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. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 //