MYLK_PIG
ID MYLK_PIG Reviewed; 139 AA.
AC P79280;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Myosin light chain kinase, smooth muscle;
DE Short=MLCK;
DE EC=2.7.11.18;
DE Flags: Fragment;
GN Name=MYLK;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Pulmonary artery;
RA Sakihara C.;
RL Submitted (DEC-1996) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Phosphorylates a specific serine in the N-terminus of a
CC myosin light chain. Also regulates actin-myosin interaction through a
CC non-kinase activity (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: Interacts with SVIL. {ECO:0000250}.
CC -!- PTM: The C-terminus is deglutamylated by AGTPBP1/CCP1, AGBL1/CCP4 and
CC AGBL4/CCP6, leading to the formation of Myosin light chain kinase,
CC smooth muscle, deglutamylated form. The consequences of C-terminal
CC deglutamylation are unknown (By similarity). {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; D89497; BAA13970.1; -; mRNA.
DR AlphaFoldDB; P79280; -.
DR STRING; 9823.ENSSSCP00000012639; -.
DR PaxDb; P79280; -.
DR PeptideAtlas; P79280; -.
DR PRIDE; P79280; -.
DR eggNOG; KOG0613; Eukaryota.
DR ChiTaRS; MYLK; pig.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR GO; GO:0032154; C:cleavage furrow; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0030027; C:lamellipodium; IBA:GO_Central.
DR GO; GO:0001725; C:stress fiber; IBA:GO_Central.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0004687; F:myosin light chain kinase activity; IBA:GO_Central.
DR GO; GO:0004672; F:protein kinase activity; IBA:GO_Central.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0014820; P:tonic smooth muscle contraction; IBA:GO_Central.
DR Gene3D; 2.60.40.10; -; 2.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR013098; Ig_I-set.
DR Pfam; PF07679; I-set; 2.
DR SUPFAM; SSF48726; SSF48726; 2.
PE 2: Evidence at transcript level;
KW Actin-binding; ATP-binding; Calmodulin-binding; Kinase; Nucleotide-binding;
KW Reference proteome; Serine/threonine-protein kinase; Transferase.
FT CHAIN <1..>139
FT /note="Myosin light chain kinase, smooth muscle"
FT /id="PRO_0000086406"
FT REGION 48..97
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT NON_TER 139
SQ SEQUENCE 139 AA; 15000 MW; 757EBD733367CD17 CRC64;
FIVLSQEGSL CSISIEKALP EDRGLYKCVA KNSAGQAECS CQVTVDDAPT GENAKAPEMK
ARRPKSSLPP VLGTESDATV KKKPAPKTPP KAAMPPQIIQ FPEDQKVRAG ESVELFGKVA
GTQPITCTWM KFRKQIQES
