscle.";
RL Nucleic Acids Res. 14:2951-2969(1986).
RN [5]
RP VARIANTS [LARGE SCALE ANALYSIS] LEU-1306; THR-1445 AND MET-1598.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
RN [6]
RP VARIANT [LARGE SCALE ANALYSIS] SER-640.
RX PubMed=18987736; DOI=10.1038/nature07485;
RA Ley T.J., Mardis E.R., Ding L., Fulton B., McLellan M.D., Chen K.,
RA Dooling D., Dunford-Shore B.H., McGrath S., Hickenbotham M., Cook L.,
RA Abbott R., Larson D.E., Koboldt D.C., Pohl C., Smith S., Hawkins A.,
RA Abbott S., Locke D., Hillier L.W., Miner T., Fulton L., Magrini V.,
RA Wylie T., Glasscock J., Conyers J., Sander N., Shi X., Osborne J.R.,
RA Minx P., Gordon D., Chinwalla A., Zhao Y., Ries R.E., Payton J.E.,
RA Westervelt P., Tomasson M.H., Watson M., Baty J., Ivanovich J., Heath S.,
RA Shannon W.D., Nagarajan R., Walter M.J., Link D.C., Graubert T.A.,
RA DiPersio J.F., Wilson R.K.;
RT "DNA sequencing of a cytogenetically normal acute myeloid leukaemia
RT genome.";
RL Nature 456:66-72(2008).
RN [7]
RP VARIANT LYS-1566.
RX PubMed=21248752; DOI=10.1038/nature09639;
RA Varela I., Tarpey P., Raine K., Huang D., Ong C.K., Stephens P., Davies H.,
RA Jones D., Lin M.L., Teague J., Bignell G., Butler A., Cho J.,
RA Dalgliesh G.L., Galappaththige D., Greenman C., Hardy C., Jia M.,
RA Latimer C., Lau K.W., Marshall J., McLaren S., Menzies A., Mudie L.,
RA Stebbings L., Largaespada D.A., Wessels L.F.A., Richard S., Kahnoski R.J.,
RA Anema J., Tuveson D.A., Perez-Mancera P.A., Mustonen V., Fischer A.,
RA Adams D.J., Rust A., Chan-On W., Subimerb C., Dykema K., Furge K.,
RA Campbell P.J., Teh B.T., Stratton M.R., Futreal P.A.;
RT "Exome sequencing identifies frequent mutation of the SWI/SNF complex gene
RT PBRM1 in renal carcinoma.";
RL Nature 469:539-542(2011).
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 -!- INTERACTION:
CC P12882; Q86Z20: CCDC125; NbExp=3; IntAct=EBI-366238, EBI-11977221;
CC P12882; A1A4E9: KRT13; NbExp=3; IntAct=EBI-366238, EBI-10171552;
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-1 (MYO1). {ECO:0000305}.
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DR EMBL; AF111785; AAD29951.1; -; mRNA.
DR EMBL; AC005323; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC114545; AAI14546.1; -; mRNA.
DR EMBL; X03740; CAA27380.1; -; mRNA.
DR CCDS; CCDS11155.1; -.
DR PIR; A23767; A23767.
DR RefSeq; NP_005954.3; NM_005963.3.
DR RefSeq; XP_016880164.1; XM_017024675.1.
DR AlphaFoldDB; P12882; -.
DR SMR; P12882; -.
DR BioGRID; 110704; 62.
DR IntAct; P12882; 25.
DR MINT; P12882; -.
DR STRING; 9606.ENSP00000226207; -.
DR CarbonylDB; P12882; -.
DR GlyGen; P12882; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P12882; -.
DR PhosphoSitePlus; P12882; -.
DR BioMuta; MYH1; -.
DR DMDM; 226694176; -.
DR UCD-2DPAGE; P12882; -.
DR EPD; P12882; -.
DR jPOST; P12882; -.
DR MassIVE; P12882; -.
DR MaxQB; P12882; -.
DR PaxDb; P12882; -.
DR PeptideAtlas; P12882; -.
DR PRIDE; P12882; -.
DR ProteomicsDB; 52882; -.
DR Antibodypedia; 4383; 192 antibodies from 28 providers.
DR DNASU; 4619; -.
DR Ensembl; ENST00000226207.6; ENSP00000226207.5; ENSG00000109061.10.
DR GeneID; 4619; -.
DR KEGG; hsa:4619; -.
DR MANE-Select; ENST00000226207.6; ENSP00000226207.5; NM_005963.4; NP_005954.3.
DR UCSC; uc002gmo.4; human.
DR CTD; 4619; -.
DR DisGeNET; 4619; -.
DR GeneCards; MYH1; -.
DR HGNC; HGNC:7567; MYH1.
DR HPA; ENSG00000109061; Tissue enriched (skeletal).
DR MIM; 160730; gene.
DR neXtProt; NX_P12882; -.
DR OpenTargets; ENSG00000109061; -.
DR PharmGKB; PA31365; -.
DR VEuPathDB; HostDB:ENSG00000109061; -.
DR eggNOG; KOG0161; Eukaryota.
DR GeneTree; ENSGT00940000154760; -.
DR HOGENOM; CLU_000192_8_1_1; -.
DR InParanoid; P12882; -.
DR OMA; TWDWFLL; -.
DR OrthoDB; 47111at2759; -.
DR PhylomeDB; P12882; -.
DR TreeFam; TF314375; -.
DR PathwayCommons; P12882; -.
DR SignaLink; P12882; -.
DR SIGNOR; P12882; -.
DR BioGRID-ORCS; 4619; 8 hits in 1074 CRISPR screens.
DR GeneWiki; MYH1; -.
DR GenomeRNAi; 4619; -.
DR Pharos; P12882; Tbio.
DR PRO; PR:P12882; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; P12882; protein.
DR Bgee; ENSG00000109061; Expressed in skeletal muscle tissue of rectus abdominis and 96 other tissues.
DR Genevisible; P12882; HS.
DR GO; GO:0031672; C:A band; IEA:Ensembl.
DR GO; GO:0036464; C:cytoplasmic ribonucleoprotein granule; IDA:ParkinsonsUK-UCL.
DR GO; GO:0014704; C:intercalated disc; IEA:Ensembl.
DR GO; GO:0005859; C:muscle myosin complex; IDA:MGI.
DR GO; GO:0032982; C:myosin filament; IBA:GO_Central.
DR GO; GO:0016460; C:myosin II complex; IBA:GO_Central.
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; IBA:GO_Central.
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; 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-1"
FT /id="PRO_0000123391"
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 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 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 757
FT /note="Pros-methylhistidine"
FT /evidence="ECO:0000250|UniProtKB:Q28641"
FT MOD_RES 1092
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1096
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 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 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 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 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 640
FT /note="G -> S (in dbSNP:rs150346984)"
FT /evidence="ECO:0000269|PubMed:18987736"
FT /id="VAR_054159"
FT VARIANT 1306
FT /note="S -> L (in a breast cancer sample; somatic mutation;
FT dbSNP:rs752643679)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036003"
FT VARIANT 1341
FT /note="R -> C (in dbSNP:rs3744564)"
FT /id="VAR_030193"
FT VARIANT 1445
FT /note="A -> T (in a breast cancer sample; somatic mutation;
FT dbSNP:rs139860229)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036004"
FT VARIANT 1539
FT /note="Q -> H (in dbSNP:rs3764850)"
FT /id="VAR_030194"
FT VARIANT 1566
FT /note="Q -> K (found in a renal cell carcinoma sample;
FT somatic mutation)"
FT /evidence="ECO:0000269|PubMed:21248752"
FT /id="VAR_064735"
FT VARIANT 1598
FT /note="V -> M (in a breast cancer sample; somatic mutation;
FT dbSNP:rs150456818)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036005"
FT VARIANT 1716
FT /note="R -> C (in dbSNP:rs1077841)"
FT /id="VAR_030195"
FT CONFLICT 1070
FT /note="T -> A (in Ref. 1; AAD29951 and 4; CAA27380)"
FT /evidence="ECO:0000305"
FT CONFLICT 1131
FT /note="A -> T (in Ref. 4; CAA27380)"
FT /evidence="ECO:0000305"
FT CONFLICT 1139
FT /note="Q -> L (in Ref. 4; CAA27380)"
FT /evidence="ECO:0000305"
FT CONFLICT 1158
FT /note="G -> V (in Ref. 4; CAA27380)"
FT /evidence="ECO:0000305"
FT CONFLICT 1163
FT /note="A -> T (in Ref. 4; CAA27380)"
FT /evidence="ECO:0000305"
FT CONFLICT 1286..1289
FT /note="TESG -> QNQV (in Ref. 4; CAA27380)"
FT /evidence="ECO:0000305"
FT CONFLICT 1302..1303
FT /note="VS -> ET (in Ref. 4; CAA27380)"
FT /evidence="ECO:0000305"
FT CONFLICT 1451
FT /note="R -> T (in Ref. 4; CAA27380)"
FT /evidence="ECO:0000305"
FT CONFLICT 1470
FT /note="E -> V (in Ref. 4; CAA27380)"
FT /evidence="ECO:0000305"
FT CONFLICT 1473..1474
FT /note="AS -> SF (in Ref. 4; CAA27380)"
FT /evidence="ECO:0000305"
FT CONFLICT 1531
FT /note="E -> K (in Ref. 3; AAI14546)"
FT /evidence="ECO:0000305"
FT CONFLICT 1569
FT /note="L -> V (in Ref. 4; CAA27380)"
FT /evidence="ECO:0000305"
FT CONFLICT 1598
FT /note="V -> E (in Ref. 4; CAA27380)"
FT /evidence="ECO:0000305"
FT CONFLICT 1606
FT /note="D -> N (in Ref. 4; CAA27380)"
FT /evidence="ECO:0000305"
FT CONFLICT 1643
FT /note="A -> D (in Ref. 4; CAA27380)"
FT /evidence="ECO:0000305"
FT CONFLICT 1648
FT /note="R -> Q (in Ref. 4; CAA27380)"
FT /evidence="ECO:0000305"
FT CONFLICT 1750
FT /note="Q -> K (in Ref. 4; CAA27380)"
FT /evidence="ECO:0000305"
FT CONFLICT 1822
FT /note="R -> K (in Ref. 4; CAA27380)"
FT /evidence="ECO:0000305"
FT CONFLICT 1845
FT /note="R -> H (in Ref. 4; CAA27380)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1939 AA; 223145 MW; D2B6F28C2C63CBDF CRC64;
MSSDSEMAIF GEAAPFLRKS ERERIEAQNK PFDAKTSVFV VDPKESFVKA TVQSREGGKV
TAKTEAGATV TVKDDQVFPM NPPKYDKIED MAMMTHLHEP AVLYNLKERY AAWMIYTYSG
LFCVTVNPYK WLPVYNAEVV TAYRGKKRQE APPHIFSISD NAYQFMLTDR ENQSILITGE
SGAGKTVNTK RVIQYFATIA VTGEKKKEEV TSGKMQGTLE DQIISANPLL EAFGNAKTVR
NDNSSRFGKF IRIHFGTTGK LASADIETYL LEKSRVTFQL KAERSYHIFY QIMSNKKPDL
IEMLLITTNP YDYAFVSQGE ITVPSIDDQE ELMATDSAIE ILGFTSDERV SIYKLTGAVM
HYGNMKFKQK QREEQAEPDG TEVADKAAYL QNLNSADLLK ALCYPRVKVG NEYVTKGQTV
QQVYNAVGAL AKAVYDKMFL WMVTRINQQL DTKQPRQYFI GVLDIAGFEI FDFNSLEQLC
INFTNEKLQQ FFNHHMFVLE QEEYKKEGIE WTFIDFGMDL AACIELIEKP MGIFSILEEE
CMFPKATDTS FKNKLYEQHL GKSNNFQKPK PAKGKPEAHF SLIHYAGTVD YNIAGWLDKN
KDPLNETVVG LYQKSAMKTL ALLFVGATGA EAEAGGGKKG GKKKGSSFQT VSALFRENLN
KLMTNLRSTH PHFVRCIIPN ETKTPGAMEH ELVLHQLRCN GVLEGIRICR KGFPSRILYA
DFKQRYKVLN ASAIPEGQFI DSKKASEKLL GSIDIDHTQY KFGHTKVFFK AGLLGLLEEM
RDEKLAQLIT RTQAMCRGFL ARVEYQKMVE RRESIFCIQY NVRAFMNVKH WPWMKLYFKI
KPLLKSAETE KEMANMKEEF EKTKEELAKT EAKRKELEEK MVTLMQEKND LQLQVQAEAD
SLADAEERCD QLIKTKIQLE AKIKEVTERA EDEEEINAEL TAKKRKLEDE CSELKKDIDD
LELTLAKVEK EKHATENKVK NLTEEMAGLD ETIAKLTKEK KALQEAHQQT LDDLQAEEDK
VNTLTKAKIK LEQQVDDLEG SLEQEKKIRM DLERAKRKLE GDLKLAQEST MDIENDKQQL
DEKLKKKEFE MSGLQSKIED EQALGMQLQK KIKELQARIE ELEEEIEAER ASRAKAEKQR
SDLSRELEEI SERLEEAGGA TSAQIEMNKK REAEFQKMRR DLEEATLQHE ATAATLRKKH
ADSVAELGEQ IDNLQRVKQK LEKEKSEMKM EIDDLASNME TVSKAKGNLE KMCRALEDQL
SEIKTKEEEQ QRLINDLTAQ RARLQTESGE YSRQLDEKDT LVSQLSRGKQ AFTQQIEELK
RQLEEEIKAK SALAHALQSS RHDCDLLREQ YEEEQEAKAE LQRAMSKANS EVAQWRTKYE
TDAIQRTEEL EEAKKKLAQR LQDAEEHVEA VNAKCASLEK TKQRLQNEVE DLMIDVERTN
AACAALDKKQ RNFDKILAEW KQKCEETHAE LEASQKESRS LSTELFKIKN AYEESLDQLE
TLKRENKNLQ QEISDLTEQI AEGGKRIHEL EKIKKQVEQE KSELQAALEE AEASLEHEEG
KILRIQLELN QVKSEVDRKI AEKDEEIDQM KRNHIRIVES MQSTLDAEIR SRNDAIRLKK
KMEGDLNEME IQLNHANRMA AEALRNYRNT QAILKDTQLH LDDALRSQED LKEQLAMVER
RANLLQAEIE ELRATLEQTE RSRKIAEQEL LDASERVQLL HTQNTSLINT KKKLETDISQ
IQGEMEDIIQ EARNAEEKAK KAITDAAMMA EELKKEQDTS AHLERMKKNL EQTVKDLQHR
LDEAEQLALK GGKKQIQKLE ARVRELEGEV ESEQKRNVEA VKGLRKHERK VKELTYQTEE
DRKNILRLQD LVDKLQAKVK SYKRQAEEAE EQSNVNLSKF RRIQHELEEA EERADIAESQ
VNKLRVKSRE VHTKIISEE
