ID MYH7_PIG Reviewed; 1935 AA.
AC P79293; Q9GKR1;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 2.
DT 24-JAN-2024, entry version 153.
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 Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Ko Y.-L.;
RL Submitted (OCT-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Landrace; TISSUE=Skeletal muscle;
RA Chikuni K., Muroya S., Tanabe R., Nakajima I.;
RT "Comparative sequence analysis of four myosin heavy chain isoforms
RT expressed in porcine skeletal muscles: sequencing and characterization of
RT the porcine myosin heavy chain slow isoform.";
RL Anim. Sci. J. 73:257-262(2002).
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; U75316; AAB37320.1; -; mRNA.
DR EMBL; AB053226; BAB20630.1; -; mRNA.
DR PIR; A59286; A59286.
DR RefSeq; NP_999020.1; NM_213855.1.
DR PDB; 7JH7; EM; 3.80 A; F/G/H=1-1935.
DR PDBsum; 7JH7; -.
DR AlphaFoldDB; P79293; -.
DR EMDB; EMD-22335; -.
DR SMR; P79293; -.
DR STRING; 9823.ENSSSCP00000070632; -.
DR BindingDB; P79293; -.
DR ChEMBL; CHEMBL4295792; -.
DR PaxDb; 9823-ENSSSCP00000002219; -.
DR PeptideAtlas; P79293; -.
DR ABCD; P79293; 1 sequenced antibody.
DR Ensembl; ENSSSCT00000002271.5; ENSSSCP00000002219.3; ENSSSCG00000053614.1.
DR Ensembl; ENSSSCT00060094134.1; ENSSSCP00060040726.1; ENSSSCG00060067314.1.
DR Ensembl; ENSSSCT00060094188.1; ENSSSCP00060040753.1; ENSSSCG00060067314.1.
DR Ensembl; ENSSSCT00060094233.1; ENSSSCP00060040767.1; ENSSSCG00060067314.1.
DR Ensembl; ENSSSCT00070002533.1; ENSSSCP00070002110.1; ENSSSCG00070000936.1.
DR GeneID; 396860; -.
DR KEGG; ssc:396860; -.
DR CTD; 4625; -.
DR eggNOG; KOG0161; Eukaryota.
DR GeneTree; ENSGT00940000159432; -.
DR HOGENOM; CLU_000192_8_1_1; -.
DR InParanoid; P79293; -.
DR OrthoDB; 2877572at2759; -.
DR Proteomes; UP000008227; Chromosome 7.
DR Proteomes; UP000314985; Chromosome 7.
DR Proteomes; UP000694570; Unplaced.
DR Proteomes; UP000694571; Unplaced.
DR Proteomes; UP000694720; Unplaced.
DR Proteomes; UP000694722; Unplaced.
DR Proteomes; UP000694723; Unplaced.
DR Proteomes; UP000694724; Unplaced.
DR Proteomes; UP000694725; Unplaced.
DR Proteomes; UP000694726; Unplaced.
DR Proteomes; UP000694727; Unplaced.
DR Proteomes; UP000694728; Unplaced.
DR Bgee; ENSSSCG00000002029; Expressed in heart left ventricle and 33 other cell types or tissues.
DR ExpressionAtlas; P79293; baseline and differential.
DR Genevisible; P79293; SS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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 CDD; cd01377; MYSc_class_II; 1.
DR Gene3D; 1.10.10.820; -; 1.
DR Gene3D; 1.20.5.340; -; 5.
DR Gene3D; 1.20.5.370; -; 4.
DR Gene3D; 1.20.5.4820; -; 1.
DR Gene3D; 1.20.58.530; -; 1.
DR Gene3D; 6.10.250.2420; -; 1.
DR Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR Gene3D; 2.30.30.360; Myosin S1 fragment, N-terminal; 1.
DR Gene3D; 1.20.120.720; Myosin VI head, motor domain, U50 subdomain; 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 PANTHER; PTHR45615; MYOSIN HEAVY CHAIN, NON-MUSCLE; 1.
DR PANTHER; PTHR45615:SF1; MYOSIN-7; 1.
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; SSF90257; Myosin rod fragments; 5.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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; Methylation; Motor protein; Muscle protein; Myosin;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Thick filament.
FT CHAIN 1..1935
FT /note="Myosin-7"
FT /id="PRO_0000123410"
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 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:0000255"
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 149
FT /note="E -> D (in Ref. 1; AAB37320)"
FT /evidence="ECO:0000305"
FT CONFLICT 841
FT /note="K -> E (in Ref. 1; AAB37320)"
FT /evidence="ECO:0000305"
FT CONFLICT 899..901
FT /note="ADA -> SDS (in Ref. 1; AAB37320)"
FT /evidence="ECO:0000305"
FT CONFLICT 942..943
FT /note="KL -> NV (in Ref. 1; AAB37320)"
FT /evidence="ECO:0000305"
FT CONFLICT 1035
FT /note="E -> A (in Ref. 1; AAB37320)"
FT /evidence="ECO:0000305"
FT CONFLICT 1339..1340
FT /note="DC -> AA (in Ref. 1; AAB37320)"
FT /evidence="ECO:0000305"
FT CONFLICT 1353
FT /note="A -> T (in Ref. 1; AAB37320)"
FT /evidence="ECO:0000305"
FT CONFLICT 1498
FT /note="F -> S (in Ref. 1; AAB37320)"
FT /evidence="ECO:0000305"
FT CONFLICT 1547
FT /note="A -> S (in Ref. 1; AAB37320)"
FT /evidence="ECO:0000305"
FT CONFLICT 1748
FT /note="C -> S (in Ref. 1; AAB37320)"
FT /evidence="ECO:0000305"
FT CONFLICT 1879
FT /note="K -> N (in Ref. 1; AAB37320)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1935 AA; 223298 MW; 270556D9A3E86C4A CRC64;
MVDAEMAAFG EAAPYLRKSE KERLEAQTRP FDLKKDVYVP DDKEEFVKAK ILSREGGKVT
AETEHGKTVT VKEDQVLQQN PPKFDKIEDM AMLTFLHEPA VLYNLKERYA SWMIYTYSGL
FCVTINPYKW LPVYNAEVVA AYRGKKRSEA PPHIFSISDN AYQYMLTDRE NQSILITGES
GAGKTVNTKR VIQYFAVIAA IGDRSKKEQT PGKGTLEDQI IQANPALEAF GNAKTVRNDN
SSRFGKFIRI HFGATGKLAS ADIETYLLEK SRVIFQLKAE RDYHIFYQIL SNKKPELLDM
LLITNNPYDY AFISQGETTV ASIDDAEELM ATDNAFDVLG FTSEEKNSMY KLTGAIMHFG
NMKFKLKQRE EQAEPDGTEE ADKSAYLMGL NSADLLKGLC HPRVKVGNEY VTKGQNVQQV
MYATGALAKA VYEKMFNWMV TRINTTLETK QPRQYFIGVL DIAGFEIFDF NSFEQLCINF
TNEKLQQFFN HHMFVLEQEE YKKEGIEWEF IDFGMDLQAC IDLIEKPMGI MSILEEECMF
PKATDMTFKA KLYDNHLGKS NNFQKPRNIK GRPEAHFALI HYAGTVDYNI IGWLQKNKDP
LNETVVDLYK KSSLKLLSNL FANYAGADTP VEKGKGKAKK GSSFQTVSAL HRENLNKLMT
NLRSTHPHFV RCIIPNETKS PGVIDNPLVM HQLRCNGVLE GIRICRKGFP NRILYGDFRQ
RYRILNPAAI PEGQFIDSRK GAEKLLGSLD IDHNQYKFGH TKVFFKAGLL GLLEEMRDER
LSRIITRIQA QSRGVLSRME FKKLLERRDS LLIIQWNIRA FMSVKNWPWM KLYFKIKPLL
KSAETEKEMA TMKEEFGRLK 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
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 EMERKLAEKD EEMEQAKRNH LRVVDSLQTS LDAETRSRNE ALRVKKKMEG
DLNEMEIQLS HANRMAAEAQ 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
//
