DESM_MOUSE
ID DESM_MOUSE Reviewed; 469 AA.
AC P31001;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 188.
DE RecName: Full=Desmin;
GN Name=Des;
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].
RX PubMed=8120103; DOI=10.1083/jcb.124.5.827;
RA Li H., Choudhary S.K., Milner D.J., Munir M.I., Kuisk I.R., Capetanaki Y.;
RT "Inhibition of desmin expression blocks myoblast fusion and interferes with
RT the myogenic regulators MyoD and myogenin.";
RL J. Cell Biol. 124:827-841(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Colon;
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 [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-40.
RC STRAIN=BALB/cJ; TISSUE=Spleen;
RX PubMed=8382796; DOI=10.1093/nar/21.2.335;
RA Li H., Capetanaki Y.;
RT "Regulation of the mouse desmin gene: transactivated by MyoD, myogenin,
RT MRF4 and Myf5.";
RL Nucleic Acids Res. 21:335-343(1993).
RN [4]
RP INTERACTION WITH DST.
RX PubMed=10357897; DOI=10.1006/dbio.1999.9263;
RA Dalpe G., Mathieu M., Comtois A., Zhu E., Wasiak S., De Repentigny Y.,
RA Leclerc N., Kothary R.;
RT "Dystonin-deficient mice exhibit an intrinsic muscle weakness and an
RT instability of skeletal muscle cytoarchitecture.";
RL Dev. Biol. 210:367-380(1999).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-68, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-17; SER-25; SER-28; SER-31;
RP SER-32; SER-68 AND SER-423, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
RP SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Kidney, Lung, Pancreas, Spleen, and
RC Testis;
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 [7]
RP INTERACTION WITH PLEC.
RX PubMed=24940650; DOI=10.1038/jid.2014.255;
RA Bouameur J.E., Favre B., Fontao L., Lingasamy P., Begre N., Borradori L.;
RT "Interaction of plectin with keratins 5 and 14: dependence on several
RT plectin domains and keratin quaternary structure.";
RL J. Invest. Dermatol. 134:2776-2783(2014).
RN [8]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-16; ARG-37 AND ARG-70, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Embryo;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
RN [9]
RP FUNCTION, MUTAGENESIS OF ARG-349, AND SUBCELLULAR LOCATION.
RX PubMed=25394388; DOI=10.1007/s00401-014-1363-2;
RA Clemen C.S., Stoeckigt F., Strucksberg K.H., Chevessier F., Winter L.,
RA Schuetz J., Bauer R., Thorweihe J.M., Wenzel D., Schloetzer-Schrehardt U.,
RA Rasche V., Krsmanovic P., Katus H.A., Rottbauer W., Just S., Mueller O.J.,
RA Friedrich O., Meyer R., Herrmann H., Schrickel J.W., Schroeder R.;
RT "The toxic effect of R350P mutant desmin in striated muscle of man and
RT mouse.";
RL Acta Neuropathol. 129:297-315(2015).
RN [10]
RP INTERACTION WITH ASB2, SUBCELLULAR LOCATION, AND PROTEASOMAL DEGRADATION.
RX PubMed=26343497; DOI=10.1016/j.yjmcc.2015.08.020;
RA Thottakara T., Friedrich F.W., Reischmann S., Braumann S., Schlossarek S.,
RA Kraemer E., Juhr D., Schlueter H., van der Velden J., Muench J., Patten M.,
RA Eschenhagen T., Moog-Lutz C., Carrier L.;
RT "The E3 ubiquitin ligase Asb2beta is downregulated in a mouse model of
RT hypertrophic cardiomyopathy and targets desmin for proteasomal
RT degradation.";
RL J. Mol. Cell. Cardiol. 87:214-224(2015).
RN [11]
RP PHOSPHORYLATION AT SER-7; SER-28; SER-32; SER-60 AND THR-76, AND
RP MUTAGENESIS OF SER-7; SER-28; SER-32; SER-60 AND THR-76.
RX PubMed=27565725; DOI=10.1016/j.bbrc.2016.08.122;
RA Makihara H., Inaba H., Enomoto A., Tanaka H., Tomono Y., Ushida K.,
RA Goto M., Kurita K., Nishida Y., Kasahara K., Goto H., Inagaki M.;
RT "Desmin phosphorylation by Cdk1 is required for efficient separation of
RT desmin intermediate filaments in mitosis and detected in murine
RT embryonic/newborn muscle and human rhabdomyosarcoma tissues.";
RL Biochem. Biophys. Res. Commun. 478:1323-1329(2016).
RN [12]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=26787680; DOI=10.1242/bio.014993;
RA Fuchs C., Gawlas S., Heher P., Nikouli S., Paar H., Ivankovic M.,
RA Schultheis M., Klammer J., Gottschamel T., Capetanaki Y., Weitzer G.;
RT "Desmin enters the nucleus of cardiac stem cells and modulates Nkx2.5
RT expression by participating in transcription factor complexes that interact
RT with the nkx2.5 gene.";
RL Biol. Open 5:140-153(2016).
RN [13]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=27733623; DOI=10.1091/mbc.e16-04-0237;
RA Hernandez D.A., Bennett C.M., Dunina-Barkovskaya L., Wedig T.,
RA Capetanaki Y., Herrmann H., Conover G.M.;
RT "Nebulette is a powerful cytolinker organizing desmin and actin in mouse
RT hearts.";
RL Mol. Biol. Cell 27:3869-3882(2016).
RN [14]
RP FUNCTION, AND INTERACTION WITH TUBULIN.
RX PubMed=27102488; DOI=10.1126/science.aaf0659;
RA Robison P., Caporizzo M.A., Ahmadzadeh H., Bogush A.I., Chen C.Y.,
RA Margulies K.B., Shenoy V.B., Prosser B.L.;
RT "Detyrosinated microtubules buckle and bear load in contracting
RT cardiomyocytes.";
RL Science 352:417-428(2016).
RN [15]
RP MUTAGENESIS OF ARG-349, AND SUBCELLULAR LOCATION.
RX PubMed=28469177; DOI=10.1038/s41598-017-01485-x;
RA Diermeier S., Iberl J., Vetter K., Haug M., Pollmann C., Reischl B.,
RA Buttgereit A., Schuermann S., Spoerrer M., Goldmann W.H., Fabry B.,
RA Elhamine F., Stehle R., Pfitzer G., Winter L., Clemen C.S., Herrmann H.,
RA Schroeder R., Friedrich O.;
RT "Early signs of architectural and biomechanical failure in isolated
RT myofibers and immortalized myoblasts from desmin-mutant knock-in mice.";
RL Sci. Rep. 7:1391-1391(2017).
CC -!- FUNCTION: Muscle-specific type III intermediate filament essential for
CC proper muscular structure and function. Plays a crucial role in
CC maintaining the structure of sarcomeres, inter-connecting the Z-disks
CC and forming the myofibrils, linking them not only to the sarcolemmal
CC cytoskeleton, but also to the nucleus and mitochondria, thus providing
CC strength for the muscle fiber during activity (By similarity). In adult
CC striated muscle they form a fibrous network connecting myofibrils to
CC each other and to the plasma membrane from the periphery of the Z-line
CC structures (PubMed:25394388). May act as a sarcomeric microtubule-
CC anchoring protein: specifically associates with detyrosinated tubulin-
CC alpha chains, leading to buckled microtubules and mechanical resistance
CC to contraction (PubMed:27102488). Contributes to the transcriptional
CC regulation of the NKX2-5 gene in cardiac progenitor cells during a
CC short period of cardiomyogenesis and in cardiac side population stem
CC cells in the adult. Plays a role in maintaining an optimal conformation
CC of nebulette (NEB) on heart muscle sarcomeres to bind and recruit
CC cardiac alpha-actin (PubMed:27733623). {ECO:0000250|UniProtKB:P17661,
CC ECO:0000269|PubMed:25394388, ECO:0000269|PubMed:27102488,
CC ECO:0000269|PubMed:27733623}.
CC -!- SUBUNIT: Homomer (By similarity). Interacts with MTM1 (By similarity).
CC Interacts with DST (PubMed:10357897). Interacts with tubulin-alpha;
CC specifically associates with detyrosinated tubulin-alpha
CC (PubMed:27102488). Interacts with EPPK1; interaction is dependent of
CC higher-order structure of intermediate filament. Interacts with CRYAB
CC (By similarity). Interacts with NEB (via nebulin repeats 160-164) (By
CC similarity). Interacts (via rod region) with NEBL (via nebulin repeats
CC 1-5) (By similarity). Interacts with ASB2 isoform 1; the interaction
CC targets DES for proteasomal degradation (PubMed:26343497). Interacts
CC with PLEC isoform 1C (PubMed:24940650). {ECO:0000250|UniProtKB:P17661,
CC ECO:0000269|PubMed:10357897, ECO:0000269|PubMed:24940650,
CC ECO:0000269|PubMed:26343497, ECO:0000269|PubMed:27102488}.
CC -!- INTERACTION:
CC P31001; Q9Z2C5: Mtm1; NbExp=4; IntAct=EBI-298565, EBI-6861578;
CC P31001; Q9UBX2: DUX4; Xeno; NbExp=2; IntAct=EBI-298565, EBI-11600078;
CC P31001; Q13496: MTM1; Xeno; NbExp=4; IntAct=EBI-298565, EBI-2864109;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, myofibril, sarcomere, Z line
CC {ECO:0000269|PubMed:26343497, ECO:0000269|PubMed:26787680,
CC ECO:0000269|PubMed:28469177}. Cytoplasm {ECO:0000269|PubMed:25394388,
CC ECO:0000269|PubMed:26787680}. Cell membrane, sarcolemma
CC {ECO:0000269|PubMed:25394388}. Nucleus {ECO:0000269|PubMed:26787680}.
CC Note=Localizes in the intercalated disks which occur at the Z line of
CC cardiomyocytes (By similarity). Localizes in the nucleus exclusively in
CC differentiating cardiac progenitor cells and premature cardiomyocytes
CC (PubMed:26787680). {ECO:0000250|UniProtKB:P17661,
CC ECO:0000269|PubMed:26787680}.
CC -!- TISSUE SPECIFICITY: Cardiac progenitor cells and immature
CC cardiomyocytes (at protein level). {ECO:0000269|PubMed:26787680}.
CC -!- PTM: ADP-ribosylation prevents ability to form intermediate filaments.
CC {ECO:0000250|UniProtKB:P48675}.
CC -!- PTM: Phosphorylation at Ser-7, Ser-28 and Ser-32 by CDK1,
CC phosphorylation at Ser-60 by AURKB and phosphorylation at Thr-76 by
CC ROCK1 contribute to efficient separation of desmin intermediate
CC filaments during mitosis. {ECO:0000269|PubMed:27565725}.
CC -!- PTM: Ubiquitination by a SCF-like complex containing ASB2 isoform 1
CC leads to proteasomal degradation. {ECO:0000269|PubMed:26343497}.
CC -!- DISRUPTION PHENOTYPE: Mice hearts have reduced nebulette (NEB) and
CC elevated actin levels, with intact myofibers showing disordered NEB
CC organization. {ECO:0000269|PubMed:27733623}.
CC -!- SIMILARITY: Belongs to the intermediate filament family.
CC {ECO:0000255|PROSITE-ProRule:PRU01188}.
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DR EMBL; L22550; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BC031760; AAH31760.1; -; mRNA.
DR EMBL; Z18892; CAA79330.1; -; Genomic_DNA.
DR CCDS; CCDS15071.1; -.
DR PIR; A54104; A54104.
DR RefSeq; NP_034173.1; NM_010043.2.
DR AlphaFoldDB; P31001; -.
DR SMR; P31001; -.
DR BioGRID; 199210; 10.
DR DIP; DIP-256N; -.
DR IntAct; P31001; 14.
DR MINT; P31001; -.
DR STRING; 10090.ENSMUSP00000027409; -.
DR iPTMnet; P31001; -.
DR PhosphoSitePlus; P31001; -.
DR SWISS-2DPAGE; P31001; -.
DR EPD; P31001; -.
DR jPOST; P31001; -.
DR PaxDb; P31001; -.
DR PeptideAtlas; P31001; -.
DR PRIDE; P31001; -.
DR ProteomicsDB; 277981; -.
DR Antibodypedia; 3503; 1513 antibodies from 53 providers.
DR DNASU; 13346; -.
DR Ensembl; ENSMUST00000027409; ENSMUSP00000027409; ENSMUSG00000026208.
DR GeneID; 13346; -.
DR KEGG; mmu:13346; -.
DR UCSC; uc007box.2; mouse.
DR CTD; 1674; -.
DR MGI; MGI:94885; Des.
DR VEuPathDB; HostDB:ENSMUSG00000026208; -.
DR eggNOG; KOG0977; Eukaryota.
DR GeneTree; ENSGT00940000155522; -.
DR HOGENOM; CLU_012560_7_4_1; -.
DR InParanoid; P31001; -.
DR OMA; TMSQSYS; -.
DR OrthoDB; 655109at2759; -.
DR PhylomeDB; P31001; -.
DR TreeFam; TF330122; -.
DR Reactome; R-MMU-390522; Striated Muscle Contraction.
DR BioGRID-ORCS; 13346; 4 hits in 73 CRISPR screens.
DR PRO; PR:P31001; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; P31001; protein.
DR Bgee; ENSMUSG00000026208; Expressed in hindlimb stylopod muscle and 159 other tissues.
DR ExpressionAtlas; P31001; baseline and differential.
DR Genevisible; P31001; MM.
DR GO; GO:0097512; C:cardiac myofibril; ISO:MGI.
DR GO; GO:0005911; C:cell-cell junction; IDA:MGI.
DR GO; GO:0043292; C:contractile fiber; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005856; C:cytoskeleton; IDA:MGI.
DR GO; GO:0005916; C:fascia adherens; IDA:MGI.
DR GO; GO:0005921; C:gap junction; ISO:MGI.
DR GO; GO:0014704; C:intercalated disc; ISO:MGI.
DR GO; GO:0045111; C:intermediate filament cytoskeleton; ISO:MGI.
DR GO; GO:0031594; C:neuromuscular junction; IDA:MGI.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0042383; C:sarcolemma; IDA:UniProtKB.
DR GO; GO:0045098; C:type III intermediate filament; ISO:MGI.
DR GO; GO:0030018; C:Z disc; IDA:UniProtKB.
DR GO; GO:0008092; F:cytoskeletal protein binding; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0005200; F:structural constituent of cytoskeleton; IBA:GO_Central.
DR GO; GO:0045109; P:intermediate filament organization; ISS:UniProtKB.
DR GO; GO:0007517; P:muscle organ development; TAS:MGI.
DR GO; GO:0060538; P:skeletal muscle organ development; IBA:GO_Central.
DR InterPro; IPR018039; IF_conserved.
DR InterPro; IPR039008; IF_rod_dom.
DR InterPro; IPR006821; Intermed_filament_DNA-bd.
DR Pfam; PF00038; Filament; 1.
DR Pfam; PF04732; Filament_head; 1.
DR SMART; SM01391; Filament; 1.
DR PROSITE; PS00226; IF_ROD_1; 1.
DR PROSITE; PS51842; IF_ROD_2; 1.
PE 1: Evidence at protein level;
KW ADP-ribosylation; Cell membrane; Coiled coil; Cytoplasm;
KW Intermediate filament; Membrane; Methylation; Muscle protein; Nucleus;
KW Phosphoprotein; Reference proteome; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P02542"
FT CHAIN 2..469
FT /note="Desmin"
FT /id="PRO_0000063773"
FT DOMAIN 107..415
FT /note="IF rod"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01188"
FT REGION 2..108
FT /note="Head"
FT REGION 109..140
FT /note="Coil 1A"
FT REGION 141..150
FT /note="Linker 1"
FT REGION 151..251
FT /note="Coil 1B"
FT REGION 252..267
FT /note="Linker 12"
FT REGION 267..414
FT /note="Interaction with NEB"
FT /evidence="ECO:0000250|UniProtKB:P17661"
FT REGION 268..286
FT /note="Coil 2A"
FT REGION 287..294
FT /note="Linker 2"
FT REGION 295..411
FT /note="Coil 2B"
FT REGION 412..469
FT /note="Tail"
FT REGION 437..452
FT /note="Interaction with CRYAB"
FT /evidence="ECO:0000250|UniProtKB:P17661"
FT SITE 353
FT /note="Stutter"
FT MOD_RES 7
FT /note="Phosphoserine; by CDK1"
FT /evidence="ECO:0000269|PubMed:27565725"
FT MOD_RES 12
FT /note="Phosphoserine; by AURKB"
FT /evidence="ECO:0000250|UniProtKB:P17661"
FT MOD_RES 16
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 17
FT /note="Phosphothreonine; by AURKB and ROCK1"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 25
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 28
FT /note="Phosphoserine; by CDK1"
FT /evidence="ECO:0000269|PubMed:27565725,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 31
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 32
FT /note="Phosphoserine; by CDK1"
FT /evidence="ECO:0000269|PubMed:27565725,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 37
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 37
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 45
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P48675"
FT MOD_RES 58
FT /note="ADP-ribosylarginine"
FT /evidence="ECO:0000250|UniProtKB:P48675"
FT MOD_RES 60
FT /note="Phosphoserine; by AURKB"
FT /evidence="ECO:0000269|PubMed:27565725"
FT MOD_RES 68
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 70
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 76
FT /note="Phosphothreonine; by ROCK1"
FT /evidence="ECO:0000269|PubMed:27565725"
FT MOD_RES 77
FT /note="Phosphothreonine; by ROCK1"
FT /evidence="ECO:0000250|UniProtKB:P17661"
FT MOD_RES 81
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P48675"
FT MOD_RES 289
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P48675"
FT MOD_RES 357
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P48675"
FT MOD_RES 423
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MUTAGEN 7
FT /note="S->A: Reduced phosphorylation. Almost complete loss
FT of phosphorylation; when associated with A-28 and A-32."
FT /evidence="ECO:0000269|PubMed:27565725"
FT MUTAGEN 28
FT /note="S->A: Reduced phosphorylation. Almost complete loss
FT of phosphorylation; when associated with A-7 and A-32."
FT /evidence="ECO:0000269|PubMed:27565725"
FT MUTAGEN 32
FT /note="S->A: Reduced phosphorylation and formation of
FT unusual long bridge-like intermediate filament structures
FT between two daughter cells during cytokinesis. Almost
FT complete loss of phosphorylation; when associated with A-7
FT and A-28. Increased formation of unusual long bridge-like
FT intermediate filament structures between two daughter cells
FT during cytokinesis; when associated with A-60 and A-76."
FT /evidence="ECO:0000269|PubMed:27565725"
FT MUTAGEN 60
FT /note="S->A: Formation of unusual long bridge-like
FT intermediate filament structures between two daughter cells
FT during cytokinesis; when associated with A-76. Increased
FT formation of unusual long bridge-like intermediate filament
FT structures between two daughter cells during cytokinesis;
FT when associated with A-32 and A-76."
FT /evidence="ECO:0000269|PubMed:27565725"
FT MUTAGEN 76
FT /note="T->A: Formation of unusual long bridge-like
FT intermediate filament structures between two daughter cells
FT during cytokinesis; when associated with A-60. Increased
FT formation of unusual long bridge-like intermediate filament
FT structures between two daughter cells during cytokinesis;
FT when associated with A-32 and A-60."
FT /evidence="ECO:0000269|PubMed:27565725"
FT MUTAGEN 349
FT /note="R->P: Increases protein decay. forms subsarcolemmal
FT aggregates. Changes the subcellular localization and
FT turnover of its direct, extrasarcomeric binding partners.
FT Knockin mice develop age-dependent desmin-positive protein
FT aggregation pathology, skeletal muscle weakness, dilated
FT cardiomyopathy, as well as cardiac arrhythmias and
FT conduction defects. Knockin mice exhibit altered axial
FT myofibrillar lattice arrangement in fast- and slow-twitch
FT muscle fibers, increased axial stiffness and stretch-
FT induced vulnerability in soleus muscle fiber bundles,
FT reduced Ca(2+)-sensitivity in heterozygous fiber bundles
FT and increased Ca(2+)-sensitivity in homozygous fiber
FT bundles."
FT /evidence="ECO:0000269|PubMed:25394388"
SQ SEQUENCE 469 AA; 53498 MW; 58A8A13C7CC11EEF CRC64;
MSQAYSSSQR VSSYRRTFGG APGFSLGSPL SSPVFPRAGF GTKGSSSSMT SRVYQVSRTS
GGAGGLGSLR SSRLGTTRAP SYGAGELLDF SLADAVNQEF LATRTNEKVE LQELNDRFAN
YIEKVRFLEQ QNAALAAEVN RLKGREPTRV AELYEEEMRE LRRQVEVLTN QRARVDVERD
NLIDDLQRLK AKLQEEIQLR EEAENNLAAF RADVDAATLA RIDLERRIES LNEEIAFLKK
VHEEEIRELQ AQLQEQQVQV EMDMSKPDLT AALRDIRAQY ETIAAKNISE AEEWYKSKVS
DLTQAANKNN DALRQAKQEM MEYRHQIQSY TCEIDALKGT NDSLMRQMRE LEDRFASEAN
GYQDNIARLE EEIRHLKDEM ARHLREYQDL LNVKMALDVE IATYRKLLEG EESRINLPIQ
TFSALNFRET SPEQRGSEVH TKKTVMIKTI ETRDGEVVSE ATQQQHEVL
