Search by BoMiProt ID - Bomi7314


Primary Information

BoMiProt ID Bomi7314
Protein Name Myosin-1/Myosin heavy chain 1/Myosin heavy chain 2x/Myosin heavy chain, skeletal muscle, adult 1
Organism Bos taurus
Uniprot IdQ9BE40
Milk FractionWhey
Ref Sequence Id NP_776542.1
Aminoacid Length 1938
Molecular Weight 222990
Fasta Sequence https://www.uniprot.org/uniprot/Q9BE40.fasta
Gene Name MYH1
Gene Id 281337
Protein Existence Status reviewed

Secondary Information

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).
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
PTMs Phosphorylation
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
Predicted Disorder Regions NA
DisProt Annotation
TM Helix Prediction No TM helices
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.
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.