Primary Information |
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| BoMiProt ID | Bomi7306 |
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| Protein Name | Myosin light chain kinase, smooth muscle/MLCK/smMLCK/Telokin |
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| Organism | Bos taurus |
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| Uniprot ID | Q28824 |
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| Milk Fraction | Whey |
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| Ref Sequence ID | NP_788809.1 |
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| Aminoacid Length | 1176 |
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| Molecular Weight | 128825 |
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| FASTA Sequence |
Download |
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| Gene Name | MYLK |
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| Gene ID | 338037 |
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| Protein Existence Status | reviewed |
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Secondary Information |
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| Protein Function | phosphorylates the light chain of smooth muscle myosin enabling its interaction with actin.This interaction initiates smooth muscle contraction. |
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| Biochemical Properties | The catalytic site is located at the centre part of the enzyme.The regulatory site, which consists of pseudosubstrate and CaM-binding sequences, lies on the C terminal side of the catalytic site. Ca2+-CaM binds to the CaM-binding site and activates the kinase activity of the catalytic site by interacting with the pseudosubstrate sequence. |
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| PTMs | Phosphorylation and disulfide bond formation |
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| Significance of PTMs | PAK2(p21 activated kinase) catalyzes MLCK phosphorylation on serine residues 439 and 991.This phosphorylation inhibits MLCK phosphorylation of myosin II Regulatory light chain.Binding calmodulin to MLCK blocks phosphorylation of Ser-991 by PAK2. Acetylated at Lys-608 by NAA10/ARD1 via a calcium-dependent signaling; this acetylation represses kinase activity and reduces tumor cell migration. |
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| Linking IDs | Bomi7306 |
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| Bibliography | 1.Goeckeler ZM, Masaracchia RA, Zeng Q, Chew TL, Gallagher P, Wysolmerski RB. Phosphorylation of myosin light chain kinase by p21-activated kinase PAK2. J Biol Chem. 2000 Jun 16;275(24):18366-74. doi: 10.1074/jbc.M001339200. PMID: 10748018. 2.Okagaki T, Hayakawa K, Samizo K, Kohama K. Inhibition of the ATP-dependent interaction of actin and myosin by the catalytic domain of the myosin light chain kinase of smooth muscle: possible involvement in smooth muscle relaxation. J Biochem. 1999 Mar;125(3):619-26. doi: 10.1093/oxfordjournals.jbchem.a022328. PMID: 10050052. 3.Shin DH, Chun YS, Lee KH, Shin HW, Park JW. Arrest defective-1 controls tumor cell behavior by acetylating myosin light chain kinase. PLoS One. 2009 Oct 14;4(10):e7451. doi: 10.1371/journal.pone.0007451. PMID: 19826488; PMCID: PMC2758594. |
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| Protein Function | phosphorylates the light chain of smooth muscle myosin enabling its interaction with actin.This interaction initiates smooth muscle contraction. |
|---|
| Biochemical Properties | The catalytic site is located at the centre part of the enzyme.The regulatory site, which consists of pseudosubstrate and CaM-binding sequences, lies on the C terminal side of the catalytic site. Ca2+-CaM binds to the CaM-binding site and activates the kinase activity of the catalytic site by interacting with the pseudosubstrate sequence. |
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| PTMs | Phosphorylation and disulfide bond formation |
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Site(s) of PTM(s)
N-glycosylation,
O-glycosylation,
Phosphorylation
| >sp|Q28824|MYLK_BOVIN Myosin light chain kinase, smooth muscle OS=Bos taurus OX=9913 GN=MYLK PE=1 SV=1
MDFRANLQRQVKPKTLSEEERKVHGPQQVDFRSVLAKKGTPKTPVPEKVPPPKPATPDFR
SVLGSKKKLPTENGSNNTEALNAKAAEGLKPVGNAQPSGFLKPVGNAKLADTPKPLSSTK
PAETPKPLGNVKPAETPKPLGSTKPAETPKPLGSTKPAETPKPLGNVKPAETPKPLGNIK
PTETPKPLGSTKPAETPKPLGS*202TKPAETPKPLGNVKPAETPKPLGNVKPAETPKPLGNVK
PAETPKPVSNAKPAETLKPVGNAKPAETPKPLSNVKPAETPKLVGNAKPAETSKPLDNAK
PAEAPKPLGNAKPAEIPKPTGKEELKKEIKNDVNCKKGHAGATDSEKRPESRGTAPTFEE
KLQDLHVAEGQKLLLQCRVSSDPPATITWTLNGKTLKTTKFIVLSQEGSLCSVSIEKALP
EDRGLYKCVAKNSAGQAESSCQVTVDVPDAPTSENAKAPEMKARRPKSSLPPVLGTESDA
TVKKKPAPKTPPKAAMPPQIIQFPEDQKVRAGESVELFGKVAGTQPITCTWMKFRKQIQD
SEHIKVENSEQGSKLTIRAARQEHCGCYTLLVENKLGSRQAQVNLTVVDKPDPPAGTPCA
SDIRSSSLTLSWYGSSYDGGSAVQSYSVEIWDSVDKTWKELATCRSTSFNVQDLLPDREY
KFRVRAINVYGTSEPSQESELTALGEKPEEEPKDEVEVS*699DDDEKEPEVDY*710RTVTVNTEQK
VSDFYDIEERLGSGKFGQVFRLVEKKTGKIWAGKFFKAYSAKEKENIRQEISIMNCLHHP
KLVQCVDAFEEKANIVMVLEIVSGGELFERIIDEDFELTERECIKYMKQISEGVEY*836IHKQ
GIVHLDLKPENIMCVNKTGTRIKLIDFGLARRLENAGSLKVLFGTPEFVAPEVINY*896EPIG
YATDMWSIGVICYILVSGLSPFMGDNDNETLANVTSATWDFDDEAFDEISDDAKDFISNL
LKKDMKNRLNCTQCLQHPWLMKDTKNMEAKKLSKDRMKKYMARRKWQKTGNAVRAIGRLS*1020
S*1021MAMISGLSGRKS*1033S*1034TGS*1037PT*1039S*1040PLNAEKLESEDVSQAFLEAVAEEKPHVKPYFSKTIRDLEV
VEGSAARFDCKIEGYPDPEVVWFKDDQSIRESRHFQIDYDEDGNCSLIISDVCGDDDAKY
TCKAVNSLGEATCTAELIVETMEEGEGEGGEEEEEE
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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 | PAK2(p21 activated kinase) catalyzes MLCK phosphorylation on serine residues 439 and 991.This phosphorylation inhibits MLCK phosphorylation of myosin II Regulatory light chain.Binding calmodulin to MLCK blocks phosphorylation of Ser-991 by PAK2. Acetylated at Lys-608 by NAA10/ARD1 via a calcium-dependent signaling; this acetylation represses kinase activity and reduces tumor cell migration. |
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| Linking IDs | |
|---|
| Bibliography | 1.Goeckeler ZM, Masaracchia RA, Zeng Q, Chew TL, Gallagher P, Wysolmerski RB. Phosphorylation of myosin light chain kinase by p21-activated kinase PAK2. J Biol Chem. 2000 Jun 16;275(24):18366-74. doi: 10.1074/jbc.M001339200. PMID: 10748018. 2.Okagaki T, Hayakawa K, Samizo K, Kohama K. Inhibition of the ATP-dependent interaction of actin and myosin by the catalytic domain of the myosin light chain kinase of smooth muscle: possible involvement in smooth muscle relaxation. J Biochem. 1999 Mar;125(3):619-26. doi: 10.1093/oxfordjournals.jbchem.a022328. PMID: 10050052. 3.Shin DH, Chun YS, Lee KH, Shin HW, Park JW. Arrest defective-1 controls tumor cell behavior by acetylating myosin light chain kinase. PLoS One. 2009 Oct 14;4(10):e7451. doi: 10.1371/journal.pone.0007451. PMID: 19826488; PMCID: PMC2758594. |
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