MLRV_MOUSE
ID MLRV_MOUSE Reviewed; 166 AA.
AC P51667; Q6P8P4; Q9QVP3;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2007, sequence version 3.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Myosin regulatory light chain 2, ventricular/cardiac muscle isoform {ECO:0000305};
DE Short=MLC-2 {ECO:0000303|PubMed:1379240};
DE Short=MLC-2v;
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};
GN Name=Myl2 {ECO:0000312|MGI:MGI:97272};
GN Synonyms=Mylpc {ECO:0000312|MGI:MGI:97272};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=BALB/cJ; TISSUE=Heart muscle;
RX PubMed=1379240; DOI=10.1016/s0021-9258(19)49616-6;
RA Lee K.J., Ross R.S., Rockman H.A., Harris A.N., O'Brien T.X., Bilsen M.,
RA Shubeita H.E., Kandolf R., Brem G., Price J., Evans S.M., Zhu H.,
RA Franz W.M., Chien K.R.;
RT "Myosin light chain-2 luciferase transgenic mice reveal distinct regulatory
RT programs for cardiac and skeletal muscle-specific expression of a single
RT contractile protein gene.";
RL J. Biol. Chem. 267:15875-15885(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryonic heart, and Kidney;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [4]
RP DEVELOPMENTAL STAGE.
RX PubMed=8506363; DOI=10.1073/pnas.90.11.5157;
RA O'Brien T.X., Lee K.J., Chien K.R.;
RT "Positional specification of ventricular myosin light chain 2 expression in
RT the primitive murine heart tube.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:5157-5161(1993).
RN [5]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=9422794; DOI=10.1074/jbc.273.2.1252;
RA Chen J., Kubalak S.W., Minamisawa S., Price R.L., Becker K.D., Hickey R.,
RA Ross J. Jr., Chien K.R.;
RT "Selective requirement of myosin light chain 2v in embryonic heart
RT function.";
RL J. Biol. Chem. 273:1252-1256(1998).
RN [6]
RP MUTAGENESIS OF SER-14; SER-15 AND SER-19, AND FUNCTION.
RX PubMed=10409661; DOI=10.1074/jbc.274.30.21085;
RA Sanbe A., Fewell J.G., Gulick J., Osinska H., Lorenz J., Hall D.G.,
RA Murray L.A., Kimball T.R., Witt S.A., Robbins J.;
RT "Abnormal cardiac structure and function in mice expressing
RT nonphosphorylatable cardiac regulatory myosin light chain 2.";
RL J. Biol. Chem. 274:21085-21094(1999).
RN [7]
RP FUNCTION.
RX PubMed=16908724; DOI=10.1085/jgp.200609547;
RA Stelzer J.E., Patel J.R., Moss R.L.;
RT "Acceleration of stretch activation in murine myocardium due to
RT phosphorylation of myosin regulatory light chain.";
RL J. Gen. Physiol. 128:261-272(2006).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14; SER-15 AND SER-19, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, and Lung;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [9]
RP PHOSPHORYLATION BY DAPK3.
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 [10]
RP PHOSPHORYLATION AT SER-14 AND SER-15, AND IDENTIFICATION BY MASS
RP 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 [11]
RP CLEAVAGE OF INITIATOR METHIONINE, AND METHYLATION AT ALA-2.
RX PubMed=20668449; DOI=10.1038/nature09343;
RA Tooley C.E., Petkowski J.J., Muratore-Schroeder T.L., Balsbaugh J.L.,
RA Shabanowitz J., Sabat M., Minor W., Hunt D.F., Macara I.G.;
RT "NRMT is an alpha-N-methyltransferase that methylates RCC1 and
RT retinoblastoma protein.";
RL Nature 466:1125-1128(2010).
RN [12]
RP PHOSPHORYLATION BY MYLK3.
RX PubMed=23095280; DOI=10.1161/circulationaha.112.116202;
RA Warren S.A., Briggs L.E., Zeng H., Chuang J., Chang E.I., Terada R., Li M.,
RA Swanson M.S., Lecker S.H., Willis M.S., Spinale F.G., Maupin-Furlowe J.,
RA McMullen J.R., Moss R.L., Kasahara H.;
RT "Myosin light chain phosphorylation is critical for adaptation to cardiac
RT stress.";
RL Circulation 126:2575-2588(2012).
RN [13]
RP MUTAGENESIS OF SER-14 AND SER-15, PHOSPHORYLATION AT SER-14 AND SER-15 BY
RP MYLK3 AND MYLK2, PHOSPHORYLATION AT SER-14; SER-15 AND SER-19,
RP IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=22426213; DOI=10.1172/jci61134;
RA Sheikh F., Ouyang K., Campbell S.G., Lyon R.C., Chuang J., Fitzsimons D.,
RA Tangney J., Hidalgo C.G., Chung C.S., Cheng H., Dalton N.D., Gu Y.,
RA Kasahara H., Ghassemian M., Omens J.H., Peterson K.L., Granzier H.L.,
RA Moss R.L., McCulloch A.D., Chen J.;
RT "Mouse and computational models link Mlc2v dephosphorylation to altered
RT myosin kinetics in early cardiac disease.";
RL J. Clin. Invest. 122:1209-1221(2012).
CC -!- FUNCTION: Contractile protein that plays a role in heart development
CC and function (PubMed:10409661). Following phosphorylation, plays a role
CC in cross-bridge cycling kinetics and cardiac muscle contraction by
CC increasing myosin lever arm stiffness and promoting myosin head
CC diffusion; as a consequence of the increase in maximum contraction
CC force and calcium sensitivity of contraction force. These events
CC altogether slow down myosin kinetics and prolong duty cycle resulting
CC in accumulated myosins being cooperatively recruited to actin binding
CC sites to sustain thin filament activation as a means to fine-tune
CC myofilament calcium sensitivity to force (By similarity)
CC (PubMed:22426213, PubMed:16908724, PubMed:10409661). During
CC cardiogenesis plays an early role in cardiac contractility by promoting
CC cardiac myofibril assembly (PubMed:9422794).
CC {ECO:0000250|UniProtKB:P08733, ECO:0000269|PubMed:10409661,
CC ECO:0000269|PubMed:16908724, ECO:0000269|PubMed:22426213,
CC ECO:0000269|PubMed:9422794}.
CC -!- SUBUNIT: Myosin is a hexamer of 2 heavy chains and 4 light chains (By
CC similarity). Interacts with MYOC (By similarity). {ECO:0000250,
CC ECO:0000250|UniProtKB:P10916}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, myofibril, sarcomere, A band
CC {ECO:0000250|UniProtKB:P08733}.
CC -!- TISSUE SPECIFICITY: Abundantly expressed in both cardiac and slow
CC skeletal muscle (PubMed:1379240). In the adult heart, the
CC phosphorylated form is highly expressed in epicardium and weakly in
CC endocardium (PubMed:22426213). {ECO:0000269|PubMed:1379240,
CC ECO:0000269|PubMed:22426213}.
CC -!- DEVELOPMENTAL STAGE: At 8 dpc highly expressed in the ventricular
CC portion of the heart tube, with no detectable expression in the atrial
CC or sinus venosus regions; also expressed in the proximal outflow tract
CC of the heart tube at minimally detectable levels. At 9-10 dpc
CC expression is well established in the proximal outflow tract region
CC adjacent to the ventricular segment. At 11 dpc, expression becomes
CC restricted to the ventricular region. {ECO:0000269|PubMed:8506363}.
CC -!- PTM: N-terminus is methylated by METTL11A/NTM1.
CC {ECO:0000269|PubMed:20668449}.
CC -!- PTM: Phosphorylated by MYLK3 and MYLK2; promotes cardiac muscle
CC contraction and function. Dephosphorylated by PPP1CB complexed to
CC PPP1R12B (By similarity). The phosphorylated form in adult is expressed
CC as gradients across the heart from endocardium (low phosphorylation) to
CC epicardium (high phosphorylation); regulates cardiac torsion and
CC workload distribution (PubMed:22426213). {ECO:0000250|UniProtKB:P08733,
CC ECO:0000269|PubMed:22426213, ECO:0000269|PubMed:23095280}.
CC -!- DISRUPTION PHENOTYPE: Myl2 homozygous die at 12.5 dpc, which is
CC associated with ultrastructural defects in ventricular sarcomere
CC assembly, that included disruptions and disorganization of the normal
CC parallel alignment of the thick and thin filaments, narrower fiber
CC widths and larger distances between Z disks and misalignment of Z-band
CC between sarcomeres. {ECO:0000269|PubMed:9422794}.
CC -!- MISCELLANEOUS: This chain binds calcium.
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DR EMBL; M91602; AAA39796.1; -; mRNA.
DR EMBL; AK002367; BAB22045.1; -; mRNA.
DR EMBL; AK146674; BAE27350.1; -; mRNA.
DR EMBL; BC061144; AAH61144.1; -; mRNA.
DR CCDS; CCDS39252.1; -.
DR PIR; A42858; A42858.
DR RefSeq; NP_034991.3; NM_010861.4.
DR AlphaFoldDB; P51667; -.
DR SMR; P51667; -.
DR IntAct; P51667; 3.
DR MINT; P51667; -.
DR STRING; 10090.ENSMUSP00000014080; -.
DR iPTMnet; P51667; -.
DR PhosphoSitePlus; P51667; -.
DR MaxQB; P51667; -.
DR PaxDb; P51667; -.
DR PeptideAtlas; P51667; -.
DR PRIDE; P51667; -.
DR ProteomicsDB; 291468; -.
DR TopDownProteomics; P51667; -.
DR Antibodypedia; 31071; 414 antibodies from 38 providers.
DR DNASU; 17906; -.
DR Ensembl; ENSMUST00000014080; ENSMUSP00000014080; ENSMUSG00000013936.
DR Ensembl; ENSMUST00000111751; ENSMUSP00000107380; ENSMUSG00000013936.
DR GeneID; 17906; -.
DR KEGG; mmu:17906; -.
DR UCSC; uc008zkp.1; mouse.
DR CTD; 4633; -.
DR MGI; MGI:97272; Myl2.
DR VEuPathDB; HostDB:ENSMUSG00000013936; -.
DR eggNOG; KOG0031; Eukaryota.
DR GeneTree; ENSGT00940000155578; -.
DR HOGENOM; CLU_061288_9_0_1; -.
DR InParanoid; P51667; -.
DR OMA; AMMEIAN; -.
DR OrthoDB; 1435392at2759; -.
DR PhylomeDB; P51667; -.
DR TreeFam; TF314218; -.
DR Reactome; R-MMU-390522; Striated Muscle Contraction.
DR BioGRID-ORCS; 17906; 0 hits in 72 CRISPR screens.
DR ChiTaRS; Myl2; mouse.
DR PRO; PR:P51667; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; P51667; protein.
DR Bgee; ENSMUSG00000013936; Expressed in cardiac muscle of left ventricle and 111 other tissues.
DR ExpressionAtlas; P51667; baseline and differential.
DR Genevisible; P51667; MM.
DR GO; GO:0031672; C:A band; IEA:UniProtKB-SubCell.
DR GO; GO:0015629; C:actin cytoskeleton; ISO:MGI.
DR GO; GO:0097512; C:cardiac myofibril; ISO:MGI.
DR GO; GO:0043292; C:contractile fiber; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005856; C:cytoskeleton; ISO:MGI.
DR GO; GO:0030016; C:myofibril; IDA:MGI.
DR GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
DR GO; GO:0003785; F:actin monomer binding; ISO:MGI.
DR GO; GO:0005509; F:calcium ion binding; ISO:MGI.
DR GO; GO:0008307; F:structural constituent of muscle; ISS:UniProtKB.
DR GO; GO:0060048; P:cardiac muscle contraction; IGI:MGI.
DR GO; GO:0055003; P:cardiac myofibril assembly; IMP:MGI.
DR GO; GO:0060047; P:heart contraction; IDA:UniProtKB.
DR GO; GO:0007507; P:heart development; IDA:UniProtKB.
DR GO; GO:0003007; P:heart morphogenesis; IGI:MGI.
DR GO; GO:0055001; P:muscle cell development; IGI:MGI.
DR GO; GO:0042694; P:muscle cell fate specification; IMP:MGI.
DR GO; GO:0030308; P:negative regulation of cell growth; ISO:MGI.
DR GO; GO:0098735; P:positive regulation of the force of heart contraction; IDA:UniProtKB.
DR GO; GO:0009791; P:post-embryonic development; IGI:MGI.
DR GO; GO:0002026; P:regulation of the force of heart contraction; ISO:MGI.
DR GO; GO:0055010; P:ventricular cardiac muscle tissue morphogenesis; ISO:MGI.
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 Calcium; Cytoplasm; Metal-binding; Methylation; Motor protein;
KW Muscle protein; Myosin; Phosphoprotein; Reference proteome; Repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:20668449"
FT CHAIN 2..166
FT /note="Myosin regulatory light chain 2, ventricular/cardiac
FT muscle isoform"
FT /id="PRO_0000198728"
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:0000269|PubMed:20668449"
FT MOD_RES 14
FT /note="Phosphoserine; by MLCK"
FT /evidence="ECO:0000269|PubMed:20445002,
FT ECO:0000269|PubMed:22426213, ECO:0007744|PubMed:21183079"
FT MOD_RES 15
FT /note="Phosphoserine; by MLCK"
FT /evidence="ECO:0000269|PubMed:20445002,
FT ECO:0000269|PubMed:22426213, ECO:0007744|PubMed:21183079"
FT MOD_RES 19
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:22426213,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 52
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P08733"
FT MUTAGEN 14
FT /note="S->A: Loss of cardiac myofibril assembly; when
FT associated with A-15 and A-19. Loss of phosphorylation;
FT when associated with A-15 and A-19. Loss of calcium
FT sensitivity of force development; when associated with A-15
FT and A-19. Phosphorylation at Ser-19; when associated with
FT A-15. Significant decrease in phosphorylation by MLCK; when
FT associated with A-15. Adult lethality associated with early
FT defects in cardiac twitch relaxation and torsion leading to
FT dilated cardiomyopathy, heart failure and premature death;
FT when associated with A-15.Significant acceleration of
FT twitch relaxation in absence of changes in calcium
FT transients; when associated with A-15. Absence of
FT transmural phosphorylation gradient leading to alteration
FT of torsion; when associated with A-14."
FT /evidence="ECO:0000269|PubMed:10409661,
FT ECO:0000269|PubMed:22426213"
FT MUTAGEN 15
FT /note="S->A: Loss of cardiac myofibril assembly; when
FT associated with A-14 and A-19. Loss of phosphorylation;
FT when associated with A-14 and A-19. Loss of calcium
FT sensitivity of force development; when associated with A-14
FT and A-19. Increase of phosphorylation. Phosphorylation at
FT Ser-14 and at Ser-19. Phosphorylation at Ser-19; when
FT associated with A-14. Significant decrease in
FT phosphorylation by MLCK; when associated with A-14. Adult
FT lethality associated with early defects in cardiac twitch
FT relaxation and torsion leading to dilated cardiomyopathy,
FT heart failure and premature death; when associated with A-
FT 14. Significant acceleration of twitch relaxation in
FT absence of changes in calcium transients; when associated
FT with A-14. Absence of transmural phosphorylation gradient
FT leading to alteration of torsion; when associated with A-
FT 14."
FT /evidence="ECO:0000269|PubMed:10409661,
FT ECO:0000269|PubMed:22426213"
FT MUTAGEN 19
FT /note="S->A: Loss of cardiac myofibril assembly; when
FT associated with A-14 and A-15. Loss of phosphorylation;
FT when associated with A-14 and A-15. Loss of calcium
FT sensitivity of force development; when associated with A-14
FT and A-15."
FT /evidence="ECO:0000269|PubMed:10409661"
FT CONFLICT 4..5
FT /note="KK -> LF (in Ref. 1; AAA39796)"
FT /evidence="ECO:0000305"
FT CONFLICT 14
FT /note="S -> T (in Ref. 1; AAA39796)"
FT /evidence="ECO:0000305"
FT CONFLICT 128
FT /note="E -> G (in Ref. 3; AAH61144)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 166 AA; 18864 MW; EA25C1FAA18E2EA8 CRC64;
MAPKKAKKRI EGGSSNVFSM FEQTQIQEFK EAFTIMDQNR DGFIDKNDLR DTFAALGRVN
VKNEEIDEMI KEAPGPINFT VFLTMFGEKL KGADPEETIL NAFKVFDPEG KGSLKADYVR
EMLTTQAERF SKEEIDQMFA AFPPDVTGNL DYKNLVHIIT HGEEKD
