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MYH7_HORSE
ID   MYH7_HORSE              Reviewed;        1935 AA.
AC   Q8MJU9;
DT   06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   03-AUG-2022, entry version 101.
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   Equus caballus (Horse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus.
OX   NCBI_TaxID=9796;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Thoroughbred; TISSUE=Skeletal muscle;
RA   Chikuni K., Nakajima I., Muroya S.;
RT   "Sequencing of the horse myosin heavy chain isoforms.";
RL   Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases.
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; AB088367; BAC05681.1; -; mRNA.
DR   RefSeq; NP_001075227.1; NM_001081758.1.
DR   AlphaFoldDB; Q8MJU9; -.
DR   SMR; Q8MJU9; -.
DR   PaxDb; Q8MJU9; -.
DR   PRIDE; Q8MJU9; -.
DR   GeneID; 791234; -.
DR   KEGG; ecb:791234; -.
DR   CTD; 4625; -.
DR   InParanoid; Q8MJU9; -.
DR   OrthoDB; 47111at2759; -.
DR   Proteomes; UP000002281; 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; -; 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; SM00015; IQ; 1.
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..1935
FT                   /note="Myosin-7"
FT                   /id="PRO_0000274176"
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"
SQ   SEQUENCE   1935 AA;  223162 MW;  26ED2993C06D7A5A CRC64;
     MGDAELAVFG SAAPYLRKTE KERLEDQTRP FDLKKDVFVP DDKEEFVKAK IISREGGKIT
     AETEHGKTVT VKEDQVLQQN PPKFDKIEDM AMLTFLHEPA VLYNLKDRYA AWMIYTYSGL
     FCVTINPYKW LPVYTAEVVA AYRGKKRSEA PPHIFSISDN AYQYMLTDRE NQSILITGES
     GAGKTVNTKR VIQYFAVIAA IGDRSKKDQT SGKGTLEDQI IEANPALEAF GNAKTVRNDN
     SSRFGKFIRI HFGATGKLAS ADIETYLLEK SRVIFQLKAE RDYHIFYQIL SNKKPELLDM
     LLITNNPYDY AFISQGETTV ASIDDAEELM ATDNAFDVLG FTSEEKNSMY KLTGAIMHFG
     NMKFKQKQRE EQAEPDGTEE ADKSAYLMGL NSADLLKGLC HPRVKVGNEY VTKGQNVQQV
     AYAKGALAKA VYERMFNWMV ARINATLETK QPRQYFIGVL DIAGFEIFDF NSFEQLCINF
     TNEKLQQFFN HHMFVLEQEE YKKEGIEWEF IDFGMDLQAC IDLIEKPMGI MSILEEECMF
     PKATDMTFKA KLFDNHLGKS SNFQKPRNIK GKPEAHFSLI HYAGTVDYNI LGWLQKNKDP
     LNETVVDLYK KSSLKMLSNL FANYLGADAP IEKGKGKAKK GSSFQTVSAL HRENLNKLMT
     NLRSTHPHFV RCIIPNETKS PGVIDNPLVM HQLRCNGVLE GIRICRKGFP NRILYGDFRQ
     RYRILNPAAI PEGQFIDSRK GAEKLLSSLD IDHNQYRFGH TKVFFKAGLL GLLEEMRDER
     LSRIITRIQA QSRGVLARME FKKLLERRDS LLIIQWNIRA FMGVKNWPWM KLYFKIKPLL
     KSAETEKEMA TMKEEFARLK 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 FQKMKRDLEE 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 KQVKSLQSLL KDTQIQLDDA VRANDDLKEN IAIVERRNNL
     LQAELEELRA VVEQTERSRK LAEQELIETS ERVQLLHSQN TSLINQKKKM DADLSQLQTE
     VEEAVQECRD AEEKAKKAIT DAAMMAEELK KEQDTSAHLE RMKKNMEQTI KDLQHRLDEA
     EQIALKGGKK QLQKLEARVR ELENELEVEQ KRNAESIKGM RKSERRIKEL TYQTEEDRKN
     LLRLQDLVDK LQLKVKAYKR QAEEAEEQAN TNLSKFRKVQ HELDEAEERA DIAESQVNKL
     RAKSRDIGTK GLNEE
 
 
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