MYLK2_MOUSE
ID MYLK2_MOUSE Reviewed; 613 AA.
AC Q8VCR8; A2APB9;
DT 19-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 2.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Myosin light chain kinase 2, skeletal/cardiac muscle;
DE Short=MLCK2;
DE EC=2.7.11.18;
GN Name=Mylk2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-591.
RC STRAIN=C57BL/6J; TISSUE=Bone;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 374-613.
RC TISSUE=Salivary gland;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-161; SER-167 AND SER-169, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, and Lung;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Implicated in the level of global muscle contraction and
CC cardiac function. Phosphorylates a specific serine in the N-terminus of
CC a myosin light chain (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[myosin light chain] = ADP + H(+) + O-phospho-L-
CC seryl-[myosin light chain]; Xref=Rhea:RHEA:22004, Rhea:RHEA-
CC COMP:13684, Rhea:RHEA-COMP:13685, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421,
CC ChEBI:CHEBI:456216; EC=2.7.11.18;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[myosin light chain] = ADP + H(+) + O-
CC phospho-L-threonyl-[myosin light chain]; Xref=Rhea:RHEA:53900,
CC Rhea:RHEA-COMP:13686, Rhea:RHEA-COMP:13687, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977,
CC ChEBI:CHEBI:456216; EC=2.7.11.18;
CC -!- SUBUNIT: May interact with centrin. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Note=Colocalizes with
CC phosphorylated myosin light chain (RLCP) at filaments of the
CC myofibrils. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC protein kinase family. {ECO:0000305}.
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DR EMBL; AL833801; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK079396; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BC019408; AAH19408.1; -; mRNA.
DR CCDS; CCDS38282.2; -.
DR RefSeq; NP_001074513.2; NM_001081044.2.
DR AlphaFoldDB; Q8VCR8; -.
DR BMRB; Q8VCR8; -.
DR SMR; Q8VCR8; -.
DR IntAct; Q8VCR8; 2.
DR MINT; Q8VCR8; -.
DR STRING; 10090.ENSMUSP00000028970; -.
DR iPTMnet; Q8VCR8; -.
DR PhosphoSitePlus; Q8VCR8; -.
DR MaxQB; Q8VCR8; -.
DR PaxDb; Q8VCR8; -.
DR PRIDE; Q8VCR8; -.
DR ProteomicsDB; 287572; -.
DR Antibodypedia; 25246; 154 antibodies from 26 providers.
DR DNASU; 228785; -.
DR Ensembl; ENSMUST00000028970; ENSMUSP00000028970; ENSMUSG00000027470.
DR GeneID; 228785; -.
DR KEGG; mmu:228785; -.
DR UCSC; uc008ngs.2; mouse.
DR CTD; 85366; -.
DR MGI; MGI:2139434; Mylk2.
DR VEuPathDB; HostDB:ENSMUSG00000027470; -.
DR eggNOG; KOG0032; Eukaryota.
DR GeneTree; ENSGT00940000161489; -.
DR HOGENOM; CLU_000288_90_1_1; -.
DR InParanoid; Q8VCR8; -.
DR OMA; PPDPKKD; -.
DR OrthoDB; 218222at2759; -.
DR PhylomeDB; Q8VCR8; -.
DR TreeFam; TF314166; -.
DR BioGRID-ORCS; 228785; 3 hits in 75 CRISPR screens.
DR ChiTaRS; Mylk2; mouse.
DR PRO; PR:Q8VCR8; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q8VCR8; protein.
DR Bgee; ENSMUSG00000027470; Expressed in hindlimb stylopod muscle and 48 other tissues.
DR Genevisible; Q8VCR8; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0030425; C:dendrite; ISO:MGI.
DR GO; GO:0043197; C:dendritic spine; ISO:MGI.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0014069; C:postsynaptic density; ISO:MGI.
DR GO; GO:0008021; C:synaptic vesicle; ISO:MGI.
DR GO; GO:0043195; C:terminal bouton; ISO:MGI.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0032027; F:myosin light chain binding; ISO:MGI.
DR GO; GO:0004687; F:myosin light chain kinase activity; ISO:MGI.
DR GO; GO:0055007; P:cardiac muscle cell differentiation; NAS:UniProtKB.
DR GO; GO:0055008; P:cardiac muscle tissue morphogenesis; ISO:MGI.
DR GO; GO:0007274; P:neuromuscular synaptic transmission; IMP:MGI.
DR GO; GO:0018107; P:peptidyl-threonine phosphorylation; ISO:MGI.
DR GO; GO:0031448; P:positive regulation of fast-twitch skeletal muscle fiber contraction; ISO:MGI.
DR GO; GO:0010628; P:positive regulation of gene expression; ISO:MGI.
DR GO; GO:0046777; P:protein autophosphorylation; ISO:MGI.
DR GO; GO:0006468; P:protein phosphorylation; ISO:MGI.
DR GO; GO:0051726; P:regulation of cell cycle; ISO:MGI.
DR GO; GO:0043408; P:regulation of MAPK cascade; ISO:MGI.
DR GO; GO:0006937; P:regulation of muscle contraction; ISO:MGI.
DR GO; GO:0032971; P:regulation of muscle filament sliding; ISO:MGI.
DR GO; GO:0048168; P:regulation of neuronal synaptic plasticity; ISO:MGI.
DR GO; GO:0035914; P:skeletal muscle cell differentiation; ISO:MGI.
DR GO; GO:0014816; P:skeletal muscle satellite cell differentiation; IMP:UniProtKB.
DR GO; GO:0006941; P:striated muscle contraction; ISO:MGI.
DR GO; GO:0048489; P:synaptic vesicle transport; ISO:MGI.
DR GO; GO:0006833; P:water transport; ISO:MGI.
DR CDD; cd14190; STKc_MLCK2; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR042717; MLCK2_STKc.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Calmodulin-binding; Cytoplasm; Kinase; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Serine/threonine-protein kinase;
KW Transferase.
FT CHAIN 1..613
FT /note="Myosin light chain kinase 2, skeletal/cardiac
FT muscle"
FT /id="PRO_0000086409"
FT DOMAIN 302..557
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..168
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 219..240
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 591..603
FT /note="Calmodulin-binding"
FT /evidence="ECO:0000250"
FT COMPBIAS 1..23
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 125..140
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 423
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 308..316
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 331
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 161
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 167
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 169
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 462
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P20689"
SQ SEQUENCE 613 AA; 65990 MW; 1FAC64C8B09DAE25 CRC64;
MTTENGAVEL GSQSLSTEQT PKAAAGDGPS ASEKEPSAPA TEKDLSPPNA KKDPGAPDPK
NNPDPPSLKK DPAKAPGPEK KGDPVPASAS SQGPSGEGDG GGGPAEGSEG PPAALPLPTA
TAEASIQKLD PTQAPSGNQG SGEAKAGKKA AECREAGRRG SPAFLHSPSC PAIISCSEKT
LAVKPLSETT DLVFTGVSVT PDPQDPGPVK AGGTNALAEK KKEEAEKASG QAGQAKVQGD
TPQRIGFQAV PSERVEVGQA LCLTAREEDC FQILDDCPPP PAPFPHRIVE LRTGNVNSEF
SMNSKEALGG GKFGAVCTCT ERATGLKLAA KVIKKQTPKD KEMVLLEIEV MNQLNHRNLI
QLYAAIETSH EIILFMEYIE GGELFERIVD EDYHLTEVDT MVFVRQICDG ILFMHKMRVL
HLDLKPENIL CVNTTGHLVK IIDFGLARRY NPNEKLKVNF GTPEFLSPEV VNYDQISDKT
DMWSLGVITY MLLSGLSPFL GDDDTETLNN VLSANWYFDE ETFEAVSDEA KDFVSNLLTK
DQSARMSAEQ CLAHPWLNNL AEKAKRCNRR LKSQILLKKY LMKRRWKKNF IAVSAANRFK
KISSSGALMA LGV
