PLEC_HUMAN
ID PLEC_HUMAN Reviewed; 4684 AA.
AC Q15149; Q15148; Q16640; Q6S376; Q6S377; Q6S378; Q6S379; Q6S380; Q6S381;
AC Q6S382; Q6S383;
DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2008, sequence version 3.
DT 03-AUG-2022, entry version 240.
DE RecName: Full=Plectin;
DE Short=PCN;
DE Short=PLTN;
DE AltName: Full=Hemidesmosomal protein 1;
DE Short=HD1;
DE AltName: Full=Plectin-1;
GN Name=PLEC; Synonyms=PLEC1;
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 [GENOMIC DNA].
RC TISSUE=Placenta;
RX PubMed=8633055; DOI=10.1073/pnas.93.9.4278;
RA Liu C.-G., Maercker C., Castanon M.J., Hauptmann R., Wiche G.;
RT "Human plectin: organization of the gene, sequence analysis, and chromosome
RT localization (8q24).";
RL Proc. Natl. Acad. Sci. U.S.A. 93:4278-4283(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 2 AND 3), DISEASE, AND
RP VARIANT VAL-1321.
RX PubMed=8698233; DOI=10.1101/gad.10.14.1724;
RA McLean W.H.I., Pulkkinen L., Smith F.J.D., Rugg E.L., Lane E.B.,
RA Bullrich F., Burgeson R.E., Amano S., Hudson D.L., Owaribe K.,
RA McGrath J.A., McMillan J.R., Eady R.A.J., Leigh I.M., Christiano A.M.,
RA Uitto J.;
RT "Loss of plectin causes epidermolysis bullosa with muscular dystrophy: cDNA
RT cloning and genomic organization.";
RL Genes Dev. 10:1724-1735(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 4; 5; 6; 7; 8 AND 9).
RX PubMed=14672974; DOI=10.1101/gr.1225204;
RA Zhang T., Haws P., Wu Q.;
RT "Multiple variable first exons: a mechanism for cell- and tissue-specific
RT gene regulation.";
RL Genome Res. 14:79-89(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16421571; DOI=10.1038/nature04406;
RA Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M.,
RA Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L.,
RA Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S.,
RA Asakawa T., Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A.,
RA Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III,
RA Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K.,
RA Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
RA Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
RA Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B.,
RA O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K.,
RA Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L.,
RA Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G.,
RA Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W.,
RA Platzer M., Shimizu N., Lander E.S.;
RT "DNA sequence and analysis of human chromosome 8.";
RL Nature 439:331-335(2006).
RN [5]
RP PROTEIN SEQUENCE OF 14-21; 209-227; 237-248; 301-316; 329-336; 350-365;
RP 372-417; 510-517; 588-597; 631-675; 697-706; 714-724; 734-740; 751-764;
RP 857-869; 897-908; 927-934; 1029-1037; 1045-1052; 1076-1088; 1131-1139;
RP 1166-1175; 1187-1210; 1216-1224; 1227-1243; 1251-1266; 1274-1291;
RP 1318-1335; 1338-1344; 1351-1364; 1366-1382; 1411-1438; 1473-1479;
RP 1499-1508; 1554-1563; 1596-1603; 1606-1616; 1628-1638; 1649-1657;
RP 1671-1679; 1699-1709; 1732-1744; 1783-1792; 1825-1833; 1846-1854;
RP 1867-1875; 1888-1908; 1976-1994; 2006-2014; 2048-2055; 2058-2068;
RP 2079-2087; 2098-2108; 2130-2139; 2142-2150; 2172-2182; 2199-2217;
RP 2310-2316; 2319-2329; 2340-2348; 2361-2379; 2402-2409; 2420-2429;
RP 2432-2442; 2462-2473; 2483-2503; 2512-2521; 2565-2575; 2587-2594;
RP 2651-2663; 2685-2693; 2705-2761; 2768-2787; 2795-2821; 2833-2841;
RP 2847-2881; 2885-2903; 2942-2968; 2979-3007; 3028-3039; 3045-3053;
RP 3095-3106; 3109-3127; 3132-3139; 3146-3154; 3175-3183; 3213-3231;
RP 3244-3259; 3270-3285; 3289-3297; 3317-3335; 3356-3368; 3374-3384;
RP 3424-3436; 3447-3469; 3477-3485; 3506-3513; 3519-3540; 3544-3568;
RP 3601-3637; 3648-3661; 3667-3676; 3686-3702; 3739-3749; 3771-3781;
RP 3784-3804; 3839-3878; 3887-3897; 3926-3963; 3969-3999; 4004-4018;
RP 4027-4060; 4084-4091; 4122-4138; 4159-4167; 4179-4205; 4278-4296;
RP 4339-4348; 4354-4360; 4384-4401; 4429-4447; 4467-4475; 4492-4500;
RP 4543-4551; 4590-4627 AND 4668-4684, PHOSPHORYLATION AT SER-4385, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Ovarian carcinoma;
RA Bienvenut W.V., Lilla S., von Kriegsheim A., Lempens A., Kolch W.;
RL Submitted (DEC-2008) to UniProtKB.
RN [6]
RP FUNCTION, INTERACTION WITH COL17A1, AND SUBCELLULAR LOCATION.
RX PubMed=12482924; DOI=10.1242/jcs.00241;
RA Koster J., Geerts D., Favre B., Borradori L., Sonnenberg A.;
RT "Analysis of the interactions between BP180, BP230, plectin and the
RT integrin alpha6beta4 important for hemidesmosome assembly.";
RL J. Cell Sci. 116:387-399(2003).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-125; SER-149; SER-720;
RP SER-1435; SER-1721; THR-4030 AND THR-4411, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [9]
RP INTERACTION WITH TOR1A.
RX PubMed=18827015; DOI=10.1242/jcs.029454;
RA Nery F.C., Zeng J., Niland B.P., Hewett J., Farley J., Irimia D., Li Y.,
RA Wiche G., Sonnenberg A., Breakefield X.O.;
RT "TorsinA binds the KASH domain of nesprins and participates in linkage
RT between nuclear envelope and cytoskeleton.";
RL J. Cell Sci. 121:3476-3486(2008).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=T-cell;
RX PubMed=19367720; DOI=10.1021/pr800500r;
RA Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.;
RT "Phosphorylation analysis of primary human T lymphocytes using sequential
RT IMAC and titanium oxide enrichment.";
RL J. Proteome Res. 7:5167-5176(2008).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1435, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-125; SER-149; SER-720;
RP SER-4382; SER-4385; SER-4386; SER-4389; SER-4390; SER-4391; SER-4392;
RP SER-4396; SER-4613; SER-4622; SER-4626 AND SER-4642, PHOSPHORYLATION [LARGE
RP SCALE ANALYSIS] AT SER-42 (ISOFORMS 2 AND 3), PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT SER-21 (ISOFORM 4), AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-720; THR-4030 AND SER-4626,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4386; SER-4389; SER-4396;
RP SER-4613; SER-4618 AND SER-4626, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT
RP SER-42 (ISOFORMS 2 AND 3), AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
RP SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [17]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-3091 AND LYS-3420, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [18]
RP FUNCTION OF ISOFORM 9, AND INVOLVEMENT IN LGMDR17.
RX PubMed=21109228; DOI=10.1016/j.ajhg.2010.10.017;
RA Gundesli H., Talim B., Korkusuz P., Balci-Hayta B., Cirak S., Akarsu N.A.,
RA Topaloglu H., Dincer P.;
RT "Mutation in exon 1f of PLEC, leading to disruption of plectin isoform 1f,
RT causes autosomal-recessive limb-girdle muscular dystrophy.";
RL Am. J. Hum. Genet. 87:834-841(2010).
RN [19]
RP INTERACTION WITH DST.
RX PubMed=19932097; DOI=10.1016/j.yexcr.2009.11.010;
RA Steiner-Champliaud M.F., Schneider Y., Favre B., Paulhe F.,
RA Praetzel-Wunder S., Faulkner G., Konieczny P., Raith M., Wiche G.,
RA Adebola A., Liem R.K., Langbein L., Sonnenberg A., Fontao L., Borradori L.;
RT "BPAG1 isoform-b: complex distribution pattern in striated and heart muscle
RT and association with plectin and alpha-actinin.";
RL Exp. Cell Res. 316:297-313(2010).
RN [20]
RP INVOLVEMENT IN MD-EBS AND EBS-PA.
RX PubMed=20665883; DOI=10.1002/humu.21330;
RA Natsuga K., Nishie W., Shinkuma S., Arita K., Nakamura H., Ohyama M.,
RA Osaka H., Kambara T., Hirako Y., Shimizu H.;
RT "Plectin deficiency leads to both muscular dystrophy and pyloric atresia in
RT epidermolysis bullosa simplex.";
RL Hum. Mutat. 31:E1687-E1698(2010).
RN [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-113; SER-125; SER-149;
RP SER-720; SER-1435; SER-1732; THR-4030; SER-4382; SER-4396; SER-4400;
RP SER-4613; SER-4622 AND SER-4642, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT
RP SER-42 (ISOFORMS 2 AND 3), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20
RP AND SER-21 (ISOFORM 4), AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
RP SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [22]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [23]
RP INTERACTION WITH ANK3.
RX PubMed=21223964; DOI=10.1016/j.yexcr.2011.01.002;
RA Maiweilidan Y., Klauza I., Kordeli E.;
RT "Novel interactions of ankyrins-G at the costameres: the muscle-specific
RT Obscurin/Titin-Binding-related Domain (OTBD) binds plectin and filamin C.";
RL Exp. Cell Res. 317:724-736(2011).
RN [24]
RP INVOLVEMENT IN MD-EBS.
RX PubMed=21263134; DOI=10.1212/wnl.0b013e31820882bd;
RA Selcen D., Juel V.C., Hobson-Webb L.D., Smith E.C., Stickler D.E.,
RA Bite A.V., Ohno K., Engel A.G.;
RT "Myasthenic syndrome caused by plectinopathy.";
RL Neurology 76:327-336(2011).
RN [25]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1435, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [26]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-125; SER-149; SER-720;
RP SER-1435; SER-1732; SER-2782; THR-4030; SER-4385; SER-4386; SER-4389;
RP SER-4396; SER-4400; SER-4607; SER-4613; SER-4618; SER-4622; SER-4626;
RP SER-4672 AND SER-4675, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [27]
RP INTERACTION WITH KRT1; KRT5; KRT8; KRT10; KRT14; KRT15; KRT18; DES AND VIM.
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 [28]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-720; SER-1047; SER-1435;
RP SER-2631; SER-2782; SER-2802; THR-2886; SER-3036; THR-3785; THR-4030;
RP SER-4054; SER-4386; SER-4390; SER-4392; TYR-4393; SER-4396; SER-4400;
RP SER-4616; SER-4626 AND SER-4675, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [29]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-4640, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Colon carcinoma;
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 [30]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [31]
RP X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 409-640.
RX PubMed=17397861; DOI=10.1016/j.jmb.2007.02.090;
RA Sonnenberg A., Rojas A.M., de Pereda J.M.;
RT "The structure of a tandem pair of spectrin repeats of plectin reveals a
RT modular organization of the plakin domain.";
RL J. Mol. Biol. 368:1379-1391(2007).
RN [32]
RP X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 159-403.
RX PubMed=12791251; DOI=10.1016/s0969-2126(03)00090-x;
RA Garcia-Alvarez B., Bobkov A., Sonnenberg A., de Pereda J.M.;
RT "Structural and functional analysis of the actin binding domain of plectin
RT suggests alternative mechanisms for binding to F-actin and integrin
RT beta4.";
RL Structure 11:615-625(2003).
RN [33]
RP VARIANT MD-EBS 1003-GLN--ALA-1005 DEL.
RX PubMed=8894687; DOI=10.1093/hmg/5.10.1539;
RA Pulkkinen L., Smith F.J.D., Shimizu H., Murata S., Yaoita H., Hachisuka H.,
RA Nishikawa T., McLean W.H.I., Uitto J.;
RT "Homozygous deletion mutations in the plectin gene (PLEC1) in patients with
RT epidermolysis bullosa simplex associated with late-onset muscular
RT dystrophy.";
RL Hum. Mol. Genet. 5:1539-1546(1996).
RN [34]
RP VARIANT MD-EBS LEU-429 INS.
RX PubMed=11159198; DOI=10.1016/s0002-9440(10)64003-5;
RA Bauer J.W., Rouan F., Kofler B., Rezniczek G.A., Kornacker I., Muss W.,
RA Hametner R., Klausegger A., Huber A., Pohla-Gubo G., Wiche G., Uitto J.,
RA Hintner H.;
RT "A compound heterozygous one amino-acid insertion/nonsense mutation in the
RT plectin gene causes epidermolysis bullosa simplex with plectin
RT deficiency.";
RL Am. J. Pathol. 158:617-625(2001).
RN [35]
RP VARIANT O-EBS TRP-2110.
RX PubMed=11851880; DOI=10.1046/j.0022-202x.2001.01591.x;
RA Koss-Harnes D., Hoeyheim B., Anton-Lamprecht I., Gjesti A.,
RA Joergensen R.S., Jahnsen F.L., Olaisen B., Wiche G., Gedde-Dahl T. Jr.;
RT "A site-specific plectin mutation causes dominant epidermolysis bullosa
RT simplex Ogna: two identical de novo mutations.";
RL J. Invest. Dermatol. 118:87-93(2002).
RN [36]
RP INVOLVEMENT IN EBS-PA.
RX PubMed=14675180; DOI=10.1111/j.1523-1747.2003.12639.x;
RA Charlesworth A., Gagnoux-Palacios L., Bonduelle M., Ortonne J.-P.,
RA De Raeve L., Meneguzzi G.;
RT "Identification of a lethal form of epidermolysis bullosa simplex
RT associated with a homozygous genetic mutation in plectin.";
RL J. Invest. Dermatol. 121:1344-1348(2003).
RN [37]
RP INVOLVEMENT IN EBSND.
RX PubMed=25712130; DOI=10.1093/hmg/ddv066;
RA Gostynska K.B., Nijenhuis M., Lemmink H., Pas H.H., Pasmooij A.M.,
RA Lang K.K., Castanon M.J., Wiche G., Jonkman M.F.;
RT "Mutation in exon 1a of PLEC, leading to disruption of plectin isoform 1a,
RT causes autosomal-recessive skin-only epidermolysis bullosa simplex.";
RL Hum. Mol. Genet. 24:3155-3162(2015).
RN [38]
RP VARIANT HIS-102.
RX PubMed=26477546; DOI=10.1016/j.ajhg.2015.09.009;
RG Care4Rare Canada Consortium;
RA Srour M., Hamdan F.F., McKnight D., Davis E., Mandel H.,
RA Schwartzentruber J., Martin B., Patry L., Nassif C., Dionne-Laporte A.,
RA Ospina L.H., Lemyre E., Massicotte C., Laframboise R., Maranda B.,
RA Labuda D., Decarie J.C., Rypens F., Goldsher D., Fallet-Bianco C.,
RA Soucy J.F., Laberge A.M., Maftei C., Boycott K., Brais B., Boucher R.M.,
RA Rouleau G.A., Katsanis N., Majewski J., Elpeleg O., Kukolich M.K.,
RA Shalev S., Michaud J.L.;
RT "Joubert Syndrome in French Canadians and Identification of Mutations in
RT CEP104.";
RL Am. J. Hum. Genet. 97:744-753(2015).
RN [39]
RP VARIANT TRP-2005, AND VARIANT LGMDR17 SER-3945.
RX PubMed=25556389;
RA Fattahi Z., Kahrizi K., Nafissi S., Fadaee M., Abedini S.S.,
RA Kariminejad A., Akbari M.R., Najmabadi H.;
RT "Report of a patient with limb-girdle muscular dystrophy, ptosis and
RT ophthalmoparesis caused by plectinopathy.";
RL Arch. Iran. Med. 18:60-64(2015).
RN [40]
RP VARIANT LGMDR17 SER-3945.
RX PubMed=27234031; DOI=10.1111/cge.12810;
RA Fattahi Z., Kalhor Z., Fadaee M., Vazehan R., Parsimehr E., Abolhassani A.,
RA Beheshtian M., Zamani G., Nafissi S., Nilipour Y., Akbari M.R., Kahrizi K.,
RA Kariminejad A., Najmabadi H.;
RT "Improved diagnostic yield of neuromuscular disorders applying clinical
RT exome sequencing in patients arising from a consanguineous population.";
RL Clin. Genet. 91:386-402(2017).
CC -!- FUNCTION: Interlinks intermediate filaments with microtubules and
CC microfilaments and anchors intermediate filaments to desmosomes or
CC hemidesmosomes. Could also bind muscle proteins such as actin to
CC membrane complexes in muscle. May be involved not only in the filaments
CC network, but also in the regulation of their dynamics. Structural
CC component of muscle. Isoform 9 plays a major role in the maintenance of
CC myofiber integrity. {ECO:0000269|PubMed:12482924,
CC ECO:0000269|PubMed:21109228}.
CC -!- SUBUNIT: Homodimer or homotetramer. Interacts (via actin-binding
CC domain) with SYNE3. Interacts (via calponin-homology (CH) 1 domain)
CC with VIM (via rod region) (By similarity). Interacts (via N-terminus)
CC with DST isoform 2 (via N-terminus) (PubMed:19932097). Interacts with
CC FER. Interacts with TOR1A (PubMed:18827015). Interacts with ANK3
CC (PubMed:21223964). Identified in complexes that contain VIM, EZR,
CC AHNAK, BFSP1, BFSP2, ANK2, PLEC, PRX and spectrin (By similarity).
CC Interacts with COL17A1 (PubMed:12482924). {ECO:0000250,
CC ECO:0000250|UniProtKB:P30427, ECO:0000250|UniProtKB:Q9QXS1,
CC ECO:0000269|PubMed:12482924, ECO:0000269|PubMed:18827015,
CC ECO:0000269|PubMed:19932097, ECO:0000269|PubMed:21223964}.
CC -!- SUBUNIT: [Isoform 2]: Interacts with KRT14, heterodimers consisting of
CC KRT8 and KRT18, heterodimers consisting of KRT5 and KRT14, heterodimers
CC consisting of KRT14 and KRT15, and heterodimers consisting of KRT1 and
CC KRT10 (PubMed:24940650). Interacts with DES and VIM (PubMed:24940650).
CC {ECO:0000269|PubMed:24940650}.
CC -!- INTERACTION:
CC Q15149; P35637: FUS; NbExp=4; IntAct=EBI-297903, EBI-400434;
CC Q15149; P42858: HTT; NbExp=4; IntAct=EBI-297903, EBI-466029;
CC Q15149; P16144: ITGB4; NbExp=7; IntAct=EBI-297903, EBI-948678;
CC Q15149; Q14145: KEAP1; NbExp=3; IntAct=EBI-297903, EBI-751001;
CC Q15149-8; Q14145: KEAP1; NbExp=4; IntAct=EBI-28998350, EBI-751001;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:12482924}. Cell junction, hemidesmosome
CC {ECO:0000269|PubMed:12482924}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=9;
CC Name=1; Synonyms=Plectin-6;
CC IsoId=Q15149-1; Sequence=Displayed;
CC Name=2; Synonyms=Plectin-1, 1c;
CC IsoId=Q15149-2; Sequence=VSP_005030;
CC Name=3;
CC IsoId=Q15149-3; Sequence=VSP_005030, VSP_005031;
CC Name=4; Synonyms=Plectin-11, 1a;
CC IsoId=Q15149-4; Sequence=VSP_023510;
CC Name=5; Synonyms=Plectin-8, 1b;
CC IsoId=Q15149-5; Sequence=VSP_037103, VSP_037106;
CC Name=6; Synonyms=Plectin-10, 1g;
CC IsoId=Q15149-6; Sequence=VSP_037104, VSP_037105;
CC Name=7; Synonyms=Plectin-7, 1d;
CC IsoId=Q15149-7; Sequence=VSP_037100, VSP_037109;
CC Name=8; Synonyms=Plectin-3, 1e;
CC IsoId=Q15149-8; Sequence=VSP_037101, VSP_037108;
CC Name=9; Synonyms=Plectin-2, 1f;
CC IsoId=Q15149-9; Sequence=VSP_037102, VSP_037107;
CC -!- TISSUE SPECIFICITY: Widely expressed with highest levels in muscle,
CC heart, placenta and spinal cord.
CC -!- DOMAIN: The N-terminus interacts with actin, the C-terminus with
CC vimentin, desmin, GFAP, cytokeratins, lamin B; whereas both the N- and
CC the C-terminus can bind integrin beta-4.
CC -!- PTM: Phosphorylated by CDK1; regulates dissociation from intermediate
CC filaments during mitosis. {ECO:0000250}.
CC -!- DISEASE: Epidermolysis bullosa simplex with pyloric atresia (EBS-PA)
CC [MIM:612138]: Autosomal recessive genodermatosis characterized by
CC severe skin blistering at birth and congenital pyloric atresia. Death
CC usually occurs in infancy. This disorder is allelic to MD-EBS.
CC {ECO:0000269|PubMed:14675180, ECO:0000269|PubMed:20665883}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- DISEASE: Epidermolysis bullosa simplex, with muscular dystrophy (MD-
CC EBS) [MIM:226670]: A form of epidermolysis bullosa characterized by the
CC association of blister formation at the level of the hemidesmosome with
CC late-onset muscular dystrophy. {ECO:0000269|PubMed:11159198,
CC ECO:0000269|PubMed:20665883, ECO:0000269|PubMed:21263134,
CC ECO:0000269|PubMed:8894687}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Epidermolysis bullosa simplex, Ogna type (O-EBS) [MIM:131950]:
CC A form of intraepidermal epidermolysis bullosa characterized by
CC generalized skin bruising, skin fragility with non-scarring blistering
CC and small hemorrhagic blisters on hands. At the ultrastructural level,
CC it is differentiated from classical cases of K-EBS, WC-EBS and DM-EBS,
CC by the occurrence of blisters originating in basal cells above
CC hemidesmosomes, and abnormal hemidesmosome intracellular attachment
CC plates. {ECO:0000269|PubMed:11851880}. Note=The disease is caused by
CC variants affecting the gene represented in this entry.
CC -!- DISEASE: Muscular dystrophy, limb-girdle, autosomal recessive 17
CC (LGMDR17) [MIM:613723]: A form of limb-girdle muscular dystrophy
CC characterized by early childhood onset of proximal muscle weakness.
CC Limb-girdle muscular dystrophies are characterized by proximal
CC weakness, weakness of the hip and shoulder girdles and prominent
CC asymmetrical quadriceps femoris and biceps brachii atrophy.
CC {ECO:0000269|PubMed:21109228, ECO:0000269|PubMed:25556389,
CC ECO:0000269|PubMed:27234031}. Note=The disease is caused by variants
CC affecting the gene represented in this entry. A 9 bp deletion
CC containing the initiation codon in exon 1f of PLEC have been found in
CC limb-girdle muscular dystrophy patients. The mutation results in
CC deficient expression of isoform 9 and disorganization of the myofibers,
CC without any effect on the skin.
CC -!- DISEASE: Epidermolysis bullosa simplex with nail dystrophy (EBSND)
CC [MIM:616487]: A form of epidermolysis bullosa, a dermatologic disorder
CC characterized by skin blistering. EBSND patients also manifest nail
CC dystrophy. {ECO:0000269|PubMed:25712130}. Note=The disease is caused by
CC variants affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the plakin or cytolinker family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Wikipedia; Note=Plectin entry;
CC URL="https://en.wikipedia.org/wiki/Plectin";
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DR EMBL; Z54367; CAA91196.1; -; Genomic_DNA.
DR EMBL; U53204; AAB05427.1; -; mRNA.
DR EMBL; U63610; AAB05428.1; -; Genomic_DNA.
DR EMBL; U63609; AAB05428.1; JOINED; Genomic_DNA.
DR EMBL; X97053; CAA65765.1; -; mRNA.
DR EMBL; AY480044; AAR95677.1; -; mRNA.
DR EMBL; AY480045; AAR95678.1; -; mRNA.
DR EMBL; AY480046; AAR95679.1; -; mRNA.
DR EMBL; AY480047; AAR95680.1; -; mRNA.
DR EMBL; AY480048; AAR95681.1; -; mRNA.
DR EMBL; AY480049; AAR95682.1; -; mRNA.
DR EMBL; AY480050; AAR95683.1; -; mRNA.
DR EMBL; AY480051; AAR95684.1; -; mRNA.
DR EMBL; AC109322; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS43769.1; -. [Q15149-2]
DR CCDS; CCDS43770.1; -. [Q15149-9]
DR CCDS; CCDS43771.1; -. [Q15149-8]
DR CCDS; CCDS43772.1; -. [Q15149-1]
DR CCDS; CCDS43773.1; -. [Q15149-5]
DR CCDS; CCDS43774.1; -. [Q15149-6]
DR CCDS; CCDS43775.1; -. [Q15149-4]
DR CCDS; CCDS47936.1; -. [Q15149-7]
DR PIR; C59404; A59404.
DR PIR; G02520; G02520.
DR RefSeq; NP_000436.2; NM_000445.4. [Q15149-2]
DR RefSeq; NP_958780.1; NM_201378.3. [Q15149-9]
DR RefSeq; NP_958781.1; NM_201379.2. [Q15149-8]
DR RefSeq; NP_958782.1; NM_201380.3. [Q15149-1]
DR RefSeq; NP_958783.1; NM_201381.2. [Q15149-7]
DR RefSeq; NP_958784.1; NM_201382.3. [Q15149-5]
DR RefSeq; NP_958785.1; NM_201383.2. [Q15149-6]
DR RefSeq; NP_958786.1; NM_201384.2. [Q15149-4]
DR PDB; 1MB8; X-ray; 2.15 A; A=175-403.
DR PDB; 2N03; NMR; -; A=4403-4606.
DR PDB; 2ODU; X-ray; 2.30 A; A=410-640.
DR PDB; 2ODV; X-ray; 2.05 A; A=410-640.
DR PDB; 3F7P; X-ray; 2.75 A; A/B=175-403.
DR PDB; 3PDY; X-ray; 2.22 A; A/B=653-858.
DR PDB; 3PE0; X-ray; 2.95 A; A/B=750-1028.
DR PDB; 4GDO; X-ray; 1.70 A; A/B/C/D/E/F=1492-1530.
DR PDB; 4Q58; X-ray; 4.00 A; A/B=175-400.
DR PDB; 4Q59; X-ray; 2.30 A; A/B=175-400.
DR PDB; 5J1F; X-ray; 3.00 A; A/B=860-928, A/B=999-1116.
DR PDB; 5J1G; X-ray; 1.80 A; A/B=1114-1343.
DR PDB; 5J1H; X-ray; 2.80 A; A/B=860-928, A/B=999-1116.
DR PDB; 5J1I; X-ray; 2.80 A; A/B=1114-1482.
DR PDBsum; 1MB8; -.
DR PDBsum; 2N03; -.
DR PDBsum; 2ODU; -.
DR PDBsum; 2ODV; -.
DR PDBsum; 3F7P; -.
DR PDBsum; 3PDY; -.
DR PDBsum; 3PE0; -.
DR PDBsum; 4GDO; -.
DR PDBsum; 4Q58; -.
DR PDBsum; 4Q59; -.
DR PDBsum; 5J1F; -.
DR PDBsum; 5J1G; -.
DR PDBsum; 5J1H; -.
DR PDBsum; 5J1I; -.
DR SASBDB; Q15149; -.
DR SMR; Q15149; -.
DR BioGRID; 111355; 309.
DR IntAct; Q15149; 191.
DR MINT; Q15149; -.
DR STRING; 9606.ENSP00000323856; -.
DR BindingDB; Q15149; -.
DR ChEMBL; CHEMBL1293240; -.
DR CarbonylDB; Q15149; -.
DR GlyGen; Q15149; 5 sites, 2 O-linked glycans (5 sites).
DR iPTMnet; Q15149; -.
DR MetOSite; Q15149; -.
DR PhosphoSitePlus; Q15149; -.
DR SwissPalm; Q15149; -.
DR BioMuta; PLEC; -.
DR DMDM; 209572726; -.
DR CPTAC; CPTAC-564; -.
DR CPTAC; CPTAC-565; -.
DR EPD; Q15149; -.
DR jPOST; Q15149; -.
DR MassIVE; Q15149; -.
DR MaxQB; Q15149; -.
DR PaxDb; Q15149; -.
DR PeptideAtlas; Q15149; -.
DR PRIDE; Q15149; -.
DR ProteomicsDB; 60462; -. [Q15149-1]
DR ProteomicsDB; 60463; -. [Q15149-2]
DR ProteomicsDB; 60464; -. [Q15149-3]
DR ProteomicsDB; 60465; -. [Q15149-4]
DR ProteomicsDB; 60466; -. [Q15149-5]
DR ProteomicsDB; 60467; -. [Q15149-6]
DR ProteomicsDB; 60468; -. [Q15149-7]
DR ProteomicsDB; 60469; -. [Q15149-8]
DR ProteomicsDB; 60470; -. [Q15149-9]
DR Antibodypedia; 3549; 209 antibodies from 32 providers.
DR DNASU; 5339; -.
DR Ensembl; ENST00000322810.8; ENSP00000323856.4; ENSG00000178209.17. [Q15149-1]
DR Ensembl; ENST00000345136.8; ENSP00000344848.3; ENSG00000178209.17. [Q15149-4]
DR Ensembl; ENST00000354589.7; ENSP00000346602.3; ENSG00000178209.17. [Q15149-5]
DR Ensembl; ENST00000354958.6; ENSP00000347044.2; ENSG00000178209.17. [Q15149-8]
DR Ensembl; ENST00000356346.7; ENSP00000348702.3; ENSG00000178209.17. [Q15149-9]
DR Ensembl; ENST00000357649.6; ENSP00000350277.2; ENSG00000178209.17. [Q15149-6]
DR Ensembl; ENST00000398774.6; ENSP00000381756.2; ENSG00000178209.17. [Q15149-7]
DR Ensembl; ENST00000436759.6; ENSP00000388180.2; ENSG00000178209.17. [Q15149-2]
DR Ensembl; ENST00000527096.5; ENSP00000434583.1; ENSG00000178209.17. [Q15149-3]
DR GeneID; 5339; -.
DR KEGG; hsa:5339; -.
DR MANE-Select; ENST00000345136.8; ENSP00000344848.3; NM_201384.3; NP_958786.1. [Q15149-4]
DR UCSC; uc003zab.2; human. [Q15149-1]
DR CTD; 5339; -.
DR DisGeNET; 5339; -.
DR GeneCards; PLEC; -.
DR GeneReviews; PLEC; -.
DR HGNC; HGNC:9069; PLEC.
DR HPA; ENSG00000178209; Tissue enhanced (skeletal).
DR MalaCards; PLEC; -.
DR MIM; 131950; phenotype.
DR MIM; 226670; phenotype.
DR MIM; 601282; gene.
DR MIM; 612138; phenotype.
DR MIM; 613723; phenotype.
DR MIM; 616487; phenotype.
DR neXtProt; NX_Q15149; -.
DR OpenTargets; ENSG00000178209; -.
DR Orphanet; 1114; Aplasia cutis congenita.
DR Orphanet; 257; Epidermolysis bullosa simplex with muscular dystrophy.
DR Orphanet; 158684; Epidermolysis bullosa simplex with pyloric atresia.
DR Orphanet; 79401; PLEC-related intermediate epidermolysis bullosa simplex without extracutaneous involvement.
DR Orphanet; 254361; Plectin-related limb-girdle muscular dystrophy R17.
DR PharmGKB; PA33399; -.
DR VEuPathDB; HostDB:ENSG00000178209; -.
DR eggNOG; KOG0516; Eukaryota.
DR eggNOG; KOG3344; Eukaryota.
DR GeneTree; ENSGT00940000159045; -.
DR HOGENOM; CLU_000132_0_0_1; -.
DR InParanoid; Q15149; -.
DR OMA; REERWVY; -.
DR OrthoDB; 2464at2759; -.
DR PhylomeDB; Q15149; -.
DR TreeFam; TF335163; -.
DR PathwayCommons; Q15149; -.
DR Reactome; R-HSA-2022090; Assembly of collagen fibrils and other multimeric structures.
DR Reactome; R-HSA-264870; Caspase-mediated cleavage of cytoskeletal proteins.
DR Reactome; R-HSA-446107; Type I hemidesmosome assembly.
DR SignaLink; Q15149; -.
DR SIGNOR; Q15149; -.
DR BioGRID-ORCS; 5339; 40 hits in 1083 CRISPR screens.
DR ChiTaRS; PLEC; human.
DR EvolutionaryTrace; Q15149; -.
DR GeneWiki; Plectin; -.
DR GenomeRNAi; 5339; -.
DR Pharos; Q15149; Tbio.
DR PRO; PR:Q15149; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; Q15149; protein.
DR Bgee; ENSG00000178209; Expressed in sural nerve and 198 other tissues.
DR ExpressionAtlas; Q15149; baseline and differential.
DR Genevisible; Q15149; HS.
DR GO; GO:0030424; C:axon; IEA:Ensembl.
DR GO; GO:0005903; C:brush border; IEA:Ensembl.
DR GO; GO:0043034; C:costamere; TAS:BHF-UCL.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0030425; C:dendrite; IEA:Ensembl.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005925; C:focal adhesion; IDA:HPA.
DR GO; GO:0030056; C:hemidesmosome; IDA:UniProtKB.
DR GO; GO:0045111; C:intermediate filament cytoskeleton; IDA:HPA.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005741; C:mitochondrial outer membrane; IEA:Ensembl.
DR GO; GO:0043209; C:myelin sheath; IEA:Ensembl.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; NAS:ProtInc.
DR GO; GO:0042383; C:sarcolemma; IDA:UniProtKB.
DR GO; GO:0016528; C:sarcoplasm; ISS:BHF-UCL.
DR GO; GO:0030018; C:Z disc; IEA:Ensembl.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0030506; F:ankyrin binding; IPI:BHF-UCL.
DR GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL.
DR GO; GO:0002162; F:dystroglycan binding; IEA:Ensembl.
DR GO; GO:0043621; F:protein self-association; IEA:Ensembl.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0005200; F:structural constituent of cytoskeleton; IBA:GO_Central.
DR GO; GO:0008307; F:structural constituent of muscle; IMP:UniProtKB.
DR GO; GO:0005198; F:structural molecule activity; IBA:GO_Central.
DR GO; GO:0031532; P:actin cytoskeleton reorganization; IEA:Ensembl.
DR GO; GO:2000689; P:actomyosin contractile ring assembly actin filament organization; IEA:Ensembl.
DR GO; GO:0034332; P:adherens junction organization; IEA:Ensembl.
DR GO; GO:0055013; P:cardiac muscle cell development; IEA:Ensembl.
DR GO; GO:0000902; P:cell morphogenesis; IEA:Ensembl.
DR GO; GO:0031668; P:cellular response to extracellular stimulus; IEA:Ensembl.
DR GO; GO:0071498; P:cellular response to fluid shear stress; IEA:Ensembl.
DR GO; GO:0071464; P:cellular response to hydrostatic pressure; IEA:Ensembl.
DR GO; GO:0071260; P:cellular response to mechanical stimulus; IEA:Ensembl.
DR GO; GO:0061436; P:establishment of skin barrier; IEA:Ensembl.
DR GO; GO:0010761; P:fibroblast migration; IEA:Ensembl.
DR GO; GO:0010467; P:gene expression; IEA:Ensembl.
DR GO; GO:0031581; P:hemidesmosome assembly; IDA:UniProtKB.
DR GO; GO:0045104; P:intermediate filament cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0045109; P:intermediate filament organization; IEA:Ensembl.
DR GO; GO:0003334; P:keratinocyte development; IEA:Ensembl.
DR GO; GO:0002522; P:leukocyte migration involved in immune response; IEA:Ensembl.
DR GO; GO:0070584; P:mitochondrion morphogenesis; IEA:Ensembl.
DR GO; GO:0035264; P:multicellular organism growth; IEA:Ensembl.
DR GO; GO:0045445; P:myoblast differentiation; IEA:Ensembl.
DR GO; GO:0006469; P:negative regulation of protein kinase activity; IEA:Ensembl.
DR GO; GO:0006997; P:nucleus organization; IEA:Ensembl.
DR GO; GO:0032287; P:peripheral nervous system myelin maintenance; IEA:Ensembl.
DR GO; GO:0008104; P:protein localization; IEA:Ensembl.
DR GO; GO:0043933; P:protein-containing complex organization; IEA:Ensembl.
DR GO; GO:2000983; P:regulation of ATP citrate synthase activity; IEA:Ensembl.
DR GO; GO:0043114; P:regulation of vascular permeability; IEA:Ensembl.
DR GO; GO:0022904; P:respiratory electron transport chain; IEA:Ensembl.
DR GO; GO:0032094; P:response to food; IEA:Ensembl.
DR GO; GO:0045214; P:sarcomere organization; IEA:Ensembl.
DR GO; GO:0048741; P:skeletal muscle fiber development; IEA:Ensembl.
DR GO; GO:0014866; P:skeletal myofibril assembly; IEA:Ensembl.
DR GO; GO:0010818; P:T cell chemotaxis; IEA:Ensembl.
DR GO; GO:0120193; P:tight junction organization; IEA:Ensembl.
DR GO; GO:0019226; P:transmission of nerve impulse; IEA:Ensembl.
DR GO; GO:0042060; P:wound healing; IBA:GO_Central.
DR CDD; cd00014; CH; 2.
DR CDD; cd00176; SPEC; 3.
DR Gene3D; 1.10.10.10; -; 1.
DR Gene3D; 1.10.418.10; -; 2.
DR Gene3D; 3.90.1290.10; -; 6.
DR InterPro; IPR001589; Actinin_actin-bd_CS.
DR InterPro; IPR001715; CH-domain.
DR InterPro; IPR036872; CH_dom_sf.
DR InterPro; IPR041615; Desmoplakin_SH3.
DR InterPro; IPR041573; Desmoplakin_Spectrin-like.
DR InterPro; IPR043197; Plakin.
DR InterPro; IPR035915; Plakin_repeat_sf.
DR InterPro; IPR030269; Plectin.
DR InterPro; IPR001101; Plectin_repeat.
DR InterPro; IPR005326; S10_plectin_N.
DR InterPro; IPR001452; SH3_domain.
DR InterPro; IPR018159; Spectrin/alpha-actinin.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR PANTHER; PTHR23169; PTHR23169; 3.
DR PANTHER; PTHR23169:SF20; PTHR23169:SF20; 3.
DR Pfam; PF00307; CH; 2.
DR Pfam; PF00681; Plectin; 17.
DR Pfam; PF03501; S10_plectin; 1.
DR Pfam; PF17902; SH3_10; 1.
DR Pfam; PF18373; Spectrin_like; 1.
DR SMART; SM00033; CH; 2.
DR SMART; SM00250; PLEC; 32.
DR SMART; SM00150; SPEC; 7.
DR SUPFAM; SSF47576; SSF47576; 1.
DR SUPFAM; SSF75399; SSF75399; 7.
DR PROSITE; PS00019; ACTININ_1; 1.
DR PROSITE; PS00020; ACTININ_2; 1.
DR PROSITE; PS50021; CH; 2.
DR PROSITE; PS50002; SH3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Actin-binding; Alternative splicing;
KW Cell junction; Coiled coil; Cytoplasm; Cytoskeleton;
KW Direct protein sequencing; Disease variant; Epidermolysis bullosa;
KW Limb-girdle muscular dystrophy; Methylation; Phosphoprotein;
KW Reference proteome; Repeat; SH3 domain.
FT CHAIN 1..4684
FT /note="Plectin"
FT /id="PRO_0000078135"
FT DOMAIN 179..282
FT /note="Calponin-homology (CH) 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT DOMAIN 295..400
FT /note="Calponin-homology (CH) 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT REPEAT 645..710
FT /note="Spectrin 1"
FT REPEAT 740..824
FT /note="Spectrin 2"
FT REPEAT 837..930
FT /note="Spectrin 3"
FT DOMAIN 941..998
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REPEAT 1315..1415
FT /note="Spectrin 4"
FT REPEAT 2826..2863
FT /note="Plectin 1"
FT REPEAT 2864..2901
FT /note="Plectin 2"
FT REPEAT 2902..2939
FT /note="Plectin 3"
FT REPEAT 2940..2977
FT /note="Plectin 4"
FT REPEAT 2981..3015
FT /note="Plectin 5"
FT REPEAT 3116..3153
FT /note="Plectin 6"
FT REPEAT 3154..3191
FT /note="Plectin 7"
FT REPEAT 3192..3229
FT /note="Plectin 8"
FT REPEAT 3230..3267
FT /note="Plectin 9"
FT REPEAT 3268..3305
FT /note="Plectin 10"
FT REPEAT 3306..3343
FT /note="Plectin 11"
FT REPEAT 3485..3522
FT /note="Plectin 12"
FT REPEAT 3523..3560
FT /note="Plectin 13"
FT REPEAT 3561..3598
FT /note="Plectin 14"
FT REPEAT 3599..3636
FT /note="Plectin 15"
FT REPEAT 3640..3674
FT /note="Plectin 16"
FT REPEAT 3820..3857
FT /note="Plectin 17"
FT REPEAT 3858..3895
FT /note="Plectin 18"
FT REPEAT 3896..3933
FT /note="Plectin 19"
FT REPEAT 3934..3971
FT /note="Plectin 20"
FT REPEAT 3975..4008
FT /note="Plectin 21"
FT REPEAT 4063..4100
FT /note="Plectin 22"
FT REPEAT 4101..4138
FT /note="Plectin 23"
FT REPEAT 4139..4176
FT /note="Plectin 24"
FT REPEAT 4177..4214
FT /note="Plectin 25"
FT REPEAT 4218..4252
FT /note="Plectin 26"
FT REPEAT 4265..4305
FT /note="Plectin 27"
FT REPEAT 4319..4356
FT /note="Plectin 28"
FT REPEAT 4408..4445
FT /note="Plectin 29"
FT REPEAT 4446..4483
FT /note="Plectin 30"
FT REPEAT 4484..4521
FT /note="Plectin 31"
FT REPEAT 4522..4559
FT /note="Plectin 32"
FT REPEAT 4560..4597
FT /note="Plectin 33"
FT REGION 1..1470
FT /note="Globular 1"
FT REGION 144..179
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 175..400
FT /note="Actin-binding"
FT REGION 1471..2755
FT /note="Central fibrous rod domain"
FT REGION 1618..1650
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1794..1836
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2105..2139
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2217..2307
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2668..2707
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2756..4684
FT /note="Globular 2"
FT REGION 2763..2784
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3310..3331
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 4250..4300
FT /note="Binding to intermediate filaments"
FT /evidence="ECO:0000250"
FT REGION 4611..4684
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 4625..4640
FT /note="4 X 4 AA tandem repeats of G-S-R-X"
FT COILED 1469..2756
FT /evidence="ECO:0000255"
FT COMPBIAS 1797..1835
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2218..2259
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2271..2285
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2668..2683
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2684..2707
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 4611..4677
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 113
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 125
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 149
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 720
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19369195,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 1047
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 1435
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 1721
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983"
FT MOD_RES 1725
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9QXS1"
FT MOD_RES 1732
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 2631
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 2636
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9QXS1"
FT MOD_RES 2782
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 2802
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 2886
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 3033
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9QXS1"
FT MOD_RES 3036
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 3053
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9QXS1"
FT MOD_RES 3091
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 3362
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9QXS1"
FT MOD_RES 3420
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 3580
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P30427"
FT MOD_RES 3785
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 4030
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 4054
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 4382
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 4384
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QXS1"
FT MOD_RES 4385
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|Ref.5, ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 4386
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 4389
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163"
FT MOD_RES 4390
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 4391
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 4392
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 4393
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 4396
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 4400
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 4406
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P30427"
FT MOD_RES 4411
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17081983"
FT MOD_RES 4539
FT /note="Phosphothreonine; by CDK1"
FT /evidence="ECO:0000250|UniProtKB:Q9JI55"
FT MOD_RES 4607
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 4613
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 4615
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9QXS1"
FT MOD_RES 4616
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 4618
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 4622
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 4623
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9QXS1"
FT MOD_RES 4626
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 4627
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q9QXS1"
FT MOD_RES 4640
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 4642
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 4672
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 4675
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT VAR_SEQ 1..174
FT /note="MVAGMLMPRDQLRAIYEVLFREGVMVAKKDRRPRSLHPHVPGVTNLQVMRAM
FT ASLRARGLVRETFAWCHFYWYLTNEGIAHLRQYLHLPPEIVPASLQRVRRPVAMVMPAR
FT RTPHVQAVQGPLGSPPKRGPLPTEEQRVYRRKELEEVSPETPVVPATTQRTLARPGPEP
FT APAT -> MSGEDAEVRAVSEDVSNGSSGSPSPGDTLPWNLGKTQRSRRSGGGAGSNGS
FT VLDPAERAVIRIA (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:14672974,
FT ECO:0000303|PubMed:8698233"
FT /id="VSP_005030"
FT VAR_SEQ 1..174
FT /note="MVAGMLMPRDQLRAIYEVLFREGVMVAKKDRRPRSLHPHVPGVTNLQVMRAM
FT ASLRARGLVRETFAWCHFYWYLTNEGIAHLRQYLHLPPEIVPASLQRVRRPVAMVMPAR
FT RTPHVQAVQGPLGSPPKRGPLPTEEQRVYRRKELEEVSPETPVVPATTQRTLARPGPEP
FT APAT -> MSQHQLRVPQPEGLGRKRTSSEDNLYLAVLRASEGKK (in isoform
FT 4)"
FT /evidence="ECO:0000303|PubMed:14672974"
FT /id="VSP_023510"
FT VAR_SEQ 1..169
FT /note="Missing (in isoform 7)"
FT /evidence="ECO:0000303|PubMed:14672974"
FT /id="VSP_037100"
FT VAR_SEQ 1..159
FT /note="Missing (in isoform 8)"
FT /evidence="ECO:0000303|PubMed:14672974"
FT /id="VSP_037101"
FT VAR_SEQ 1..151
FT /note="Missing (in isoform 9)"
FT /evidence="ECO:0000303|PubMed:14672974"
FT /id="VSP_037102"
FT VAR_SEQ 1..137
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14672974"
FT /id="VSP_037103"
FT VAR_SEQ 1..133
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:14672974"
FT /id="VSP_037104"
FT VAR_SEQ 134..174
FT /note="TEEQRVYRRKELEEVSPETPVVPATTQRTLARPGPEPAPAT -> MSGAGGA
FT FASPREVLLERPCWLDGGCEPARRGYLYQQLCCV (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:14672974"
FT /id="VSP_037105"
FT VAR_SEQ 138..174
FT /note="RVYRRKELEEVSPETPVVPATTQRTLARPGPEPAPAT -> MEPSGSLFPSL
FT VVVGHVVTLAAVWHWRRGRRWAQDEQ (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14672974"
FT /id="VSP_037106"
FT VAR_SEQ 152..174
FT /note="TPVVPATTQRTLARPGPEPAPAT -> MAGPLPDEQDFIQAYEEVREKYK
FT (in isoform 9)"
FT /evidence="ECO:0000303|PubMed:14672974"
FT /id="VSP_037107"
FT VAR_SEQ 160..174
FT /note="QRTLARPGPEPAPAT -> MDPSRAIQNEISSLK (in isoform 8)"
FT /evidence="ECO:0000303|PubMed:14672974"
FT /id="VSP_037108"
FT VAR_SEQ 170..174
FT /note="PAPAT -> MKIVP (in isoform 7)"
FT /evidence="ECO:0000303|PubMed:14672974"
FT /id="VSP_037109"
FT VAR_SEQ 409..412
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:8698233"
FT /id="VSP_005031"
FT VARIANT 102
FT /note="R -> H (in dbSNP:rs200335928)"
FT /evidence="ECO:0000269|PubMed:26477546"
FT /id="VAR_075706"
FT VARIANT 429
FT /note="L -> LL (in MD-EBS)"
FT /evidence="ECO:0000269|PubMed:11159198"
FT /id="VAR_011336"
FT VARIANT 641
FT /note="A -> V (in dbSNP:rs11136336)"
FT /id="VAR_053585"
FT VARIANT 1003..1005
FT /note="Missing (in MD-EBS)"
FT /evidence="ECO:0000269|PubMed:8894687"
FT /id="VAR_011337"
FT VARIANT 1321
FT /note="L -> V (in dbSNP:rs3135109)"
FT /evidence="ECO:0000269|PubMed:8698233"
FT /id="VAR_060088"
FT VARIANT 1386
FT /note="R -> Q (in dbSNP:rs11136334)"
FT /id="VAR_060089"
FT VARIANT 1459
FT /note="H -> R (in dbSNP:rs55895668)"
FT /id="VAR_062133"
FT VARIANT 2005
FT /note="R -> W (in dbSNP:rs200543521)"
FT /evidence="ECO:0000269|PubMed:25556389"
FT /id="VAR_076564"
FT VARIANT 2110
FT /note="R -> W (in O-EBS; dbSNP:rs80338756)"
FT /evidence="ECO:0000269|PubMed:11851880"
FT /id="VAR_015817"
FT VARIANT 2150
FT /note="R -> W (in dbSNP:rs34893635)"
FT /id="VAR_053586"
FT VARIANT 2194
FT /note="A -> V (in dbSNP:rs7002002)"
FT /id="VAR_053587"
FT VARIANT 2791
FT /note="S -> P (in dbSNP:rs7833924)"
FT /id="VAR_053588"
FT VARIANT 2821
FT /note="R -> W (in dbSNP:rs35723243)"
FT /id="VAR_053589"
FT VARIANT 2969
FT /note="R -> H (in dbSNP:rs6558407)"
FT /id="VAR_053590"
FT VARIANT 3162
FT /note="V -> I (in dbSNP:rs35027700)"
FT /id="VAR_053591"
FT VARIANT 3171
FT /note="A -> V (in dbSNP:rs35858667)"
FT /id="VAR_053592"
FT VARIANT 3486
FT /note="T -> M (in dbSNP:rs34725742)"
FT /id="VAR_053593"
FT VARIANT 3490
FT /note="G -> A (in dbSNP:rs35261863)"
FT /id="VAR_053594"
FT VARIANT 3945
FT /note="G -> S (in LGMDR17)"
FT /evidence="ECO:0000269|PubMed:25556389,
FT ECO:0000269|PubMed:27234031"
FT /id="VAR_076565"
FT CONFLICT 71
FT /note="Y -> F (in Ref. 1; CAA91196)"
FT /evidence="ECO:0000305"
FT CONFLICT 94
FT /note="P -> A (in Ref. 1; CAA91196)"
FT /evidence="ECO:0000305"
FT CONFLICT 139
FT /note="V -> L (in Ref. 1; CAA91196)"
FT /evidence="ECO:0000305"
FT CONFLICT 185
FT /note="F -> S (in Ref. 1; CAA91196)"
FT /evidence="ECO:0000305"
FT CONFLICT 259
FT /note="N -> D (in Ref. 2; AAB05427/AAB05428)"
FT /evidence="ECO:0000305"
FT CONFLICT 550
FT /note="N -> H (in Ref. 1; CAA91196)"
FT /evidence="ECO:0000305"
FT CONFLICT 560
FT /note="V -> I (in Ref. 1; CAA91196)"
FT /evidence="ECO:0000305"
FT CONFLICT 706
FT /note="R -> Q (in Ref. 1; CAA91196)"
FT /evidence="ECO:0000305"
FT CONFLICT 886
FT /note="Y -> N (in Ref. 1; CAA91196)"
FT /evidence="ECO:0000305"
FT CONFLICT 1002
FT /note="A -> V (in Ref. 1; CAA91196)"
FT /evidence="ECO:0000305"
FT CONFLICT 1309
FT /note="V -> L (in Ref. 2; AAB05427/AAB05428)"
FT /evidence="ECO:0000305"
FT CONFLICT 1334
FT /note="V -> L (in Ref. 2; AAB05427/AAB05428)"
FT /evidence="ECO:0000305"
FT CONFLICT 1534
FT /note="M -> I (in Ref. 1; CAA91196)"
FT /evidence="ECO:0000305"
FT CONFLICT 1662
FT /note="A -> T (in Ref. 2; AAB05427/AAB05428)"
FT /evidence="ECO:0000305"
FT CONFLICT 1688..1690
FT /note="RLR -> WLC (in Ref. 1; CAA91196)"
FT /evidence="ECO:0000305"
FT CONFLICT 1767
FT /note="E -> Q (in Ref. 1; CAA91196)"
FT /evidence="ECO:0000305"
FT CONFLICT 1789
FT /note="A -> L (in Ref. 1; CAA91196)"
FT /evidence="ECO:0000305"
FT CONFLICT 1910
FT /note="R -> K (in Ref. 1; CAA91196)"
FT /evidence="ECO:0000305"
FT CONFLICT 2154
FT /note="K -> N (in Ref. 2; AAB05427/AAB05428/CAA65765 and 3;
FT AAR95680/AAR95682/AAR95683)"
FT /evidence="ECO:0000305"
FT CONFLICT 2160
FT /note="R -> S (in Ref. 1; CAA91196)"
FT /evidence="ECO:0000305"
FT CONFLICT 2215
FT /note="Q -> R (in Ref. 1; CAA91196)"
FT /evidence="ECO:0000305"
FT CONFLICT 2244
FT /note="S -> A (in Ref. 1; CAA91196 and 2; AAB05427/
FT AAB05428/CAA65765)"
FT /evidence="ECO:0000305"
FT CONFLICT 3027
FT /note="K -> E (in Ref. 2; AAB05427/AAB05428)"
FT /evidence="ECO:0000305"
FT CONFLICT 3310
FT /note="A -> E (in Ref. 1; CAA91196)"
FT /evidence="ECO:0000305"
FT CONFLICT 3361
FT /note="L -> F (in Ref. 1; CAA91196)"
FT /evidence="ECO:0000305"
FT CONFLICT 3408
FT /note="L -> F (in Ref. 1; CAA91196)"
FT /evidence="ECO:0000305"
FT CONFLICT 3447
FT /note="A -> S (in Ref. 1; CAA91196)"
FT /evidence="ECO:0000305"
FT CONFLICT 3531
FT /note="A -> G (in Ref. 1; CAA91196)"
FT /evidence="ECO:0000305"
FT CONFLICT 3580
FT /note="S -> R (in Ref. 1; CAA91196)"
FT /evidence="ECO:0000305"
FT CONFLICT 3589
FT /note="Q -> K (in Ref. 1; CAA91196)"
FT /evidence="ECO:0000305"
FT CONFLICT 3596
FT /note="Q -> E (in Ref. 1; CAA91196)"
FT /evidence="ECO:0000305"
FT CONFLICT 3616
FT /note="H -> N (in Ref. 1; CAA91196)"
FT /evidence="ECO:0000305"
FT CONFLICT 3686
FT /note="A -> V (in Ref. 1; CAA91196)"
FT /evidence="ECO:0000305"
FT CONFLICT 3786
FT /note="A -> G (in Ref. 1; CAA91196)"
FT /evidence="ECO:0000305"
FT CONFLICT 3808
FT /note="R -> K (in Ref. 1; CAA91196)"
FT /evidence="ECO:0000305"
FT CONFLICT 3816
FT /note="A -> G (in Ref. 1; CAA91196)"
FT /evidence="ECO:0000305"
FT CONFLICT 3821
FT /note="C -> F (in Ref. 1; CAA91196)"
FT /evidence="ECO:0000305"
FT CONFLICT 3915
FT /note="Q -> K (in Ref. 1; CAA91196)"
FT /evidence="ECO:0000305"
FT CONFLICT 3999
FT /note="R -> K (in Ref. 1; CAA91196)"
FT /evidence="ECO:0000305"
FT CONFLICT 4007
FT /note="T -> S (in Ref. 1; CAA91196)"
FT /evidence="ECO:0000305"
FT CONFLICT 4467
FT /note="F -> L (in Ref. 1; CAA91196)"
FT /evidence="ECO:0000305"
FT HELIX 174..193
FT /evidence="ECO:0007829|PDB:1MB8"
FT HELIX 194..196
FT /evidence="ECO:0007829|PDB:4Q59"
FT TURN 203..209
FT /evidence="ECO:0007829|PDB:1MB8"
FT HELIX 211..221
FT /evidence="ECO:0007829|PDB:1MB8"
FT HELIX 233..249
FT /evidence="ECO:0007829|PDB:1MB8"
FT HELIX 259..263
FT /evidence="ECO:0007829|PDB:1MB8"
FT HELIX 267..282
FT /evidence="ECO:0007829|PDB:1MB8"
FT TURN 283..285
FT /evidence="ECO:0007829|PDB:4Q59"
FT HELIX 297..308
FT /evidence="ECO:0007829|PDB:1MB8"
FT TURN 309..311
FT /evidence="ECO:0007829|PDB:1MB8"
FT HELIX 322..324
FT /evidence="ECO:0007829|PDB:1MB8"
FT HELIX 328..337
FT /evidence="ECO:0007829|PDB:1MB8"
FT HELIX 339..341
FT /evidence="ECO:0007829|PDB:1MB8"
FT HELIX 344..347
FT /evidence="ECO:0007829|PDB:1MB8"
FT HELIX 352..367
FT /evidence="ECO:0007829|PDB:1MB8"
FT HELIX 375..378
FT /evidence="ECO:0007829|PDB:1MB8"
FT STRAND 380..382
FT /evidence="ECO:0007829|PDB:1MB8"
FT HELIX 385..398
FT /evidence="ECO:0007829|PDB:1MB8"
FT HELIX 414..440
FT /evidence="ECO:0007829|PDB:2ODV"
FT HELIX 448..464
FT /evidence="ECO:0007829|PDB:2ODV"
FT HELIX 466..488
FT /evidence="ECO:0007829|PDB:2ODV"
FT STRAND 490..492
FT /evidence="ECO:0007829|PDB:2ODU"
FT HELIX 500..562
FT /evidence="ECO:0007829|PDB:2ODV"
FT TURN 563..566
FT /evidence="ECO:0007829|PDB:2ODV"
FT HELIX 572..598
FT /evidence="ECO:0007829|PDB:2ODV"
FT HELIX 604..628
FT /evidence="ECO:0007829|PDB:2ODV"
FT HELIX 656..678
FT /evidence="ECO:0007829|PDB:3PDY"
FT HELIX 685..714
FT /evidence="ECO:0007829|PDB:3PDY"
FT HELIX 715..718
FT /evidence="ECO:0007829|PDB:3PDY"
FT HELIX 721..778
FT /evidence="ECO:0007829|PDB:3PDY"
FT HELIX 788..821
FT /evidence="ECO:0007829|PDB:3PDY"
FT HELIX 827..854
FT /evidence="ECO:0007829|PDB:3PDY"
FT HELIX 861..886
FT /evidence="ECO:0007829|PDB:5J1H"
FT HELIX 894..913
FT /evidence="ECO:0007829|PDB:5J1H"
FT HELIX 915..926
FT /evidence="ECO:0007829|PDB:5J1H"
FT HELIX 932..934
FT /evidence="ECO:0007829|PDB:3PE0"
FT STRAND 944..948
FT /evidence="ECO:0007829|PDB:3PE0"
FT STRAND 964..970
FT /evidence="ECO:0007829|PDB:3PE0"
FT STRAND 975..979
FT /evidence="ECO:0007829|PDB:3PE0"
FT STRAND 985..989
FT /evidence="ECO:0007829|PDB:3PE0"
FT HELIX 990..992
FT /evidence="ECO:0007829|PDB:3PE0"
FT HELIX 999..1044
FT /evidence="ECO:0007829|PDB:5J1H"
FT HELIX 1048..1052
FT /evidence="ECO:0007829|PDB:5J1H"
FT HELIX 1056..1076
FT /evidence="ECO:0007829|PDB:5J1H"
FT STRAND 1077..1079
FT /evidence="ECO:0007829|PDB:5J1H"
FT STRAND 1080..1082
FT /evidence="ECO:0007829|PDB:5J1F"
FT HELIX 1085..1109
FT /evidence="ECO:0007829|PDB:5J1H"
FT HELIX 1118..1144
FT /evidence="ECO:0007829|PDB:5J1G"
FT HELIX 1152..1188
FT /evidence="ECO:0007829|PDB:5J1G"
FT STRAND 1190..1192
FT /evidence="ECO:0007829|PDB:5J1G"
FT HELIX 1197..1252
FT /evidence="ECO:0007829|PDB:5J1G"
FT HELIX 1259..1277
FT /evidence="ECO:0007829|PDB:5J1G"
FT HELIX 1280..1304
FT /evidence="ECO:0007829|PDB:5J1G"
FT HELIX 1311..1340
FT /evidence="ECO:0007829|PDB:5J1G"
FT HELIX 1378..1397
FT /evidence="ECO:0007829|PDB:5J1I"
FT HELIX 1399..1430
FT /evidence="ECO:0007829|PDB:5J1I"
FT HELIX 1445..1476
FT /evidence="ECO:0007829|PDB:5J1I"
FT HELIX 1493..1527
FT /evidence="ECO:0007829|PDB:4GDO"
FT STRAND 4417..4422
FT /evidence="ECO:0007829|PDB:2N03"
FT TURN 4423..4425
FT /evidence="ECO:0007829|PDB:2N03"
FT HELIX 4431..4437
FT /evidence="ECO:0007829|PDB:2N03"
FT HELIX 4442..4454
FT /evidence="ECO:0007829|PDB:2N03"
FT STRAND 4456..4458
FT /evidence="ECO:0007829|PDB:2N03"
FT TURN 4461..4464
FT /evidence="ECO:0007829|PDB:2N03"
FT HELIX 4469..4475
FT /evidence="ECO:0007829|PDB:2N03"
FT HELIX 4480..4482
FT /evidence="ECO:0007829|PDB:2N03"
FT HELIX 4483..4494
FT /evidence="ECO:0007829|PDB:2N03"
FT TURN 4499..4501
FT /evidence="ECO:0007829|PDB:2N03"
FT HELIX 4507..4513
FT /evidence="ECO:0007829|PDB:2N03"
FT HELIX 4518..4531
FT /evidence="ECO:0007829|PDB:2N03"
FT STRAND 4532..4535
FT /evidence="ECO:0007829|PDB:2N03"
FT STRAND 4537..4543
FT /evidence="ECO:0007829|PDB:2N03"
FT HELIX 4545..4551
FT /evidence="ECO:0007829|PDB:2N03"
FT HELIX 4556..4563
FT /evidence="ECO:0007829|PDB:2N03"
FT HELIX 4565..4567
FT /evidence="ECO:0007829|PDB:2N03"
FT STRAND 4575..4577
FT /evidence="ECO:0007829|PDB:2N03"
FT HELIX 4583..4589
FT /evidence="ECO:0007829|PDB:2N03"
FT STRAND 4591..4597
FT /evidence="ECO:0007829|PDB:2N03"
FT STRAND 4599..4603
FT /evidence="ECO:0007829|PDB:2N03"
FT REGION Q15149-2:964..4574
FT /note="Required for interaction with intermediate filament
FT proteins"
FT /evidence="ECO:0000269|PubMed:24940650"
FT REGION Q15149-2:3956..4293
FT /note="Required for interaction with type2 keratins, DES
FT and VIM"
FT /evidence="ECO:0000250|UniProtKB:Q9QXS1"
FT REGION Q15149-2:4505..4574
FT /note="Required for efficient interaction with KRT5 and
FT KRT14 heterodimers"
FT /evidence="ECO:0000250|UniProtKB:Q9QXS1"
FT MOD_RES Q15149-2:42
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231"
FT MOD_RES Q15149-3:42
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231"
FT MOD_RES Q15149-4:20
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES Q15149-4:21
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES Q15149-4:26
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9QXS1"
SQ SEQUENCE 4684 AA; 531791 MW; 04772E4F70A304C8 CRC64;
MVAGMLMPRD QLRAIYEVLF REGVMVAKKD RRPRSLHPHV PGVTNLQVMR AMASLRARGL
VRETFAWCHF YWYLTNEGIA HLRQYLHLPP EIVPASLQRV RRPVAMVMPA RRTPHVQAVQ
GPLGSPPKRG PLPTEEQRVY RRKELEEVSP ETPVVPATTQ RTLARPGPEP APATDERDRV
QKKTFTKWVN KHLIKAQRHI SDLYEDLRDG HNLISLLEVL SGDSLPREKG RMRFHKLQNV
QIALDYLRHR QVKLVNIRND DIADGNPKLT LGLIWTIILH FQISDIQVSG QSEDMTAKEK
LLLWSQRMVE GYQGLRCDNF TSSWRDGRLF NAIIHRHKPL LIDMNKVYRQ TNLENLDQAF
SVAERDLGVT RLLDPEDVDV PQPDEKSIIT YVSSLYDAMP RVPDVQDGVR ANELQLRWQE
YRELVLLLLQ WMRHHTAAFE ERRFPSSFEE IEILWSQFLK FKEMELPAKE ADKNRSKGIY
QSLEGAVQAG QLKVPPGYHP LDVEKEWGKL HVAILEREKQ LRSEFERLEC LQRIVTKLQM
EAGLCEEQLN QADALLQSDV RLLAAGKVPQ RAGEVERDLD KADSMIRLLF NDVQTLKDGR
HPQGEQMYRR VYRLHERLVA IRTEYNLRLK AGVAAPATQV AQVTLQSVQR RPELEDSTLR
YLQDLLAWVE ENQHRVDGAE WGVDLPSVEA QLGSHRGLHQ SIEEFRAKIE RARSDEGQLS
PATRGAYRDC LGRLDLQYAK LLNSSKARLR SLESLHSFVA AATKELMWLN EKEEEEVGFD
WSDRNTNMTA KKESYSALMR ELELKEKKIK ELQNAGDRLL REDHPARPTV ESFQAALQTQ
WSWMLQLCCC IEAHLKENAA YFQFFSDVRE AEGQLQKLQE ALRRKYSCDR SATVTRLEDL
LQDAQDEKEQ LNEYKGHLSG LAKRAKAVVQ LKPRHPAHPM RGRLPLLAVC DYKQVEVTVH
KGDECQLVGP AQPSHWKVLS SSGSEAAVPS VCFLVPPPNQ EAQEAVTRLE AQHQALVTLW
HQLHVDMKSL LAWQSLRRDV QLIRSWSLAT FRTLKPEEQR QALHSLELHY QAFLRDSQDA
GGFGPEDRLM AEREYGSCSH HYQQLLQSLE QGAQEESRCQ RCISELKDIR LQLEACETRT
VHRLRLPLDK EPARECAQRI AEQQKAQAEV EGLGKGVARL SAEAEKVLAL PEPSPAAPTL
RSELELTLGK LEQVRSLSAI YLEKLKTISL VIRGTQGAEE VLRAHEEQLK EAQAVPATLP
ELEATKASLK KLRAQAEAQQ PTFDALRDEL RGAQEVGERL QQRHGERDVE VERWRERVAQ
LLERWQAVLA QTDVRQRELE QLGRQLRYYR ESADPLGAWL QDARRRQEQI QAMPLADSQA
VREQLRQEQA LLEEIERHGE KVEECQRFAK QYINAIKDYE LQLVTYKAQL EPVASPAKKP
KVQSGSESVI QEYVDLRTHY SELTTLTSQY IKFISETLRR MEEEERLAEQ QRAEERERLA
EVEAALEKQR QLAEAHAQAK AQAEREAKEL QQRMQEEVVR REEAAVDAQQ QKRSIQEELQ
QLRQSSEAEI QAKARQAEAA ERSRLRIEEE IRVVRLQLEA TERQRGGAEG ELQALRARAE
EAEAQKRQAQ EEAERLRRQV QDESQRKRQA EVELASRVKA EAEAAREKQR ALQALEELRL
QAEEAERRLR QAEVERARQV QVALETAQRS AEAELQSKRA SFAEKTAQLE RSLQEEHVAV
AQLREEAERR AQQQAEAERA REEAERELER WQLKANEALR LRLQAEEVAQ QKSLAQAEAE
KQKEEAEREA RRRGKAEEQA VRQRELAEQE LEKQRQLAEG TAQQRLAAEQ ELIRLRAETE
QGEQQRQLLE EELARLQREA AAATQKRQEL EAELAKVRAE MEVLLASKAR AEEESRSTSE
KSKQRLEAEA GRFRELAEEA ARLRALAEEA KRQRQLAEED AARQRAEAER VLAEKLAAIG
EATRLKTEAE IALKEKEAEN ERLRRLAEDE AFQRRRLEEQ AAQHKADIEE RLAQLRKASD
SELERQKGLV EDTLRQRRQV EEEILALKAS FEKAAAGKAE LELELGRIRS NAEDTLRSKE
QAELEAARQR QLAAEEERRR REAEERVQKS LAAEEEAARQ RKAALEEVER LKAKVEEARR
LRERAEQESA RQLQLAQEAA QKRLQAEEKA HAFAVQQKEQ ELQQTLQQEQ SVLDQLRGEA
EAARRAAEEA EEARVQAERE AAQSRRQVEE AERLKQSAEE QAQARAQAQA AAEKLRKEAE
QEAARRAQAE QAALRQKQAA DAEMEKHKKF AEQTLRQKAQ VEQELTTLRL QLEETDHQKN
LLDEELQRLK AEATEAARQR SQVEEELFSV RVQMEELSKL KARIEAENRA LILRDKDNTQ
RFLQEEAEKM KQVAEEAARL SVAAQEAARL RQLAEEDLAQ QRALAEKMLK EKMQAVQEAT
RLKAEAELLQ QQKELAQEQA RRLQEDKEQM AQQLAEETQG FQRTLEAERQ RQLEMSAEAE
RLKLRVAEMS RAQARAEEDA QRFRKQAEEI GEKLHRTELA TQEKVTLVQT LEIQRQQSDH
DAERLREAIA ELEREKEKLQ QEAKLLQLKS EEMQTVQQEQ LLQETQALQQ SFLSEKDSLL
QRERFIEQEK AKLEQLFQDE VAKAQQLREE QQRQQQQMEQ ERQRLVASME EARRRQHEAE
EGVRRKQEEL QQLEQQRRQQ EELLAEENQR LREQLQLLEE QHRAALAHSE EVTASQVAAT
KTLPNGRDAL DGPAAEAEPE HSFDGLRRKV SAQRLQEAGI LSAEELQRLA QGHTTVDELA
RREDVRHYLQ GRSSIAGLLL KATNEKLSVY AALQRQLLSP GTALILLEAQ AASGFLLDPV
RNRRLTVNEA VKEGVVGPEL HHKLLSAERA VTGYKDPYTG QQISLFQAMQ KGLIVREHGI
RLLEAQIATG GVIDPVHSHR VPVDVAYRRG YFDEEMNRVL ADPSDDTKGF FDPNTHENLT
YLQLLERCVE DPETGLCLLP LTDKAAKGGE LVYTDSEARD VFEKATVSAP FGKFQGKTVT
IWEIINSEYF TAEQRRDLLR QFRTGRITVE KIIKIIITVV EEQEQKGRLC FEGLRSLVPA
AELLESRVID RELYQQLQRG ERSVRDVAEV DTVRRALRGA NVIAGVWLEE AGQKLSIYNA
LKKDLLPSDM AVALLEAQAG TGHIIDPATS ARLTVDEAVR AGLVGPEFHE KLLSAEKAVT
GYRDPYTGQS VSLFQALKKG LIPREQGLRL LDAQLSTGGI VDPSKSHRVP LDVACARGCL
DEETSRALSA PRADAKAYSD PSTGEPATYG ELQQRCRPDQ LTGLSLLPLS EKAARARQEE
LYSELQARET FEKTPVEVPV GGFKGRTVTV WELISSEYFT AEQRQELLRQ FRTGKVTVEK
VIKILITIVE EVETLRQERL SFSGLRAPVP ASELLASGVL SRAQFEQLKD GKTTVKDLSE
LGSVRTLLQG SGCLAGIYLE DTKEKVSIYE AMRRGLLRAT TAALLLEAQA ATGFLVDPVR
NQRLYVHEAV KAGVVGPELH EQLLSAEKAV TGYRDPYSGS TISLFQAMQK GLVLRQHGIR
LLEAQIATGG IIDPVHSHRV PVDVAYQRGY FSEEMNRVLA DPSDDTKGFF DPNTHENLTY
RQLLERCVED PETGLRLLPL KGAEKAEVVE TTQVYTEEET RRAFEETQID IPGGGSHGGS
TMSLWEVMQS DLIPEEQRAQ LMADFQAGRV TKERMIIIII EIIEKTEIIR QQGLASYDYV
RRRLTAEDLF EARIISLETY NLLREGTRSL REALEAESAW CYLYGTGSVA GVYLPGSRQT
LSIYQALKKG LLSAEVARLL LEAQAATGFL LDPVKGERLT VDEAVRKGLV GPELHDRLLS
AERAVTGYRD PYTEQTISLF QAMKKELIPT EEALRLLDAQ LATGGIVDPR LGFHLPLEVA
YQRGYLNKDT HDQLSEPSEV RSYVDPSTDE RLSYTQLLRR CRRDDGTGQL LLPLSDARKL
TFRGLRKQIT MEELVRSQVM DEATALQLRE GLTSIEEVTK NLQKFLEGTS CIAGVFVDAT
KERLSVYQAM KKGIIRPGTA FELLEAQAAT GYVIDPIKGL KLTVEEAVRM GIVGPEFKDK
LLSAERAVTG YKDPYSGKLI SLFQAMKKGL ILKDHGIRLL EAQIATGGII DPEESHRLPV
EVAYKRGLFD EEMNEILTDP SDDTKGFFDP NTEENLTYLQ LMERCITDPQ TGLCLLPLKE
KKRERKTSSK SSVRKRRVVI VDPETGKEMS VYEAYRKGLI DHQTYLELSE QECEWEEITI
SSSDGVVKSM IIDRRSGRQY DIDDAIAKNL IDRSALDQYR AGTLSITEFA DMLSGNAGGF
RSRSSSVGSS SSYPISPAVS RTQLASWSDP TEETGPVAGI LDTETLEKVS ITEAMHRNLV
DNITGQRLLE AQACTGGIID PSTGERFPVT DAVNKGLVDK IMVDRINLAQ KAFCGFEDPR
TKTKMSAAQA LKKGWLYYEA GQRFLEVQYL TGGLIEPDTP GRVPLDEALQ RGTVDARTAQ
KLRDVGAYSK YLTCPKTKLK ISYKDALDRS MVEEGTGLRL LEAAAQSTKG YYSPYSVSGS
GSTAGSRTGS RTGSRAGSRR GSFDATGSGF SMTFSSSSYS SSGYGRRYAS GSSASLGGPE
SAVA
