MYH14_MOUSE
ID MYH14_MOUSE Reviewed; 2000 AA.
AC Q6URW6; B3F3T1; Q80V64; Q80ZE6;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Myosin-14;
DE AltName: Full=Myosin heavy chain 14;
DE AltName: Full=Myosin heavy chain, non-muscle IIc;
DE AltName: Full=Non-muscle myosin heavy chain IIc;
DE Short=NMHC II-C;
GN Name=Myh14;
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 [MRNA] (ISOFORMS 1 AND 2), TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RC STRAIN=C57BL/6J; TISSUE=Lung;
RX PubMed=14594953; DOI=10.1074/jbc.m309981200;
RA Golomb E., Ma X., Jana S.S., Preston Y.A., Kawamoto S., Shoham N.G.,
RA Goldin E., Conti M.A., Sellers J.R., Adelstein R.S.;
RT "Identification and characterization of nonmuscle myosin II-C, a new member
RT of the myosin II family.";
RL J. Biol. Chem. 279:2800-2808(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), ALTERNATIVE SPLICING, TISSUE
RP SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC TISSUE=Cerebellum;
RX PubMed=19240025; DOI=10.1074/jbc.m806574200;
RA Jana S.S., Kim K.Y., Mao J., Kawamoto S., Sellers J.R., Adelstein R.S.;
RT "An alternatively spliced isoform of non-muscle myosin II-C is not
RT regulated by myosin light chain phosphorylation.";
RL J. Biol. Chem. 284:11563-11571(2009).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1220-2000.
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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 [5]
RP PROTEIN SEQUENCE OF 1618-1630, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=OF1; TISSUE=Hippocampus;
RA Lubec G., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-33; SER-925; SER-1249;
RP SER-1280; SER-1973 AND THR-1998, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Kidney, Liver, Lung, and Pancreas;
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 [7]
RP DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=20861308; DOI=10.1091/mbc.e10-04-0293;
RA Ma X., Jana S.S., Conti M.A., Kawamoto S., Claycomb W.C., Adelstein R.S.;
RT "Ablation of nonmuscle myosin II-B and II-C reveals a role for nonmuscle
RT myosin II in cardiac myocyte karyokinesis.";
RL Mol. Biol. Cell 21:3952-3962(2010).
CC -!- FUNCTION: Cellular myosin that appears to play a role in cytokinesis,
CC cell shape, and specialized functions such as secretion and capping.
CC {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). {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=NM II-C1;
CC IsoId=Q6URW6-1; Sequence=Displayed;
CC Name=2; Synonyms=NM II-C0;
CC IsoId=Q6URW6-2; Sequence=VSP_014633;
CC Name=3; Synonyms=NM II-C2;
CC IsoId=Q6URW6-3; Sequence=VSP_014633, VSP_044759;
CC -!- TISSUE SPECIFICITY: Highest levels in lung, kidney, brain and colon,
CC very low levels in liver and bladder and no expression in spleen or
CC seminal vesicle (at protein level). Isoform 1 is expressed in liver,
CC kidney and testis with low levels in skeletal muscle and heart. Isoform
CC 1 and isoform 2 are expressed in brain and lung. Isoform 2 is the main
CC isoform expressed in skeletal muscle and heart. Isoform 3 is limited to
CC brain stem, cerebellum and spinal cord. {ECO:0000269|PubMed:14594953,
CC ECO:0000269|PubMed:19240025}.
CC -!- DEVELOPMENTAL STAGE: Widely expressed throughout the embryo at 11.5
CC dpc. Enhanced expression in the developing pituitary at 11.5 dpc.
CC Expressed in developing lung from 13.5 dpc. At 16.5 dpc, confined to
CC airway epithelial cells, developing sensory area of the cochlea and
CC intestinal epithelial cells, particularly concentrated at their apical
CC border. {ECO:0000269|PubMed:14594953, ECO:0000269|PubMed:19240025,
CC ECO:0000269|PubMed:20861308}.
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. {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Survival to adulthood with no obvious defects in
CC brain structure, lung and heart development and no evidence for
CC defective cell division. Deletion in animals expressing only 12% of
CC wild-type amounts of Myh10 results in an increase in cardiac myocyte
CC hypertrophy and interstitial fibrosis compared with the Myh10
CC hypomorphic animal. {ECO:0000269|PubMed:20861308}.
CC -!- MISCELLANEOUS: [Isoform 1]: Requires phosphorylation of the myosin
CC regulatory light chain for activity.
CC -!- MISCELLANEOUS: [Isoform 2]: Requires phosphorylation of the myosin
CC regulatory light chain for activity. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 3]: Constitutively active isoform which does
CC not require phosphorylation of the regulatory myosin light chain for
CC activity. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Myosin family. {ECO:0000305}.
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DR EMBL; AY363100; AAQ24173.1; -; mRNA.
DR EMBL; AY205605; AAO47092.1; -; mRNA.
DR EMBL; EF602040; ABR10605.1; -; mRNA.
DR EMBL; AC150895; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC157653; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC041796; AAH41796.1; -; mRNA.
DR CCDS; CCDS39943.1; -. [Q6URW6-2]
DR CCDS; CCDS71951.1; -. [Q6URW6-1]
DR RefSeq; NP_001258467.1; NM_001271538.1. [Q6URW6-3]
DR RefSeq; NP_001258469.1; NM_001271540.1. [Q6URW6-1]
DR RefSeq; NP_082297.1; NM_028021.3. [Q6URW6-2]
DR RefSeq; XP_011249204.1; XM_011250902.2. [Q6URW6-2]
DR RefSeq; XP_011249205.1; XM_011250903.2. [Q6URW6-1]
DR RefSeq; XP_017167802.1; XM_017312313.1. [Q6URW6-1]
DR AlphaFoldDB; Q6URW6; -.
DR SMR; Q6URW6; -.
DR BioGRID; 215057; 7.
DR IntAct; Q6URW6; 3.
DR MINT; Q6URW6; -.
DR STRING; 10090.ENSMUSP00000103531; -.
DR BindingDB; Q6URW6; -.
DR ChEMBL; CHEMBL4295870; -.
DR iPTMnet; Q6URW6; -.
DR PhosphoSitePlus; Q6URW6; -.
DR SwissPalm; Q6URW6; -.
DR EPD; Q6URW6; -.
DR jPOST; Q6URW6; -.
DR MaxQB; Q6URW6; -.
DR PaxDb; Q6URW6; -.
DR PeptideAtlas; Q6URW6; -.
DR PRIDE; Q6URW6; -.
DR ProteomicsDB; 287335; -. [Q6URW6-1]
DR ProteomicsDB; 287336; -. [Q6URW6-2]
DR ProteomicsDB; 287337; -. [Q6URW6-3]
DR Antibodypedia; 32261; 268 antibodies from 33 providers.
DR DNASU; 71960; -.
DR Ensembl; ENSMUST00000048102; ENSMUSP00000046059; ENSMUSG00000030739. [Q6URW6-1]
DR Ensembl; ENSMUST00000107899; ENSMUSP00000103531; ENSMUSG00000030739. [Q6URW6-2]
DR Ensembl; ENSMUST00000207775; ENSMUSP00000147115; ENSMUSG00000030739. [Q6URW6-3]
DR GeneID; 71960; -.
DR KEGG; mmu:71960; -.
DR UCSC; uc009gqi.2; mouse. [Q6URW6-2]
DR UCSC; uc009gqj.2; mouse. [Q6URW6-1]
DR UCSC; uc012fjt.2; mouse. [Q6URW6-3]
DR CTD; 79784; -.
DR MGI; MGI:1919210; Myh14.
DR VEuPathDB; HostDB:ENSMUSG00000030739; -.
DR eggNOG; KOG0161; Eukaryota.
DR GeneTree; ENSGT00940000158808; -.
DR HOGENOM; CLU_000192_4_0_1; -.
DR InParanoid; Q6URW6; -.
DR OMA; HGGLQQF; -.
DR OrthoDB; 47111at2759; -.
DR TreeFam; TF333601; -.
DR Reactome; R-MMU-5627123; RHO GTPases activate PAKs.
DR BioGRID-ORCS; 71960; 3 hits in 73 CRISPR screens.
DR ChiTaRS; Myh14; mouse.
DR PRO; PR:Q6URW6; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q6URW6; protein.
DR Bgee; ENSMUSG00000030739; Expressed in substantia propria of cornea and 211 other tissues.
DR ExpressionAtlas; Q6URW6; baseline and differential.
DR Genevisible; Q6URW6; 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:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0030426; C:growth cone; IDA:MGI.
DR GO; GO:0043209; C:myelin sheath; HDA:UniProtKB.
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; ISO:MGI.
DR GO; GO:0097513; C:myosin II filament; ISO:MGI.
DR GO; GO:0001725; C:stress fiber; IDA:MGI.
DR GO; GO:0051015; F:actin filament binding; IDA:MGI.
DR GO; GO:0005524; F:ATP binding; IDA:MGI.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0000146; F:microfilament motor activity; IDA:MGI.
DR GO; GO:0030048; P:actin filament-based movement; IDA:MGI.
DR GO; GO:0031032; P:actomyosin structure organization; ISO:MGI.
DR GO; GO:0070584; P:mitochondrion morphogenesis; ISO:MGI.
DR GO; GO:0019228; P:neuronal action potential; ISO:MGI.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR GO; GO:0007605; P:sensory perception of sound; ISO:MGI.
DR GO; GO:0003009; P:skeletal muscle contraction; ISO:MGI.
DR GO; GO:0007519; P:skeletal muscle tissue development; ISO:MGI.
DR GO; GO:0071625; P:vocalization behavior; ISO:MGI.
DR DisProt; DP01022; -.
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; 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; Alternative splicing; ATP-binding;
KW Calmodulin-binding; Cell shape; Coiled coil; Direct protein sequencing;
KW Motor protein; Myosin; Nucleotide-binding; Phosphoprotein;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q7Z406"
FT CHAIN 2..2000
FT /note="Myosin-14"
FT /id="PRO_0000123432"
FT DOMAIN 47..97
FT /note="Myosin N-terminal SH3-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01190"
FT DOMAIN 101..804
FT /note="Myosin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT DOMAIN 807..836
FT /note="IQ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT REGION 682..704
FT /note="Actin-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT REGION 1173..1197
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1260..1311
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1597..1629
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1720..1751
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1910..1942
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1967..2000
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 866..1951
FT /evidence="ECO:0000255"
FT COMPBIAS 1289..1305
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1720..1738
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1910..1936
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 194..201
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z406"
FT MOD_RES 33
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 56
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z406"
FT MOD_RES 925
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1198
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z406"
FT MOD_RES 1249
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1280
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1973
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1985
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z406"
FT MOD_RES 1998
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 228..235
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:14594953,
FT ECO:0000303|PubMed:19240025"
FT /id="VSP_014633"
FT VAR_SEQ 644
FT /note="D -> DEQGGLQQFTLLGSFPSPSPGPAGRLGSGASPPGVGSLCAPT (in
FT isoform 3)"
FT /evidence="ECO:0000303|PubMed:19240025"
FT /id="VSP_044759"
SQ SEQUENCE 2000 AA; 228586 MW; 1957C1A42EF2A21A CRC64;
MAAVTMSVSG RKVASRPGPV PEAAQSFLYA PRTPNVGGPG GPQVEWTARR MVWVPSELHG
FEAAALRDEG EEEAEVELAE SGRRLRLPRD QIQRMNPPKF SKAEDMAELT CLNEASVLHN
LRERYYSGLI YTYSGLFCVV INPYKQLPIY TEAIVEMYRG KKRHEVPPHV YAVTEGAYRS
MLQDREDQSI LCTGESGAGK TENTKKVIQY LAHVASSPKG RKEPGVPASV STMSYGELER
QLLQANPILE AFGNAKTVKN DNSSRFGKFI RINFDIAGYI VGANIETYLL EKSRAIRQAK
DECSFHIFYQ LLGGAGEQLK ADLLLEPCSH YRFLTNGPSS SPGQERELFQ ETLESLRVLG
LLPEEITAML RTVSAVLQFG NIVLKKERNT DQATMPDNTA AQKLCRLLGL GVTDFSRALL
TPRIKVGRDY VQKAQTKEQA DFALEALAKA TYERLFRWLV LRLNRALDRS PRQGASFLGI
LDIAGFEIFQ LNSFEQLCIN YTNEKLQQLF NHTMFVLEQE EYQREGIPWT FLDFGLDLQP
CIDLIERPAN PPGLLALLDE ECWFPKATDK SFVEKVAQEQ GSHPKFQRPR NLRDQADFSV
LHYAGKVDYK ASEWLMKNMD PLNDNVAALL HQSTDRLTAE IWKDVEGIVG LEQVSSLGDG
PPGGRPRRGM FRTVGQLYKE SLSRLMATLS NTNPSFVRCI VPNHEKRAGK LEPRLVLDQL
RCNGVLEGIR ICRQGFPNRI LFQEFRQRYE ILTPNAIPKG FMDGKQACEK MIQALELDPN
LYRVGQSKIF FRAGVLAQLE EERDLKVTDI IVSFQAAARG YLARRAFQRR QQQQSALRVM
QRNCAAYLKL RNWQWWRLFI KVKPLLQVTR QDEVLQARAQ ELQKVQELQQ QSAREVGELQ
GRVAQLEEER TRLAEQLRAE AELCSEAEET RARLAARKQE LELVVTELEA RVGEEEECSR
QLQSEKKRLQ QHIQELESHL EAEEGARQKL QLEKVTTEAK MKKFEEDLLL LEDQNSKLSK
ERRLLEERLA EFSSQAAEEE EKVKSLNKLR LKYEATISDM EDRLKKEEKG RQELEKLKRR
LDGESSELQE QMVEQKQRAE ELLAQLGRKE DELQAALLRA EEEGGARAQL LKSLREAQAG
LAEAQEDLEA ERVARAKAEK QRRDLGEELE ALRGELEDTL DSTNAQQELR SKREQEVTEL
KKALEEESRA HEVSMQELRQ RHSQALVEMA EQLEQARRGK GVWEKTRLSL EAEVSELKAE
LSSLQTSRQE GEQKRRRLES QLQEVQGRSS DSERARSEAA EKLQRAQAEL ESVSTALSEA
ESKAIRLGKE LSSAESQLHD TQELLQEETR AKLALGSRVR ALEAEAAGLR EQMEEEVVAR
ERAGRELQST QAQLSEWRRR QEEEAAVLEA GEEARRRAAR EAETLTQRLA EKTEAVERLE
RARRRLQQEL DDATVDLGQQ KQLLSTLEKK QRKFDQLLAE EKAAVLRAVE DRERIEAEGR
EREARALSLT RALEEEQEAR EELERQNRAL RAELEALLSS KDDVGKNVHE LERARKAAEQ
AASDLRTQVT ELEDELTAAE DAKLRLEVTV QALKAQHERD LQGRDDAGEE RRRQLAKQLR
DAEVERDEER KQRALAMAAR KKLELELEEL KAQTSAAGQG KEEAVKQLKK MQVQMKELWR
EVEETRSSRD EMFTLSRENE KKLKGLEAEV LRLQEELAAS DRARRQAQQD RDEMAEEVAS
GNLSKAATLE EKRQLEGRLS QLEEELEEEQ NNSELLKDHY RKLVLQVESL TTELSAERSF
SAKAESGRQQ LERQIQELRA RLGEEDAGAR ARQKMLIAAL ESKLAQAEEQ LEQESRERIL
SGKLVRRAEK RLKEVVLQVD EERRVADQVR DQLEKSNLRL KQLKRQLEEA EEEASRAQAG
RRRLQRELED VTESAESMNR EVTTLRNRLR RGPLTFTTRT VRQVFRLEEG VASDEEEAEG
AEPGSAPGQE PEAPPPATPQ
