ID MYLK3_PONAB Reviewed; 819 AA.
AC Q5RDG7;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 3.
DT 08-NOV-2023, entry version 90.
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;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Heart;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Kinase that phosphorylates MYL2 in vitro. Promotes sarcomere
CC formation in cardiomyocytes and increases cardiomyocyte contractility
CC (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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
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}.
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DR EMBL; CR857943; CAH90190.1; -; mRNA.
DR RefSeq; NP_001125070.1; NM_001131598.2.
DR AlphaFoldDB; Q5RDG7; -.
DR SMR; Q5RDG7; -.
DR STRING; 9601.ENSPPYP00000008714; -.
DR GeneID; 100171951; -.
DR KEGG; pon:100171951; -.
DR CTD; 91807; -.
DR eggNOG; KOG0032; Eukaryota.
DR InParanoid; Q5RDG7; -.
DR OrthoDB; 5402680at2759; -.
DR Proteomes; UP000001595; 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; IEA:UniProtKB-EC.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd14192; STKc_MLCK3; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
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 PANTHER; PTHR24342:SF15; DEATH-ASSOCIATED PROTEIN KINASE 2; 1.
DR PANTHER; PTHR24342; SERINE/THREONINE-PROTEIN KINASE 17; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 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; Magnesium; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Serine/threonine-protein kinase;
KW Transferase.
FT CHAIN 1..819
FT /note="Myosin light chain kinase 3"
FT /id="PRO_0000272202"
FT DOMAIN 515..770
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 146..460
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 152..172
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 636
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 521..529
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 544
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 152
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:E9PT87"
FT MOD_RES 355
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:E9PT87"
FT MOD_RES 401
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q32MK0"
FT MOD_RES 408
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q32MK0"
SQ SEQUENCE 819 AA; 88376 MW; A2D3BB10DFA6DFC1 CRC64;
MSGTSKESLG HGGLPGLGKA CLTTMDKKLN MLNEKVDQLL HFQEDVTEKL QSMCRDMGHL
ERGLHRLEAS RAPGPGGTDG VLRVDTQAGW PEVLELVRAM QQDAAQHGAR LEALFRMVAA
VDRAIALVGA TFQKSKVADF LMQGRVPWRR GSPGDSPEEN KERVEEEGAK PKHVLSASGV
QSDAREPGEE SQKADVLEGT VERLPPIRAS GLGADPAQAV VSPGQGDGVP GPAQAFPGHL
PLPTKGEAKA PETPSENLRT GLELAPAPGR VSVVSPSLEV APGAGQGASS SRPDPEPLEE
GTRLTPGPGP QCPGPPGLPA QARAAHSGGE TPPRISIHIQ EMGTPGEMLV TGRGSLGPTL
TTDAPAAAQP GKQGPPGTGR CHQAPGTEPG EQTPEGAREL SLLQESSSPG GVKAEEEQRA
GAEPGTRPSL ARSDDNDHKV GALGLQQGKS PGVGNPEPEQ DCAARAPVRA EAVRRTPPGA
EAGSMVLDDS PAPPAPFEHR LVSVKETSIS AGYEVCQHEV LGGGRFGQVH RCTEKSTGLP
LAAKIIKVKS AKDREDVKNE INIMNQLSHV NLIQLYDAFE SKHSCTLVME YVDGGELFDR
ITDEKYHLTE LDVVLFTRQI CEGVHYLHQH YILHLDLKPE NILCVNQTGH QIKIIDFGLA
RRYKPREKLK VNFGTPEFLA PEVVNYEFVS FPTDMWSVGV ITYMLLSGLS PFLGETDAET
MNFIVNCSWD FDADTFEGLS EEAKDFVSRL LVKEESCRMS ATQCLKHEWL NNLPAKALRS
KTRLKSQLLL QKYIAQRKWK KHFYVVTAAN RLRKFPTCP
//
