Primary Information |
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| BoMiProt ID | Bomi7314 |
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| Protein Name | Myosin-1/Myosin heavy chain 1/Myosin heavy chain 2x/Myosin heavy chain, skeletal muscle, adult 1 |
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| Organism | Bos taurus |
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| Uniprot ID | Q9BE40 |
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| Milk Fraction | Whey |
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| Ref Sequence ID | NP_776542.1 |
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| Aminoacid Length | 1938 |
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| Molecular Weight | 222990 |
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| FASTA Sequence |
Download |
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| Gene Name | MYH1 |
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| Gene ID | 281337 |
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| Protein Existence Status | reviewed |
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Secondary Information |
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| Protein Function | myosin 1 regulates the actin dependent post-Golgi traffic of cargo and generates force that controls the assembly of F-actin foci and promotes with the actin cytoskeleton the formation of tubules at the TGN( trans-Golgi network). |
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| Biochemical Properties | Muscle myosin is a hexameric protein that consists of 2 heavy chain subunits (MHC), 2 alkali light chain subunits (MLC) and 2 regulatory light chain subunits (MLC-2).provided long tail that interacts with NPF via an acidic motif at its C-terminus |
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| PTMs | Phosphorylation |
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Site(s) of PTM(s)
N-glycosylation,
O-glycosylation,
Phosphorylation
| >sp|Q9BE40|MYH1_BOVIN Myosin-1 OS=Bos taurus OX=9913 GN=MYH1 PE=2 SV=2
MSSDQEMAVFGEAAPYLRKSEKERIEAQNKPFDAKTSVFVADPKESFVKATVQSREGGKV
TAKT*64EAGAT*69VTVKEDQVFPMNPPKFDKIEDMAMMTHLHEPAVLYNLKERYAAWMIYTYSG
LFCVTVNPYKWLPVYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE
SGAGKTVNTKRVIQYFATIAVTGEKKKEEPTSGKMQGTLEDQIISANPLLEAFGNAKTVR
NDNSSRFGKFIRIHFGTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPEL
IEMLLITTNPYDYAYVSQGEITVPSIDDQEELMATDSAIEILGFTSDERVSIYKLTGAVM
HYGNLKFKQKQREEQAEPDGTEVADKAAY*389LQGLNSADLLKALCYPRVKVGNEFVTKGQT*419V
EQVY*424NAVGALAKAVYDKMFLWMVARINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLC
INFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILEEE
CMFPKATDMSFKNKLYEQHLGKSNNFQKPKPAKGKAEAHFSLIHYAGTVDYNITGWLDKN
KDPLNETVVGLYQKSSVKTLALLFS*625GPASGEAEGGPKKGGKKKGSSFQTVSALFRENLNK
LMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYAD
FKQRYKVLNASAIPEGQFIDSKKASEKLLASIDVDHTQYKFGHTKVFFKAGLLGLLEEMR
DEKLAQLITRTQARCRGFLARVEYQKMVERRESIFCIQYNVRAFMNVKHWPWMKLYFKIK
PLLKSAETEKEMANMKEEFEKTKEELAKSEAKRKELEEKMVTLTQEKNDLQLQVQSEADA
LADAEERCDQLIKTKIQLEAKIKEVTERAEDEEEINAELTAKKRKLEDECSELKKDIDDL
ELTLAKVEKEKHATENKVKNLTEEMAGLDETIAKLTKEKKALQEAHQQTLDDLQAEEDKV
NTLTKAKTKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQESTMDIENDKQQLD
EKLKKKEFEMS*1091NLQS*1095KIEDEQALAMQLQKKIKELQARIEELEEEIEAERASRAKAEKQRS
DLSRELEEISERLEEAGGATS*1161AQIEMNKKREAEFQKMRRDLEEATLQHEATAAALRKKHA
DSVAELGEQIDNLQRVKQKLEKEKSEMKMEIDDLAS*1236NMET*1240VS*1242KAKGNLEKMCRALEDQLS*1260ELKT*1264KEDEQQRLINDLTTQRARLQT*1285ES*1287GEFS*1291RQLDEKDALVS*1302QLS*1305RGKQAFTQQIEELKRQLEEEIKAKSALAHALQSARHDCDLLREQYEEEQEGKAELQRAMSKANSEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQDAEEHVEAVNAKCASLEKTKQRLQNEVEDLMIDVERTNA
ACAALDKKQRNFDKILSEWKQKY*1463EET*1466HAELEAS*1473QKESRSLSTELFKIKNAY*1491EES*1494LDQLET*1500LKRENKNLQQEIS*1513DLT*1516EQIAEGGKRIHELEKVKKQVEQEKS*1541EIQAALEEAEAS*1553LEHEEGKILRIQLELNQVKS*1573EIDRKIAEKDEEIDQLKRNHIRIVES*1599MQS*1602TLDAEIRSRNDAIRLKKKMEGDLNEMEIQLNHANRMAAEALKNYRSTQAILKDTQIHLDDALRGQEDLKEQLAMVERRANLLQAEIEELRATLEQTERSRKIAEQELLDAS*1713ERVQLLHTQNTS*1725LINT*1729KKKLET*1735DITQIQGEMEDIIQEARNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNLEQTVKDLQHRL
DEAEQLALKGGKKQIQKLEARVRELEGEVESEQKRNVEAVKGLRKHERRVKELTYQTEED
RKNILRLQDLVDKLQAKVKSYKRQAEEAEEQSNVNLSKFRKLQHELEEAEERADIAESQV
NKLRVKSREVHTKIISEE
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| Predicted Disorder Regions | NA |
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| DisProt Annotation | |
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| TM Helix Prediction | No TM helices |
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| Significance of PTMs | Ser-19-phosphorylation and on Thr-18 on Myosin Light chain by Rho-kinase and MLC kinase respectively,results in the facilitation of the actin activation of myosin ATPase and then induces myosin-actin interaction.MLC phosphorylation has role in smooth muscle contraction which then induces smooth muscle contraction.When MLC is phosphorylated at Ser-1, Ser-2, and Thr-9 by protein kinase C, and this phosphorylation by protein kinase C inhibits the actin activation of myosin ATPase.The Km value of Rho-kinase for MLC was lower than that of MLC kinase, but the molecular activity of Rho-kinase was lower than that of MLC kinase.This indicates that Rho-kinase efficiently phosphorylates MLC at lower concentrations. |
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| Bibliography | Amano M, Ito M, Kimura K, Fukata Y, Chihara K, Nakano T, Matsuura Y, Kaibuchi K. Phosphorylation and activation of myosin by Rho-associated kinase (Rho-kinase). J Biol Chem. 1996 Aug 23;271(34):20246-9. doi: 10.1074/jbc.271.34.20246. PMID: 8702756. |
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