MYH7_RAT
ID MYH7_RAT Reviewed; 1935 AA.
AC P02564;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1989, sequence version 2.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=Myosin-7;
DE AltName: Full=Myosin heavy chain 7;
DE AltName: Full=Myosin heavy chain slow isoform;
DE Short=MyHC-slow;
DE AltName: Full=Myosin heavy chain, cardiac muscle beta isoform;
DE Short=MyHC-beta;
GN Name=Myh7;
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=2798112; DOI=10.1093/nar/17.18.7529;
RA Kraft R., Bravo-Zehnder M., Taylor D., Leinwand L.A.;
RT "Complete nucleotide sequence of full length cDNA for rat beta cardiac
RT myosin heavy chain.";
RL Nucleic Acids Res. 17:7529-7530(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 [MRNA] OF 1524-1935.
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 [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1871-1935.
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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1510, AND IDENTIFICATION BY
RP MASS 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).
RN [6]
RP DOMAIN, FUNCTION, MUTAGENESIS OF THR-1188; GLU-1385; GLU-1582 AND GLY-1807,
RP AND SUBCELLULAR LOCATION.
RX PubMed=26150528; DOI=10.1073/pnas.1505813112;
RA Taylor K.C., Buvoli M., Korkmaz E.N., Buvoli A., Zheng Y., Heinze N.T.,
RA Cui Q., Leinwand L.A., Rayment I.;
RT "Skip residues modulate the structural properties of the myosin rod and
RT guide thick filament assembly.";
RL Proc. Natl. Acad. Sci. U.S.A. 112:E3806-E3815(2015).
CC -!- FUNCTION: Myosins are actin-based motor molecules with ATPase activity
CC essential for muscle contraction. Forms regular bipolar thick filaments
CC that, together with actin thin filaments, constitute the fundamental
CC contractile unit of skeletal and cardiac muscle.
CC {ECO:0000305|PubMed:26150528}.
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). Interacts with ECPAS.
CC Interacts (via C-terminus) with LRRC39. {ECO:0000250|UniProtKB:P12883}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, myofibril
CC {ECO:0000269|PubMed:26150528}. Cytoplasm, myofibril, sarcomere
CC {ECO:0000269|PubMed:26150528}. Note=Thick filaments of the myofibrils.
CC {ECO:0000269|PubMed:26150528}.
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. Four skip residues
CC (Skip1: Thr-1188, Skip2: Glu-1385, Skip3: Glu-1582 and Skip4: Gly-1807)
CC introduce discontinuities in the coiled-coil heptad repeats. The first
CC three skip residues are structurally comparable and induce a unique
CC local relaxation of the coiled-coil superhelical pitch and the fourth
CC skip residue lies within a highly flexible molecular hinge that is
CC necessary for myosin incorporation in the bare zone of sarcomeres
CC (PubMed:26150528). {ECO:0000269|PubMed:26150528}.
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-7 (MYO7). {ECO:0000305}.
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DR EMBL; X15939; CAA34065.1; -; mRNA.
DR EMBL; J00752; AAA41654.1; -; mRNA.
DR EMBL; M32698; AAA41659.1; -; mRNA.
DR PIR; S06006; S06006.
DR RefSeq; NP_058936.1; NM_017240.2.
DR AlphaFoldDB; P02564; -.
DR SMR; P02564; -.
DR BioGRID; 248191; 2.
DR IntAct; P02564; 1.
DR STRING; 10116.ENSRNOP00000024186; -.
DR iPTMnet; P02564; -.
DR PhosphoSitePlus; P02564; -.
DR jPOST; P02564; -.
DR PaxDb; P02564; -.
DR PRIDE; P02564; -.
DR ABCD; P02564; 1 sequenced antibody.
DR GeneID; 29557; -.
DR KEGG; rno:29557; -.
DR UCSC; RGD:62030; rat.
DR CTD; 4625; -.
DR RGD; 62030; Myh7.
DR eggNOG; KOG0161; Eukaryota.
DR InParanoid; P02564; -.
DR OrthoDB; 47111at2759; -.
DR PhylomeDB; P02564; -.
DR PRO; PR:P02564; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005859; C:muscle myosin complex; IDA:RGD.
DR GO; GO:0030016; C:myofibril; IDA:UniProtKB.
DR GO; GO:0016459; C:myosin complex; ISO:RGD.
DR GO; GO:0032982; C:myosin filament; IDA:UniProtKB.
DR GO; GO:0016460; C:myosin II complex; IBA:GO_Central.
DR GO; GO:0030017; C:sarcomere; IDA:UniProtKB.
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; IMP:RGD.
DR GO; GO:0016887; F:ATP hydrolysis activity; IMP:RGD.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; IPI:RGD.
DR GO; GO:0000146; F:microfilament motor activity; IMP:RGD.
DR GO; GO:0044877; F:protein-containing complex binding; IDA: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: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:1904385; P:cellular response to angiotensin; IEP:RGD.
DR GO; GO:0006936; P:muscle contraction; IMP:RGD.
DR GO; GO:0030049; P:muscle filament sliding; ISO:RGD.
DR GO; GO:0002027; P:regulation of heart rate; ISO:RGD.
DR GO; GO:0031449; P:regulation of slow-twitch skeletal muscle fiber contraction; ISO:RGD.
DR GO; GO:0002026; P:regulation of the force of heart contraction; ISO:RGD.
DR GO; GO:0014728; P:regulation of the force of skeletal muscle contraction; ISO:RGD.
DR GO; GO:0045214; P:sarcomere organization; IBA:GO_Central.
DR GO; GO:0003009; P:skeletal muscle contraction; ISO:RGD.
DR GO; GO:0006941; P:striated muscle contraction; ISO:RGD.
DR GO; GO:0014883; P:transition between fast and slow fiber; ISO:RGD.
DR GO; GO:0055010; P:ventricular cardiac muscle tissue morphogenesis; 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..1935
FT /note="Myosin-7"
FT /id="PRO_0000123411"
FT DOMAIN 32..81
FT /note="Myosin N-terminal SH3-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01190"
FT DOMAIN 85..778
FT /note="Myosin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT DOMAIN 781..810
FT /note="IQ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT REGION 655..677
FT /note="Actin-binding"
FT REGION 757..771
FT /note="Actin-binding"
FT REGION 1915..1935
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 840..1935
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 378
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P02563"
FT MOD_RES 1137
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02563"
FT MOD_RES 1269
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q02566"
FT MOD_RES 1282
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P02563"
FT MOD_RES 1308
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P02563"
FT MOD_RES 1309
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P02563"
FT MOD_RES 1510
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1513
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P02563"
FT MUTAGEN 1188
FT /note="Missing: No effect on myosin incorporation into
FT sarcomeres."
FT /evidence="ECO:0000269|PubMed:26150528"
FT MUTAGEN 1385
FT /note="Missing: No effect on myosin incorporation into
FT sarcomeres."
FT /evidence="ECO:0000269|PubMed:26150528"
FT MUTAGEN 1582
FT /note="Missing: No effect on myosin incorporation into
FT sarcomeres. Causes myosin cytoplasmic aggregates that show
FT a sponge-like structure."
FT /evidence="ECO:0000269|PubMed:26150528"
FT MUTAGEN 1807
FT /note="Missing: No effect on myosin incorporation into
FT sarcomeres. Disrupts location on the sarcomere bare zone."
FT /evidence="ECO:0000269|PubMed:26150528"
FT CONFLICT 1529..1531
FT /note="IRK -> VRR (in Ref. 3; AAA41654)"
FT /evidence="ECO:0000305"
FT CONFLICT 1731
FT /note="D -> H (in Ref. 3; AAA41654)"
FT /evidence="ECO:0000305"
FT CONFLICT 1784
FT /note="N -> K (in Ref. 3; AAA41654)"
FT /evidence="ECO:0000305"
FT CONFLICT 1851
FT /note="T -> N (in Ref. 3; AAA41654)"
FT /evidence="ECO:0000305"
FT CONFLICT 1858
FT /note="R -> K (in Ref. 3; AAA41654)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1935 AA; 223083 MW; C8376C324A7BD82B CRC64;
MADREMAAFG AGAPFLRKSE KERLEAQTRP FDLKKDVFVP DDKEEFVKAK IVSREGGKVT
AETENGKTVT VKEDQVMQQN PPKFDKIEDM AMLTFLHEPA VLYNLKERYA SWMIYTYSGL
FCVTVNPYKW LPVYNAQVVA AYRGKKRSEA PPHIFSISDN AYQYMLTDRE NQSILITGES
GAGKTVNTKR VIQYFAVIAA IGDRSKKDQT PGKGTLEDQI IQANPALEAF GNAKTVRNDN
SSRFGKFIRI HFGATGKLAS ADIETYLLEK SRVIFQLKAE RDYHIFYQIL SNKKPELLDM
LLITNNPYDY AFFSQGETTV ASIDDSEEHM ATDSAFDVLG FTPEEKNSIY KLTGAIMHFG
NMKFKQKQRE EQAEPDGTEE ADKSAYLMGL NSADLLKGLC HPRVKVGNEY VTKGQNVQQV
AYAIGALAKS VYEKMFNWMV TRINATLETK QPRQYFIGVL DIAGFEIFDF NSFEQLCINF
TNEKLQQFFN HHMFVLEQEE YKKEGIEWTF IDFGMDLQAC IDLIEKPMGI MSILEEECMF
PKATDMTFKA KLYDNHLGKS NNFQKPRNIK GKQEAHFSLI HYAGTVDYNI LGWLQKNKDP
LNETVVGLYQ KSSLKLLSNL FANYAGADAP VDKGKGKAKK GSSFQTVSAL HRENLNKLMT
NLRSTHPHFV RCIIPNETKS PGVMDNPLVM HQLRCNGVLE GIRICRKGFP NRILYGDFRQ
RYRILNPAAI PEGQFIDSRK GAEKLLGSLD IDHNQYKFGH TKVFFKAGLL GLLEEMRDER
LSRIITRIQA QSRGVLSRME FKKLLERRDS LLIIQWNIRA FMGVKNWPWM KLYFKIKPLL
KSAETEKEMA NMKEEFGRVK DALEKSEARR KELEEKMVSL LQEKNDLQLQ VQAEQDNLAD
AEERCDQLIK NKIQLEAKVK EMTERLEDEE EMNAELTAKK RKLEDECSEL KRDIDDLELT
LAKVEKEKHA TENKVKNLTE EMAGLDEIIV KLTKEKKALQ EAHQQALDDL QAEEDKVNTL
TKAKVKLEQQ VDDLEGSLDQ DKKVRMDLER AKRKLEGDLK LTQESIMDLE NDKQQLDERL
KKKDFELNAL NARIEDEQAL GSQLQKKLKE LQARIEELEE ELEAERTARA KVEKLRSDLS
RELEEISERL EEAGGATSVQ IEMNKKREAE FQKMRRDLEE ATLQHEATAA ALRKKHADSV
AELGEQIDNL QRVKQKLEKE KSEFKLELDD VTSNMEQIIK AKANLEKMCR TLEDQMNEHR
SKAEETQRSV NDLTRQRAKL QTENGELSRQ LDEKEALISQ LTRGKLTYTQ QLEDLKRQLE
EEVKAKNALA HALQSARHDC DLLREQYEEE TEAKAELQRV LSKANSEVAQ WRTKYETDAI
QRTEELEEAK KKLAQRLQDA EEAVEAVNAK CSSLEKTKHR LQNEIEDLMV DVERSNAAAA
ALDKKQRNFD KILVEWKQKY EESQSELESS QKEARSLSTE LFKLKNAYEE SLEHLETFKR
ENKNLQEEIS DLTEQLGSTG KSIHELEKIR KQLEAEKLEL QSALEEAEAS LEHEEGKILR
AQLEFNQIKA EIERKLAEKD EEMEQAKRNH LRVVDSLQTS LDAETRSRNE ALRVKKKMEG
DLNEMEIQLS HANRMAAEAQ KQVKSLQSLL KDTQIQLDDA VRANDDLKEN IAIVERRNNL
LQAELEELRA VVEQTERSRK LAEQELIETS ERVQLLHSQN TSLINQKKKM DADLSQLQTE
VEEAVQECRN AEEKAKKAIT DAAMMAEELK KEQDTSAHLE RMKNNMEQTI KDLQHRLDEA
EQIALKGGKK QLQKLEARVR ELENELEAEQ KRNAESVKGM RKSERRIKEL TYQTEEDRKN
LLRLQDLVDK LQLKVKAYKR QAEEAEEQAN TNLSKFRKVQ HELDEAEERA DIAESQVNKL
RAKSRDIGAK GLNEE
