LOCUS       NP_001104280             786 aa            linear   ROD 27-APR-2025
DEFINITION  myosin light chain kinase 3 [Rattus norvegicus].
ACCESSION   NP_001104280 XP_001064628 XP_214645
VERSION     NP_001104280.1
DBSOURCE    REFSEQ: accession NM_001110810.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 786)
  AUTHORS   Avila-Rodriguez,D., Solano Agama,C., Gonzalez-Pozos,S., Vicente
            Mendez-Mendez,J., Ortiz Plata,A., Arreola-Mendoza,L. and
            Mendoza-Garrido,M.E.
  TITLE     The shift in GH3 cell shape and cell motility is dependent on MLCK
            and ROCK
  JOURNAL   Exp Cell Res 354 (1), 1-17 (2017)
   PUBMED   28300565
  REMARK    GeneRIF: We found that a rounded shape with high cortical tension
            depends on MLCK and ROCK, whereas in cells with an elongated shape,
            MLCK is the primary protein responsible for cell spreading.
            Further, in cells with a slow and directionally persistent
            motility, MLCK predominates, while rapid and erratic movement is
            ROCK-dependent
REFERENCE   2  (residues 1 to 786)
  AUTHORS   Eikemo,H., Moltzau,L.R., Hussain,R.I., Nguyen,C.H., Qvigstad,E.,
            Levy,F.O., Skomedal,T. and Osnes,J.B.
  TITLE     CaMKII in addition to MLCK contributes to phosphorylation of
            regulatory light chain in cardiomyocytes
  JOURNAL   Biochem Biophys Res Commun 471 (1), 219-225 (2016)
   PUBMED   26809094
  REMARK    GeneRIF: In conclusion, in addition to MLCK, CaMKII phosphorylates
            RLC in cardiomyocytes.
REFERENCE   3  (residues 1 to 786)
  AUTHORS   Gao,L., Zheng,Y.J., Gu,S.S., Tan,J.L., Paul,C., Wang,Y.G. and
            Yang,H.T.
  TITLE     Degradation of cardiac myosin light chain kinase by matrix
            metalloproteinase-2 contributes to myocardial contractile
            dysfunction during ischemia/reperfusion
  JOURNAL   J Mol Cell Cardiol 77, 102-112 (2014)
   PUBMED   25451385
  REMARK    GeneRIF: Ischemia/reperfusion-activated MMP-2 leads to the
            degradation of cardiac MLCK.
REFERENCE   4  (residues 1 to 786)
  AUTHORS   Al-Sadi,R., Ye,D., Dokladny,K. and Ma,T.Y.
  TITLE     Mechanism of IL-1beta-induced increase in intestinal epithelial
            tight junction permeability
  JOURNAL   J Immunol 180 (8), 5653-5661 (2008)
   PUBMED   18390750
REFERENCE   5  (residues 1 to 786)
  AUTHORS   Chan,J.Y., Takeda,M., Briggs,L.E., Graham,M.L., Lu,J.T.,
            Horikoshi,N., Weinberg,E.O., Aoki,H., Sato,N., Chien,K.R. and
            Kasahara,H.
  TITLE     Identification of cardiac-specific myosin light chain kinase
  JOURNAL   Circ Res 102 (5), 571-580 (2008)
   PUBMED   18202317
REFERENCE   6  (residues 1 to 786)
  AUTHORS   Seguchi,O., Takashima,S., Yamazaki,S., Asakura,M., Asano,Y.,
            Shintani,Y., Wakeno,M., Minamino,T., Kondo,H., Furukawa,H.,
            Nakamaru,K., Naito,A., Takahashi,T., Ohtsuka,T., Kawakami,K.,
            Isomura,T., Kitamura,S., Tomoike,H., Mochizuki,N. and Kitakaze,M.
  TITLE     A cardiac myosin light chain kinase regulates sarcomere assembly in
            the vertebrate heart
  JOURNAL   J Clin Invest 117 (10), 2812-2824 (2007)
   PUBMED   17885681
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from EU236721.1.
            
            On or before Nov 24, 2007 this sequence version replaced
            XP_001064628.1, XP_214645.4.
            
            ##Evidence-Data-START##
            Transcript exon combination :: EU236721.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760434, SAMN06621351
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..786
                     /organism="Rattus norvegicus"
                     /strain="W"
                     /db_xref="taxon:10116"
                     /chromosome="19"
                     /map="19q11"
     Protein         1..786
                     /product="myosin light chain kinase 3"
                     /EC_number="2.7.11.18"
                     /function="phosphorylates MLC-2v"
                     /note="cardiac-MLCK; cardiac-MyBP-C-associated Ca/CaM
                     kinase; putative myosin light chain kinase 3"
                     /calculated_mol_wt=85380
     Site            155
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (E9PT87.1)"
     Region          233..258
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (E9PT87.1)"
     Region          279..315
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (E9PT87.1)"
     Region          333..443
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (E9PT87.1)"
     Site            341
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (E9PT87.1)"
     Site            422
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (E9PT87.1)"
     Region          477..737
                     /region_name="STKc_MLCK3"
                     /note="Catalytic domain of the Serine/Threonine Kinase,
                     Myosin Light Chain Kinase 3; cd14192"
                     /db_xref="CDD:271094"
     Site            order(488..492,494,496,509,511,540,556..557,559,563,565,
                     603,605,607..608,610,622..623,626,641..644)
                     /site_type="active"
                     /db_xref="CDD:271094"
     Site            order(488..492,494,496,509,511,540,556..557,559,563,
                     607..608,610,622..623)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:271094"
     Site            order(492,563,565,603,605,607,626,641..644)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:271094"
     Site            622..644
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:271094"
     CDS             1..786
                     /gene="Mylk3"
                     /gene_synonym="MLCK; RGD1305801"
                     /coded_by="NM_001110810.1:238..2598"
                     /db_xref="GeneID:291926"
                     /db_xref="RGD:1305801"
ORIGIN      
        1 msgvseedpe glgpqglpal ggaclvtvdk klnvltekvd rllhfqedvt eklqcvcqgm
       61 dhleqglhrl easqelglag pgstspaaaq aawpevlelv ravrqegaqh garlealfkm
      121 vvavdraitl vgstiqnskv ddfilqgtvp wrkgsladgp eenkeqaeva gvkpkhvlnt
      181 gsvqaatsra lweesqkqdt pvgtveglpl iidtslkgad ltqagaslrq gvealdpgqe
      241 pppaeaesrl palasedtgt tlelsvaidr isevltslrm sqsagegtss skpdcsepgp
      301 qplgplttds dihsdeglpr isvrmremtt peelfetqgg spigsaeapg pgtvledqip
      361 kgarpfpplp krscnnggas aeeatgpgae pirgpslvtr dwrdepvgtt dlqqgrdpga
      421 vspepgkdha aqgpgrteag rrvssaaeaa ivvlddsaap papfehrvvs ikdtlistsy
      481 tvsqhevlgg grfgqvhrct erstglalaa kiikvknikd redvkneini mnqlshvnli
      541 qlydafeskn sftlimeyvd ggelfdritd ekyhlteldv vlftrqiceg vhylhqhyil
      601 hldlkpenil cvsqtghqik iidfglarry kpreklkvnf gtpeflapev vnyefvsfpt
      661 dmwsvgvity mllsglspfl getdaetmnf ivncswdfda dtfkglseea kdfvsrllvk
      721 ekscrmsatq clkhewlnhl iakasgsnvr lrsqlllqky maqrkwkkhf hvvtavnrlr
      781 kfptcp
//
