MYH6_MESAU
ID MYH6_MESAU Reviewed; 1939 AA.
AC P13539; Q60562;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-1998, sequence version 2.
DT 03-AUG-2022, entry version 121.
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;
OS Mesocricetus auratus (Golden hamster).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Mesocricetus.
OX NCBI_TaxID=10036;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=F1B; TISSUE=Liver;
RX PubMed=7815459; DOI=10.1006/jmcc.1994.1134;
RA Wang R., Sole M.J., Cukerman E., Liew C.-C.;
RT "Characterization and nucleotide sequence of the cardiac alpha-myosin heavy
RT chain gene from Syrian hamster.";
RL J. Mol. Cell. Cardiol. 26:1155-1165(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1630-1939.
RX PubMed=3458174; DOI=10.1073/pnas.83.10.3175;
RA Liew C.-C., Jandreski M.A.;
RT "Construction and characterization of the alpha form of a cardiac myosin
RT heavy chain cDNA clone and its developmental expression in the Syrian
RT hamster.";
RL Proc. Natl. Acad. Sci. U.S.A. 83:3175-3179(1986).
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 -!- 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; L15351; AAB59701.1; -; Genomic_DNA.
DR EMBL; M12995; AAA37081.1; -; mRNA.
DR PIR; I48175; I48175.
DR AlphaFoldDB; P13539; -.
DR SMR; P13539; -.
DR Proteomes; UP000189706; Unplaced.
DR GO; GO:0030016; C:myofibril; IEA:UniProtKB-SubCell.
DR GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
DR GO; GO:0032982; C:myosin filament; IEA:UniProtKB-KW.
DR GO; GO:0051015; F:actin filament binding; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0003774; F:cytoskeletal motor activity; IEA:InterPro.
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 2: Evidence at transcript 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-6"
FT /id="PRO_0000123402"
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 1908..1939
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 842..1939
FT /evidence="ECO:0000255"
FT BINDING 178..185
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
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:0000250|UniProtKB:Q02566"
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:0000250|UniProtKB:Q02566"
FT MOD_RES 1515
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P02563"
FT MOD_RES 1681
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P02563"
FT CONFLICT 1633
FT /note="Q -> L (in Ref. 2; AAA37081)"
FT /evidence="ECO:0000305"
FT CONFLICT 1651
FT /note="H -> Q (in Ref. 2; AAA37081)"
FT /evidence="ECO:0000305"
FT CONFLICT 1686..1687
FT /note="EL -> DV (in Ref. 2; AAA37081)"
FT /evidence="ECO:0000305"
FT CONFLICT 1693
FT /note="V -> G (in Ref. 2; AAA37081)"
FT /evidence="ECO:0000305"
FT CONFLICT 1844
FT /note="K -> R (in Ref. 2; AAA37081)"
FT /evidence="ECO:0000305"
FT CONFLICT 1879
FT /note="A -> T (in Ref. 2; AAA37081)"
FT /evidence="ECO:0000305"
FT CONFLICT 1885
FT /note="E -> Q (in Ref. 2; AAA37081)"
FT /evidence="ECO:0000305"
FT CONFLICT 1907
FT /note="E -> V (in Ref. 2; AAA37081)"
FT /evidence="ECO:0000305"
FT CONFLICT 1928
FT /note="D -> N (in Ref. 2; AAA37081)"
FT /evidence="ECO:0000305"
FT CONFLICT 1933..1935
FT /note="QKM -> KR (in Ref. 2; AAA37081)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1939 AA; 223627 MW; DBC8297DFE83115A CRC64;
MTDSQMADFG AAAEYLRKSE KERLEAQTRP FDIRTECFVP DDKEEFVKAK IVSREGGKVT
AETENGKTVT VKEDQVMQQN PPKFDKIEDM AMLTFLHEPA VLYNLKERYA AWMIYTYSGL
FCVTVNPYKW LPVYNAEVVA AYRGKKRSEA PAHIFSISDN AYQYMLTDRE NQSILITGES
GAGKTVNTKR VIQYFASIAA IGDRSKKDNP NANKGTLEDQ IIQANPALEA FGNAKTVRND
NSSRFGKFIR IHFGATGKLA SADIETYLLE KSRVIFQLKA ERNYHIFYQI LSNKKPELLD
MLLVTNNPYD YAFVSQGEVS VASIDDSEEL LATDSAFDVL GFTAEEKAGV YKLTGAIMHY
GNMKFKQKQR EEQAEPDGTE DADKSAYLMG LNSADLLKGL CHPRVKVGNE YVTKGQSVQQ
VYYSIGALGK SVYEKMFNWM VTRINATLET KQPRQYFIGV LDIAGFEIFD FNSFEQLCIN
FTNEKLQQFF NHHMFVLEQE EYKKEGIEWE FIDFGMDLQA CIDLIEKPMG IMSILEEECM
FPKATDMTFK AKLYDNHLGK SNNFQKPRNV KGKQEAHFSL VHYAGTVDYN ILGWLEKNKD
PLNETVVGLY QKSSLKLMAT LFSTYASADA GDSGKGKGGK KKGSSFQTVS ALHRENLNKL
MTNLRTTHPH FVRCIIPNER KAPGVMDNPL VMHQLRCNGV LEGIRICRKG FPNRILYGDF
RQRYRILNPA AIPEGQFIDS RKGAEKLLSS LDIDHNQYKF GHTKVFFKAG LLGLLEEMRD
ERLSRIITRI QAQARGQLMR IEFKKMVERR DALLVIQWNI RAFMGVKNWP WMKLYFKIKP
LLKSAETEKE MANMKEEFGR VKESLEKSEA RRKELEEKMV SLLQEKNDLQ FQVQAEQDNL
NDAEERCDQL IKNKIQLEAK VKEMTERLED EEEMNAELTS KKRKLEDECS ELKKDIDDLE
LTLAKVEKEK HATENKVKNL TEEMAGLDEI IAKLTKEKKA LQEAHQQALD DLQAEEDKVN
TLTKSKVKLE QQVDDLEGSL EQEKKVRMDL ERAKRKLEGD LNVTQESIMD LENDKLQLEE
KLKKKEFDIS QQNSKIEDEQ ALALQLQKKL KENQARIEEL EEELEAERTA RAKVEKLRSD
LTRELEEISE RLEEAGGATS VQIEMNKKRE AEFQKMRRDL EEATLQHEAT AAALRKKHAD
SVAELGEQID NLQRVKQKLE KEKSEFKLEL DDVTSNMEQI IKAKANLEKV SRTLEDQANE
YRVKLEESQR SLNDFTTQRA KLQTENGELA RQLEEKEALI SQLTRGKLSY TQQMEDLKRQ
LEEEGKAKNA LAHALQSARH DCDLLREQYE EEMEAKAELQ RVLSKANSEV AQWRTKYETD
AIQRTEELEE AKKKLAQRLQ DAEEAVEAVN AKCSSLEKTK HRLQNEIEDL MVDVERSNAA
AAALDKKQRN FDKILAEWKQ KYEESQSELE SSQKEARSLS TELFKLKNAY EESLEHLETF
KRENKNLQEE ISDLTEQLGE GGKNVHELEK VRKQLEVEKM ELQSALEEAE ASLEHEEGKI
LRAQLEFNQI KAEIERKLAE KDEEMEQAKR NHLRVVDSLQ TSLDAETRSR NEALRVKKKM
EGDLNEMEIQ LSQANRIASE AQKHLKNAQA HLKDTQLQLD DALHANDDLK ENIAIVERRN
TLLQAELEEL RAVVEQTERS RKLAEQELIE TSERVQLLHS QNTSLINQKK KMEADLTQLQ
TEVEEAVQEC RNAEEKAKKA ITDAAMMAEE LKKEQDTSAH LERMKKNMEQ TIKDLQHRLD
EAEQIALKGG KKQLQKLEAR VRELENELEA EQKRNAESVK GMRKSERRIK ELTYQTEEDK
KNLVRLQDLV DKLQLKVKAY KRQAEEAEEQ ANTNLSKFRK VQHELDEAEE RADIAESQVN
KLRAKSRDIG AKQKMHDEE
