MYLK2_RAT
ID MYLK2_RAT Reviewed; 610 AA.
AC P20689;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Myosin light chain kinase 2, skeletal/cardiac muscle;
DE Short=MLCK2 {ECO:0000303|PubMed:2839493};
DE EC=2.7.11.18 {ECO:0000305|PubMed:2839493};
GN Name=Mylk2;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND CATALYTIC ACTIVITY.
RX PubMed=2839493; DOI=10.1016/s0021-9258(19)81545-4;
RA Roush C.L., Kennelly P.J., Glaccum M.B., Helfman D.M., Scott J.D.,
RA Krebs E.G.;
RT "Isolation of the cDNA encoding rat skeletal muscle myosin light chain
RT kinase. Sequence and tissue distribution.";
RL J. Biol. Chem. 263:10510-10516(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 296-610.
RX PubMed=2465691; DOI=10.1152/ajpcell.1989.256.2.c399;
RA Herring B.P., Nunnally M.H., Gallagher P.J., Stull J.T.;
RT "Molecular characterization of rat skeletal muscle myosin light chain
RT kinase.";
RL Am. J. Physiol. 256:C399-C404(1989).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-459, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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 Evidence={ECO:0000305|PubMed:2839493};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22005;
CC Evidence={ECO:0000305|PubMed:2839493};
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 Evidence={ECO:0000305|PubMed:2839493};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53901;
CC Evidence={ECO:0000305|PubMed:2839493};
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; J03886; AAA41625.1; ALT_SEQ; mRNA.
DR PIR; A28798; A28798.
DR RefSeq; NP_476557.1; NM_057209.1.
DR AlphaFoldDB; P20689; -.
DR BMRB; P20689; -.
DR SMR; P20689; -.
DR IntAct; P20689; 2.
DR MINT; P20689; -.
DR STRING; 10116.ENSRNOP00000011255; -.
DR iPTMnet; P20689; -.
DR PhosphoSitePlus; P20689; -.
DR jPOST; P20689; -.
DR PaxDb; P20689; -.
DR PRIDE; P20689; -.
DR DNASU; 117558; -.
DR GeneID; 117558; -.
DR KEGG; rno:117558; -.
DR UCSC; RGD:620934; rat.
DR CTD; 85366; -.
DR RGD; 620934; Mylk2.
DR eggNOG; KOG0032; Eukaryota.
DR InParanoid; P20689; -.
DR OrthoDB; 218222at2759; -.
DR PhylomeDB; P20689; -.
DR BRENDA; 2.7.11.18; 5301.
DR PRO; PR:P20689; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0030425; C:dendrite; IDA:RGD.
DR GO; GO:0043197; C:dendritic spine; IDA:RGD.
DR GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0014069; C:postsynaptic density; IDA:RGD.
DR GO; GO:0008021; C:synaptic vesicle; IDA:RGD.
DR GO; GO:0043195; C:terminal bouton; IDA:RGD.
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; IMP:RGD.
DR GO; GO:0004687; F:myosin light chain kinase activity; IDA:RGD.
DR GO; GO:0055008; P:cardiac muscle tissue morphogenesis; ISO:RGD.
DR GO; GO:0006936; P:muscle contraction; IEP:RGD.
DR GO; GO:0007274; P:neuromuscular synaptic transmission; ISO:RGD.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; TAS:RGD.
DR GO; GO:0018107; P:peptidyl-threonine phosphorylation; ISO:RGD.
DR GO; GO:0031448; P:positive regulation of fast-twitch skeletal muscle fiber contraction; IMP:RGD.
DR GO; GO:0010628; P:positive regulation of gene expression; ISO:RGD.
DR GO; GO:0046777; P:protein autophosphorylation; ISO:RGD.
DR GO; GO:0006468; P:protein phosphorylation; IDA:RGD.
DR GO; GO:0051726; P:regulation of cell cycle; IMP:RGD.
DR GO; GO:0043408; P:regulation of MAPK cascade; IMP:RGD.
DR GO; GO:0006937; P:regulation of muscle contraction; IMP:RGD.
DR GO; GO:0032971; P:regulation of muscle filament sliding; ISO:RGD.
DR GO; GO:0048168; P:regulation of neuronal synaptic plasticity; IMP:RGD.
DR GO; GO:0035914; P:skeletal muscle cell differentiation; ISO:RGD.
DR GO; GO:0014816; P:skeletal muscle satellite cell differentiation; ISO:RGD.
DR GO; GO:0006941; P:striated muscle contraction; ISO:RGD.
DR GO; GO:0048489; P:synaptic vesicle transport; IMP:RGD.
DR GO; GO:0006833; P:water transport; IMP:RGD.
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 Acetylation; ATP-binding; Calmodulin-binding; Cytoplasm; Kinase;
KW Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P07313"
FT CHAIN 2..610
FT /note="Myosin light chain kinase 2, skeletal/cardiac
FT muscle"
FT /id="PRO_0000086411"
FT DOMAIN 299..554
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 196..240
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 588..600
FT /note="Calmodulin-binding"
FT /evidence="ECO:0000250"
FT COMPBIAS 1..20
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 36..77
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 119..139
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 420
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 305..313
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 328
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:0000250|UniProtKB:P07313"
FT MOD_RES 160
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8VCR8"
FT MOD_RES 166
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8VCR8"
FT MOD_RES 168
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8VCR8"
FT MOD_RES 459
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
SQ SEQUENCE 610 AA; 65816 MW; E26BF76EFF88701F CRC64;
MATENGAVEL GTQSLSTDHP PTDAAGDGSP ASEKEPSLPD TEKDLGPTNT KKDPGAPDPK
KNPDPPSLKK TPEAPGPEKK GDSAPASASN QGPSGEGDGG GGPAEGGTGP PAVLPQPTAT
ADASIQKLDA TQAPSGNQES GEAKAGKKAA ECREAGRRGS PAFLHSPSCP AIISCSEKTL
AMKPLSETTE LIFAGVSETP DPQDPGPAKD EGGTNTLADG KEEAEAGQAE QAKVQGDTSQ
RIGFQAVPSE RAEVGQALCL TAKEEDCFQI LDDCPPPPAP FPHRIVELRT GNVSSEFSMN
SKEALGGGKF GAVCTCTERS TGLKLAAKVI KKQTPKDKEM VLLEIEVMNQ LNHRNLIQLY
SAIETSHEII LFMEYIEGGE LFERIVDEDY QLTEVDTMVF VRQICDGILF MHKMRVLHLD
LKPENILCVN TTGHLVKIID FGLARRYNPN EKLKVNFGTP EFLSPEVVNY DQISDKTDMW
SLGVITYMLL SGLSPFLGDD DTETLNNVLS ANWYFDEETF EAVSDEAKDF VSNLITKDQS
ARMSAEQCLA HPWLNNLAEK AKRCNRRLKS QILLKKYLMK RRWKKNFIAV SAANRFKKIS
SSGALMALGV
