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Myosin regulatory light chain 2, ventricular/cardiac muscle isoform (MLC-2) (MLC-2v) (Cardiac myosin light chain 2) (Myosin light chain 2, slow skeletal/ventricular muscle isoform) (MLC-2s/v) (Ventricular myosin light chain 2)

 MLRV_HUMAN              Reviewed;         166 AA.
P10916; Q16123;
01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
28-FEB-2018, entry version 180.
RecName: Full=Myosin regulatory light chain 2, ventricular/cardiac muscle isoform {ECO:0000305};
Short=MLC-2 {ECO:0000250|UniProtKB:P08733};
Short=MLC-2v;
AltName: Full=Cardiac myosin light chain 2 {ECO:0000303|Ref.3};
AltName: Full=Myosin light chain 2, slow skeletal/ventricular muscle isoform {ECO:0000250|UniProtKB:Q7M2V4};
Short=MLC-2s/v {ECO:0000250|UniProtKB:Q7M2V4};
AltName: Full=Ventricular myosin light chain 2 {ECO:0000303|PubMed:2704627};
Name=MYL2 {ECO:0000312|HGNC:HGNC:7583};
Synonyms=MLC2 {ECO:0000303|PubMed:8287067};
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Heart;
PubMed=2704627; DOI=10.1093/nar/17.6.2360;
Libera L.D., Hoffmann E., Floroff M., Jackowski G.;
"Isolation and nucleotide sequence of the cDNA encoding human
ventricular myosin light chain 2.";
Nucleic Acids Res. 17:2360-2360(1989).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Muscle;
Wu Q.L.;
Submitted (MAR-1996) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [MRNA].
Margossian S.S., Umeda P.K., Sciaky D., Anderson P.A.W.;
Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=8287067;
Wadgaonkar R., Shafiq S., Rajmanickam C., Siddiqui M.A.;
"Interaction of a conserved peptide domain in recombinant human
ventricular myosin light chain-2 with myosin heavy chain.";
Cell. Mol. Biol. Res. 39:13-26(1993).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Prostate, and Skeletal muscle;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
PROTEIN SEQUENCE OF 138-144.
TISSUE=Heart;
PubMed=7498159; DOI=10.1002/elps.11501601192;
Kovalyov L.I., Shishkin S.S., Efimochkin A.S., Kovalyova M.A.,
Ershova E.S., Egorov T.A., Musalyamov A.K.;
"The major protein expression profile and two-dimensional protein
database of human heart.";
Electrophoresis 16:1160-1169(1995).
[7]
INTERACTION WITH MYOC.
PubMed=11773029;
Wentz-Hunter K., Ueda J., Yue B.Y.;
"Protein interactions with myocilin.";
Invest. Ophthalmol. Vis. Sci. 43:176-182(2002).
[8]
PHOSPHORYLATION AT SER-15 BY DAPK3, AND IDENTIFICATION BY MASS
SPECTROMETRY.
PubMed=20038585; DOI=10.1074/jbc.C109.076489;
Chang A.N., Chen G., Gerard R.D., Kamm K.E., Stull J.T.;
"Cardiac myosin is a substrate for zipper-interacting protein kinase
(ZIPK).";
J. Biol. Chem. 285:5122-5126(2010).
[9]
PHOSPHORYLATION AT SER-15, DEAMIDATION AT ASN-14, AND IDENTIFICATION
BY MASS SPECTROMETRY.
PubMed=20445002; DOI=10.1074/mcp.M110.000075;
Scruggs S.B., Reisdorph R., Armstrong M.L., Warren C.M., Reisdorph N.,
Solaro R.J., Buttrick P.M.;
"A novel, in-solution separation of endogenous cardiac sarcomeric
proteins and identification of distinct charged variants of regulatory
light chain.";
Mol. Cell. Proteomics 9:1804-1818(2010).
[10]
VARIANTS CMH10 THR-13; LYS-22 AND ALA-95.
PubMed=8673105; DOI=10.1038/ng0596-63;
Poetter K., Jiang H., Hassanzadeh S., Master S.R., Chang A.,
Dalakas M.C., Rayment I., Sellers J.R., Fananapazir L., Epstein N.D.;
"Mutations in either the essential or regulatory light chains of
myosin are associated with a rare myopathy in human heart and skeletal
muscle.";
Nat. Genet. 13:63-69(1996).
[11]
VARIANTS CMH10 LEU-18 AND GLN-58.
PubMed=9535554; DOI=10.1007/s001090050210;
Flavigny J., Richard P., Isnard R., Carrier L., Charron P., Bonne G.,
Forissier J.F., Desnos M., Dubourg O., Komajda M., Schwartz K.,
Hainque B.;
"Identification of two novel mutations in the ventricular regulatory
myosin light chain gene (MYL2) associated with familial and classical
forms of hypertrophic cardiomyopathy.";
J. Mol. Med. 76:208-214(1998).
[12]
VARIANTS CMH10 THR-13; LEU-18; LYS-22; GLN-58 AND ALA-95, AND
CHARACTERIZATION OF VARIANTS CMH10 THR-13; LEU-18; LYS-22; GLN-58 AND
ALA-95.
PubMed=11102452; DOI=10.1074/jbc.M009823200;
Szczesna D., Ghosh D., Li Q., Gomes A.V., Guzman G., Arana C., Zhi G.,
Stull J.T., Potter J.D.;
"Familial hypertrophic cardiomyopathy mutations in the regulatory
light chains of myosin affect their structure, Ca2+ binding, and
phosphorylation.";
J. Biol. Chem. 276:7086-7092(2001).
[13]
VARIANTS CMH10 LYS-22 AND GLN-58.
PubMed=12404107; DOI=10.1038/sj.ejhg.5200872;
Kabaeva Z.T., Perrot A., Wolter B., Dietz R., Cardim N., Correia J.M.,
Schulte H.D., Aldashev A.A., Mirrakhimov M.M., Osterziel K.J.;
"Systematic analysis of the regulatory and essential myosin light
chain genes: genetic variants and mutations in hypertrophic
cardiomyopathy.";
Eur. J. Hum. Genet. 10:741-748(2002).
[14]
VARIANT CMH10 VAL-166.
PubMed=12707239; DOI=10.1161/01.CIR.0000066323.15244.54;
Richard P., Charron P., Carrier L., Ledeuil C., Cheav T.,
Pichereau C., Benaiche A., Isnard R., Dubourg O., Burban M.,
Gueffet J.-P., Millaire A., Desnos M., Schwartz K., Hainque B.,
Komajda M.;
"Hypertrophic cardiomyopathy: distribution of disease genes, spectrum
of mutations, and implications for a molecular diagnosis strategy.";
Circulation 107:2227-2232(2003).
[15]
ERRATUM.
Richard P., Charron P., Carrier L., Ledeuil C., Cheav T.,
Pichereau C., Benaiche A., Isnard R., Dubourg O., Burban M.,
Gueffet J.-P., Millaire A., Desnos M., Schwartz K., Hainque B.,
Komajda M.;
Circulation 109:3258-3258(2004).
[16]
VARIANT CMH10 GLN-58.
PubMed=12818575; DOI=10.1016/S0022-2828(03)00146-9;
Moerner S., Richard P., Kazzam E., Hellman U., Hainque B.,
Schwartz K., Waldenstroem A.;
"Identification of the genotypes causing hypertrophic cardiomyopathy
in northern Sweden.";
J. Mol. Cell. Cardiol. 35:841-849(2003).
-!- FUNCTION: Contractile protein that plays a role in heart
development and function (By similarity). Following
phosphorylation, plays a role in cross-bridge cycling kinetics and
cardiac muscle contraction by increasing myosin lever arm
stiffness and promoting myosin head diffusion; as a consequence of
the increase in maximum contraction force and calcium sensitivity
of contraction force. These events altogether slow down myosin
kinetics and prolong duty cycle resulting in accumulated myosins
being cooperatively recruited to actin binding sites to sustain
thin filament activation as a means to fine-tune myofilament
calcium sensitivity to force (By similarity). During cardiogenesis
plays an early role in cardiac contractility by promoting cardiac
myofibril assembly (By similarity). {ECO:0000250|UniProtKB:P08733,
ECO:0000250|UniProtKB:P51667}.
-!- SUBUNIT: Myosin is a hexamer of 2 heavy chains and 4 light chains.
Interacts with MYOC (PubMed:11773029). {ECO:0000250,
ECO:0000269|PubMed:11773029}.
-!- INTERACTION:
Q99972:MYOC; NbExp=7; IntAct=EBI-725770, EBI-11692272;
P35125-3:USP6; NbExp=5; IntAct=EBI-725770, EBI-954590;
-!- SUBCELLULAR LOCATION: Cytoplasm, myofibril, sarcomere, A band
{ECO:0000250|UniProtKB:P08733}.
-!- PTM: N-terminus is methylated by METTL11A/NTM1.
{ECO:0000250|UniProtKB:P51667}.
-!- PTM: Phosphorylated by MYLK3 and MYLK2; promotes cardiac muscle
contraction and function (By similarity). Dephosphorylated by
PPP1CB complexed to PPP1R12B (By similarity). The phosphorylated
form in adult is expressed as gradients across the heart from
endocardium (low phosphorylation) to epicardium (high
phosphorylation); regulates cardiac torsion and workload
distribution (By similarity). {ECO:0000250|UniProtKB:P08733,
ECO:0000250|UniProtKB:P51667}.
-!- DISEASE: Cardiomyopathy, familial hypertrophic 10 (CMH10)
[MIM:608758]: A hereditary heart disorder characterized by
ventricular hypertrophy, which is usually asymmetric and often
involves the interventricular septum. The symptoms include
dyspnea, syncope, collapse, palpitations, and chest pain. They can
be readily provoked by exercise. The disorder has inter- and
intrafamilial variability ranging from benign to malignant forms
with high risk of cardiac failure and sudden cardiac death.
Rarely, patients present a variant of familial hypertrophic
cardiomyopathy, characterized by mid-left ventricular chamber
thickening. {ECO:0000269|PubMed:11102452,
ECO:0000269|PubMed:12404107, ECO:0000269|PubMed:12707239,
ECO:0000269|PubMed:12818575, ECO:0000269|PubMed:8673105,
ECO:0000269|PubMed:9535554}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- MISCELLANEOUS: This chain binds calcium.
-----------------------------------------------------------------------
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EMBL; X14332; CAA32510.1; -; mRNA.
EMBL; M22815; AAA91832.1; -; mRNA.
EMBL; AF020768; AAB91993.1; -; mRNA.
EMBL; S69022; AAB29658.2; -; mRNA.
EMBL; BC015821; AAH15821.1; -; mRNA.
EMBL; BC031006; AAH31006.1; -; mRNA.
EMBL; BC031008; AAH31008.1; -; mRNA.
CCDS; CCDS31901.1; -.
RefSeq; NP_000423.2; NM_000432.3.
UniGene; Hs.75535; -.
PDB; 5TBY; EM; 20.00 A; E/F=1-166.
PDBsum; 5TBY; -.
ProteinModelPortal; P10916; -.
SMR; P10916; -.
BioGrid; 110717; 13.
IntAct; P10916; 6.
STRING; 9606.ENSP00000228841; -.
ChEMBL; CHEMBL3831286; -.
iPTMnet; P10916; -.
PhosphoSitePlus; P10916; -.
BioMuta; MYL2; -.
DMDM; 6166556; -.
UCD-2DPAGE; P10916; -.
PaxDb; P10916; -.
PeptideAtlas; P10916; -.
PRIDE; P10916; -.
DNASU; 4633; -.
Ensembl; ENST00000228841; ENSP00000228841; ENSG00000111245.
GeneID; 4633; -.
KEGG; hsa:4633; -.
CTD; 4633; -.
DisGeNET; 4633; -.
EuPathDB; HostDB:ENSG00000111245.14; -.
GeneCards; MYL2; -.
GeneReviews; MYL2; -.
HGNC; HGNC:7583; MYL2.
HPA; HPA019763; -.
HPA; HPA039262; -.
MalaCards; MYL2; -.
MIM; 160781; gene.
MIM; 608758; phenotype.
neXtProt; NX_P10916; -.
OpenTargets; ENSG00000111245; -.
Orphanet; 2020; Congenital fiber-type disproportion myopathy.
Orphanet; 155; Familial isolated hypertrophic cardiomyopathy.
PharmGKB; PA31380; -.
eggNOG; KOG0031; Eukaryota.
eggNOG; COG5126; LUCA.
GeneTree; ENSGT00760000119196; -.
HOGENOM; HOG000233018; -.
HOVERGEN; HBG012180; -.
InParanoid; P10916; -.
KO; K10351; -.
OMA; IVTHRAE; -.
OrthoDB; EOG091G0QF6; -.
PhylomeDB; P10916; -.
TreeFam; TF314218; -.
Reactome; R-HSA-390522; Striated Muscle Contraction.
SIGNOR; P10916; -.
ChiTaRS; MYL2; human.
GeneWiki; MYL2; -.
GenomeRNAi; 4633; -.
PRO; PR:P10916; -.
Proteomes; UP000005640; Chromosome 12.
Bgee; ENSG00000111245; -.
CleanEx; HS_MYL2; -.
ExpressionAtlas; P10916; baseline and differential.
Genevisible; P10916; HS.
GO; GO:0031672; C:A band; IEA:UniProtKB-SubCell.
GO; GO:0097512; C:cardiac myofibril; IDA:CAFA.
GO; GO:0005856; C:cytoskeleton; IDA:BHF-UCL.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0030016; C:myofibril; NAS:BHF-UCL.
GO; GO:0016459; C:myosin complex; TAS:BHF-UCL.
GO; GO:0030017; C:sarcomere; TAS:BHF-UCL.
GO; GO:0003785; F:actin monomer binding; IDA:BHF-UCL.
GO; GO:0005509; F:calcium ion binding; IDA:MGI.
GO; GO:0032036; F:myosin heavy chain binding; NAS:BHF-UCL.
GO; GO:0008307; F:structural constituent of muscle; TAS:ProtInc.
GO; GO:0060048; P:cardiac muscle contraction; IEA:Ensembl.
GO; GO:0055003; P:cardiac myofibril assembly; ISS:BHF-UCL.
GO; GO:0060047; P:heart contraction; ISS:BHF-UCL.
GO; GO:0007507; P:heart development; ISS:UniProtKB.
GO; GO:0042694; P:muscle cell fate specification; IEA:Ensembl.
GO; GO:0048747; P:muscle fiber development; IEA:Ensembl.
GO; GO:0030049; P:muscle filament sliding; TAS:Reactome.
GO; GO:0030308; P:negative regulation of cell growth; IMP:BHF-UCL.
GO; GO:0098735; P:positive regulation of the force of heart contraction; ISS:UniProtKB.
GO; GO:0009791; P:post-embryonic development; IEA:Ensembl.
GO; GO:0006942; P:regulation of striated muscle contraction; TAS:ProtInc.
GO; GO:0002026; P:regulation of the force of heart contraction; ISS:UniProtKB.
GO; GO:0055010; P:ventricular cardiac muscle tissue morphogenesis; IMP:BHF-UCL.
CDD; cd00051; EFh; 1.
InterPro; IPR011992; EF-hand-dom_pair.
InterPro; IPR018247; EF_Hand_1_Ca_BS.
InterPro; IPR002048; EF_hand_dom.
Pfam; PF13405; EF-hand_6; 1.
SMART; SM00054; EFh; 3.
SUPFAM; SSF47473; SSF47473; 1.
PROSITE; PS00018; EF_HAND_1; 1.
PROSITE; PS50222; EF_HAND_2; 3.
1: Evidence at protein level;
3D-structure; Calcium; Cardiomyopathy; Complete proteome; Cytoplasm;
Direct protein sequencing; Disease mutation; Metal-binding;
Methylation; Motor protein; Muscle protein; Myosin; Phosphoprotein;
Polymorphism; Reference proteome; Repeat.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:P51667}.
CHAIN 2 166 Myosin regulatory light chain 2,
ventricular/cardiac muscle isoform.
/FTId=PRO_0000198727.
DOMAIN 24 59 EF-hand 1. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
DOMAIN 94 129 EF-hand 2. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
DOMAIN 130 165 EF-hand 3. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
CA_BIND 37 48
MOD_RES 2 2 N,N,N-trimethylalanine.
{ECO:0000250|UniProtKB:P51667}.
MOD_RES 14 14 Deamidated asparagine.
{ECO:0000269|PubMed:20445002}.
MOD_RES 15 15 Phosphoserine; by ZIPK/DAPK3.
{ECO:0000269|PubMed:20038585,
ECO:0000269|PubMed:20445002}.
MOD_RES 19 19 Phosphoserine.
{ECO:0000250|UniProtKB:P51667}.
MOD_RES 52 52 Phosphothreonine.
{ECO:0000250|UniProtKB:P08733}.
VARIANT 13 13 A -> T (in CMH10; with mid-left
ventricular chamber thickening; decrease
calcium binding affinity; large increase
in its calcium binding affinity upon
phosphorylation; dbSNP:rs104894363).
{ECO:0000269|PubMed:11102452,
ECO:0000269|PubMed:8673105}.
/FTId=VAR_004601.
VARIANT 18 18 F -> L (in CMH10; decrease calcium
binding affinity; dbSNP:rs104894370).
{ECO:0000269|PubMed:11102452,
ECO:0000269|PubMed:9535554}.
/FTId=VAR_004602.
VARIANT 22 22 E -> K (in CMH10; some patients present
with mid-left ventricular chamber
thickening; significantly decrease
calcium binding affinity; loss of
phosphorylation; dbSNP:rs104894368).
{ECO:0000269|PubMed:11102452,
ECO:0000269|PubMed:12404107,
ECO:0000269|PubMed:8673105}.
/FTId=VAR_004603.
VARIANT 57 57 G -> R (in dbSNP:rs2428140).
/FTId=VAR_029449.
VARIANT 58 58 R -> Q (in CMH10; impairs calcium
binding; bind calcium upon
phosphorylation; dbSNP:rs104894369).
{ECO:0000269|PubMed:11102452,
ECO:0000269|PubMed:12404107,
ECO:0000269|PubMed:12818575,
ECO:0000269|PubMed:9535554}.
/FTId=VAR_004604.
VARIANT 95 95 P -> A (in CMH10; with mid-left
ventricular chamber thickening; decrease
calcium binding affinity;
dbSNP:rs121913658).
{ECO:0000269|PubMed:11102452,
ECO:0000269|PubMed:8673105}.
/FTId=VAR_004605.
VARIANT 166 166 D -> V (in CMH10; dbSNP:rs199474815).
{ECO:0000269|PubMed:12707239}.
/FTId=VAR_019844.
SEQUENCE 166 AA; 18789 MW; EA0BEF886AA3FAF5 CRC64;
MAPKKAKKRA GGANSNVFSM FEQTQIQEFK EAFTIMDQNR DGFIDKNDLR DTFAALGRVN
VKNEEIDEMI KEAPGPINFT VFLTMFGEKL KGADPEETIL NAFKVFDPEG KGVLKADYVR
EMLTTQAERF SKEEVDQMFA AFPPDVTGNL DYKNLVHIIT HGEEKD


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