MYH10_MOUSE
ID MYH10_MOUSE Reviewed; 1976 AA.
AC Q61879; Q5SV63;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 2.
DT 03-AUG-2022, entry version 195.
DE RecName: Full=Myosin-10;
DE AltName: Full=Cellular myosin heavy chain, type B;
DE AltName: Full=Myosin heavy chain 10;
DE AltName: Full=Myosin heavy chain, non-muscle IIb;
DE AltName: Full=Non-muscle myosin heavy chain B;
DE Short=NMMHC-B;
DE AltName: Full=Non-muscle myosin heavy chain IIb;
DE Short=NMMHC II-b;
DE Short=NMMHC-IIB;
GN Name=Myh10;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-115.
RX PubMed=8931991;
RA Weir L., Chen D.;
RT "Characterization of the nonmuscle myosin heavy chain IIB promoter:
RT regulation by E2F.";
RL Gene Expr. 6:45-57(1996).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1952 AND SER-1956, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=16452087; DOI=10.1074/mcp.t500041-mcp200;
RA Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.;
RT "Comprehensive identification of phosphorylation sites in postsynaptic
RT density preparations.";
RL Mol. Cell. Proteomics 5:914-922(2006).
RN [5]
RP PHOSPHORYLATION.
RX PubMed=17892306; DOI=10.1021/bi701119s;
RA Boyle S.N., Koleske A.J.;
RT "Use of a chemical genetic technique to identify myosin IIb as a substrate
RT of the Abl-related gene (Arg) tyrosine kinase.";
RL Biochemistry 46:11614-11620(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1952 AND SER-1956, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1956, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1939; SER-1952 AND SER-1956,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [9]
RP INTERACTION WITH KIF26B, AND TISSUE SPECIFICITY.
RX PubMed=20439720; DOI=10.1073/pnas.0913748107;
RA Uchiyama Y., Sakaguchi M., Terabayashi T., Inenaga T., Inoue S.,
RA Kobayashi C., Oshima N., Kiyonari H., Nakagata N., Sato Y., Sekiguchi K.,
RA Miki H., Araki E., Fujimura S., Tanaka S.S., Nishinakamura R.;
RT "Kif26b, a kinesin family gene, regulates adhesion of the embryonic kidney
RT mesenchyme.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:9240-9245(2010).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-1241 AND LYS-1301, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [11]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-18; ARG-1930 AND ARG-1940, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Embryo;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
CC -!- FUNCTION: Involved with LARP6 in the stabilization of type I collagen
CC mRNAs for CO1A1 and CO1A2. During cell spreading, plays an important
CC role in cytoskeleton reorganization, focal contacts formation (in the
CC central part but not the margins of spreading cells), and lamellipodial
CC extension; this function is mechanically antagonized by MYH9 (By
CC similarity). Cellular myosin that appears to play a role in
CC cytokinesis, cell shape, and specialized functions such as secretion
CC and capping. {ECO:0000250}.
CC -!- SUBUNIT: Myosin is a hexameric protein that consists of 2 heavy chain
CC subunits (MHC), 2 alkali light chain subunits (MLC) and 2 regulatory
CC light chain subunits (MLC-2). Interacts with PLEKHG6 (By similarity).
CC Interacts with ECPAS (By similarity). Interacts with LARP6 (By
CC similarity). Interacts with MCC (By similarity). Interacts with KIF26B
CC (PubMed:20439720). Interacts with CFAP95 (By similarity).
CC {ECO:0000250|UniProtKB:P35580, ECO:0000269|PubMed:20439720}.
CC -!- INTERACTION:
CC Q61879; Q7TNC6: Kif26b; NbExp=3; IntAct=EBI-400918, EBI-15852098;
CC -!- SUBCELLULAR LOCATION: Cell projection, lamellipodium {ECO:0000250}.
CC Note=Colocalizes with MCC at the leading edge of migrating cells.
CC {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: In newborn kidney, expressed in the mesenchyme and
CC ureteric buds. {ECO:0000269|PubMed:20439720}.
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 -!- PTM: Phosphorylated by ABL2. {ECO:0000269|PubMed:17892306}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Myosin family. {ECO:0000305}.
CC -!- CAUTION: Represents a conventional non-muscle myosin. This protein
CC should not be confused with the unconventional myosin-10 (MYO10).
CC {ECO:0000305}.
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DR EMBL; AL603662; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL645644; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC089011; AAH89011.1; -; mRNA.
DR EMBL; AH003264; AAA84879.1; -; Genomic_DNA.
DR CCDS; CCDS24869.1; -.
DR RefSeq; NP_780469.1; NM_175260.2.
DR AlphaFoldDB; Q61879; -.
DR SMR; Q61879; -.
DR BioGRID; 218774; 173.
DR DIP; DIP-31956N; -.
DR IntAct; Q61879; 154.
DR MINT; Q61879; -.
DR STRING; 10090.ENSMUSP00000099671; -.
DR iPTMnet; Q61879; -.
DR PhosphoSitePlus; Q61879; -.
DR SwissPalm; Q61879; -.
DR EPD; Q61879; -.
DR jPOST; Q61879; -.
DR MaxQB; Q61879; -.
DR PaxDb; Q61879; -.
DR PRIDE; Q61879; -.
DR ProteomicsDB; 287653; -.
DR Antibodypedia; 24686; 168 antibodies from 31 providers.
DR DNASU; 77579; -.
DR Ensembl; ENSMUST00000102611; ENSMUSP00000099671; ENSMUSG00000020900.
DR GeneID; 77579; -.
DR KEGG; mmu:77579; -.
DR UCSC; uc007jny.1; mouse.
DR CTD; 4628; -.
DR MGI; MGI:1930780; Myh10.
DR VEuPathDB; HostDB:ENSMUSG00000020900; -.
DR eggNOG; KOG0160; Eukaryota.
DR eggNOG; KOG0161; Eukaryota.
DR GeneTree; ENSGT00940000155159; -.
DR HOGENOM; CLU_000192_4_4_1; -.
DR InParanoid; Q61879; -.
DR PhylomeDB; Q61879; -.
DR TreeFam; TF333601; -.
DR Reactome; R-MMU-5627123; RHO GTPases activate PAKs.
DR BioGRID-ORCS; 77579; 2 hits in 74 CRISPR screens.
DR ChiTaRS; Myh10; mouse.
DR PRO; PR:Q61879; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q61879; protein.
DR Bgee; ENSMUSG00000020900; Expressed in undifferentiated genital tubercle and 72 other tissues.
DR ExpressionAtlas; Q61879; baseline and differential.
DR Genevisible; Q61879; MM.
DR GO; GO:0042641; C:actomyosin; ISO:MGI.
DR GO; GO:0030424; C:axon; IDA:MGI.
DR GO; GO:0005903; C:brush border; IDA:UniProtKB.
DR GO; GO:0005938; C:cell cortex; IDA:MGI.
DR GO; GO:0032154; C:cleavage furrow; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0009898; C:cytoplasmic side of plasma membrane; IDA:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0043197; C:dendritic spine; IDA:MGI.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0030426; C:growth cone; IDA:MGI.
DR GO; GO:0030027; C:lamellipodium; ISO:MGI.
DR GO; GO:0030496; C:midbody; ISO:MGI.
DR GO; GO:0016459; C:myosin complex; IDA:MGI.
DR GO; GO:0032982; C:myosin filament; IBA:GO_Central.
DR GO; GO:0016460; C:myosin II complex; IDA:MGI.
DR GO; GO:0097513; C:myosin II filament; ISO:MGI.
DR GO; GO:0031594; C:neuromuscular junction; IDA:MGI.
DR GO; GO:0043005; C:neuron projection; IDA:MGI.
DR GO; GO:0043025; C:neuronal cell body; IDA:MGI.
DR GO; GO:0005844; C:polysome; ISO:MGI.
DR GO; GO:0098871; C:postsynaptic actin cytoskeleton; ISO:MGI.
DR GO; GO:0016528; C:sarcoplasm; IDA:MGI.
DR GO; GO:0005819; C:spindle; IDA:MGI.
DR GO; GO:0001725; C:stress fiber; IDA:MGI.
DR GO; GO:0051015; F:actin filament binding; ISO:MGI.
DR GO; GO:0043531; F:ADP binding; ISO:MGI.
DR GO; GO:0005524; F:ATP binding; ISO:MGI.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0000146; F:microfilament motor activity; ISO:MGI.
DR GO; GO:0048027; F:mRNA 5'-UTR binding; ISO:MGI.
DR GO; GO:0035613; F:RNA stem-loop binding; ISO:MGI.
DR GO; GO:0030036; P:actin cytoskeleton organization; IGI:MGI.
DR GO; GO:0051017; P:actin filament bundle assembly; ISO:MGI.
DR GO; GO:0070650; P:actin filament bundle distribution; ISO:MGI.
DR GO; GO:0030048; P:actin filament-based movement; ISO:MGI.
DR GO; GO:0031032; P:actomyosin structure organization; ISO:MGI.
DR GO; GO:0007512; P:adult heart development; IMP:MGI.
DR GO; GO:0035904; P:aorta development; IMP:MGI.
DR GO; GO:0007411; P:axon guidance; IMP:MGI.
DR GO; GO:0007409; P:axonogenesis; IMP:MGI.
DR GO; GO:0007420; P:brain development; IMP:MGI.
DR GO; GO:0060038; P:cardiac muscle cell proliferation; IMP:MGI.
DR GO; GO:0055003; P:cardiac myofibril assembly; IMP:MGI.
DR GO; GO:0003279; P:cardiac septum development; IMP:MGI.
DR GO; GO:0007155; P:cell adhesion; ISO:MGI.
DR GO; GO:0021680; P:cerebellar Purkinje cell layer development; IMP:MGI.
DR GO; GO:0060976; P:coronary vasculature development; IMP:MGI.
DR GO; GO:0006887; P:exocytosis; IMP:MGI.
DR GO; GO:0021592; P:fourth ventricle development; IMP:MGI.
DR GO; GO:0007507; P:heart development; IMP:MGI.
DR GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR GO; GO:0021670; P:lateral ventricle development; IMP:MGI.
DR GO; GO:0000281; P:mitotic cytokinesis; IMP:MGI.
DR GO; GO:0098885; P:modification of postsynaptic actin cytoskeleton; ISO:MGI.
DR GO; GO:0030239; P:myofibril assembly; IMP:MGI.
DR GO; GO:0050885; P:neuromuscular process controlling balance; IMP:MGI.
DR GO; GO:0001764; P:neuron migration; IMP:MGI.
DR GO; GO:0031175; P:neuron projection development; IMP:MGI.
DR GO; GO:0007097; P:nuclear migration; IMP:MGI.
DR GO; GO:0001778; P:plasma membrane repair; IMP:MGI.
DR GO; GO:0050714; P:positive regulation of protein secretion; ISO:MGI.
DR GO; GO:0098974; P:postsynaptic actin cytoskeleton organization; IDA:SynGO.
DR GO; GO:0008360; P:regulation of cell shape; IMP:MGI.
DR GO; GO:1905274; P:regulation of modification of postsynaptic actin cytoskeleton; ISO:MGI.
DR GO; GO:0060041; P:retina development in camera-type eye; IMP:MGI.
DR GO; GO:0006930; P:substrate-dependent cell migration, cell extension; IMP:MGI.
DR GO; GO:0021678; P:third ventricle development; IMP:MGI.
DR GO; GO:0055015; P:ventricular cardiac muscle cell development; IMP:MGI.
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 Pfam; PF00612; IQ; 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; 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 Acetylation; Actin-binding; ATP-binding; Calmodulin-binding; Cell adhesion;
KW Cell projection; Cell shape; Coiled coil; Methylation; Motor protein;
KW Myosin; Nucleotide-binding; Phosphoprotein; Reference proteome.
FT CHAIN 1..1976
FT /note="Myosin-10"
FT /id="PRO_0000123422"
FT DOMAIN 31..81
FT /note="Myosin N-terminal SH3-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01190"
FT DOMAIN 85..783
FT /note="Myosin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT DOMAIN 786..815
FT /note="IQ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT REGION 661..683
FT /note="Actin-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT REGION 1125..1175
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1697..1718
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1874..1976
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 845..1976
FT /evidence="ECO:0000255"
FT COMPBIAS 1125..1156
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1697..1717
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1874..1915
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1950..1965
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 178..185
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MOD_RES 18
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 442
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P35580"
FT MOD_RES 1145
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P35580"
FT MOD_RES 1241
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 1301
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 1645
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P35580"
FT MOD_RES 1930
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 1935
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P35580"
FT MOD_RES 1937
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P35580"
FT MOD_RES 1938
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P35580"
FT MOD_RES 1939
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1940
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 1952
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16452087,
FT ECO:0007744|PubMed:17242355, ECO:0007744|PubMed:21183079"
FT MOD_RES 1956
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16452087,
FT ECO:0007744|PubMed:17242355, ECO:0007744|PubMed:19131326,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 1960
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P35580"
FT MOD_RES 1975
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9JLT0"
SQ SEQUENCE 1976 AA; 228996 MW; D00F922EB6682AEF CRC64;
MAQRTGLEDP ERYLFVDRAV IYNPATQADW TAKKLVWIPS ERHGFEAASI KEERGDEVMV
ELAENGKKAM VNKDDIQKMN PPKFSKVEDM AELTCLNEAS VLHNLKDRYY SGLIYTYSGL
FCVVINPYKN LPIYSENIIE MYRGKKRHEM PPHIYAISES AYRCMLQDRE DQSILCTGES
GAGKTENTKK VIQYLAHVAS SHKGRKDHNI PGELERQLLQ ANPILESFGN AKTVKNDNSS
RFGKFIRINF DVTGYIVGAN IETYLLEKSR AVRQAKDERT FHIFYQLLSG AGEHLKSDLL
LEGFNNYRFL SNGYIPIPGQ QDKDNFQETM EAMHIMGFSH EEILSMLKVV SSVLQFGNIS
FKKERNTDQA SMPENTVAQK LCHLLGMNVM EFTRAILTPR IKVGRDYVQK AQTKEQADFA
VEALAKATYE RLFRWLVHRI NKALDRTKRQ GASFIGILDI AGFEIFELNS FEQLCINYTN
EKLQQLFNHT MFILEQEEYQ REGIEWNFID FGLDLQPCID LIERPANPPG VLALLDEECW
FPKATDKTFV EKLVQEQGSH SKFQKPRQLK DKADFCIIHY AGKVDYKADE WLMKNMDPLN
DNVATLLHQS SDRFVAELWK DVDRIVGLDQ VTGMTETAFG SAYKTKKGMF RTVGQLYKES
LTKLMATLRN TNPNFVRCII PNHEKRAGKL DPHLVLDQLR CNGVLEGIRI CRQGFPNRIV
FQEFRQRYEI LTPNAIPKGF MDGKQACERM IRALELDPNL YRIGQSKIFF RAGVLAHLEE
ERDLKITDII IFFQAVCRGY LARKAFAKKQ QQLSALKVLQ RNCAAYLKLR HWQWWRVFTK
VKPLLQVTRQ EEELQAKDEE LLKVKEKQTK VEGELEEMER KHQQLLEEKN ILAEQLQAET
ELFAEAEEMR ARLAAKKQEL EEILHDLESR VEEEEERNQI LQNEKKKMQA HIQDLEEQLD
EEEGARQKLQ LEKVTAEAKI KKMEEEVLLL EDQNSKFIKE KKLMEDRIAE CSSQLAEEEE
KAKNLAKIRN KQEVMISDLE ERLKKEEKTR QELEKAKRKL DGETTDLQDQ IAELQAQVDE
LKVQLTKKEE ELQGALARGD DETLHKNNAL KVARELQAQI AELQEDFESE KASRNKAEKQ
KRDLSEELEA LKTELEDTLD TTAAQQELRT KREQEVAELK KALEDETKNH EAQIQDMRQR
HATALEELSE QLEQAKRFKA NLEKNKQGLE TDNKELACEV KVLQQVKAES EHKRKKLDAQ
VQELHAKVSE GDRLRVELAE KANKLQNELD NVSTLLEEAE KKGIKFAKDA AGLESQLQDT
QELLQEETRQ KLNLSSRIRQ LEEEKNSLQE QQEEEEEARK NLEKQVLALQ SQLADTKKKV
DDDLGTIESL EEAKKKLLKD VEALSQRLEE KVLAYDKLEK TKNRLQQELD DLTVDLDHQR
QIVSNLEKKQ KKFDQLLAEE KGISARYAEE RDRAEAEARE KETKALSLAR ALEEALEAKE
EFERQNKQLR ADMEDLMSSK DDVGKNVHEL EKSKRALEQQ VEEMRTQLEE LEDELQATED
AKLRLEVNMQ AMKAQFERDL QTRDEQNEEK KRLLLKQVRE LEAELEDERK QRALAVASKK
KMEIDLKDLE AQIEAANKAR DEVIKQLRKL QAQMKDYQRE LEEARASRDE IFAQSKESEK
KLKSLEAEIL QLQEELASSE RARRHAEQER DELADEIANS ASGKSALLDE KRRLEARIAQ
LEEELEEEQS NMELLNDRFR KTTLQVDTLN TELAAERSAA QKSDNARQQL ERQNKELKAK
LQELEGAVKS KFKATISALE AKIGQLEEQL EQEAKERAAA NKLVRRTEKK LKEIFMQVED
ERRHADQYKE QMEKANARMK QLKRQLEEAE EEATRANASR RKLQRELDDA TEANEGLSRE
VSTLKNRLRR GGPISFSSSR SGRRQLHIEG ASLELSDDDT ESKTSDVNDT QPPQSE
