MYH7_BOVIN
ID MYH7_BOVIN Reviewed; 1935 AA.
AC Q9BE39;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 121.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Holstein; TISSUE=Skeletal muscle;
RX AGRICOLA=IND43619651; DOI=10.1016/j.meatsci.2003.09.011;
RA Chikuni K., Muroya S., Nakajima I.;
RT "Myosin heavy chain isoforms expressed in bovine skeletal muscles.";
RL Meat Sci. 67:87-94(2004).
RN [2]
RP PROTEIN SEQUENCE OF 745-757, AND LACK OF METHYLATION AT HIS-753.
RC TISSUE=Heart;
RX PubMed=5058224; DOI=10.1016/s0021-9258(19)45670-6;
RA Huszar G., Elzinga M.;
RT "Homologous methylated and nonmethylated histidine peptides in skeletal and
RT cardiac myosins.";
RL J. Biol. Chem. 247:745-753(1972).
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:0000250|UniProtKB:P12883}.
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:0000250|UniProtKB:P02564}. Cytoplasm, myofibril, sarcomere
CC {ECO:0000250|UniProtKB:P02564}. Note=Thick filaments of the myofibrils.
CC {ECO:0000250|UniProtKB:P02564}.
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 -!- 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 {ECO:0000250|UniProtKB:P12883}.
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; AB059400; BAB40922.1; -; mRNA.
DR RefSeq; NP_777152.1; NM_174727.1.
DR PDB; 5N69; X-ray; 2.45 A; A/B=1-828.
DR PDB; 5N6A; X-ray; 3.10 A; A=1-828.
DR PDB; 6FSA; X-ray; 2.33 A; A/B=1-1935.
DR PDB; 6X5Z; EM; 4.24 A; D/G/J=1-850.
DR PDBsum; 5N69; -.
DR PDBsum; 5N6A; -.
DR PDBsum; 6FSA; -.
DR PDBsum; 6X5Z; -.
DR AlphaFoldDB; Q9BE39; -.
DR SASBDB; Q9BE39; -.
DR SMR; Q9BE39; -.
DR STRING; 9913.ENSBTAP00000053217; -.
DR PaxDb; Q9BE39; -.
DR PRIDE; Q9BE39; -.
DR ABCD; Q9BE39; 1 sequenced antibody.
DR GeneID; 282714; -.
DR KEGG; bta:282714; -.
DR CTD; 4625; -.
DR eggNOG; KOG0161; Eukaryota.
DR InParanoid; Q9BE39; -.
DR OrthoDB; 47111at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0030016; C:myofibril; ISS:UniProtKB.
DR GO; GO:0032982; C:myosin filament; ISS:UniProtKB.
DR GO; GO:0016460; C:myosin II complex; IBA:GO_Central.
DR GO; GO:0030017; C:sarcomere; ISS:UniProtKB.
DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0000146; F:microfilament motor activity; IBA:GO_Central.
DR GO; GO:0007512; P:adult heart development; IBA:GO_Central.
DR GO; GO:0060048; P:cardiac muscle contraction; IBA:GO_Central.
DR GO; GO:0030049; P:muscle filament sliding; IBA:GO_Central.
DR GO; GO:0045214; P:sarcomere organization; IBA:GO_Central.
DR DisProt; DP02522; -.
DR Gene3D; 1.20.5.370; -; 5.
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 3D-structure; Actin-binding; ATP-binding; Calmodulin-binding; Coiled coil;
KW Cytoplasm; Direct protein sequencing; Methylation; Motor protein;
KW Muscle protein; Myosin; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Thick filament.
FT CHAIN 1..1935
FT /note="Myosin-7"
FT /id="PRO_0000274175"
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 /evidence="ECO:0000250"
FT REGION 757..771
FT /note="Actin-binding"
FT /evidence="ECO:0000250"
FT REGION 1907..1935
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 839..1935
FT /evidence="ECO:0000255"
FT BINDING 178..185
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
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:0000250|UniProtKB:P02564"
FT MOD_RES 1513
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P02563"
FT CONFLICT 754..755
FT /note="NQ -> QN (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT HELIX 4..15
FT /evidence="ECO:0007829|PDB:6FSA"
FT HELIX 20..27
FT /evidence="ECO:0007829|PDB:6FSA"
FT TURN 33..35
FT /evidence="ECO:0007829|PDB:6FSA"
FT STRAND 36..41
FT /evidence="ECO:0007829|PDB:6FSA"
FT TURN 42..44
FT /evidence="ECO:0007829|PDB:6FSA"
FT STRAND 45..53
FT /evidence="ECO:0007829|PDB:6FSA"
FT STRAND 56..63
FT /evidence="ECO:0007829|PDB:6FSA"
FT HELIX 64..66
FT /evidence="ECO:0007829|PDB:6FSA"
FT STRAND 68..72
FT /evidence="ECO:0007829|PDB:6FSA"
FT HELIX 73..75
FT /evidence="ECO:0007829|PDB:6FSA"
FT HELIX 82..84
FT /evidence="ECO:0007829|PDB:6FSA"
FT HELIX 90..92
FT /evidence="ECO:0007829|PDB:6FSA"
FT HELIX 98..110
FT /evidence="ECO:0007829|PDB:6FSA"
FT STRAND 115..118
FT /evidence="ECO:0007829|PDB:6FSA"
FT STRAND 121..125
FT /evidence="ECO:0007829|PDB:6FSA"
FT HELIX 136..142
FT /evidence="ECO:0007829|PDB:6FSA"
FT HELIX 147..149
FT /evidence="ECO:0007829|PDB:6FSA"
FT HELIX 154..168
FT /evidence="ECO:0007829|PDB:6FSA"
FT STRAND 171..178
FT /evidence="ECO:0007829|PDB:6FSA"
FT HELIX 184..198
FT /evidence="ECO:0007829|PDB:6FSA"
FT HELIX 216..231
FT /evidence="ECO:0007829|PDB:6FSA"
FT STRAND 244..252
FT /evidence="ECO:0007829|PDB:6FSA"
FT HELIX 254..256
FT /evidence="ECO:0007829|PDB:6FSA"
FT STRAND 257..266
FT /evidence="ECO:0007829|PDB:6FSA"
FT HELIX 270..273
FT /evidence="ECO:0007829|PDB:6FSA"
FT HELIX 285..290
FT /evidence="ECO:0007829|PDB:6FSA"
FT HELIX 296..301
FT /evidence="ECO:0007829|PDB:6FSA"
FT HELIX 307..309
FT /evidence="ECO:0007829|PDB:6FSA"
FT TURN 311..313
FT /evidence="ECO:0007829|PDB:6FSA"
FT HELIX 325..338
FT /evidence="ECO:0007829|PDB:6FSA"
FT HELIX 343..359
FT /evidence="ECO:0007829|PDB:6FSA"
FT STRAND 364..366
FT /evidence="ECO:0007829|PDB:6FSA"
FT STRAND 368..371
FT /evidence="ECO:0007829|PDB:5N69"
FT STRAND 373..376
FT /evidence="ECO:0007829|PDB:6FSA"
FT HELIX 379..388
FT /evidence="ECO:0007829|PDB:6FSA"
FT HELIX 392..400
FT /evidence="ECO:0007829|PDB:6FSA"
FT STRAND 403..406
FT /evidence="ECO:0007829|PDB:5N6A"
FT STRAND 407..410
FT /evidence="ECO:0007829|PDB:5N69"
FT HELIX 417..446
FT /evidence="ECO:0007829|PDB:6FSA"
FT STRAND 455..461
FT /evidence="ECO:0007829|PDB:6FSA"
FT STRAND 469..471
FT /evidence="ECO:0007829|PDB:6FSA"
FT HELIX 473..504
FT /evidence="ECO:0007829|PDB:6FSA"
FT HELIX 515..525
FT /evidence="ECO:0007829|PDB:6FSA"
FT HELIX 530..538
FT /evidence="ECO:0007829|PDB:6FSA"
FT HELIX 545..556
FT /evidence="ECO:0007829|PDB:6FSA"
FT TURN 557..559
FT /evidence="ECO:0007829|PDB:6FSA"
FT STRAND 576..581
FT /evidence="ECO:0007829|PDB:6FSA"
FT STRAND 584..588
FT /evidence="ECO:0007829|PDB:6FSA"
FT HELIX 593..598
FT /evidence="ECO:0007829|PDB:6FSA"
FT HELIX 603..610
FT /evidence="ECO:0007829|PDB:6FSA"
FT HELIX 615..621
FT /evidence="ECO:0007829|PDB:6FSA"
FT HELIX 647..662
FT /evidence="ECO:0007829|PDB:6FSA"
FT STRAND 665..673
FT /evidence="ECO:0007829|PDB:6FSA"
FT HELIX 686..695
FT /evidence="ECO:0007829|PDB:6FSA"
FT HELIX 698..705
FT /evidence="ECO:0007829|PDB:6FSA"
FT STRAND 706..708
FT /evidence="ECO:0007829|PDB:5N6A"
FT STRAND 711..714
FT /evidence="ECO:0007829|PDB:6FSA"
FT HELIX 715..722
FT /evidence="ECO:0007829|PDB:6FSA"
FT HELIX 723..725
FT /evidence="ECO:0007829|PDB:6FSA"
FT TURN 727..729
FT /evidence="ECO:0007829|PDB:6FSA"
FT HELIX 738..748
FT /evidence="ECO:0007829|PDB:6FSA"
FT STRAND 749..751
FT /evidence="ECO:0007829|PDB:6FSA"
FT STRAND 755..758
FT /evidence="ECO:0007829|PDB:6FSA"
FT STRAND 760..765
FT /evidence="ECO:0007829|PDB:6FSA"
FT HELIX 769..799
FT /evidence="ECO:0007829|PDB:6FSA"
FT HELIX 802..805
FT /evidence="ECO:0007829|PDB:6FSA"
SQ SEQUENCE 1935 AA; 223229 MW; DEA05200BCF42557 CRC64;
MVDAEMAAFG EAAPYLRKSE KERLEAQTRP FDLKKDVFVP DDKEEFVKAT ILSREGGKVT
AETEHGKTVT VKEDQVLQQN PPKFDKIEDM AMLTFLHEPA VLYNLKERYA SWMIYTYSGL
FCVTINPYKW LPVYNAEVVA AYRGKKRSEA PPHIFSISDN AYQYMLTDRE NQSILITGES
GAGKTVNTKR VIQYFAVIAA IGDRSKKEQA TGKGTLEDQI IQANPALEAF GNAKTVRNDN
SSRFGKFIRI HFGATGKLAS ADIETYLLEK SRVIFQLKAE RDYHIFYQIL SNKKPELLDM
LLITNNPYDY AFISQGETTV ASIDDAEELM ATDNAFDVLG FTTEEKNSMY KLTGAIMHFG
NMKFKLKQRE EQAEPDGTEE ADKSAYLMGL NSADLLKGLC HPRVKVGNEY VTKGQNVQQV
VYAKGALAKA VYERMFNWMV TRINATLETK QPRQYFIGVL DIAGFEIFDF NSFEQLCINF
TNEKLQQFFN HHMFVLEQEE YKKEGIEWEF IDFGMDLQAC IDLIEKPMGI MSILEEECMF
PKATDMTFKA KLFDNHLGKS SNFQKPRNIK GKPEAHFSLI HYAGTVDYNI IGWLQKNKDP
LNETVVDLYK KSSLKMLSSL FANYAGFDTP IEKGKGKAKK GSSFQTVSAL HRENLNKLMT
NLRSTHPHFV RCIIPNETKS PGVIDNPLVM HQLRCNGVLE GIRICRKGFP NRILYGDFRQ
RYRILNPAAI PEGQFIDSRK GAEKLLGSLD IDHNQYKFGH TKVFFKAGLL GLLEEMRDER
LSRIITRIQA QSRGVLSRME FKKLLERRDS LLIIQWNIRA FMGVKNWPWM KLYFKIKPLL
KSAETEKEIA LMKEEFGRLK EALEKSEARR KELEEKMVSL LQEKNDLQLQ VQAEQDNLAD
AEERCDQLIK NKIQLEAKVK EMTERLEDEE EMNAELTAKK RKLEDECSEL KRDIDDLELT
LAKVEKEKHA TENKVKNLTE EMAGLDEIIA KLTKEKKALQ EAHQQALDDL QAEEDKVNTL
TKAKVKLEQH VDDLEGSLEQ EKKVRMDLER AKRKLEGDLK LTQESIMDLE NDKQQLDERL
KKKDFELNAL NARIEDEQAL GSQLQKKLKE LQARIEELEE ELEAERTARA KVEKLRSDLS
RELEEISERL EEAGGATSVQ IEMNKKREAE FQKMRRDLEE ATLQHEATAA ALRKKHADSV
AELSEQIDNL QRVKQKLEKE KSEFKLELDD VTSNMEQIIK AKANLEKMCR TLEDQMNEHR
SKAEETQRSV NDLTSQRAKL QTENGELSRQ LDEKEALISQ LTRGKLTYTQ QLEDLKRQLE
EEVKAKNALA HALQSARHDC DLLREQYEEE TEAKAELQRV LSKANSEVAQ WRTKYETDAI
QRTEELEEAK KKLAQRLQDA EEAVEAVNAK CSSLEKTKHR LQNEIEDLMV DVERSNAAAA
ALDKKQRNFD KILAEWKQKY EESQSELESS QKEARSLSTE LFKLKNAYEE SLEHLETFKR
ENKNLQEEIS DLTEQLGSSG KTIHELEKVR KQLEAEKLEL QSALEEAEAS LEQEEGKILR
AQLEFNQIKA EMERKLAEKD EEMEQAKRNH LRVVDSLQTS LDAETRSRNE ALRVKKKMEG
DLNEMEIQLS HANRLAAEAQ KQVKSLQSLL KDTQIQLDDA VRANDDLKEN IAIVERRNNL
LQAELEELRA VVEQTERSRK LAEQELIETS ERVQLLHSQN TSLINQKKKM EADLSQLQTE
VEEAVQECRN AEEKAKKAIT DAAMMAEELK KEQDTSAHLE RMKKNMEQTI KDLQHRLDEA
EQIALKGGKK QLQKLEARVR ELENELEAEQ KRNAESVKGM RKSERRIKEL TYQTEEDRKN
LLRLQDLVDK LQLKVKAYKR QAEEAEEQAN TNLSKFRKVQ HELDEAEERA DIAESQVNKL
RAKSRDIGTK GLNEE
