MYH6_RAT
ID MYH6_RAT Reviewed; 1938 AA.
AC P02563; Q63351;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1989, sequence version 2.
DT 03-AUG-2022, entry version 172.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Heart;
RX PubMed=2798111; DOI=10.1093/nar/17.18.7527;
RA Kraft R., Bravo-Zehnder M., Taylor D., Leinwand L.A.;
RT "Complete nucleotide sequence of full length cDNA for rat alpha cardiac
RT myosin heavy chain.";
RL Nucleic Acids Res. 17:7527-7528(1989).
RN [2]
RP DISCUSSION OF SEQUENCE.
RX PubMed=2614840; DOI=10.1016/0022-2836(89)90141-1;
RA McNally E.M., Kraft R., Bravo-Zehnder M., Taylor D., Leinwand L.A.;
RT "Full-length rat alpha and beta cardiac myosin heavy chain sequences.
RT Comparisons suggest a molecular basis for functional differences.";
RL J. Mol. Biol. 210:665-671(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-167.
RX PubMed=6585819; DOI=10.1073/pnas.81.9.2626;
RA Mahdavi V., Chambers A.P., Nadal-Ginard B.;
RT "Cardiac alpha- and beta-myosin heavy chain genes are organized in
RT tandem.";
RL Proc. Natl. Acad. Sci. U.S.A. 81:2626-2630(1984).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1512-1938.
RX PubMed=7045682; DOI=10.1038/297659a0;
RA Mahdavi V., Periasamy M., Nadal-Ginard B.;
RT "Molecular characterization of two myosin heavy chain genes expressed in
RT the adult heart.";
RL Nature 297:659-664(1982).
RN [5]
RP NUCLEOTIDE SEQUENCE OF 1872-1938.
RC STRAIN=Wistar; TISSUE=Heart;
RX PubMed=6241892; DOI=10.1093/eurheartj/5.suppl_f.181;
RA Mahdavi V., Lompre A.M., Chambers A.P., Nadal-Ginard B.;
RT "Cardiac myosin heavy chain isozymic transitions during development and
RT under pathological conditions are regulated at the level of mRNA
RT availability.";
RL Eur. Heart J. 5:181-191(1984).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-378; SER-416; SER-1089;
RP SER-1138; TYR-1260; SER-1270; THR-1276; THR-1283; SER-1308; TYR-1309;
RP THR-1310; SER-1511; THR-1514 AND THR-1680, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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 P02563; P02563: Myh6; NbExp=6; IntAct=EBI-6122328, EBI-6122328;
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; X15938; CAA34064.1; -; mRNA.
DR EMBL; K01464; AAA41648.1; -; Genomic_DNA.
DR EMBL; J00751; AAA41653.1; -; mRNA.
DR EMBL; M32697; AAA41658.1; -; mRNA.
DR PIR; S06005; S06005.
DR AlphaFoldDB; P02563; -.
DR SMR; P02563; -.
DR DIP; DIP-41048N; -.
DR IntAct; P02563; 2.
DR MINT; P02563; -.
DR STRING; 10116.ENSRNOP00000023301; -.
DR iPTMnet; P02563; -.
DR PhosphoSitePlus; P02563; -.
DR jPOST; P02563; -.
DR PaxDb; P02563; -.
DR PeptideAtlas; P02563; -.
DR PRIDE; P02563; -.
DR UCSC; RGD:62029; rat.
DR RGD; 62029; Myh6.
DR eggNOG; KOG0161; Eukaryota.
DR InParanoid; P02563; -.
DR PhylomeDB; P02563; -.
DR Reactome; R-RNO-390522; Striated Muscle Contraction.
DR PRO; PR:P02563; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0005739; C:mitochondrion; IDA:RGD.
DR GO; GO:0005859; C:muscle myosin complex; IDA:RGD.
DR GO; GO:0030016; C:myofibril; IDA:RGD.
DR GO; GO:0016459; C:myosin complex; ISO:RGD.
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; ISO:RGD.
DR GO; GO:0030018; C:Z disc; ISO:RGD.
DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IDA:RGD.
DR GO; GO:0030899; F:calcium-dependent ATPase activity; IMP:RGD.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0000146; F:microfilament motor activity; IMP:RGD.
DR GO; GO:0019901; F:protein kinase binding; ISO:RGD.
DR GO; GO:0044877; F:protein-containing complex binding; IDA:RGD.
DR GO; GO:0030048; P:actin filament-based movement; ISO:RGD.
DR GO; GO:0007512; P:adult heart development; ISO:RGD.
DR GO; GO:0007568; P:aging; IEP:RGD.
DR GO; GO:0046034; P:ATP metabolic process; ISO:RGD.
DR GO; GO:0055009; P:atrial cardiac muscle tissue morphogenesis; ISO:RGD.
DR GO; GO:0055013; P:cardiac muscle cell development; ISO:RGD.
DR GO; GO:0060048; P:cardiac muscle contraction; ISO:RGD.
DR GO; GO:0014898; P:cardiac muscle hypertrophy in response to stress; ISO:RGD.
DR GO; GO:1905243; P:cellular response to 3,3',5-triiodo-L-thyronine; IEP:RGD.
DR GO; GO:0001701; P:in utero embryonic development; ISO:RGD.
DR GO; GO:0006936; P:muscle contraction; IMP:RGD.
DR GO; GO:0030049; P:muscle filament sliding; ISO:RGD.
DR GO; GO:0030239; P:myofibril assembly; ISO:RGD.
DR GO; GO:0043462; P:regulation of ATP-dependent activity; ISO:RGD.
DR GO; GO:0008217; P:regulation of blood pressure; ISO:RGD.
DR GO; GO:0008016; P:regulation of heart contraction; ISO:RGD.
DR GO; GO:0060420; P:regulation of heart growth; ISO:RGD.
DR GO; GO:0002027; P:regulation of heart rate; ISO:RGD.
DR GO; GO:0002026; P:regulation of the force of heart contraction; ISO:RGD.
DR GO; GO:0009408; P:response to heat; IEP:RGD.
DR GO; GO:0045214; P:sarcomere organization; ISO:RGD.
DR GO; GO:0006941; P:striated muscle contraction; ISO:RGD.
DR GO; GO:0055010; P:ventricular cardiac muscle tissue morphogenesis; ISO:RGD.
DR GO; GO:0007522; P:visceral muscle development; ISO:RGD.
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_0000123404"
FT DOMAIN 31..80
FT /note="Myosin N-terminal SH3-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01190"
FT DOMAIN 84..779
FT /note="Myosin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT DOMAIN 782..811
FT /note="IQ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT REGION 656..678
FT /note="Actin-binding"
FT REGION 758..772
FT /note="Actin-binding"
FT REGION 789..806
FT /note="Calmodulin-binding"
FT /evidence="ECO:0000250"
FT REGION 815..832
FT /note="Calmodulin-binding"
FT /evidence="ECO:0000250"
FT REGION 1907..1938
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 842..1938
FT /evidence="ECO:0000255"
FT BINDING 177..184
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT MOD_RES 128
FT /note="N6,N6,N6-trimethyllysine"
FT /evidence="ECO:0000255"
FT MOD_RES 378
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 416
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1089
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1138
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1260
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1270
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1276
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1283
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1308
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1309
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1310
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1511
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1514
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1680
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT CONFLICT 13
FT /note="R -> AP (in Ref. 3)"
FT /evidence="ECO:0000305"
FT CONFLICT 46
FT /note="V -> A (in Ref. 3; AAA41648)"
FT /evidence="ECO:0000305"
FT CONFLICT 51..52
FT /note="VS -> AP (in Ref. 3; AAA41648)"
FT /evidence="ECO:0000305"
FT CONFLICT 87
FT /note="E -> Q (in Ref. 3; AAA41648)"
FT /evidence="ECO:0000305"
FT CONFLICT 109
FT /note="Missing (in Ref. 3; AAA41648)"
FT /evidence="ECO:0000305"
FT CONFLICT 1566
FT /note="F -> FF (in Ref. 4)"
FT /evidence="ECO:0000305"
FT CONFLICT 1575
FT /note="R -> S (in Ref. 4; AAA41653)"
FT /evidence="ECO:0000305"
FT CONFLICT 1721
FT /note="N -> T (in Ref. 4)"
FT /evidence="ECO:0000305"
FT CONFLICT 1852
FT /note="T -> N (in Ref. 4; AAA41653)"
FT /evidence="ECO:0000305"
FT CONFLICT 1870
FT /note="D -> N (in Ref. 4; AAA41653)"
FT /evidence="ECO:0000305"
FT CONFLICT 1934
FT /note="M -> I (in Ref. 4 and 5)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1938 AA; 223508 MW; D7BD33FC2B19E3C2 CRC64;
MTDAQMADFG AARYLRKSEK ERLEAQTRPF DIRTECFVPD DKEEYVKAKI VSREGGKVTA
ETENGKTVTV KEDQVMQQNP PKFDKIEDMA MLTFLHEPAV LYNLKERYAA WMIYTYSGLF
CVTVNPYKWL PVYNAEVVAA YRGKKRSEAP PHIFSISDNA YQYMLTDREN QSILITGESG
AGKTVNTKRV IQYFASIAAI GDRSKKDNPN ANKGTLEDQI IQANPALEAF GNAKTVRNDN
SSRFGKFIRI HFGATGKLAS ADIETYLLEK SRVIFQLKAE RNYHIFYQIL SNKKPELLDM
LLVTNNPYDY AFVSQGEVSV ASIDDSEELL ATDSAFDVLG FTAEEKAGVY KLTGAIMHYG
NMKFKQKQRE EQAEPDGTED ADKSAYLMGL NSADLLKGLC HPRVKVGNEY VTKGQSVQQV
YYSIGALAKS VYEKMFNWMV TRINATLETK QPRQYFIGVL DIAGFEIFDF NSFEQLCINF
TNEKLQQFFN HHMFVLEQEE YKKEGIEWEF IDFGMDLQAC IDLIEKPMGI MSILEEECMF
PKATDMTFKA KLYDNHLGKS NNFQKPRNVK GKQEAHFSLV HYAGTVDYNI LGWLEKNKDP
LNETVVGLYQ KSSLKLMATL FSTYASADTG DSGKGKGGKK KGSSFQTVSA LHRENLNKLM
TNLRTTHPHF VRCIIPNERK APGVMDNPLV MHQLRCNGVL EGIRICRKGF PNRILYGDFR
QRYRILNPAA IPEGQFIDSG KGAEKLLGSL DIDHNQYKFG HTKVFFKAGL LGLLEEMRDE
RLSRIITRIQ AQARGQLMRI EFKKMVERRD ALLVIQWNIR AFMGVKNWPW MKLYFKIKPL
LKSAETEKEM ANMKEEFGRV KDALEKSEAR RKELEEKMVS LLQEKNDLQL QVQAEQDNLA
DAEERCDQLI KNKIQLEAKV KEMTERLEDE EEMNAELTAK KRKLEDECSE LKKDIDDLEL
TLAKVEKEKH ATENKVKNLT EEMAGLDEII AKLTKEKKAL QEAHQQALDD LQAEEDKVNT
LTKSKVKLEQ QVDDLEGSLE QEKKVRMDLE RAKRKLEGDL KLTQESIMDL ENDKLQLEEK
LKKKEFDISQ QNSKIEDEQA LALQLQKKLK ENQARIEELE EELEAERTAR AKVEKLRSDL
TRELEEISER LEEAGGATSV QIEMNKKREA EFQKMRRDLE EATLQHEATA AALRKKHADS
VAELGEQIDN LQRVKQKLEK EKSEFKLELD DVTSHMEQII KAKANLEKVS RTLEDQANEY
RVKLEEAQRS LNDFTTQRAK LQTENGELAR QLEEKEALIW QLTRGKLSYT QQMEDLKRQL
EEEGKAKNAL AHALQSARHD CDLLREQYEE EMEAKAELQR VLSKANSEVA QWRTKYETDA
IQRTEELEEA KKKLAQRLQD AEEAVEAVNA KCSSLEKTKH RLQNEIEDLM VDVERSNAAA
AALDKKQRNF DKILAEWKQK YEESQSELES SQKEARSLST ELFKLKNAYE ESLEHLETFK
RENKNLQEEI SDLTEQLGEG GKNVHELEKI RKQLEVEKLE LQSALEEAEA SLEHEEGKIL
RAQLEFNQIK AEIERKLAEK DEEMEQAKRN HLRVVDSLQT SLDAETRSRN EALRVKKKME
GDLNEMEIQL SQANRIASEA QKHLKNAQAH LKDTQLQLDD AVRANDDLKE NIAIVERRNT
LLQAELEELR AVVEQTERSR KLAEQELIET SERVQLLHSQ NTSLINQKKK MDADLSQLQT
EVEEAVQECR NAEEKAKKAI TDAAMMAEEL KKEQDTSAHL ERMKKNMEQT IKDLQHRLDE
AEQIALKGGK KQLQKLEARV RELENELEAE QKRNAESVKG MRKSERRIKE LTYQTEEDKK
NLVRLQDLVD KLQLKVKAYK RQAEEAEEQA NTNLSKFRKV QHELDEAEER ADIAESQVNK
LRAKSRDIGA KQKMHDEE
