ID G1RYI6_NOMLE Unreviewed; 1899 AA.
AC G1RYI6;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 2.
DT 27-MAR-2024, entry version 69.
DE RecName: Full=Myosin-7 {ECO:0000256|ARBA:ARBA00039815};
DE AltName: Full=Myosin heavy chain 7 {ECO:0000256|ARBA:ARBA00041438};
DE AltName: Full=Myosin heavy chain slow isoform {ECO:0000256|ARBA:ARBA00043207};
DE AltName: Full=Myosin heavy chain, cardiac muscle beta isoform {ECO:0000256|ARBA:ARBA00041905};
GN Name=MYH7 {ECO:0000313|Ensembl:ENSNLEP00000018313.2};
OS Nomascus leucogenys (Northern white-cheeked gibbon) (Hylobates leucogenys).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hylobatidae;
OC Nomascus.
OX NCBI_TaxID=61853 {ECO:0000313|Ensembl:ENSNLEP00000018313.2, ECO:0000313|Proteomes:UP000001073};
RN [1] {ECO:0000313|Ensembl:ENSNLEP00000018313.2, ECO:0000313|Proteomes:UP000001073}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Gibbon Genome Sequencing Consortium;
RL Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSNLEP00000018313.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) 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:0000256|ARBA:ARBA00037090}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, myofibril, sarcomere
CC {ECO:0000256|ARBA:ARBA00004204}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Myosin family. {ECO:0000256|ARBA:ARBA00008314,
CC ECO:0000256|PROSITE-ProRule:PRU00782}.
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DR EMBL; ADFV01192144; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01192145; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01192146; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR STRING; 61853.ENSNLEP00000018313; -.
DR Ensembl; ENSNLET00000019224.2; ENSNLEP00000018313.2; ENSNLEG00000015043.2.
DR GeneTree; ENSGT00940000159432; -.
DR HOGENOM; CLU_000192_8_1_1; -.
DR InParanoid; G1RYI6; -.
DR OMA; DQLADNE; -.
DR Proteomes; UP000001073; Chromosome 22a.
DR GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
DR GO; GO:0032982; C:myosin filament; IEA:UniProtKB-KW.
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; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0000146; F:microfilament motor activity; IEA:Ensembl.
DR GO; GO:0007512; P:adult heart development; IEA:Ensembl.
DR GO; GO:0046034; P:ATP metabolic process; IEA:Ensembl.
DR GO; GO:0060048; P:cardiac muscle contraction; IEA:Ensembl.
DR GO; GO:0014898; P:cardiac muscle hypertrophy in response to stress; IEA:Ensembl.
DR GO; GO:0030049; P:muscle filament sliding; IEA:Ensembl.
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: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 CDD; cd14917; MYSc_Myh7; 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; 2.
DR PRINTS; PR00193; MYOSINHEAVY.
DR SMART; SM00015; IQ; 1.
DR SMART; SM00242; MYSc; 1.
DR SUPFAM; SSF90257; Myosin rod fragments; 4.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF57997; Tropomyosin; 1.
DR PROSITE; PS50096; IQ; 1.
DR PROSITE; PS51456; MYOSIN_MOTOR; 1.
DR PROSITE; PS51844; SH3_LIKE; 1.
PE 3: Inferred from homology;
KW Actin-binding {ECO:0000256|ARBA:ARBA00023203, ECO:0000256|PROSITE-
KW ProRule:PRU00782};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00782};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW Motor protein {ECO:0000256|ARBA:ARBA00023175, ECO:0000256|PROSITE-
KW ProRule:PRU00782}; Muscle protein {ECO:0000256|ARBA:ARBA00023179};
KW Myosin {ECO:0000256|ARBA:ARBA00023123, ECO:0000256|PROSITE-
KW ProRule:PRU00782};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00782}; Reference proteome {ECO:0000313|Proteomes:UP000001073};
KW Thick filament {ECO:0000256|ARBA:ARBA00022433}.
FT DOMAIN 32..81
FT /note="Myosin N-terminal SH3-like"
FT /evidence="ECO:0000259|PROSITE:PS51844"
FT DOMAIN 85..771
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT REGION 648..670
FT /note="Actin-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT REGION 1879..1899
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 835..1642
FT /evidence="ECO:0000256|SAM:Coils"
FT BINDING 171..178
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ SEQUENCE 1899 AA; 218397 MW; 71FF85EE246A62F3 CRC64;
MGDSEMAIFG EAAPYLRKSE KERLEAQTRP FDLKKDVFVP DDKQEFVKAK IMSREGGKVT
AETENGKTVT VKEDQVMQQN PPKFDKIEDM AMLTFLHEPA VLYNLKERYG SWMIYTYSGL
FCVTVNPYKW LPVYTPEVVA AYRGKKRSEA PPHIFSISDN AYQYMLTGES GESGAGKTVN
TKRVIQYFAV IAAIGDRSKK DQSPGKGTLE DQIIQANPAL EAFGNAKTVR NDNSSRFGKF
IRIHFGATGK LASADIETYL LEKSRVIFQL KAERDYHIFY QILSNKKPEL LDMLLITNNP
YDYAFISQGE TTVASIDDAE ELMATDNAFD VLGFTSEEKN SIYKLTGAIM HFGNMKFKLK
QREEQAEPDG TEEADKSAYL MGLNSADLLK GLCHPRVKVG NEYVTKGQNV QQVIYATGAL
AKAVYERMFN WMVTRINATL ETKQPRQYFI GVLDIAGFEI FDFNSFEQLC INFTNEKLQQ
FFNHHMFVLE QEEYKKEGIE WTFIDFGMDL QACIDLIEKP MGIMSILEEE CMFPKATDMT
FKAKLFDNHL GKSSNFQKPR NIKGKPEAHF SLIHYAGIVD YNIIGWLQKN KDPLNETVVG
LYQKSSLKLL SSLFANYAGA DAPVEKGKGK AKKGSSFQTV SALHRENLNK LMTNLRSTHP
HFVRCIIPNE TKSPGVMDNP LVMHQLRCNG VLEGIRICRK GFPNRILYGD FRQRYRILNP
AAIPEGQFID SRKGAEKLLG SLDIDHNQYK FGHTKVFFKA GLLGLLEEMR DERLSRIITR
IQAQSRGVLA RMEYKKLLER RDSLLVIQWN IRAFMGVKNW PWMKLYFKIK PLLKSAEREK
EMASMKEEFT RLKEALEKSE ARRKELEEKM VSLLQEKNDL QLQVQAEQDN LADAEERCDQ
LIKNKIQLEA KVKEMNERLE DEEEMNAELT AKKRKLEDEC SELKRDIDDL ELTLAKVEKE
KHATENKVKN LTEEMAGLDE IIAKLTKEKK ALQEAHQQAL DDLQAEEDKV NTLTKAKVKL
EQQVDDLEGS LEQEKKVRMD LERAKRKLEG DLKLTQESIM DLENDKQQLD ERLKKKDFEL
NALNARIEDE QALGSQLQKK LKELQARIEE LEEELEAERT ARAKVEKLRS DLSRELEEIS
ERLEEAGGAT SVQIEMNKKR EAEFQKMRRD LEEATLQHEA TAAALRKKHA DSVAELGEQI
DNLQRVKQKL EKEKSEFKLE LDDVTSNMEQ IIKAKANLEK MCRTLEDQMN EHRSKAEETQ
RSVNDLTSQR AKLQTENGEL SRQLDEKEAL ISQLTRGKLT YTQQLEDLKR QLEEEVKAKN
ALAHALQSAR HDCDLLREQY EEETEAKAEL QRVLSKANSE VAQWRTKYET DAIQRTEELE
EAKKKLAQRL QEAEEAVEAV NAKCSSLEKT KHRLQNEIED LMVDVERSNA AAAALDKKQR
NFDKILAEWK QKYEESQSEL ESSQKEARSL STELFKLKNA YEESLEHLET FKRENKNLQE
EISDLTEQLG SSGKTIHELE KVRKQLESAL EEAEASLEHE EGKILRAQLE FNQIKAEIER
KLAEKDEEME QAKRNHLRVV DSLQTSLDAE TRSRNEALRV KKKMEGDLNE MEIQLSHANR
MAAEAQKQVK TLQSLLKDTQ IQLDDAVRAN DDPEGEHRHR GAAQQPAMLN AFSCSAQPSL
QPRTPASSNQ KKKMDADLSQ LQTEVEEAVQ ECRNAEEKAK KAITDAAMMA EELKKEQDTS
AHLERMKKNM EQTIKDLQHR LDEAEQIALK GGKKQLQKLE ARVRELENEL EAEQKRNAES
VKGMRKSERR IKELTYQTEE DRKNLLRLQD LVDKLQLKVK AYKRQAEEAE EQANTNLSKF
RKVQHELDEA EERADIAESQ VNKLRAKSRD IGAKGLNEE
//
