MYH6_MOUSE
ID MYH6_MOUSE Reviewed; 1938 AA.
AC Q02566; Q64258; Q64738;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 2.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=Myosin-6;
DE AltName: Full=Myosin heavy chain 6;
DE AltName: Full=Myosin heavy chain, cardiac muscle alpha isoform;
DE Short=MyHC-alpha;
GN Name=Myh6; Synonyms=Myhca;
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].
RC STRAIN=A/J, BALB/cJ, C57BL/6J, and DBA/2J;
RX PubMed=1577481; DOI=10.1016/0888-7543(92)90218-h;
RA Quinn-Laquer B.K., Kennedy J.E., Wei S.J., Beisel K.W.;
RT "Characterization of the allelic differences in the mouse cardiac alpha-
RT myosin heavy chain coding sequence.";
RL Genomics 13:176-188(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-67.
RC STRAIN=AKR/J;
RX PubMed=2026617; DOI=10.1016/s0021-9258(18)31568-0;
RA Gulick J., Subramaniam A., Neumann J., Robbins J.;
RT "Isolation and characterization of the mouse cardiac myosin heavy chain
RT genes.";
RL J. Biol. Chem. 266:9180-9185(1991).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1271 AND SER-1512, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Heart;
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).
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 Q02566; O70468: Mybpc3; NbExp=5; IntAct=EBI-299157, EBI-8347074;
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 -!- MISCELLANEOUS: The cardiac alpha isoform is a 'fast' ATPase myosin,
CC while the beta isoform is a 'slow' ATPase.
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-6 (MYO6). {ECO:0000305}.
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DR EMBL; M76598; AAA37159.1; -; mRNA.
DR EMBL; M76599; AAA37160.1; -; mRNA.
DR EMBL; M76600; AAA37161.1; -; mRNA.
DR EMBL; M76601; AAA37162.1; -; mRNA.
DR EMBL; M62404; AAA37424.1; -; Genomic_DNA.
DR CCDS; CCDS36927.1; -.
DR PIR; I49464; I49464.
DR RefSeq; NP_001157643.1; NM_001164171.1.
DR RefSeq; NP_034986.1; NM_010856.4.
DR AlphaFoldDB; Q02566; -.
DR SMR; Q02566; -.
DR BioGRID; 201651; 3.
DR DIP; DIP-31385N; -.
DR IntAct; Q02566; 3.
DR STRING; 10090.ENSMUSP00000080538; -.
DR iPTMnet; Q02566; -.
DR PhosphoSitePlus; Q02566; -.
DR SWISS-2DPAGE; Q02566; -.
DR EPD; Q02566; -.
DR MaxQB; Q02566; -.
DR PaxDb; Q02566; -.
DR PRIDE; Q02566; -.
DR ProteomicsDB; 287656; -.
DR ABCD; Q02566; 6 sequenced antibodies.
DR Antibodypedia; 91; 166 antibodies from 27 providers.
DR DNASU; 17888; -.
DR Ensembl; ENSMUST00000081857; ENSMUSP00000080538; ENSMUSG00000040752.
DR Ensembl; ENSMUST00000226297; ENSMUSP00000154634; ENSMUSG00000040752.
DR GeneID; 17888; -.
DR KEGG; mmu:17888; -.
DR UCSC; uc007txr.2; mouse.
DR CTD; 4624; -.
DR MGI; MGI:97255; Myh6.
DR VEuPathDB; HostDB:ENSMUSG00000040752; -.
DR eggNOG; KOG0161; Eukaryota.
DR GeneTree; ENSGT00940000154805; -.
DR HOGENOM; CLU_000192_8_0_1; -.
DR InParanoid; Q02566; -.
DR OMA; IRAWCTL; -.
DR OrthoDB; 47111at2759; -.
DR PhylomeDB; Q02566; -.
DR TreeFam; TF314375; -.
DR Reactome; R-MMU-390522; Striated Muscle Contraction.
DR BioGRID-ORCS; 17888; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Myh6; mouse.
DR PRO; PR:Q02566; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; Q02566; protein.
DR Bgee; ENSMUSG00000040752; Expressed in cardiac muscle of left ventricle and 109 other tissues.
DR ExpressionAtlas; Q02566; baseline and differential.
DR Genevisible; Q02566; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; ISO:MGI.
DR GO; GO:0005859; C:muscle myosin complex; ISO:MGI.
DR GO; GO:0030016; C:myofibril; IDA: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; IBA:GO_Central.
DR GO; GO:0001725; C:stress fiber; IDA:MGI.
DR GO; GO:0030018; C:Z disc; IDA:MGI.
DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; ISO:MGI.
DR GO; GO:0030899; F:calcium-dependent ATPase activity; 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; IMP:MGI.
DR GO; GO:0019901; F:protein kinase binding; ISO:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0030048; P:actin filament-based movement; IMP:MGI.
DR GO; GO:0007512; P:adult heart development; IMP:MGI.
DR GO; GO:0046034; P:ATP metabolic process; ISO:MGI.
DR GO; GO:0055009; P:atrial cardiac muscle tissue morphogenesis; ISO:MGI.
DR GO; GO:0055013; P:cardiac muscle cell development; IMP:MGI.
DR GO; GO:0060048; P:cardiac muscle contraction; IMP:BHF-UCL.
DR GO; GO:0014898; P:cardiac muscle hypertrophy in response to stress; IDA:MGI.
DR GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR GO; GO:0006936; P:muscle contraction; ISO:MGI.
DR GO; GO:0030049; P:muscle filament sliding; ISO:MGI.
DR GO; GO:0030239; P:myofibril assembly; IMP:MGI.
DR GO; GO:0043462; P:regulation of ATP-dependent activity; IMP:MGI.
DR GO; GO:0008217; P:regulation of blood pressure; IMP:MGI.
DR GO; GO:0008016; P:regulation of heart contraction; IMP:MGI.
DR GO; GO:0060420; P:regulation of heart growth; IDA:MGI.
DR GO; GO:0002027; P:regulation of heart rate; IMP:MGI.
DR GO; GO:0002026; P:regulation of the force of heart contraction; IMP:MGI.
DR GO; GO:0045214; P:sarcomere organization; IMP:MGI.
DR GO; GO:0006941; P:striated muscle contraction; IMP:MGI.
DR GO; GO:0055010; P:ventricular cardiac muscle tissue morphogenesis; ISO:MGI.
DR GO; GO:0007522; P:visceral muscle development; IMP: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; 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..1938
FT /note="Myosin-6"
FT /id="PRO_0000123403"
FT DOMAIN 32..81
FT /note="Myosin N-terminal SH3-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01190"
FT DOMAIN 85..780
FT /note="Myosin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT DOMAIN 783..812
FT /note="IQ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT REGION 657..679
FT /note="Actin-binding"
FT REGION 759..773
FT /note="Actin-binding"
FT REGION 790..807
FT /note="Calmodulin-binding"
FT /evidence="ECO:0000250"
FT REGION 816..833
FT /note="Calmodulin-binding"
FT /evidence="ECO:0000250"
FT REGION 1909..1938
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 842..1938
FT /evidence="ECO:0000255"
FT BINDING 178..185
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT MOD_RES 129
FT /note="N6,N6,N6-trimethyllysine"
FT /evidence="ECO:0000255"
FT MOD_RES 379
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P02563"
FT MOD_RES 417
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02563"
FT MOD_RES 1090
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02563"
FT MOD_RES 1139
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02563"
FT MOD_RES 1261
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P02563"
FT MOD_RES 1271
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1277
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P02563"
FT MOD_RES 1284
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P02563"
FT MOD_RES 1309
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02563"
FT MOD_RES 1310
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P02563"
FT MOD_RES 1311
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P02563"
FT MOD_RES 1512
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1515
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P02563"
FT VARIANT 194
FT /note="Y -> D"
FT VARIANT 545
FT /note="S -> A"
FT VARIANT 838
FT /note="I -> S"
SQ SEQUENCE 1938 AA; 223565 MW; EAD789ADA68818FB CRC64;
MTDAQMADFG AAAQYLRKSE KERLEAQTRP FDIRTECFVP DDKEEYVKAK VVSREGGKVT
AETENGKTVT IKEDQVMQQN PPKFDKIEDM AMLTFLHEPA VLYNLKERYA AWMIYTYSGL
FCVTVNPYKW LPVYNAEVVA AYRGKKRSEA PPHIFSISDN AYQYMLTDRE NQSILITGES
GAGKTVNTKR VIQYFASIAA IGDRSKKENP NANKGTLEDQ IIQANPALEA FGNAKTVRND
NSSRFGKFIR IHFGATGKLA SADIETYLLE KSRVIFQLKA ERNYHIFYQI LSNKKPELLD
MLLVTNNPYD YAFVSQGEVS VASIDDSEEL LATDSAFDVL SFTAEEKAGV YKLTGAIMHY
GNMKFKQKQR EEQAEPDGTE DADKSAYLMG LNSADLLKGL CHPRVKVGNE YVTKGQSVQQ
VYYSIGALAK SVYEKMFNWM VTRINATLET KQPRQYFIGV LDIAGFEIFD FNSFEQLCIN
FTNEKLQQFF NHHMFVLEQE EYKKEGIEWE FIDFGMDLQA CIDLIEKPMG IMSILEEECM
FPKASDMTFK AKLYDNHLGK SNNFQKPRNV KGKQEAHFSL VHYAGTVDYN IMGWLEKNKD
PLNETVVGLY QKSSLKLMAT LFSTYASADT GDSGKGKGGK KKGSSFQTVS ALHRENLNKL
MTNLKTTHPH FVRCIIPNER KAPGVMDNPL VMHQLRCNGV LEGIRICRKG FPNRILYGDF
RQRYRILNPA AIPEGQFIDS RKGAEKLLGS LDIDHNQYKF GHTKVFFKAG LLGLLEEMRD
ERLSRIITRI QAQARGQLMR IEFKKIVERR DALLVIQWNI RAFMGVKNWP WMKLYFKIKP
LLKSAETEKE MANMKEEFGR VKDALEKSEA RRKELEEKMV SLLQEKNDLQ LQVQAEQDNL
NDAEERCDQL IKNKIQLEAK VKEMTERLED EEEMNAELTA KKRKLEDECS ELKKDIDDLE
LTLAKVEKEK HATENKVKNL TEEMAGLDEI IAKLTKEKKA LQEAHQQALD DLQAEEDKVN
TLTKSKVKLE QQVDDLEGSL EQEKKVRMDL ERAKRKLEGD LKLTQESIMD LENDKLQLEE
KLKKKEFDIS QQNSKIEDEQ ALALQLQKKL KENQARIEEL EEELEAERTA RAKVEKLRSD
LSRELEEISE RLEEAGGATS VQIEMNKKRE AEFQKMRRDL EEATLQHEAT AAALRKKHAD
SVAELGEQID NLQRVKQKLE KEKSEFKLEL DDVTSNMEQI IKAKANLEKV SRTLEDQANE
YRVKLEEAQR SLNDFTTQRA KLQTENGELA RQLEEKEALI SQLTRGKLSY TQQMEDLKRQ
LEEEGKAKNA LAHALQSSRH DCDLLREQYE EEMEAKAELQ RVLSKANSEV AQWRTKYETD
AIQRTEELEE AKKKLAQRLQ DAEEAVEAVN AKCSSLEKTK HRLQNEIEDL MVDVERSNAA
AAALDKKQRN FDKILAEWKQ KYEESQSELE SSQKEARSLS TELFKLKNAY EESLEHLETF
KRENKNLQEE ISDLTEQLGE GGKNVHELEK IRKQLEVEKL ELQSALEEAE ASLEHEEGKI
LRAQLEFNQI KAEIERKLAE KDEEMEQAKR NHLRMVDSLQ TSLDAETRSR NEALRVKKKM
EGDLNEMEIQ LSQANRIASE AQKHLKNSQA HLKDTQLQLD DAVHANDDLK ENIAIVERRN
NLLQAELEEL RAVVEQTERS RKLAEQELIE TSERVQLLHS QNTSLINQKK KMESDLTQLQ
TEVEEAVQEC RNAEEKAKKA ITDAAMMAEE LKKEQDTSAH LERMKKNMEQ TIKDLQHRLD
EAEQIALKGG KKQLQKLEAR VRELENELEA EQKRNAESVK GMRKSERRIK ELTYQTEEDK
KNLMRLQDLV DKLQLKVKAY KRQAEEAEEQ ANTNLSKFRK VQHELDEAEE RADIAESQVN
KLRAKSRDIG AKKMHDEE
