MYLK2_BOVIN
ID MYLK2_BOVIN Reviewed; 623 AA.
AC A4IFM7;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Myosin light chain kinase 2, skeletal/cardiac muscle;
DE Short=MLCK2;
DE EC=2.7.11.18;
GN Name=MYLK2;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal muscle;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
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}.
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; BC134664; AAI34665.1; -; mRNA.
DR RefSeq; NP_001077188.1; NM_001083719.1.
DR RefSeq; XP_005214824.1; XM_005214767.3.
DR RefSeq; XP_005214826.1; XM_005214769.3.
DR RefSeq; XP_010809800.1; XM_010811498.2.
DR AlphaFoldDB; A4IFM7; -.
DR BMRB; A4IFM7; -.
DR SMR; A4IFM7; -.
DR STRING; 9913.ENSBTAP00000019875; -.
DR PaxDb; A4IFM7; -.
DR PRIDE; A4IFM7; -.
DR Ensembl; ENSBTAT00000019875; ENSBTAP00000019875; ENSBTAG00000014930.
DR Ensembl; ENSBTAT00000071955; ENSBTAP00000063850; ENSBTAG00000014930.
DR GeneID; 533378; -.
DR KEGG; bta:533378; -.
DR CTD; 85366; -.
DR VEuPathDB; HostDB:ENSBTAG00000014930; -.
DR VGNC; VGNC:31806; MYLK2.
DR eggNOG; KOG0032; Eukaryota.
DR GeneTree; ENSGT00940000161489; -.
DR HOGENOM; CLU_000288_90_1_1; -.
DR InParanoid; A4IFM7; -.
DR OMA; PPDPKKD; -.
DR OrthoDB; 218222at2759; -.
DR TreeFam; TF314166; -.
DR Proteomes; UP000009136; Chromosome 13.
DR Bgee; ENSBTAG00000014930; Expressed in infraspinatus muscle and 56 other tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IEA:Ensembl.
DR GO; GO:0045202; C:synapse; IEA:GOC.
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; IBA:GO_Central.
DR GO; GO:0004687; F:myosin light chain kinase activity; IBA:GO_Central.
DR GO; GO:0055008; P:cardiac muscle tissue morphogenesis; IBA:GO_Central.
DR GO; GO:0007274; P:neuromuscular synaptic transmission; IEA:Ensembl.
DR GO; GO:0018107; P:peptidyl-threonine phosphorylation; IEA:Ensembl.
DR GO; GO:0010628; P:positive regulation of gene expression; IEA:Ensembl.
DR GO; GO:0046777; P:protein autophosphorylation; IEA:Ensembl.
DR GO; GO:0032971; P:regulation of muscle filament sliding; IEA:Ensembl.
DR GO; GO:0014816; P:skeletal muscle satellite cell differentiation; IEA:Ensembl.
DR GO; GO:0006941; P:striated muscle contraction; IBA:GO_Central.
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 2: Evidence at transcript 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..623
FT /note="Myosin light chain kinase 2, skeletal/cardiac
FT muscle"
FT /id="PRO_0000295167"
FT DOMAIN 312..567
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..179
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 204..251
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 601..613
FT /note="Calmodulin-binding"
FT /evidence="ECO:0000250"
FT COMPBIAS 37..85
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 433
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 318..326
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 341
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 169
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8VCR8"
FT MOD_RES 175
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8VCR8"
FT MOD_RES 177
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8VCR8"
FT MOD_RES 472
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P20689"
SQ SEQUENCE 623 AA; 67243 MW; 854E709465C00B4E CRC64;
MATENGAVEL EIPSSSTDTA PKAAAGEGPP AAEKDPGPPD PQKDPGPPDP EKDAGPPNPE
KELESPDPKK EPDPDSTKDT EAPAPEKGDG ASAQPSASSQ GPEGEGGLQG EPAEGSAGQP
AALPQETATA EASVKKPEAE QGTPGSQDPG EAKEQKKVAE GQAPSKKGSP AFLHSPSCPA
AISSLEKPLA EKPLDETLEL IFEGVPVTPG PTETEPAKVA EGEKNLPGGS QKEGEEKAAG
HAGQDGVQGD TSRGIEFQAV PSERSEVGQA LSPTAKEEDC FQILDDCPPP PAPFPHRIVE
LRPGNINSQF SLNSKEALGG GKFGAVCTCT EKATGLKLAA KVIKKQTPKD KEMVLLEIEV
MNQLNHRNLI QLYAAIETPH EIVLFMEYIE GGELFERIVD EDYQLTEVDT MVFVRQICDG
ILFMHKMRVL HLDLKPENIL CVNTTGHLVK IIDFGLARRY NPNEKLKVNF GTPEFLSPEV
VNYDQISDKT DMWSLGVITY MLLSGLSPFL GDDDTETLNN VLSSNWYFDE ETFEAVSDEA
KDFVSNLIVK DQRARMSAAQ CLAHPWLNNL AEKAKRCNRR LKSQILLKKY LMKRRWKKNF
IAVSAANRFK KISSSGALMA LGV
