MYLK3_DANRE
ID MYLK3_DANRE Reviewed; 715 AA.
AC A8C984; Q6ZM37;
DT 03-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Myosin light chain kinase 3;
DE EC=2.7.11.18;
DE AltName: Full=Cardiac-MyBP-C-associated Ca/CaM kinase;
DE Short=Cardiac-MLCK;
GN Name=mylk3; Synonyms=mlck;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND DEVELOPMENTAL STAGE.
RX PubMed=17885681; DOI=10.1172/jci30804;
RA Seguchi O., Takashima S., Yamazaki S., Asakura M., Asano Y., Shintani Y.,
RA Wakeno M., Minamino T., Kondo H., Furukawa H., Nakamaru K., Naito A.,
RA Takahashi T., Ohtsuka T., Kawakami K., Isomura T., Kitamura S., Tomoike H.,
RA Mochizuki N., Kitakaze M.;
RT "A cardiac myosin light chain kinase regulates sarcomere assembly in the
RT vertebrate heart.";
RL J. Clin. Invest. 117:2812-2824(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
CC -!- FUNCTION: Kinase that phosphorylates MYL2 in vitro (By similarity).
CC Increases cardiomyocyte contractility (By similarity). Required for
CC sarcomere formation in the developing heart. {ECO:0000250,
CC ECO:0000269|PubMed:17885681}.
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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- DEVELOPMENTAL STAGE: At 24 and 48 hours post fertilization, expressed
CC only in the heart. {ECO:0000269|PubMed:17885681}.
CC -!- PTM: Phosphorylated on serine residues. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC protein kinase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAE49228.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB267907; BAF80631.1; -; mRNA.
DR EMBL; AL928906; CAE49228.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; NP_001099057.1; NM_001105587.1.
DR AlphaFoldDB; A8C984; -.
DR SMR; A8C984; -.
DR STRING; 7955.ENSDARP00000102547; -.
DR PaxDb; A8C984; -.
DR PeptideAtlas; A8C984; -.
DR GeneID; 561635; -.
DR KEGG; dre:561635; -.
DR CTD; 91807; -.
DR ZFIN; ZDB-GENE-030131-3497; mylk3.
DR eggNOG; KOG0032; Eukaryota.
DR HOGENOM; CLU_023683_0_0_1; -.
DR InParanoid; A8C984; -.
DR OMA; MNCAATS; -.
DR OrthoDB; 218222at2759; -.
DR PhylomeDB; A8C984; -.
DR TreeFam; TF314166; -.
DR PRO; PR:A8C984; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004687; F:myosin light chain kinase activity; IBA:GO_Central.
DR GO; GO:0003007; P:heart morphogenesis; IMP:ZFIN.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:0048769; P:sarcomerogenesis; IMP:BHF-UCL.
DR GO; GO:0055005; P:ventricular cardiac myofibril assembly; IMP:BHF-UCL.
DR InterPro; IPR011009; Kinase-like_dom_sf.
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 2: Evidence at transcript level;
KW ATP-binding; Cytoplasm; Kinase; Nucleotide-binding; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..715
FT /note="Myosin light chain kinase 3"
FT /id="PRO_0000419666"
FT DOMAIN 404..659
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 67..114
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 67..82
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 525
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 410..418
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 433
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 715 AA; 80378 MW; C498252830575577 CRC64;
MGTSLYRSTL LSTGGFSVSD YIRKFTKNKP DVNNIQPNVG FCHQSTQTSQ QVKEVISAEL
ELQQPEVTLP NDPSSQHSPE AHTGASEPLK PVSAGESSKA LQKAKEISVK SSEPTHVQTF
APAVHLEQID VHNVPKQETN SLVAAPADAK CVIETMTKVE KDIALQQERA LERADDSHVA
NKVFLKSIIP GQQLEKIEDP QQQAEVSLFV DEDSLEKSVP GQHLDKKMEV LQKQAKDLPV
VDEDSLNLSA PGQRQLEEKV DVPEKAEKKI DEAHKKMEEV PRKDELCIEK PVIRHAGIKT
QHEETMGMET TVPKHDESKC PTETYVEKTE NKNADVTLES DKIMICAVSP QNTSLDEDEK
SKAAPLRKVE STLLIIDDSP PLPAPFDHRI VSAKQVPINS YYAVNPVEVL GGGRFGQVHK
CAELSSGLTL AAKIIKVRGM KERDEVKNEI GVMNQLNHVN LIQLYDAFES RTNLTLIMEY
VEGGELFERI IDESYQLTEL DAIVFTRQIC EGVQYLHQQY ILHLDLKPEN ILCVNSTGNQ
IKIIDFGLAR KYRPREKLKV NFGTPEFLAP EVVNYDFVSF PTDMWSVGVI TYMLLSGLSP
FMGDNDAETM NNILHAKWEF DTEAFENVSE EAKDFISSLL VSAKCSRLSA SGCMKHSWLN
NLEDKAKMYK VRLKSQMMLQ RYLVAHRQWK KHFYAVAAAN RLKRFQQSRS ISTPN
