EPIPL_HUMAN
ID EPIPL_HUMAN Reviewed; 5088 AA.
AC P58107; A0A087X1U6; Q76E58; Q9NSU9;
DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 28-MAR-2018, sequence version 3.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Epiplakin {ECO:0000303|PubMed:11278896};
DE AltName: Full=450 kDa epidermal antigen;
GN Name=EPPK1 {ECO:0000303|PubMed:14708632, ECO:0000312|HGNC:HGNC:15577};
GN Synonyms=EPIPL;
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], AND TISSUE SPECIFICITY.
RC TISSUE=Cervix carcinoma;
RX PubMed=11278896; DOI=10.1074/jbc.m011386200;
RA Fujiwara S., Takeo N., Otani Y., Parry D.A.D., Kunimatsu M., Lu R.,
RA Sasaki M., Matsuo N., Khaleduzzaman M., Yoshioka H.;
RT "Epiplakin, a novel member of the plakin family originally identified as a
RT 450-kDa human epidermal autoantigen: structure and tissue localization.";
RL J. Biol. Chem. 276:13340-13347(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=14708632; DOI=10.1046/j.1523-1747.2003.12550_5.x;
RA Takeo N., Wang W., Matsuo N., Sumiyoshi H., Yoshioka H., Fujiwara S.;
RT "Structure and heterogeneity of the human gene for epiplakin (EPPK1).";
RL J. Invest. Dermatol. 121:1224-1226(2003).
RN [3] {ECO:0000312|Proteomes:UP000005640}
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 [4]
RP PROTEIN SEQUENCE OF 266-274.
RC TISSUE=Platelet;
RX PubMed=12665801; DOI=10.1038/nbt810;
RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R.,
RA Vandekerckhove J.;
RT "Exploring proteomes and analyzing protein processing by mass spectrometric
RT identification of sorted N-terminal peptides.";
RL Nat. Biotechnol. 21:566-569(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 4714-5088.
RC TISSUE=Testis;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, INDUCTION, INTERACTION WITH VIM; KRT14;
RP KRT5/KRT14 AND KRT8/KRT18 HETEROTETRAMERS, AND DOMAIN.
RX PubMed=15671067; DOI=10.1242/jcs.01647;
RA Jang S.I., Kalinin A., Takahashi K., Marekov L.N., Steinert P.M.;
RT "Characterization of human epiplakin: RNAi-mediated epiplakin depletion
RT leads to the disruption of keratin and vimentin IF networks.";
RL J. Cell Sci. 118:781-793(2005).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2508; SER-3044; SER-3575;
RP SER-4109 AND SER-4645, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 INTERACTION WITH KRT1; VIM AND DES, AND DOMAIN.
RX PubMed=16923132; DOI=10.1111/j.1346-8138.2006.00127.x;
RA Wang W., Sumiyoshi H., Yoshioka H., Fujiwara S.;
RT "Interactions between epiplakin and intermediate filaments.";
RL J. Dermatol. 33:518-527(2006).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2718; SER-3249; SER-3783;
RP SER-4317 AND SER-4850, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [10]
RP 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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2422; SER-2508; SER-2718;
RP SER-2958; SER-3044; SER-3489; SER-3575; SER-3783; SER-4023; SER-4109;
RP SER-4317; SER-4557; SER-4645 AND SER-4850, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE 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 [12]
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 [13]
RP IDENTIFICATION BY 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 [14]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=23398049; DOI=10.1111/1346-8138.12076;
RA Shimada H., Nambu-Niibori A., Wilson-Morifuji M., Mizuguchi S., Araki N.,
RA Sumiyoshi H., Sato M., Mezaki Y., Senoo H., Ishikawa K., Hatano Y.,
RA Okamoto O., Fujiwara S.;
RT "Epiplakin modifies the motility of the HeLa cells and accumulates at the
RT outer surfaces of 3-D cell clusters.";
RL J. Dermatol. 40:249-258(2013).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-34; THR-1543; SER-2508;
RP SER-2718; SER-3044; SER-3249; SER-3575; SER-3783; SER-4109; SER-4317;
RP SER-4645 AND SER-4850, 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 [16]
RP IDENTIFICATION BY MASS SPECTROMETRY [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 [17]
RP FUNCTION.
RX PubMed=27206504; DOI=10.1186/s13104-016-2082-7;
RA Kokado M., Okada Y., Miyamoto T., Yamanaka O., Saika S.;
RT "Effects of epiplakin-knockdown in cultured corneal epithelial cells.";
RL BMC Res. Notes 9:278-278(2016).
RN [18]
RP VARIANT ASN-1094.
RX PubMed=29463886; DOI=10.1038/s41380-018-0020-x;
RA Eising E., Carrion-Castillo A., Vino A., Strand E.A., Jakielski K.J.,
RA Scerri T.S., Hildebrand M.S., Webster R., Ma A., Mazoyer B., Francks C.,
RA Bahlo M., Scheffer I.E., Morgan A.T., Shriberg L.D., Fisher S.E.;
RT "A set of regulatory genes co-expressed in embryonic human brain is
RT implicated in disrupted speech development.";
RL Mol. Psychiatry 24:1065-1078(2019).
CC -!- FUNCTION: Cytoskeletal linker protein that connects to intermediate
CC filaments and controls their reorganization in response to stress
CC (PubMed:15671067, PubMed:27206504, PubMed:23398049). In response to
CC mechanical stress like wound healing, is associated with the machinery
CC for cellular motility by slowing down keratinocyte migration and
CC proliferation and accelerating keratin bundling in proliferating
CC keratinocytes thus contributing to tissue architecture
CC (PubMed:27206504, PubMed:23398049). However in wound healing in corneal
CC epithelium also positively regulates cell differentiation and
CC proliferation and negatively regulates migration thereby controlling
CC corneal epithelium morphogenesis and integrity. In response to cellular
CC stress, plays a role in keratin filament reorganization, probably by
CC protecting keratin filaments against disruption. During liver and
CC pancreas injuries, plays a protective role by chaperoning disease-
CC induced intermediate filament reorganization (By similarity).
CC {ECO:0000250|UniProtKB:Q8R0W0, ECO:0000269|PubMed:15671067,
CC ECO:0000269|PubMed:23398049, ECO:0000269|PubMed:27206504}.
CC -!- SUBUNIT: Interacts with KRT5, KRT14 and KRT5/KRT14 heterotetramer;
CC interacts preferentially with assembled filaments rather than keratin
CC monomers (PubMed:15671067). Interacts with KRT8 and KRT18 and
CC KRT8/KRT18 heterotetramer; interacts preferentially with assembled
CC filaments rather than keratin monomers (PubMed:15671067). Interacts
CC with KRT1, VIM and DES; interaction is stronger with KRT1 than with VIM
CC or DES; interaction is dependent of higher-order structure of
CC intermediate filament (PubMed:16923132). {ECO:0000269|PubMed:15671067,
CC ECO:0000269|PubMed:16923132}.
CC -!- INTERACTION:
CC P58107; P42566: EPS15; NbExp=5; IntAct=EBI-297954, EBI-396684;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:15671067, ECO:0000269|PubMed:23398049}. Cell
CC junction, hemidesmosome {ECO:0000269|PubMed:23398049}. Cell junction,
CC tight junction {ECO:0000269|PubMed:23398049}. Cell projection
CC {ECO:0000269|PubMed:23398049}. Apicolateral cell membrane
CC {ECO:0000250|UniProtKB:Q8R0W0}. Basolateral cell membrane
CC {ECO:0000250|UniProtKB:Q8R0W0}. Cell junction
CC {ECO:0000250|UniProtKB:Q8R0W0}. Note=May move dynamically from bundling
CC intermediate filaments in the cytoplasm or at the cell periphery and
CC reinforcing them (PubMed:23398049). Decorates the keratin intermediate
CC filaments (IF) network and partially that of vimentin
CC (PubMed:15671067). {ECO:0000269|PubMed:15671067,
CC ECO:0000269|PubMed:23398049}.
CC -!- TISSUE SPECIFICITY: Expressed in epithelial cells of liver, small
CC intestine, colon, salivary glands, stomach and appendix.
CC {ECO:0000269|PubMed:11278896}.
CC -!- INDUCTION: Up-regulated upon calcium-mediated keratinocyte
CC differentiation. {ECO:0000269|PubMed:15671067}.
CC -!- DOMAIN: Plectin repeats are important for the binding to keratin and
CC VIM and controls intermediate filament networks organization.
CC {ECO:0000269|PubMed:15671067, ECO:0000269|PubMed:16923132}.
CC -!- SIMILARITY: Belongs to the plakin or cytolinker family. {ECO:0000305}.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-26 is the initiator.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB40803.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC92750.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB051895; BAB40803.1; ALT_INIT; mRNA.
DR EMBL; AB107036; BAC92750.1; ALT_INIT; Genomic_DNA.
DR EMBL; AC109322; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC234917; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL137725; CAB70895.1; -; mRNA.
DR CCDS; CCDS75800.1; -.
DR RefSeq; NP_112598.3; NM_031308.3.
DR RefSeq; XP_016869379.1; XM_017013890.1.
DR SMR; P58107; -.
DR BioGRID; 123666; 169.
DR IntAct; P58107; 37.
DR MINT; P58107; -.
DR STRING; 9606.ENSP00000484472; -.
DR GlyGen; P58107; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P58107; -.
DR PhosphoSitePlus; P58107; -.
DR SwissPalm; P58107; -.
DR BioMuta; EPPK1; -.
DR DMDM; 300669637; -.
DR EPD; P58107; -.
DR jPOST; P58107; -.
DR MassIVE; P58107; -.
DR PaxDb; P58107; -.
DR PeptideAtlas; P58107; -.
DR PRIDE; P58107; -.
DR ProteomicsDB; 57049; -.
DR Antibodypedia; 74951; 39 antibodies from 8 providers.
DR DNASU; 83481; -.
DR Ensembl; ENST00000615648.2; ENSP00000484472.1; ENSG00000261150.3.
DR GeneID; 83481; -.
DR KEGG; hsa:83481; -.
DR MANE-Select; ENST00000615648.2; ENSP00000484472.1; NM_031308.4; NP_112598.3.
DR CTD; 83481; -.
DR DisGeNET; 83481; -.
DR GeneCards; EPPK1; -.
DR HGNC; HGNC:15577; EPPK1.
DR HPA; ENSG00000261150; Tissue enhanced (skin).
DR MIM; 607553; gene.
DR neXtProt; NX_P58107; -.
DR OpenTargets; ENSG00000261150; -.
DR PharmGKB; PA27835; -.
DR VEuPathDB; HostDB:ENSG00000261150; -.
DR eggNOG; KOG0516; Eukaryota.
DR GeneTree; ENSGT00940000162855; -.
DR InParanoid; P58107; -.
DR OMA; WELLYSQ; -.
DR OrthoDB; 2464at2759; -.
DR PathwayCommons; P58107; -.
DR SignaLink; P58107; -.
DR BioGRID-ORCS; 83481; 21 hits in 310 CRISPR screens.
DR GeneWiki; Epiplakin_1; -.
DR GenomeRNAi; 83481; -.
DR Pharos; P58107; Tdark.
DR PRO; PR:P58107; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; P58107; protein.
DR Bgee; ENSG00000261150; Expressed in skin of hip and 138 other tissues.
DR ExpressionAtlas; P58107; baseline and differential.
DR GO; GO:0016327; C:apicolateral plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016323; C:basolateral plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005923; C:bicellular tight junction; IDA:UniProtKB.
DR GO; GO:0030054; C:cell junction; IBA:GO_Central.
DR GO; GO:0071944; C:cell periphery; IDA:UniProtKB.
DR GO; GO:0042995; C:cell projection; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005856; C:cytoskeleton; IDA:UniProtKB.
DR GO; GO:0030056; C:hemidesmosome; IDA:UniProtKB.
DR GO; GO:0045111; C:intermediate filament cytoskeleton; IDA:HPA.
DR GO; GO:0045095; C:keratin filament; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0097356; C:perinucleolar compartment; IDA:UniProtKB.
DR GO; GO:0019215; F:intermediate filament binding; IPI:UniProtKB.
DR GO; GO:1990254; F:keratin filament binding; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0005198; F:structural molecule activity; IBA:GO_Central.
DR GO; GO:0045110; P:intermediate filament bundle assembly; IBA:GO_Central.
DR GO; GO:0045104; P:intermediate filament cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0045109; P:intermediate filament organization; IDA:UniProtKB.
DR GO; GO:0030336; P:negative regulation of cell migration; IMP:UniProtKB.
DR GO; GO:0050680; P:negative regulation of epithelial cell proliferation; IMP:UniProtKB.
DR GO; GO:0051548; P:negative regulation of keratinocyte migration; ISS:UniProtKB.
DR GO; GO:0010839; P:negative regulation of keratinocyte proliferation; ISS:UniProtKB.
DR GO; GO:0061045; P:negative regulation of wound healing; IMP:UniProtKB.
DR GO; GO:1905041; P:regulation of epithelium regeneration; ISS:UniProtKB.
DR GO; GO:0042060; P:wound healing; IMP:UniProtKB.
DR Gene3D; 3.90.1290.10; -; 13.
DR InterPro; IPR043197; Plakin.
DR InterPro; IPR035915; Plakin_repeat_sf.
DR InterPro; IPR001101; Plectin_repeat.
DR PANTHER; PTHR23169; PTHR23169; 20.
DR Pfam; PF00681; Plectin; 36.
DR SMART; SM00250; PLEC; 65.
DR SUPFAM; SSF75399; SSF75399; 13.
PE 1: Evidence at protein level;
KW Cell junction; Cell membrane; Cell projection; Coiled coil; Cytoplasm;
KW Cytoskeleton; Direct protein sequencing; Disease variant; Membrane;
KW Phosphoprotein; Reference proteome; Repeat; Tight junction.
FT CHAIN 1..5088
FT /note="Epiplakin"
FT /id="PRO_0000078145"
FT REPEAT 34..71
FT /note="Plectin 1"
FT REPEAT 72..109
FT /note="Plectin 2"
FT REPEAT 110..147
FT /note="Plectin 3"
FT REPEAT 148..185
FT /note="Plectin 4"
FT REPEAT 192..225
FT /note="Plectin 5"
FT REPEAT 278..315
FT /note="Plectin 6"
FT REPEAT 316..353
FT /note="Plectin 7"
FT REPEAT 355..391
FT /note="Plectin 8"
FT REPEAT 392..429
FT /note="Plectin 9"
FT REPEAT 546..583
FT /note="Plectin 10"
FT REPEAT 603..640
FT /note="Plectin 11"
FT REPEAT 641..678
FT /note="Plectin 12"
FT REPEAT 679..716
FT /note="Plectin 13"
FT REPEAT 717..754
FT /note="Plectin 14"
FT REPEAT 758..792
FT /note="Plectin 15"
FT REPEAT 865..903
FT /note="Plectin 16"
FT REPEAT 923..960
FT /note="Plectin 17"
FT REPEAT 961..998
FT /note="Plectin 18"
FT REPEAT 999..1036
FT /note="Plectin 19"
FT REPEAT 1037..1074
FT /note="Plectin 20"
FT REPEAT 1239..1276
FT /note="Plectin 21"
FT REPEAT 1277..1314
FT /note="Plectin 22"
FT REPEAT 1315..1352
FT /note="Plectin 23"
FT REPEAT 1353..1390
FT /note="Plectin 24"
FT REPEAT 1391..1428
FT /note="Plectin 25"
FT REPEAT 1564..1601
FT /note="Plectin 26"
FT REPEAT 1602..1639
FT /note="Plectin 27"
FT REPEAT 1640..1677
FT /note="Plectin 28"
FT REPEAT 1678..1715
FT /note="Plectin 29"
FT REPEAT 1719..1753
FT /note="Plectin 30"
FT REPEAT 1890..1927
FT /note="Plectin 31"
FT REPEAT 1928..1965
FT /note="Plectin 32"
FT REPEAT 1966..2003
FT /note="Plectin 33"
FT REPEAT 2004..2041
FT /note="Plectin 34"
FT REPEAT 2042..2079
FT /note="Plectin 35"
FT REPEAT 2217..2259
FT /note="Plectin 36"
FT REPEAT 2260..2297
FT /note="Plectin 37"
FT REPEAT 2298..2335
FT /note="Plectin 38"
FT REPEAT 2336..2373
FT /note="Plectin 39"
FT REPEAT 2377..2411
FT /note="Plectin 40"
FT REPEAT 2753..2795
FT /note="Plectin 41"
FT REPEAT 2796..2833
FT /note="Plectin 42"
FT REPEAT 2834..2871
FT /note="Plectin 43"
FT REPEAT 2872..2908
FT /note="Plectin 44"
FT REPEAT 2913..2947
FT /note="Plectin 45"
FT REPEAT 3284..3326
FT /note="Plectin 46"
FT REPEAT 3327..3364
FT /note="Plectin 47"
FT REPEAT 3365..3402
FT /note="Plectin 48"
FT REPEAT 3403..3440
FT /note="Plectin 49"
FT REPEAT 3444..3478
FT /note="Plectin 50"
FT REPEAT 3818..3860
FT /note="Plectin 51"
FT REPEAT 3861..3898
FT /note="Plectin 52"
FT REPEAT 3899..3936
FT /note="Plectin 53"
FT REPEAT 3937..3974
FT /note="Plectin 54"
FT REPEAT 3978..4012
FT /note="Plectin 55"
FT REPEAT 4352..4394
FT /note="Plectin 56"
FT REPEAT 4395..4432
FT /note="Plectin 57"
FT REPEAT 4433..4470
FT /note="Plectin 58"
FT REPEAT 4471..4508
FT /note="Plectin 59"
FT REPEAT 4512..4546
FT /note="Plectin 60"
FT REPEAT 4885..4927
FT /note="Plectin 61"
FT REPEAT 4928..4965
FT /note="Plectin 62"
FT REPEAT 4966..5003
FT /note="Plectin 63"
FT REPEAT 5004..5041
FT /note="Plectin 64"
FT REPEAT 5045..5079
FT /note="Plectin 65"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 42..1115
FT /note="Interaction with KRT5"
FT /evidence="ECO:0000250|UniProtKB:Q8R0W0"
FT REGION 1572..5085
FT /note="Interaction with KRT5"
FT /evidence="ECO:0000250|UniProtKB:Q8R0W0"
FT REGION 2578..2637
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2761..2953
FT /note="Interaction with KRT14"
FT /evidence="ECO:0000250|UniProtKB:Q8R0W0"
FT REGION 3114..3168
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3645..3702
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 4179..4236
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 4715..4769
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 3687..3714
FT /evidence="ECO:0000255"
FT COILED 4221..4248
FT /evidence="ECO:0000255"
FT MOD_RES 34
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1543
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 2422
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 2508
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 2718
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 2958
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 3044
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 3249
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 3489
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 3575
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 3783
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 4023
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 4109
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 4317
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 4557
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 4645
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 4850
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT VARIANT 1094
FT /note="S -> N (de novo variant found in a patient with
FT childhood apraxia of speech; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:29463886"
FT /id="VAR_081533"
FT CONFLICT 202
FT /note="D -> N (in Ref. 1; BAB40803)"
FT /evidence="ECO:0000305"
FT CONFLICT 544
FT /note="K -> E (in Ref. 1; BAB40803)"
FT /evidence="ECO:0000305"
FT CONFLICT 602
FT /note="V -> A (in Ref. 1; BAB40803)"
FT /evidence="ECO:0000305"
FT CONFLICT 1507
FT /note="T -> A (in Ref. 1; BAB40803 and 2; BAC92750)"
FT /evidence="ECO:0000305"
FT CONFLICT 1618
FT /note="V -> A (in Ref. 1; BAB40803)"
FT /evidence="ECO:0000305"
FT CONFLICT 1897
FT /note="G -> D (in Ref. 1; BAB40803)"
FT /evidence="ECO:0000305"
FT CONFLICT 2081
FT /note="L -> V (in Ref. 1; BAB40803 and 2; BAC92750)"
FT /evidence="ECO:0000305"
FT CONFLICT 2286..2288
FT /note="AVA -> PVP (in Ref. 1; BAB40803 and 2; BAC92750)"
FT /evidence="ECO:0000305"
FT CONFLICT 2294
FT /note="G -> S (in Ref. 1; BAB40803 and 2; BAC92750)"
FT /evidence="ECO:0000305"
FT CONFLICT 2592
FT /note="W -> R (in Ref. 1; BAB40803 and 2; BAC92750)"
FT /evidence="ECO:0000305"
FT CONFLICT 2624..2628
FT /note="Missing (in Ref. 2; BAC92750)"
FT CONFLICT 2624..2625
FT /note="Missing (in Ref. 1; BAB40803)"
FT /evidence="ECO:0000305"
FT CONFLICT 2715
FT /note="R -> C (in Ref. 2; BAC92750)"
FT /evidence="ECO:0000305"
FT CONFLICT 2900
FT /note="Q -> R (in Ref. 1; BAB40803 and 2; BAC92750)"
FT /evidence="ECO:0000305"
FT CONFLICT 2977
FT /note="T -> M (in Ref. 2; BAC92750)"
FT /evidence="ECO:0000305"
FT CONFLICT 3083
FT /note="R -> G (in Ref. 1; BAB40803 and 2; BAC92750)"
FT /evidence="ECO:0000305"
FT CONFLICT 3159
FT /note="E -> EAAA (in Ref. 1; BAB40803)"
FT /evidence="ECO:0000305"
FT CONFLICT 3161
FT /note="A -> AAAT (in Ref. 2; BAC92750)"
FT /evidence="ECO:0000305"
FT CONFLICT 3246
FT /note="C -> R (in Ref. 1; BAB40803 and 2; BAC92750)"
FT /evidence="ECO:0000305"
FT CONFLICT 3445
FT /note="D -> H (in Ref. 2; BAC92750)"
FT /evidence="ECO:0000305"
FT CONFLICT 3614
FT /note="R -> G (in Ref. 1; BAB40803 and 2; BAC92750)"
FT /evidence="ECO:0000305"
FT CONFLICT 3695
FT /note="T -> A (in Ref. 1; BAB40803)"
FT /evidence="ECO:0000305"
FT CONFLICT 3840
FT /note="R -> H (in Ref. 2; BAC92750)"
FT /evidence="ECO:0000305"
FT CONFLICT 3979
FT /note="D -> H (in Ref. 2; BAC92750)"
FT /evidence="ECO:0000305"
FT CONFLICT 4042
FT /note="T -> M (in Ref. 2; BAC92750)"
FT /evidence="ECO:0000305"
FT CONFLICT 4079
FT /note="G -> S (in Ref. 1; BAB40803)"
FT /evidence="ECO:0000305"
FT CONFLICT 4119
FT /note="R -> RPS (in Ref. 2; BAC92750)"
FT /evidence="ECO:0000305"
FT CONFLICT 4148
FT /note="R -> G (in Ref. 2; BAC92750)"
FT /evidence="ECO:0000305"
FT CONFLICT 4227..4229
FT /note="Missing (in Ref. 2; BAC92750)"
FT /evidence="ECO:0000305"
FT CONFLICT 4374
FT /note="H -> R (in Ref. 1; BAB40803 and 2; BAC92750)"
FT /evidence="ECO:0000305"
FT CONFLICT 4513
FT /note="H -> D (in Ref. 1; BAB40803 and 2; BAC92750)"
FT /evidence="ECO:0000305"
FT CONFLICT 4576
FT /note="M -> T (in Ref. 1; BAB40803 and 2; BAC92750)"
FT /evidence="ECO:0000305"
FT CONFLICT 4637..4638
FT /note="Missing (in Ref. 1; BAB40803 and 2; BAC92750)"
FT /evidence="ECO:0000305"
FT CONFLICT 4760
FT /note="E -> EAAA (in Ref. 1; BAB40803 and 2; BAC92750)"
FT /evidence="ECO:0000305"
FT CONFLICT 4804
FT /note="H -> R (in Ref. 1; BAB40803 and 2; BAC92750)"
FT /evidence="ECO:0000305"
FT CONFLICT 5066
FT /note="L -> V (in Ref. 2; BAC92750)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 5088 AA; 555658 MW; ED7799C641FA8FC5 CRC64;
MSGHTLPPLP VPGTNSTEQA SVPRAMAATL GAGTPPRPQA RSIAGVYVEA SGQAQSVYAA
MEQGLLPAGL GQALLEAQAA TGGLVDLARG QLLPVSKALQ QGLVGLELKE KLLAAERATT
GYPDPYGGEK LALFQAIGKE VVDRALGQSW LEVQLATGGL VDPAQGVLVA PEPACHQGLL
DRETWHKLSE LEPGTGDLRF LDPNTLERLT YHQLLERCVR APGSGLALLP LKITFRSMGG
AVSAAELLEV GILDEQAVQG LREGRLAAVD VSARAEVRRY LEGTGSVAGV VLLPEGHKKS
FFQAATEHLL PMGTALPLLE AQAATHTLVD PITGQRLWVD EAVRAGLVSP ELHEQLLVAE
QAVTGHHDPF SGSQIPLFQA MKKGLVDRPL ALRLLDAQLA TGGLVCPARR LRLPLEAALR
CGCLDEDTQR QLSQAGSFSD GTHGGLRYEQ LLALCVTDPE TGLAFLPLSG GPRGGEPQGP
PFIKYSTRQA LSTATATVSV GKFRGRPVSL WELLFSEAIS SEQRAMLAQQ YQEGTLSVEK
LAAKLSATLE QAAATARVTF SGLRDTVTPG ELLKAEIIDQ DLYERLEHGQ ATAKDVGSLA
SVQRYLQGTG CIAGLLLPGS QERLSIYEAR CKGLLRPGTA LILLEAQAAT GFIIDPKANK
GHSVEEALRA AVIGPDVFAK LLSAERAVTG YTDPYTGQQI SLFQAMQKGL IVREHGIRLL
EAQIATGGVI DPVHSHRVPV DVAYRRGYFD QMLNLILLDP SDDTKGFFDP NTHENLTYLQ
LLERCVRDPE TGLYLLPLSS TQSPLVDSAT QQAFQNLLLS VKYGRFQGQR VSAWELINSE
YFSEGRRRQL LRRYRQREVT LGQVAKLLEA ETQRQADIML PALRSRVTVH QLLEAGIIDQ
QLLDQVLAGT ISPEALLLMD GVRRYLCGLG AVGGVRLLPS GQRLSLYQAM RQKLLGPRVA
LALLEAQAAT GTIMDPHSPE SLSVDEAVRR GVVGPELYGR LKRAEGAIAG FRDPFSGKQV
SVFQAMKKGL IPWEQAARLL EAQVATGGII DPTSHHHLPM PVAIQRGYVD QEMETALSSS
SETFPTPDGQ GRTSYAQLLE ECPRDETSGL HLLPLPESAP ALPTEEQVQR SLQAVPGAKD
GTSLWDLLSS CHFTEEQRRG LLEDVQEGRT TVPQLLASVQ RWVQETKLLA QARVMVPGPR
GEVPAVWLLD AGIITQETLE ALAQGTQSPA QVAEQPAVKA CLWGTGCVAG VLLQPSGAKA
SIAQAVRDGL LPTGLGQRLL EAQVASGFLV DPLNNQRLSV EDAVKVGLVG RELSEQLGQA
ERAAAGYPDP YSRASLSLWQ AMEKGLVPQN EGLPLLQVQL ATGGVVDPVH GVHLPQAAAC
RLGLLDTQTS QVLTAVDKDN KFFFDPSARD QVTYQQLRER CVCDSETGLL LLPLPSDTVL
EVDDHTAVAL RAMKVPVSTG RFKGCSVSLW DLLLSEYVGA DKRRELVALC RSGRAAALRQ
VVSAVTTLVE AAERQPLQAT FRGLRKQVSA RDLFRAQLIS RKTLDELSQG TTTVKEVAEM
DSVKRSLEGG NFIAGVLIQG TQERMSIPEA LRRHILRPGT ALVLLEAQAA TGFIIDPVEN
RKLTVEEAFK AGMFGKETYV KLLSAERAVT GYTDPYTGQQ ISLFQAMQKD LIVREHGIRL
LEAQIATGGI IDPVHSHRVP VDVAYRCGYF DEEMNRILAD PSDDTKGFFD PNTHENLTYL
QLLERCVEDP ETGLYLLQII KKGENYVYIN EATRHVLQSR TAKMRVGRFA DQVVSFWDLL
SSPYFTEDRK RELIQEYGAQ SGGLEKLLEI ITTTIEETET QNQGIKVAAI RGEVTAADLF
NSRVIDQKTL HTLRVGRTGG QALSTLECVK PYLEGSGCIA GVTVPSTREV MSLHEASRKE
LIPAAFATWL LEAQAATGFL LDPCTRQKLS VDEAVDVGLV NEELRERLLK AERAATGYRD
PATGDTIPLF QAMQKQLIEK AEALRLLEVQ VATGGVIDPQ HHHRLPLETA YRRGCLHKDI
YALISDQKHM RKRFVDPNTQ EKVSYRELQE RCRPQEDTGW LLFPVNKAAR DSEHIDDETR
RALEAEQVEI TVGRFRGQKP TLWALLNSEY VTEEKKLQLV RMYRTHTRRA LQTVAQLILE
LIEKQETSNK HLWFQGIRRQ ITASELLSSA IITEEMLQDL ETGRSTTQEL MEDDRVKRYL
EGTSCIAGVL VPAKDQPGRQ EKMSIYQAMW KGVLRPGTAL VLLEAQAATG FVIDPVRNLR
LSVEEAVAAG VVGGEIQEKL LSAERAVTGY TDPYTGQQIS LFQAMQKDLI VREHGIRLLE
AQIATGGVID PVHSHRVPVD VAYRRGYFDE EMNRVLADPS DDTKGFFDPN THENLTYVQL
LRRCVPDPDT GLYMLQLAGR GSAVHQLSEE LRCALRDARV TPGSGALQGQ SVSVWELLFY
REVSEDRRQD LLSRYRAGTL TVEELGATLT SLLAQAQAQA RAEAEAGSPR PDPREALRAA
TMEVKVGRLR GRAVPVWDVL ASGYVSRAAR EELLAEFGSG TLDLPALTRR LTAIIEEAEE
APGARPQLQD AWRGPREPGP AGRGDGDSGR SQREGQGEGE TQEAAAAAAA AAARRQEQTL
RDATMEVQRG QFQGRPVSVW DVLFSSYLSE ARRDELLAQH AAGALGLPDL VAVLTRVIEE
TEERLSKVSF RGLRRQVSAS ELHTSGILGP ETLRDLAQGT KTLQEVTEMD SVKRYLEGTS
CIAGVLVPAK DQPGRQEKMS IYQAMWKGVL RPGTALVLLE AQAATGFVID PVRNLRLSVE
EAVAAGVVGG EIQEKLLSAE RAVTGYTDPY TGQQISLFQA MQKDLIVREH GIRLLEAQIA
TGGVIDPVHS HRVPVDVAYQ RGYFDEEMNR VLADPSDDTK GFFDPNTHEN LTYVQLLRRC
VPDPDTGLYM LQLAGRGSAV HQLSEELRCA LRDARVTPGS GALQGQSVSV WELLFYREVS
EDRRQDLLSR YRAGTLTVEE LGATLTSLLA QAQAQARAEA EAGSPRPDPR EALRAATMEV
KVGRLRGRAV PVWDVLASGY VSRAAREELL AEFGSGTLDL PALTRRLTAI IEEAEEAPGA
RPQLQDAWRG PREPGPAGRG DGDSGRSQRE GQGEGETQEA AAAARRQEQT LRDATMEVQR
GQFQGRPVSV WDVLFSSYLS EARRDELLAQ HAAGALGLPD LVAVLTRVIE ETEERLSKVS
FRGLRCQVSA SELHTSGILG PETLRDLAQG TKTLQEVTEM DSVKRYLEGT SCIAGVLVPA
KDQPGRQEKM SIYQAMWKGV LRPGTALVLL EAQAATGFVI DPVRNLRLSV EEAVAAGVVG
GEIQEKLLSA ERAVTGYTDP YTGQQISLFQ AMQKDLIVRE HGIRLLEAQI ATGGVIDPVH
SHRVPVDVAY RRGYFDEEMN RVLADPSDDT KGFFDPNTHE NLTYVQLLRR CVPDPDTGLY
MLQLAGRGSA VHQLSEELRC ALRDARVTPG SGALQGQSVS VWELLFYREV SEDRRQDLLS
RYRAGTLTVE ELGATLTSLL AQAQAQARAE AEAGSPRPDP REALRAATME VKVGRLRGRA
VPVWDVLASG YVSRAAREEL LAEFGSGTLD LPALTRRLTA IIEEAEEAPG ARPQLQDAWR
GPREPGPAGR GDGDSGRSQR EGQGEGETQE AAAATAAARR QEQTLRDATM EVQRGQFQGR
PVSVWDVLFS SYLSEARRDE LLAQHAAGAL GLPDLVAVLT RVIEETEERL SKVSFRGLRR
QVSASELHTS GILGPETLRD LAQGTKTLQE VTEMDSVKRY LEGTSCIAGV LVPAKDQPGR
QEKMSIYQAM WKGVLRPGTA LVLLEAQAAT GFVIDPVRNL RLSVEEAVAA GVVGGEIQEK
LLSAERAVTG YTDPYTGQQI SLFQAMQKDL IVREHGIRLL EAQIATGGVI DPVHSHRVPV
DVAYRRGYFD EEMNRVLADP SDDTKGFFDP NTHENLTYVQ LLRRCVPDPD TGLYMLQLAG
RGSAVHQLSE ELRCALRDAR VTPGSGALQG QSVSVWELLF YREVSEDRRQ DLLSRYRAGT
LTVEELGATL TSLLAQAQAQ ARAEAEAGSP RPDPREALRA ATMEVKVGRL RGRAVPVWDV
LASGYVSRAA REELLAEFGS GTLDLPALTR RLTAIIEEAE EAPGARPQLQ DAWRGPREPG
PAGRGDGDSG RSQREGQGEG ETQEAAAATA AARRQEQTLR DATMEVQRGQ FQGRPVSVWD
VLFSSYLSEA RRDELLAQHA AGALGLPDLV AVLTRVIEET EERLSKVSFR GLRRQVSASE
LHTSGILGPE TLRDLAQGTK TLQEVTEMDS VKRYLEGTSC IAGVLVPAKD QPGHQEKMSI
YQAMWKGVLR PGTALVLLEA QAATGFVIDP VRNLRLSVEE AVAAGVVGGE IQEKLLSAER
AVTGYTDPYT GQQISLFQAM QKDLIVREHG IRLLEAQIAT GGVIDPVHSH RVPVDVAYRR
GYFDEEMNRV LAHPSDDTKG FFDPNTHENL TYVQLLRRCV PDPDTGLYML QLAGRGSAVH
QLSEELRCAL RDARVMPGSG ALQGQSVSVW ELLFYREVSE DRRQDLLSRY RAGTLTVEEL
GATLTSLLAQ AQAQARAEAE AEAGSPRPDP REALRAATME VKVGRLRGRA VPVWDVLASG
YVSGAAREEL LAEFGSGTLD LPALTRRLTA IIEEAEEAPG ARPQLQDAWR GPREPGPAGR
GDGDSGRSQR EGQGEGETQE AAAAARRQEQ TLRDATMEVQ RGQFQGRPVS VWDVLFSSYL
SEAHRDELLA QHAAGALGLP DLVAVLTRVI EETEERLSKV SFRGLRRQVS ASELHTSGIL
GPETLRDLAQ GTKTLQEVTE MDSVKRYLEG TSCIAGVLVP AKDQPGRQEK MSIYQAMWKG
VLRPGTALVL LEAQAATGFV IDPVRNLRLS VEEAVAAGVV GGEIQEKLLS AERAVTGYTD
PYTGQQISLF QAMQKDLIVR EHGIRLLEAQ IATGGVIDPV HSHRVPVDVA YRRGYFDEEM
NRVLADPSDD TKGFFDPNTH ENLTYLQLLQ RATLDPETGL LFLSLSLQ
