MYH7_MESAU
ID MYH7_MESAU Reviewed; 1934 AA.
AC P13540; Q60540;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 2.
DT 03-AUG-2022, entry version 130.
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 Mesocricetus auratus (Golden hamster).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Mesocricetus.
OX NCBI_TaxID=10036;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=F1B; TISSUE=Liver;
RX PubMed=7815459; DOI=10.1006/jmcc.1994.1134;
RA Wang R., Sole M.J., Cukerman E., Liew C.-C.;
RT "Characterization and nucleotide sequence of the cardiac alpha-myosin heavy
RT chain gene from Syrian hamster.";
RL J. Mol. Cell. Cardiol. 26:1155-1165(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 961-1934.
RX PubMed=3380703; DOI=10.1093/nar/16.10.4737;
RA Jandreski M.A., Sole M.J., Liew C.-C.;
RT "Sequence of cDNA encoding the Syrian hamster cardiac beta-myosin heavy
RT chain.";
RL Nucleic Acids Res. 16:4737-4737(1988).
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-1187, Skip2: Glu-1384, Skip3: Glu-1581 and Skip4: Gly-1806)
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; L12104; AAA62313.1; -; Genomic_DNA.
DR EMBL; X07273; CAA30256.1; -; mRNA.
DR PIR; I48153; I48153.
DR AlphaFoldDB; P13540; -.
DR SMR; P13540; -.
DR STRING; 10036.XP_005139305.1; -.
DR PRIDE; P13540; -.
DR eggNOG; KOG0161; Eukaryota.
DR Proteomes; UP000189706; Unplaced.
DR GO; GO:0030016; C:myofibril; ISS:UniProtKB.
DR GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
DR GO; GO:0032982; C:myosin filament; ISS:UniProtKB.
DR GO; GO:0030017; C:sarcomere; ISS:UniProtKB.
DR GO; GO:0051015; F:actin filament binding; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0003774; F:cytoskeletal motor activity; IEA:InterPro.
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 2: Evidence at transcript 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..1934
FT /note="Myosin-7"
FT /id="PRO_0000123408"
FT DOMAIN 31..80
FT /note="Myosin N-terminal SH3-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01190"
FT DOMAIN 84..777
FT /note="Myosin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT DOMAIN 780..809
FT /note="IQ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT REGION 654..676
FT /note="Actin-binding"
FT REGION 756..770
FT /note="Actin-binding"
FT REGION 1914..1934
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 839..1934
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 377
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P02563"
FT MOD_RES 1136
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02563"
FT MOD_RES 1268
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q02566"
FT MOD_RES 1281
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P02563"
FT MOD_RES 1307
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P02563"
FT MOD_RES 1308
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P02563"
FT MOD_RES 1509
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02564"
FT MOD_RES 1512
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P02563"
FT CONFLICT 966
FT /note="D -> E (in Ref. 2; CAA30256)"
FT /evidence="ECO:0000305"
FT CONFLICT 978
FT /note="T -> TE (in Ref. 2; CAA30256)"
FT /evidence="ECO:0000305"
FT CONFLICT 986
FT /note="E -> Q (in Ref. 2; CAA30256)"
FT /evidence="ECO:0000305"
FT CONFLICT 1008..1014
FT /note="DLQAEED -> ALEARKT (in Ref. 2; CAA30256)"
FT /evidence="ECO:0000305"
FT CONFLICT 1057
FT /note="D -> Y (in Ref. 2; CAA30256)"
FT /evidence="ECO:0000305"
FT CONFLICT 1060
FT /note="L -> V (in Ref. 2; CAA30256)"
FT /evidence="ECO:0000305"
FT CONFLICT 1095
FT /note="D -> N (in Ref. 2; CAA30256)"
FT /evidence="ECO:0000305"
FT CONFLICT 1217
FT /note="E -> D (in Ref. 2; CAA30256)"
FT /evidence="ECO:0000305"
FT CONFLICT 1271
FT /note="D -> N (in Ref. 2; CAA30256)"
FT /evidence="ECO:0000305"
FT CONFLICT 1327
FT /note="T -> A (in Ref. 2; CAA30256)"
FT /evidence="ECO:0000305"
FT CONFLICT 1358
FT /note="C -> R (in Ref. 2; CAA30256)"
FT /evidence="ECO:0000305"
FT CONFLICT 1504
FT /note="L -> V (in Ref. 2; CAA30256)"
FT /evidence="ECO:0000305"
FT CONFLICT 1537
FT /note="M -> L (in Ref. 2; CAA30256)"
FT /evidence="ECO:0000305"
FT CONFLICT 1556
FT /note="N -> K (in Ref. 2; CAA30256)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1934 AA; 222929 MW; FDBAC58310B0B57D CRC64;
MADREMAAFG AAAFLRKSEK ERLEAQTRPF DLKKDVFVPD DKEEFVKAKI VSREGGKVTA
ETENGKTVTV KEDQVMQQNP PKFDKIEDMA MLTFLHEPAV LYNLKDGYAS WMIYTYSGLF
CVTVNPYKWL PVYNAEVVAA YRGKKRSEAP AHIFSISDNA YQYMLTDREN QSILITGESG
AGKTVNTKRV IQYFAVIAAI GDRSKKDQTP GKGTLEDQII QANPALEAFG NAKTVRNDNS
SRFGKFIRIH FGATGKLASA DIETYLLEKS RVIFQLKAER DYHIFYQILS NKKPELLDML
LITNNPYDYA FIPQGETTVA SIDDSEELMA TDSAFDVLGF TSEEKNSIYK LTGAIMHFGN
MKFKQKQREE QADRDGTEEE DKSAYLMGLN SADLLKGMCH PRVKVGNEYV TKGQNVQQVS
YAIGALAKSV YEKMFNWMVT RINATLETKQ PRQYFIGVLD IAGFEIFDFN SFEQLCINFT
NEKLQQFFNH HMFVLEQEEY KKEGIEWTFI DFGMDLQACI DLIEKPMRIM SILEEECMFP
KATDMTFKAK LYDNHLGKSN NFQKPRNVKG KQEAHFSLVH YAGTVDYNIL GWLQKNKDPL
NETVVGLYQK SSLKLLSNLF ANYAGADAPV DKGKGKAKKG SSFQTVSVLH RENLNKLMTN
LRSTHPHFVR CIIPNETKSP GVMDNPLVMH QLRCNGVLEG IRICRKGFPN RILYGDFRQR
YRILNPAAIP EGQFIDSRKG AEKLLSSLDI DHNQYKFGHT KVFFKAGLLG LLEEMRDERL
SRIITRIQAQ SRGLLSRMEF KKLLERRDSL LVIQWNIRAF MGVKNWPWMK LYFKIKPLLK
SAETEKEMAT MKEEFGRVKD ALEKSEARRK ELEEKMVSLL QEKNDLQLQV QAEQDNLADA
EERCDQLIKN KIQLEAKVKE MTERLEDEEE MNAELTAKKR KLEDECSELK RDIDDLELTL
AKVEKDKHAT ENKVKNLTEE MAGLDEIIAK LTKEKKALQE AHQQALDDLQ AEEDKVNTLT
KSKVKLEQQV DDLEGSLEQE KKVRMDLERA KRKLEGDLKL TQESIMDLEN DKQQLDEKLK
KKDFELNALN ARIEDEQALG SQLQKKLKEL QARIEELEEE LEAERTARAK VEKLRSDLSR
ELEEISERLE EAGGATSVQI EMNKKREAEF QKMRRDLEEA TLQHEATAAA LRKKHADSVA
ELGEQIDNLQ RVKQKLEKEK SEFKLELDDV TSNMEQIIKA KANLEKMCRT LEDQMNEHRS
KAEETQRSVN DLTSQRAKLQ TENGELSRQL DEKEALISQL TRGKLTYTQQ LEDLKRQLEE
EVKAKNTLAH ALQSARHDCD LLREQYEEET EAKAELQCVL SKANSEVAQW RTKYETDAIQ
RTEELEEAKK KLAQRLQDAE EAVEAVNAKC SSLEKTKHRL QNEIEDLMVD VERSNAAAAA
LDKKQRNFDK ILAEWKQKYE ESQSELESSQ KEARSLSTEL FKLKNAYEES LEHLETFKRE
NKNLQEEISD LTEQLGSTGK SIHELEKIRK QLEAEKMELQ SALEEAEASL EHEEGNILRA
QLEFNQIKAE IERKLAEKDE EMEQAKRNHL RVVDSLQTSL DAETRSRNEA LRVKKKMEGD
LNEMEIQLSH ANRMAAEAQK QVKSLQSLLK DTQIQLDDAV RANDDLKENI AIVERRNNLL
QAELEELRAV VEQTERSRKL AEQELIETSE RVQLLHSQNT SLINQKKKMD ADLSQLQTEV
EEAVQECRNA EEKAKKAITD AAMMAEELKK EQDTSAHLER MKKNMEQTIK DLQHRLDEAE
QIALKGGKKQ LQKLEARVRE LENELEAEQK RNAESVKGMR KSERRIKELT YQTEEDRKNL
LRLQDLVDKL QLKVKAYKRQ AEEAEEQANT NLSKFRKVQH ELDEAEERAD IAESQVNKLR
AKSRDIGAKG LNEE
