MYH7_CANLF
ID MYH7_CANLF Reviewed; 1935 AA.
AC P49824; Q076A2;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 3.
DT 03-AUG-2022, entry version 131.
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 Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Maccatrozzo L., Patruno M., Mascarello F., Reggiani C.;
RT "Canine myosin heavy chain expression.";
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PROTEIN SEQUENCE OF 1561-1573.
RC TISSUE=Heart;
RX PubMed=9504812; DOI=10.1002/elps.1150181514;
RA Dunn M.J., Corbett J.M., Wheeler C.H.;
RT "HSC-2DPAGE and the two-dimensional gel electrophoresis database of dog
RT heart proteins.";
RL Electrophoresis 18:2795-2802(1997).
RN [3]
RP PROTEIN SEQUENCE OF 1718-1726.
RC TISSUE=Heart;
RA Wheeler C.H., Dunn M.J.;
RL Submitted (JUL-1997) to UniProtKB.
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; DQ227285; ABB96412.1; -; Genomic_DNA.
DR RefSeq; NP_001107183.1; NM_001113711.1.
DR AlphaFoldDB; P49824; -.
DR SMR; P49824; -.
DR UCD-2DPAGE; P49824; -.
DR PaxDb; P49824; -.
DR ABCD; P49824; 1 sequenced antibody.
DR Ensembl; ENSCAFT00040004918; ENSCAFP00040004222; ENSCAFG00040002574.
DR Ensembl; ENSCAFT00845007051; ENSCAFP00845005623; ENSCAFG00845003780.
DR GeneID; 403807; -.
DR KEGG; cfa:403807; -.
DR CTD; 4625; -.
DR VEuPathDB; HostDB:ENSCAFG00845003780; -.
DR eggNOG; KOG0161; Eukaryota.
DR GeneTree; ENSGT00940000159432; -.
DR InParanoid; P49824; -.
DR OrthoDB; 47111at2759; -.
DR Proteomes; UP000002254; Chromosome 8.
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:0001725; C:stress fiber; IEA:Ensembl.
DR GO; GO:0030018; C:Z disc; IEA:Ensembl.
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:0046034; P:ATP metabolic process; IEA:Ensembl.
DR GO; GO:0060048; P:cardiac muscle contraction; IBA:GO_Central.
DR GO; GO:0014898; P:cardiac muscle hypertrophy in response to stress; IEA:Ensembl.
DR GO; GO:0030049; P:muscle filament sliding; IBA:GO_Central.
DR GO; GO:0002027; P:regulation of heart rate; IEA:Ensembl.
DR GO; GO:0031449; P:regulation of slow-twitch skeletal muscle fiber contraction; IEA:Ensembl.
DR GO; GO:0002026; P:regulation of the force of heart contraction; IEA:Ensembl.
DR GO; GO:0014728; P:regulation of the force of skeletal muscle contraction; IEA:Ensembl.
DR GO; GO:0045214; P:sarcomere organization; IBA:GO_Central.
DR GO; GO:0003009; P:skeletal muscle contraction; IEA:Ensembl.
DR GO; GO:0014883; P:transition between fast and slow fiber; IEA:Ensembl.
DR GO; GO:0055010; P:ventricular cardiac muscle tissue morphogenesis; IEA:Ensembl.
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 Direct protein sequencing; Methylation; Motor protein; Muscle protein;
KW Myosin; Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Thick filament.
FT CHAIN 1..1935
FT /note="Myosin-7"
FT /id="PRO_0000123406"
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 1915..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"
SQ SEQUENCE 1935 AA; 222976 MW; B3723D069A67C910 CRC64;
MVDAEMAAFG AAAPFLRKSE KERLEAQTRP FDLKKDVFVP DDKEEFVKAK IVSREGGKVT
AETENGKTVT VKEDQVMQQN PPKFDKIEDM AMLTFLHEPA VLYNLKERYA SWMIYTYSGL
FCVTVNPYKW LPVYNAEVVA AYRGKKRSEA PPHIFSISDN AYQYMLTDRE NQSILITGES
GAGKTVNTKR VIQYFAVIAA IGDRSKKDQT PGKGTLEDQI IQANPALEAF GNAKTVRNDN
SSRFGKFIRI HFGATGKLAS ADIETYLLEK SRVIFQLKAE RDYHIFYQIL SNKKPELLDM
LLITNNPYDY AFISQGETTV ASIDDSEELM ATDNAFDVLG FTSEEKNSMY KLTGAIMHFG
NMKFKQKQRE EQAEPDGTEE ADKSAYLMGL NSADLLKGLC HPRVKVGNEY VTKGQNVQQV
AYATGALAKA VYEKMFNWMV TRINATLETK QPRQYFIGVL DIAGFEIFDF NSFEQLCINF
TNEKLQQFFN HHMFVLEQEE YKKEGIEWEF IDFGMDLQAC IDLIEKPMGI MSILEEECMF
PKATDMTFKA KLYDNHLGKS NNFQKPRNIK GKQEAHFSLI HYAGTVDYNI LGWLQKNKDP
LNETVVALYQ KSSLKLLSNL FANYAGADAP VEKGKGKAKK GSSFQTVSAL HRENLNKLMT
NLRSTHPHFV RCIIPNETKS PGVIDNPLVM HQLRCNGVLE GIRICRKGFP NRILYGDFRQ
RYRILNPAAI PEGQFIDSRK GAEKLLSSLD IDHNQYKFGH TKVFFKAGLL GLLEEMRDER
LSRIITRIQA QSRGVLSRME YKKLLERRDS LLIIQWNIRA FMGVKNWPWM KLYFKIKPLL
KSAETEKEMA TMKEEFARIK EALEKSEARR KELEEKMVSL LQEKNDLQLQ VQAEQDNLAD
AEERCDQLIK NKIQLEAKVK EMTERLEDEE EMNAELTAKK RKLEDECSEL KRDIDDLELT
LAKVEKEKHA TENKVKNLTE EMAGLDEIIA KLTKEKKALQ EAHQQALDDL QAEEDKVNTL
TKAKVKLEQQ VDDLEGSLEQ EKKVRMDLER AKRKLEGDLK LTQESIMDLE NDKQQLDERL
KKKDFELNAL NARIEDEQAL GSQLQKKLKE LQARIEELEE ELEAERTARA KVEKLRSDLS
RELEEISERL EEAGGATSVQ IEMNKKREAE FQKMRRDLEE ATLQHEATAA ALRKKHADSV
AELGEQIDNL 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 LEHEEGKILR
AQLEFNQIKA EIERKLAEKD EEMEQAKRNH LRVVDSLQTS LDAETRSRNE ALRVKKKMEG
DLNEMEIQLS HANRMAAEAQ KQVKGLQSLL KDTQIQLDDA VRANDDLKEN IAIVERRNNL
LQAELEELRA VVEQTERSRK LAEQELIETS ERVQLLHSQN TSLINQKKKM DADLSQLQTE
VEEAVQECRN AEEKAKKAIT DAAMMAEELK KEQDTSAHLE RMKKNMEQTI KDLQHRLDEA
EQIALKGGKK QLQKLEARVR ELENELEAEQ KRNAESVKGM RKSERRIKEL TYQTEEDRKN
LLRLQDLVDK LQLKVKAYKR QAEEAEEQAN TNLSKFRKVQ HELDEAEERA DIAESQVNKL
RAKSRDIGAK GLNEE
