MYH8_MOUSE
ID MYH8_MOUSE Reviewed; 1937 AA.
AC P13542; Q5SX36;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 30-AUG-2005, sequence version 2.
DT 03-AUG-2022, entry version 159.
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; Synonyms=Myhsp;
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 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 [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1824-1937.
RX PubMed=3864153; DOI=10.1073/pnas.82.21.7183;
RA Weydert A., Daubas P., Lazaridis I., Barton P., Garner I., Leader D.P.,
RA Bonhomme F., Catalan J., Simon D., Guenet J.-L., Gros F., Buckingham M.E.;
RT "Genes for skeletal muscle myosin heavy chains are clustered and are not
RT located on the same mouse chromosome as a cardiac myosin heavy chain
RT gene.";
RL Proc. Natl. Acad. Sci. U.S.A. 82:7183-7187(1985).
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}.
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DR EMBL; AL596129; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; M12289; AAA39795.1; -; mRNA.
DR CCDS; CCDS24857.1; -.
DR PIR; B24733; B24733.
DR RefSeq; NP_796343.2; NM_177369.3.
DR AlphaFoldDB; P13542; -.
DR SMR; P13542; -.
DR BioGRID; 201649; 6.
DR STRING; 10090.ENSMUSP00000019625; -.
DR iPTMnet; P13542; -.
DR PhosphoSitePlus; P13542; -.
DR MaxQB; P13542; -.
DR PaxDb; P13542; -.
DR PeptideAtlas; P13542; -.
DR PRIDE; P13542; -.
DR ProteomicsDB; 287657; -.
DR Antibodypedia; 4295; 67 antibodies from 20 providers.
DR DNASU; 17885; -.
DR Ensembl; ENSMUST00000019625; ENSMUSP00000019625; ENSMUSG00000055775.
DR GeneID; 17885; -.
DR KEGG; mmu:17885; -.
DR UCSC; uc007jmn.1; mouse.
DR CTD; 4626; -.
DR MGI; MGI:1339712; Myh8.
DR VEuPathDB; HostDB:ENSMUSG00000055775; -.
DR eggNOG; KOG0161; Eukaryota.
DR GeneTree; ENSGT00940000161785; -.
DR HOGENOM; CLU_000192_8_1_1; -.
DR InParanoid; P13542; -.
DR OMA; XPLGIFS; -.
DR OrthoDB; 47111at2759; -.
DR PhylomeDB; P13542; -.
DR TreeFam; TF314375; -.
DR Reactome; R-MMU-390522; Striated Muscle Contraction.
DR BioGRID-ORCS; 17885; 1 hit in 70 CRISPR screens.
DR PRO; PR:P13542; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; P13542; protein.
DR Bgee; ENSMUSG00000055775; Expressed in masseter muscle and 105 other tissues.
DR ExpressionAtlas; P13542; baseline and differential.
DR Genevisible; P13542; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0030016; C:myofibril; IEA:UniProtKB-SubCell.
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; IBA:GO_Central.
DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; ISO:MGI.
DR GO; GO:0016887; F:ATP hydrolysis activity; ISO:MGI.
DR GO; GO:0000146; F:microfilament motor activity; ISO:MGI.
DR GO; GO:0046034; P:ATP metabolic process; ISO:MGI.
DR GO; GO:0006936; P:muscle contraction; IBA:GO_Central.
DR GO; GO:0030049; P:muscle filament sliding; ISO:MGI.
DR GO; GO:0003009; P:skeletal muscle contraction; ISO:MGI.
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 2: Evidence at transcript level;
KW Actin-binding; ATP-binding; Coiled coil; Cytoplasm; Methylation;
KW Motor protein; Muscle protein; Myosin; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Thick filament.
FT CHAIN 1..1937
FT /note="Myosin-8"
FT /id="PRO_0000123414"
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 1125..1171
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 842..1937
FT /evidence="ECO:0000255"
FT COMPBIAS 1125..1154
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 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 1254
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q29RW1"
FT MOD_RES 1260
FT /note="Phosphoserine"
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 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"
SQ SEQUENCE 1937 AA; 222708 MW; 5C215BC2757B64A3 CRC64;
MSAGSDAEMA IFGEAAPYLR KSEKERIEAQ NKPFDAKTSV FVAEPKESYV KSVIQSKDGG
KVTVKTESGA TLTVKEDQVF PMNPPKYDKI EDMAMMTHLH EPGVLYNLKE RYAAWMIYTY
SGLFCVTVNP YKWLPVYNPE VVAAYRGKKR QEAPPHIFSI SDNAYQFMLT DRENQSILIT
GESGAGKTVN TKRVIQYFAT IAVTGDKKKE ESGKMQGTLE DQIISANPLL EAFGNAKTVR
NDNSSRFGKF IRIHFGTTGK LASADIETYL LEKSRVTFQL KAERSYHIFY QITSNKKPEL
IEMLLITTNP YDYAFVSQGE ITVPSIDDQE ELMATDSAID ILGFSPEEKV SIYKLTGAVM
HYGNMKFKQK QREEQAEPDG TEVADKAAYL QCLNSADLLK ALCYPRVKVG NEYVTKGQTV
QQVYNAVGAL AKAVYEKMFL WMVTRINQQL DTKQPRQYFI GVLDIAGFEI FDFNSLEQLC
INFTNEKLQQ FFNHHMFVLE QEEYKKEGIE WTFIDFGMDL AACIELIEKP LGIFSILEEE
CMFPKATDTS FKNKLYDQHL GKSNNFQKPK PTKGKAEAHF SLVHYAGTVD YNITGWLDKN
KDPLNDTVVG LYQKSAMKTL ASLFSTYASA EADGGAKKGA KKKGSSFQTV SALFRENLNK
LMTNLRSTHP HFVRCIIPNE TKTPGAMEHE LVLHQLRCNG VLEGIRICRK GFPSRILYGD
FKQRYKVLNA SAIPEGQFID SKKASEKLLG SIDIDHTQYK FGHTKVFFKA GLLGLLEEMR
DEKLAQIITR TQAVCRGYLM RVEYQKMLLR RESIFCIQYN VRAFMNVKHW PWMKLFFKIK
PLLKSAETEK EMATMKEEFQ KTKDELAKSE AKRKELEEKM VTLLKEKNDL QLQVQSEADS
LADAEERCEQ LIKNKIQLEA KIKEVTERAE DEEEINAELT AKKRKLEDEC SELKKDIDDL
ELTLAKVEKE KHATENKVKN LTEEMAGLDE NIAKLTKEKK ALQEAHQQTL DDLQAEEDKV
NTLTKAKTKL EQQVDDLEGS LEQEKKLRMD LERAKRKLEG DLKLAQESTM DIENDKQQLD
EKLKKKEFEI SNLISKIEDE QAVEIQLQKK IKELQARIEE LEEEIEAERA SRAKAEKQRS
DLSRELEEIS ERLEEAGGAT SAQVEMNKKR ETEFQKLRRD LEEATLQHEA TAAALRKKHA
DSVAELGEQI DNLQRVKQKL EKEKSELKME IDDLSSNAEA IAKAKGNLEK MCRTLEDQVS
ELKSKEEEQQ RLINELTAQR ARLQTEAGEY SRQLDEKDAL VSQLSRSKQA STQQIEELKR
QLEEETKAKN ALAHALQSSR HDCDLLREQY EEEQEGKAEL QRALSKANSE VAQWRTKYET
DAIQRTEELE EAKKKLAQRL QAAEEHVEAV NAKCASLEKT KQRLQNEVED LMIDVERTNA
ACAALDKKQR NFDKVLSEWR QKYEETQAEL ESCQKESRTL STELFKVKNA YEESLDHLET
LRRENKNLQQ EISDLTEQIA EGGKHIHELE KIKKQVEQEK CEIQAALEEA EASLEHEEGK
ILRIQLELNQ VKSEIDRKIA EKDEEIDQLK RNHVRVVETM QSTLDAEIRS RNDALRVKKK
MEGDLNEMEI QLNHANRLAA ESLRNYRNTQ GILKDTQLHL DDALRGQEDL KEQLAIVERR
ANLLQAEIEE LRATLEQTER SRKIAEQELL DASERVQLLH TQNTSLINTK KKLENDVSQL
QSEVEEVIQE SRNAEEKAKK AITDAAMMAE ELKKEQDTSA HLERMKKNME QTVKDLQHRL
DEAEQLALKG GKKQIQKLEA RVRELEGEVE NEQKRNAEAV KGLRKHERRV KELTYQTEED
RKNVLRLQDL VDKLQAKVKS YKRQAEEAEE QSNANLAKFR KLQHELEEAE ERADIAESQV
NKLRVKSREV HTKISAE
