MLRV_HUMAN
ID MLRV_HUMAN Reviewed; 166 AA.
AC P10916; Q16123;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 203.
DE RecName: Full=Myosin regulatory light chain 2, ventricular/cardiac muscle isoform {ECO:0000305};
DE Short=MLC-2 {ECO:0000250|UniProtKB:P08733};
DE Short=MLC-2v;
DE AltName: Full=Cardiac myosin light chain 2 {ECO:0000303|Ref.3};
DE AltName: Full=Myosin light chain 2, slow skeletal/ventricular muscle isoform {ECO:0000250|UniProtKB:Q7M2V4};
DE Short=MLC-2s/v {ECO:0000250|UniProtKB:Q7M2V4};
DE AltName: Full=Ventricular myosin light chain 2 {ECO:0000303|PubMed:2704627};
GN Name=MYL2 {ECO:0000312|HGNC:HGNC:7583};
GN Synonyms=MLC2 {ECO:0000303|PubMed:8287067};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Heart;
RX PubMed=2704627; DOI=10.1093/nar/17.6.2360;
RA Libera L.D., Hoffmann E., Floroff M., Jackowski G.;
RT "Isolation and nucleotide sequence of the cDNA encoding human ventricular
RT myosin light chain 2.";
RL Nucleic Acids Res. 17:2360-2360(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Muscle;
RA Wu Q.L.;
RL Submitted (MAR-1996) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Margossian S.S., Umeda P.K., Sciaky D., Anderson P.A.W.;
RL Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8287067;
RA Wadgaonkar R., Shafiq S., Rajmanickam C., Siddiqui M.A.;
RT "Interaction of a conserved peptide domain in recombinant human ventricular
RT myosin light chain-2 with myosin heavy chain.";
RL Cell. Mol. Biol. Res. 39:13-26(1993).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Prostate, and Skeletal muscle;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP PROTEIN SEQUENCE OF 138-144.
RC TISSUE=Heart;
RX PubMed=7498159; DOI=10.1002/elps.11501601192;
RA Kovalyov L.I., Shishkin S.S., Efimochkin A.S., Kovalyova M.A.,
RA Ershova E.S., Egorov T.A., Musalyamov A.K.;
RT "The major protein expression profile and two-dimensional protein database
RT of human heart.";
RL Electrophoresis 16:1160-1169(1995).
RN [7]
RP INTERACTION WITH MYOC.
RX PubMed=11773029;
RA Wentz-Hunter K., Ueda J., Yue B.Y.;
RT "Protein interactions with myocilin.";
RL Invest. Ophthalmol. Vis. Sci. 43:176-182(2002).
RN [8]
RP PHOSPHORYLATION AT SER-15 BY DAPK3, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=20038585; DOI=10.1074/jbc.c109.076489;
RA Chang A.N., Chen G., Gerard R.D., Kamm K.E., Stull J.T.;
RT "Cardiac myosin is a substrate for zipper-interacting protein kinase
RT (ZIPK).";
RL J. Biol. Chem. 285:5122-5126(2010).
RN [9]
RP PHOSPHORYLATION AT SER-15, DEAMIDATION AT ASN-14, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=20445002; DOI=10.1074/mcp.m110.000075;
RA Scruggs S.B., Reisdorph R., Armstrong M.L., Warren C.M., Reisdorph N.,
RA Solaro R.J., Buttrick P.M.;
RT "A novel, in-solution separation of endogenous cardiac sarcomeric proteins
RT and identification of distinct charged variants of regulatory light
RT chain.";
RL Mol. Cell. Proteomics 9:1804-1818(2010).
RN [10]
RP INVOLVEMENT IN MFM12, FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=23365102; DOI=10.1093/brain/aws293;
RA Weterman M.A., Barth P.G., van Spaendonck-Zwarts K.Y., Aronica E.,
RA Poll-The B.T., Brouwer O.F., van Tintelen J.P., Qahar Z., Bradley E.J.,
RA de Wissel M., Salviati L., Angelini C., van den Heuvel L., Thomasse Y.E.,
RA Backx A.P., Nuernberg G., Nuernberg P., Baas F.;
RT "Recessive MYL2 mutations cause infantile type I muscle fibre disease and
RT cardiomyopathy.";
RL Brain 136:282-293(2013).
RN [11]
RP INVOLVEMENT IN MFM12, FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=32453731; DOI=10.1371/journal.pgen.1008639;
RA Manivannan S.N., Darouich S., Masmoudi A., Gordon D., Zender G., Han Z.,
RA Fitzgerald-Butt S., White P., McBride K.L., Kharrat M., Garg V.;
RT "Novel frameshift variant in MYL2 reveals molecular differences between
RT dominant and recessive forms of hypertrophic cardiomyopathy.";
RL PLoS Genet. 16:e1008639-e1008639(2020).
RN [12]
RP VARIANTS CMH10 THR-13; LYS-22 AND ALA-95.
RX PubMed=8673105; DOI=10.1038/ng0596-63;
RA Poetter K., Jiang H., Hassanzadeh S., Master S.R., Chang A., Dalakas M.C.,
RA Rayment I., Sellers J.R., Fananapazir L., Epstein N.D.;
RT "Mutations in either the essential or regulatory light chains of myosin are
RT associated with a rare myopathy in human heart and skeletal muscle.";
RL Nat. Genet. 13:63-69(1996).
RN [13]
RP VARIANTS CMH10 LEU-18 AND GLN-58.
RX PubMed=9535554; DOI=10.1007/s001090050210;
RA Flavigny J., Richard P., Isnard R., Carrier L., Charron P., Bonne G.,
RA Forissier J.F., Desnos M., Dubourg O., Komajda M., Schwartz K., Hainque B.;
RT "Identification of two novel mutations in the ventricular regulatory myosin
RT light chain gene (MYL2) associated with familial and classical forms of
RT hypertrophic cardiomyopathy.";
RL J. Mol. Med. 76:208-214(1998).
RN [14]
RP VARIANTS CMH10 THR-13; LEU-18; LYS-22; GLN-58 AND ALA-95, AND
RP CHARACTERIZATION OF VARIANTS CMH10 THR-13; LEU-18; LYS-22; GLN-58 AND
RP ALA-95.
RX PubMed=11102452; DOI=10.1074/jbc.m009823200;
RA Szczesna D., Ghosh D., Li Q., Gomes A.V., Guzman G., Arana C., Zhi G.,
RA Stull J.T., Potter J.D.;
RT "Familial hypertrophic cardiomyopathy mutations in the regulatory light
RT chains of myosin affect their structure, Ca2+ binding, and
RT phosphorylation.";
RL J. Biol. Chem. 276:7086-7092(2001).
RN [15]
RP VARIANTS CMH10 LYS-22 AND GLN-58.
RX PubMed=12404107; DOI=10.1038/sj.ejhg.5200872;
RA Kabaeva Z.T., Perrot A., Wolter B., Dietz R., Cardim N., Correia J.M.,
RA Schulte H.D., Aldashev A.A., Mirrakhimov M.M., Osterziel K.J.;
RT "Systematic analysis of the regulatory and essential myosin light chain
RT genes: genetic variants and mutations in hypertrophic cardiomyopathy.";
RL Eur. J. Hum. Genet. 10:741-748(2002).
RN [16]
RP VARIANT CMH10 VAL-166.
RX PubMed=12707239; DOI=10.1161/01.cir.0000066323.15244.54;
RA Richard P., Charron P., Carrier L., Ledeuil C., Cheav T., Pichereau C.,
RA Benaiche A., Isnard R., Dubourg O., Burban M., Gueffet J.-P., Millaire A.,
RA Desnos M., Schwartz K., Hainque B., Komajda M.;
RT "Hypertrophic cardiomyopathy: distribution of disease genes, spectrum of
RT mutations, and implications for a molecular diagnosis strategy.";
RL Circulation 107:2227-2232(2003).
RN [17]
RP ERRATUM OF PUBMED:12707239.
RA Richard P., Charron P., Carrier L., Ledeuil C., Cheav T., Pichereau C.,
RA Benaiche A., Isnard R., Dubourg O., Burban M., Gueffet J.-P., Millaire A.,
RA Desnos M., Schwartz K., Hainque B., Komajda M.;
RL Circulation 109:3258-3258(2004).
RN [18]
RP VARIANT CMH10 GLN-58.
RX PubMed=12818575; DOI=10.1016/s0022-2828(03)00146-9;
RA Moerner S., Richard P., Kazzam E., Hellman U., Hainque B., Schwartz K.,
RA Waldenstroem A.;
RT "Identification of the genotypes causing hypertrophic cardiomyopathy in
RT northern Sweden.";
RL J. Mol. Cell. Cardiol. 35:841-849(2003).
CC -!- FUNCTION: Contractile protein that plays a role in heart development
CC and function (PubMed:23365102, PubMed:32453731). Following
CC phosphorylation, plays a role in cross-bridge cycling kinetics and
CC cardiac muscle contraction by increasing myosin lever arm stiffness and
CC promoting myosin head diffusion; as a consequence of the increase in
CC maximum contraction force and calcium sensitivity of contraction force.
CC These events altogether slow down myosin kinetics and prolong duty
CC cycle resulting in accumulated myosins being cooperatively recruited to
CC actin binding sites to sustain thin filament activation as a means to
CC fine-tune myofilament calcium sensitivity to force (By similarity).
CC During cardiogenesis plays an early role in cardiac contractility by
CC promoting cardiac myofibril assembly (By similarity).
CC {ECO:0000250|UniProtKB:P08733, ECO:0000269|PubMed:23365102,
CC ECO:0000269|PubMed:32453731}.
CC -!- SUBUNIT: Myosin is a hexamer of 2 heavy chains and 4 light chains.
CC Interacts with MYOC (PubMed:11773029). {ECO:0000250,
CC ECO:0000269|PubMed:11773029}.
CC -!- INTERACTION:
CC P10916; P78412: IRX6; NbExp=3; IntAct=EBI-725770, EBI-12100506;
CC P10916; Q99972: MYOC; NbExp=7; IntAct=EBI-725770, EBI-11692272;
CC P10916; Q9UIG4: PSORS1C2; NbExp=3; IntAct=EBI-725770, EBI-11974061;
CC P10916; P35125-3: USP6; NbExp=5; IntAct=EBI-725770, EBI-954590;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, myofibril, sarcomere, A band
CC {ECO:0000250|UniProtKB:P08733}.
CC -!- TISSUE SPECIFICITY: Highly expressed in type I muscle fibers.
CC {ECO:0000269|PubMed:23365102, ECO:0000269|PubMed:32453731}.
CC -!- PTM: N-terminus is methylated by METTL11A/NTM1.
CC {ECO:0000250|UniProtKB:P51667}.
CC -!- PTM: Phosphorylated by MYLK3 and MYLK2; promotes cardiac muscle
CC contraction and function (By similarity). Dephosphorylated by PPP1CB
CC complexed to PPP1R12B (By similarity). The phosphorylated form in adult
CC is expressed as gradients across the heart from endocardium (low
CC phosphorylation) to epicardium (high phosphorylation); regulates
CC cardiac torsion and workload distribution (By similarity).
CC {ECO:0000250|UniProtKB:P08733, ECO:0000250|UniProtKB:P51667}.
CC -!- DISEASE: Cardiomyopathy, familial hypertrophic 10 (CMH10) [MIM:608758]:
CC A hereditary heart disorder characterized by ventricular hypertrophy,
CC which is usually asymmetric and often involves the interventricular
CC septum. The symptoms include dyspnea, syncope, collapse, palpitations,
CC and chest pain. They can be readily provoked by exercise. The disorder
CC has inter- and intrafamilial variability ranging from benign to
CC malignant forms with high risk of cardiac failure and sudden cardiac
CC death. Rarely, patients present a variant of familial hypertrophic
CC cardiomyopathy, characterized by mid-left ventricular chamber
CC thickening. {ECO:0000269|PubMed:11102452, ECO:0000269|PubMed:12404107,
CC ECO:0000269|PubMed:12707239, ECO:0000269|PubMed:12818575,
CC ECO:0000269|PubMed:8673105, ECO:0000269|PubMed:9535554}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- DISEASE: Myopathy, myofibrillar, 12, infantile-onset, with
CC cardiomyopathy (MFM12) [MIM:619424]: A form of myofibrillar myopathy, a
CC group of chronic neuromuscular disorders characterized at
CC ultrastructural level by disintegration of the sarcomeric Z disk and
CC myofibrils, and replacement of the normal myofibrillar markings by
CC small dense granules, or larger hyaline masses, or amorphous material.
CC MFM12 is an autosomal recessive, severe form characterized by
CC progressive myopathy with onset shortly after birth, tremor or clonus
CC at birth, and cardiomyopathy usually leading to death by 6 months of
CC age. Skeletal and cardiac muscle tissues show fiber-type disproportion
CC with small type I and normal sized type II fibers, and myofibrillar
CC disorganization. {ECO:0000269|PubMed:23365102,
CC ECO:0000269|PubMed:32453731}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- MISCELLANEOUS: This chain binds calcium.
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DR EMBL; X14332; CAA32510.1; -; mRNA.
DR EMBL; M22815; AAA91832.1; -; mRNA.
DR EMBL; AF020768; AAB91993.1; -; mRNA.
DR EMBL; S69022; AAB29658.2; -; mRNA.
DR EMBL; BC015821; AAH15821.1; -; mRNA.
DR EMBL; BC031006; AAH31006.1; -; mRNA.
DR EMBL; BC031008; AAH31008.1; -; mRNA.
DR CCDS; CCDS31901.1; -.
DR RefSeq; NP_000423.2; NM_000432.3.
DR PDB; 5TBY; EM; 20.00 A; E/F=1-166.
DR PDBsum; 5TBY; -.
DR AlphaFoldDB; P10916; -.
DR SMR; P10916; -.
DR BioGRID; 110717; 25.
DR IntAct; P10916; 16.
DR STRING; 9606.ENSP00000228841; -.
DR ChEMBL; CHEMBL3831286; -.
DR GlyGen; P10916; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P10916; -.
DR PhosphoSitePlus; P10916; -.
DR BioMuta; MYL2; -.
DR DMDM; 6166556; -.
DR UCD-2DPAGE; P10916; -.
DR MassIVE; P10916; -.
DR PaxDb; P10916; -.
DR PeptideAtlas; P10916; -.
DR PRIDE; P10916; -.
DR ProteomicsDB; 52678; -.
DR Antibodypedia; 31071; 414 antibodies from 38 providers.
DR DNASU; 4633; -.
DR Ensembl; ENST00000228841.15; ENSP00000228841.8; ENSG00000111245.17.
DR GeneID; 4633; -.
DR KEGG; hsa:4633; -.
DR MANE-Select; ENST00000228841.15; ENSP00000228841.8; NM_000432.4; NP_000423.2.
DR CTD; 4633; -.
DR DisGeNET; 4633; -.
DR GeneCards; MYL2; -.
DR GeneReviews; MYL2; -.
DR HGNC; HGNC:7583; MYL2.
DR HPA; ENSG00000111245; Group enriched (heart muscle, skeletal muscle, tongue).
DR MalaCards; MYL2; -.
DR MIM; 160781; gene.
DR MIM; 608758; phenotype.
DR MIM; 619424; phenotype.
DR neXtProt; NX_P10916; -.
DR OpenTargets; ENSG00000111245; -.
DR Orphanet; 2020; Congenital fiber-type disproportion myopathy.
DR Orphanet; 155; NON RARE IN EUROPE: Familial isolated hypertrophic cardiomyopathy.
DR PharmGKB; PA31380; -.
DR VEuPathDB; HostDB:ENSG00000111245; -.
DR eggNOG; KOG0031; Eukaryota.
DR GeneTree; ENSGT00940000155578; -.
DR HOGENOM; CLU_061288_9_0_1; -.
DR InParanoid; P10916; -.
DR OMA; ARNAMSK; -.
DR OrthoDB; 1435392at2759; -.
DR PhylomeDB; P10916; -.
DR TreeFam; TF314218; -.
DR PathwayCommons; P10916; -.
DR Reactome; R-HSA-390522; Striated Muscle Contraction.
DR SignaLink; P10916; -.
DR SIGNOR; P10916; -.
DR BioGRID-ORCS; 4633; 10 hits in 1069 CRISPR screens.
DR ChiTaRS; MYL2; human.
DR GeneWiki; MYL2; -.
DR GenomeRNAi; 4633; -.
DR Pharos; P10916; Tbio.
DR PRO; PR:P10916; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; P10916; protein.
DR Bgee; ENSG00000111245; Expressed in heart right ventricle and 112 other tissues.
DR ExpressionAtlas; P10916; baseline and differential.
DR Genevisible; P10916; HS.
DR GO; GO:0031672; C:A band; IEA:UniProtKB-SubCell.
DR GO; GO:0097512; C:cardiac myofibril; IDA:CAFA.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005856; C:cytoskeleton; IDA:BHF-UCL.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0030016; C:myofibril; IBA:GO_Central.
DR GO; GO:0016459; C:myosin complex; TAS:BHF-UCL.
DR GO; GO:0030017; C:sarcomere; TAS:BHF-UCL.
DR GO; GO:0003785; F:actin monomer binding; IDA:BHF-UCL.
DR GO; GO:0005509; F:calcium ion binding; IDA:MGI.
DR GO; GO:0032036; F:myosin heavy chain binding; NAS:BHF-UCL.
DR GO; GO:0008307; F:structural constituent of muscle; IMP:UniProtKB.
DR GO; GO:0060048; P:cardiac muscle contraction; IBA:GO_Central.
DR GO; GO:0055003; P:cardiac myofibril assembly; ISS:BHF-UCL.
DR GO; GO:0060047; P:heart contraction; ISS:BHF-UCL.
DR GO; GO:0007507; P:heart development; ISS:UniProtKB.
DR GO; GO:0042694; P:muscle cell fate specification; IBA:GO_Central.
DR GO; GO:0030308; P:negative regulation of cell growth; IMP:BHF-UCL.
DR GO; GO:0098735; P:positive regulation of the force of heart contraction; ISS:UniProtKB.
DR GO; GO:0006942; P:regulation of striated muscle contraction; TAS:ProtInc.
DR GO; GO:0002026; P:regulation of the force of heart contraction; ISS:UniProtKB.
DR GO; GO:0055010; P:ventricular cardiac muscle tissue morphogenesis; IMP:BHF-UCL.
DR CDD; cd00051; EFh; 1.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR Pfam; PF00036; EF-hand_1; 1.
DR SMART; SM00054; EFh; 3.
DR SUPFAM; SSF47473; SSF47473; 1.
DR PROSITE; PS00018; EF_HAND_1; 1.
DR PROSITE; PS50222; EF_HAND_2; 3.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium; Cardiomyopathy; Cytoplasm;
KW Direct protein sequencing; Disease variant; Metal-binding; Methylation;
KW Motor protein; Muscle protein; Myofibrillar myopathy; Myosin;
KW Phosphoprotein; Reference proteome; Repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P51667"
FT CHAIN 2..166
FT /note="Myosin regulatory light chain 2, ventricular/cardiac
FT muscle isoform"
FT /id="PRO_0000198727"
FT DOMAIN 24..59
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 94..129
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 130..165
FT /note="EF-hand 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 37
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 39
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 41
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 48
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT MOD_RES 2
FT /note="N,N,N-trimethylalanine"
FT /evidence="ECO:0000250|UniProtKB:P51667"
FT MOD_RES 14
FT /note="Deamidated asparagine"
FT /evidence="ECO:0000269|PubMed:20445002"
FT MOD_RES 15
FT /note="Phosphoserine; by ZIPK/DAPK3"
FT /evidence="ECO:0000269|PubMed:20038585,
FT ECO:0000269|PubMed:20445002"
FT MOD_RES 19
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P51667"
FT MOD_RES 52
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P08733"
FT VARIANT 13
FT /note="A -> T (in CMH10; with mid-left ventricular chamber
FT thickening; decrease calcium binding affinity; large
FT increase in its calcium binding affinity upon
FT phosphorylation; dbSNP:rs104894363)"
FT /evidence="ECO:0000269|PubMed:11102452,
FT ECO:0000269|PubMed:8673105"
FT /id="VAR_004601"
FT VARIANT 18
FT /note="F -> L (in CMH10; decrease calcium binding affinity;
FT dbSNP:rs104894370)"
FT /evidence="ECO:0000269|PubMed:11102452,
FT ECO:0000269|PubMed:9535554"
FT /id="VAR_004602"
FT VARIANT 22
FT /note="E -> K (in CMH10; some patients present with mid-
FT left ventricular chamber thickening; significantly decrease
FT calcium binding affinity; loss of phosphorylation;
FT dbSNP:rs104894368)"
FT /evidence="ECO:0000269|PubMed:11102452,
FT ECO:0000269|PubMed:12404107, ECO:0000269|PubMed:8673105"
FT /id="VAR_004603"
FT VARIANT 57
FT /note="G -> R (in dbSNP:rs2428140)"
FT /id="VAR_029449"
FT VARIANT 58
FT /note="R -> Q (in CMH10; impairs calcium binding; bind
FT calcium upon phosphorylation; dbSNP:rs104894369)"
FT /evidence="ECO:0000269|PubMed:11102452,
FT ECO:0000269|PubMed:12404107, ECO:0000269|PubMed:12818575,
FT ECO:0000269|PubMed:9535554"
FT /id="VAR_004604"
FT VARIANT 95
FT /note="P -> A (in CMH10; with mid-left ventricular chamber
FT thickening; decrease calcium binding affinity;
FT dbSNP:rs121913658)"
FT /evidence="ECO:0000269|PubMed:11102452,
FT ECO:0000269|PubMed:8673105"
FT /id="VAR_004605"
FT VARIANT 166
FT /note="D -> V (in CMH10; dbSNP:rs199474815)"
FT /evidence="ECO:0000269|PubMed:12707239"
FT /id="VAR_019844"
SQ SEQUENCE 166 AA; 18789 MW; EA0BEF886AA3FAF5 CRC64;
MAPKKAKKRA GGANSNVFSM FEQTQIQEFK EAFTIMDQNR DGFIDKNDLR DTFAALGRVN
VKNEEIDEMI KEAPGPINFT VFLTMFGEKL KGADPEETIL NAFKVFDPEG KGVLKADYVR
EMLTTQAERF SKEEVDQMFA AFPPDVTGNL DYKNLVHIIT HGEEKD
