MYLK2_RABIT
ID MYLK2_RABIT Reviewed; 608 AA.
AC P07313;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Myosin light chain kinase 2, skeletal/cardiac muscle;
DE Short=MLCK2;
DE EC=2.7.11.18;
GN Name=MYLK2;
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1688558; DOI=10.1016/s0021-9258(19)40076-8;
RA Herring B.P., Stull J.T., Gallagher P.J.;
RT "Domain characterization of rabbit skeletal muscle myosin light chain
RT kinase.";
RL J. Biol. Chem. 265:1724-1730(1990).
RN [2]
RP PROTEIN SEQUENCE OF 2-604, AND ACETYLATION AT ALA-2.
RX PubMed=3542042; DOI=10.1021/bi00372a038;
RA Takio K., Blumenthal D.K., Walsh K.A., Titani K., Krebs E.G.;
RT "Amino acid sequence of rabbit skeletal muscle myosin light chain kinase.";
RL Biochemistry 25:8049-8057(1986).
RN [3]
RP PROTEIN SEQUENCE OF 296-604.
RX PubMed=3841288; DOI=10.1021/bi00343a002;
RA Takio K., Blumenthal D.K., Edelman A.M., Walsh K.A., Krebs E.G., Titani K.;
RT "Amino acid sequence of an active fragment of rabbit skeletal muscle myosin
RT light chain kinase.";
RL Biochemistry 24:6028-6037(1985).
RN [4]
RP SUBCELLULAR LOCATION.
RX PubMed=11733062; DOI=10.1016/s0092-8674(01)00586-4;
RA Davis J.S., Hassanzadeh S., Winitsky S., Lin H., Satorius C., Vemuri R.,
RA Aletras A.H., Wen H., Epstein N.D.;
RT "The overall pattern of cardiac contraction depends on a spatial gradient
RT of myosin regulatory light chain phosphorylation.";
RL Cell 107:631-641(2001).
RN [5]
RP STRUCTURE BY NMR OF 578-603.
RX PubMed=1585175; DOI=10.1126/science.1585175;
RA Ikura M., Clore G.M., Gronenborn A.M., Zhu G., Klee C.B., Bax A.;
RT "Solution structure of a calmodulin-target peptide complex by
RT multidimensional NMR.";
RL Science 256:632-638(1992).
CC -!- FUNCTION: Implicated in the level of global muscle contraction and
CC cardiac function (By similarity). Phosphorylates a specific serine in
CC the N-terminus of a myosin light chain. {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:0000269|PubMed:11733062}.
CC Note=Colocalizes with phosphorylated myosin light chain (RLCP) at
CC filaments of the myofibrils.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC protein kinase family. {ECO:0000305}.
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DR EMBL; J05194; AAA31400.1; -; mRNA.
DR PIR; A35021; A35021.
DR RefSeq; NP_001075705.1; NM_001082236.1.
DR PDB; 2BBM; NMR; -; B=578-603.
DR PDB; 2BBN; NMR; -; B=578-603.
DR PDB; 6HR1; X-ray; 1.90 A; A/B=580-599.
DR PDBsum; 2BBM; -.
DR PDBsum; 2BBN; -.
DR PDBsum; 6HR1; -.
DR AlphaFoldDB; P07313; -.
DR BMRB; P07313; -.
DR SMR; P07313; -.
DR BindingDB; P07313; -.
DR ChEMBL; CHEMBL4739674; -.
DR iPTMnet; P07313; -.
DR PRIDE; P07313; -.
DR GeneID; 100009051; -.
DR KEGG; ocu:100009051; -.
DR CTD; 85366; -.
DR InParanoid; P07313; -.
DR OrthoDB; 218222at2759; -.
DR BRENDA; 2.7.11.18; 1749.
DR EvolutionaryTrace; P07313; -.
DR Proteomes; UP000001811; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005516; F:calmodulin binding; IDA:BHF-UCL.
DR GO; GO:0004683; F:calmodulin-dependent protein kinase activity; IDA:BHF-UCL.
DR GO; GO:0004687; F:myosin light chain kinase activity; IDA:BHF-UCL.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:0032971; P:regulation of muscle filament sliding; IC:BHF-UCL.
DR CDD; cd14190; STKc_MLCK2; 1.
DR IDEAL; IID50197; -.
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 3D-structure; Acetylation; ATP-binding; Calmodulin-binding; Cytoplasm;
KW Direct protein sequencing; Kinase; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Serine/threonine-protein kinase; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:3542042"
FT CHAIN 2..608
FT /note="Myosin light chain kinase 2, skeletal/cardiac
FT muscle"
FT /id="PRO_0000086410"
FT DOMAIN 297..552
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..160
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 214..235
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 586..598
FT /note="Calmodulin-binding"
FT COMPBIAS 9..23
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 33..58
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 418
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 303..311
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 326
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|PubMed:3542042"
FT MOD_RES 153
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8VCR8"
FT MOD_RES 159
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8VCR8"
FT MOD_RES 161
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8VCR8"
FT MOD_RES 457
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P20689"
FT CONFLICT 336
FT /note="K -> KK (in Ref. 2; AA sequence and 3; AA sequence)"
FT /evidence="ECO:0000305"
FT HELIX 581..599
FT /evidence="ECO:0007829|PDB:6HR1"
SQ SEQUENCE 608 AA; 65468 MW; 9B2FD074165DADFE CRC64;
MATENGAVEL GIQSLSTDEA SKGAASEESL AAEKDPAPPD PEKGPGPSDT KQDPDPSTPK
KDANTPAPEK GDVVPAQPSA GGSQGPAGEG GQVEAPAEGS AGKPAALPQQ TATAEASEKK
PEAEKGPSGH QDPGEPTVGK KVAEGQAAAR RGSPAFLHSP SCPAIIASTE KLPAQKPLSE
ASELIFEGVP ATPGPTEPGP AKAEGGVDLL AESQKEAGEK APGQADQAKV QGDTSRGIEF
QAVPSERPRP EVGQALCLPA REEDCFQILD DCPPPPAPFP HRIVELRTGN VSSEFSMNSK
EALGGGKFGA VCTCTEKSTG LKLAAKVIKK QTPKDKEMVM LEIEVMNQLN HRNLIQLYAA
IETPHEIVLF MEYIEGGELF ERIVDEDYHL TEVDTMVFVR QICDGILFMH KMRVLHLDLK
PENILCVNTT GHLVKIIDFG LARRYNPNEK LKVNFGTPEF LSPEVVNYDQ ISDKTDMWSL
GVITYMLLSG LSPFLGDDDT ETLNNVLSGN WYFDEETFEA VSDEAKDFVS NLIVKEQGAR
MSAAQCLAHP WLNNLAEKAK RCNRRLKSQI LLKKYLMKRR WKKNFIAVSA ANRFKKISSS
GALMALGV
