ID PLEC_MOUSE Reviewed; 4691 AA. AC Q9QXS1; E9QN87; Q6S384; Q6S389; Q6S394; Q9CS65; Q9QUT2; Q9QXQ8; Q9QXQ9; AC Q9QXR0; Q9QXR1; Q9QXR2; Q9QXR3; Q9QXR4; Q9QXR5; Q9QXR6; Q9QXR7; Q9QXR8; AC Q9QXR9; Q9QXS0; Q9QXS2; Q9QXS3; DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot. DT 16-APR-2014, sequence version 3. DT 27-MAR-2024, entry version 211. DE RecName: Full=Plectin; DE Short=PCN; DE Short=PLTN; DE AltName: Full=Plectin-1; DE AltName: Full=Plectin-6; GN Name=Plec; Synonyms=Plec1; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND ALTERNATIVE SPLICING. 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 [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S., RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., RA Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of the RT mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-964, ALTERNATIVE SPLICING, AND TISSUE RP SPECIFICITY. RC TISSUE=Brain, Embryo, Heart, Kidney, Skeletal muscle, and Testis; RX PubMed=10556294; DOI=10.1093/hmg/8.13.2461; RA Fuchs P., Zoerer M., Rezniczek G.A., Spazierer D., Oehler S., RA Castanon M.J., Hauptmann R., Wiche G.; RT "Unusual 5' transcript complexity of plectin isoforms: novel tissue- RT specific exons modulate actin binding activity."; RL Hum. Mol. Genet. 8:2461-2472(1999). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 181-812. RC STRAIN=C57BL/6J; TISSUE=Embryo; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J., RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [5] RP PROTEIN SEQUENCE OF 629-633, AND IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=OF1; TISSUE=Hippocampus; RA Lubec G., Sunyer B., Chen W.-Q.; RL Submitted (JAN-2009) to UniProtKB. RN [6] RP INTERACTION WITH FER. RX PubMed=12200133; DOI=10.1016/s0006-291x(02)02007-7; RA Lunter P.C., Wiche G.; RT "Direct binding of plectin to Fer kinase and negative regulation of its RT catalytic activity."; RL Biochem. Biophys. Res. Commun. 296:904-910(2002). RN [7] RP INTERACTION WITH SYNE3. RX PubMed=16330710; DOI=10.1083/jcb.200506083; RA Wilhelmsen K., Litjens S.H.M., Kuikman I., Tshimbalanga N., Janssen H., RA van den Bout I., Raymond K., Sonnenberg A.; RT "Nesprin-3, a novel outer nuclear membrane protein, associates with the RT cytoskeletal linker protein plectin."; RL J. Cell Biol. 171:799-810(2005). RN [8] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=15592455; DOI=10.1038/nbt1046; RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., RA Zha X.-M., Polakiewicz R.D., Comb M.J.; RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."; RL Nat. Biotechnol. 23:94-101(2005). RN [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-728, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain; RX PubMed=16452087; DOI=10.1074/mcp.t500041-mcp200; RA Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.; RT "Comprehensive identification of phosphorylation sites in postsynaptic RT density preparations."; RL Mol. Cell. Proteomics 5:914-922(2006). RN [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-2788; TYR-3040; TYR-3369; RP TYR-3797 AND TYR-4622, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-26 RP (ISOFORM PLEC-1A), AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. RC TISSUE=Mast cell; RX PubMed=17947660; DOI=10.4049/jimmunol.179.9.5864; RA Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y., RA Kawakami T., Salomon A.R.; RT "Quantitative time-resolved phosphoproteomic analysis of mast cell RT signaling."; RL J. Immunol. 179:5864-5876(2007). RN [11] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain cortex; RX PubMed=17114649; DOI=10.1074/mcp.m600046-mcp200; RA Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F., RA Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B., RA Panse C., Schlapbach R., Mansuy I.M.; RT "Qualitative and quantitative analyses of protein phosphorylation in naive RT and stimulated mouse synaptosomal preparations."; RL Mol. Cell. Proteomics 6:283-293(2007). RN [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-823, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=17208939; DOI=10.1074/mcp.m600218-mcp200; RA Lee J., Xu Y., Chen Y., Sprung R., Kim S.C., Xie S., Zhao Y.; RT "Mitochondrial phosphoproteome revealed by an improved IMAC method and RT MS/MS/MS."; RL Mol. Cell. Proteomics 6:669-676(2007). RN [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4633, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=17242355; DOI=10.1073/pnas.0609836104; RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.; RT "Large-scale phosphorylation analysis of mouse liver."; RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007). RN [14] 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 [15] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=18630941; DOI=10.1021/pr800223m; RA Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.; RT "Specific phosphopeptide enrichment with immobilized titanium ion affinity RT chromatography adsorbent for phosphoproteome analysis."; RL J. Proteome Res. 7:3957-3967(2008). RN [16] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4393 AND SER-4396, RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21 (ISOFORM PLEC-1A), AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006; RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M., RA Thibault P.; RT "The phagosomal proteome in interferon-gamma-activated macrophages."; RL Immunity 30:143-154(2009). RN [17] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4389 AND SER-4393, RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21 (ISOFORM PLEC-1A), AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Embryonic fibroblast; RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200; RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.; RT "Large scale localization of protein phosphorylation by use of electron RT capture dissociation mass spectrometry."; RL Mol. Cell. Proteomics 8:904-912(2009). RN [18] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-728; SER-1055; THR-4037; RP SER-4389; SER-4391; SER-4392; SER-4393; SER-4396; SER-4620; SER-4625; RP SER-4629; THR-4630; SER-4633 AND SER-4649, PHOSPHORYLATION [LARGE SCALE RP ANALYSIS] AT SER-21 (ISOFORM PLEC-1A), AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, RC Pancreas, Spleen, and Testis; RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001; RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R., RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.; RT "A tissue-specific atlas of mouse protein phosphorylation and expression."; RL Cell 143:1174-1189(2010). RN [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 TISSUE SPECIFICITY, AND IDENTIFICATION IN A COMPLEX WITH EZR; AHNAK; BFSP1; RP BFSP2; ANK2; PRX; VIM AND SPECTRIN. RX PubMed=21745462; DOI=10.1016/j.ydbio.2011.06.036; RA Maddala R., Skiba N.P., Lalane R. III, Sherman D.L., Brophy P.J., Rao P.V.; RT "Periaxin is required for hexagonal geometry and membrane organization of RT mature lens fibers."; RL Dev. Biol. 357:179-190(2011). RN [21] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-1733; LYS-2644 AND LYS-3060, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Embryonic fibroblast; RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001; RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.; RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic RT pathways."; RL Mol. Cell 50:919-930(2013). RN [22] 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 [23] RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-4634 AND ARG-4647, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain; 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 [24] RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 181-417, AND INTERACTION WITH RP VIM. RX PubMed=15128297; DOI=10.1111/j.1432-1033.2004.04095.x; RA Sevcik J., Urbanikova L., Kost'an J., Janda L., Wiche G.; RT "Actin-binding domain of mouse plectin. Crystal structure and binding to RT vimentin."; RL Eur. J. Biochem. 271:1873-1884(2004). CC -!- FUNCTION: Interlinks intermediate filaments with microtubules and CC microfilaments and anchors intermediate filaments to desmosomes or CC hemidesmosomes. May be involved not only in the cross-linking and CC stabilization of cytoskeletal intermediate filaments network, but also CC in the regulation of their dynamics. CC -!- SUBUNIT: Homodimer or homotetramer (By similarity). Interacts (via CC actin-binding domain) with SYNE3 (PubMed:16330710). Interacts (via CC calponin-homology (CH) 1 domain) with VIM (via rod region) CC (PubMed:15128297). Interacts (via N-terminus) with DST isoform 2 (via CC N-terminus) (PubMed:19932097). Interacts with FER (PubMed:12200133). CC Interacts with TOR1A (PubMed:18827015). Interacts with ANK3 (By CC similarity). Identified in complexes that contain VIM, EZR, AHNAK, CC BFSP1, BFSP2, ANK2, PLEC, PRX and spectrin (PubMed:21745462). CC {ECO:0000250, ECO:0000250|UniProtKB:P30427, CC ECO:0000269|PubMed:12200133, ECO:0000269|PubMed:15128297, CC ECO:0000269|PubMed:16330710, ECO:0000269|PubMed:18827015, CC ECO:0000269|PubMed:19932097, ECO:0000269|PubMed:21745462}. CC -!- SUBUNIT: [Isoform PLEC-0,1C]: Interacts with KRT14, heterodimers CC consisting of KRT8 and KRT18, heterodimers consisting of KRT5 and CC KRT14, heterodimers consisting of KRT14 and KRT15, and heterodimers CC consisting of KRT1 and KRT10 (PubMed:24940650). Interacts with DES and CC VIM (PubMed:24940650). {ECO:0000269|PubMed:24940650}. CC -!- INTERACTION: CC Q9QXS1; Q9D2G2: Dlst; NbExp=2; IntAct=EBI-774583, EBI-773210; CC Q9QXS1; P35486: Pdha1; NbExp=2; IntAct=EBI-774583, EBI-773613; CC Q9QXS1-3; P62158: CALM3; Xeno; NbExp=11; IntAct=EBI-16145475, EBI-397435; CC Q9QXS1-3; P16144: ITGB4; Xeno; NbExp=4; IntAct=EBI-16145475, EBI-948678; CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton CC {ECO:0000250|UniProtKB:Q15149}. Cell junction, hemidesmosome CC {ECO:0000250|UniProtKB:Q15149}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=16; CC Name=PLEC-1,2A; CC IsoId=Q9QXS1-1; Sequence=Displayed; CC Name=PLEC-1; CC IsoId=Q9QXS1-2; Sequence=VSP_005048; CC Name=PLEC-1A; CC IsoId=Q9QXS1-3; Sequence=VSP_005036, VSP_005045, VSP_005048; CC Name=PLEC-1B,2A; CC IsoId=Q9QXS1-4; Sequence=VSP_005037, VSP_005045; CC Name=PLEC-1B; CC IsoId=Q9QXS1-5; Sequence=VSP_005037, VSP_005045, VSP_005048; CC Name=PLEC-0,1C; CC IsoId=Q9QXS1-6; Sequence=VSP_005039, VSP_005047, VSP_005048; CC Name=PLEC-0,1C,2A; CC IsoId=Q9QXS1-7; Sequence=VSP_005039, VSP_005047; CC Name=PLEC-0,1C,2A,3A; CC IsoId=Q9QXS1-8; Sequence=VSP_005039, VSP_005047, VSP_005049; CC Name=PLEC-1D,2A; CC IsoId=Q9QXS1-9; Sequence=VSP_005032, VSP_005041; CC Name=PLEC-1D; CC IsoId=Q9QXS1-10; Sequence=VSP_005032, VSP_005041, VSP_005048; CC Name=PLEC-1E,2A; CC IsoId=Q9QXS1-11; Sequence=VSP_005033, VSP_005042; CC Name=PLEC-1E; CC IsoId=Q9QXS1-12; Sequence=VSP_005033, VSP_005042, VSP_005048; CC Name=PLEC-1F; CC IsoId=Q9QXS1-13; Sequence=VSP_005034, VSP_005043, VSP_005048; CC Name=PLEC-1G; CC IsoId=Q9QXS1-14; Sequence=VSP_005038, VSP_005046, VSP_005048; CC Name=PLEC-1H; CC IsoId=Q9QXS1-15; Sequence=VSP_005040; CC Name=PLEC-1I; CC IsoId=Q9QXS1-16; Sequence=VSP_005035, VSP_005044; CC -!- TISSUE SPECIFICITY: Detected in eye lens fiber cells (at protein level) CC (PubMed:21745462). Expressed at high levels in lung, brain, small CC intestine, muscle, heart and skin with lower levels found in kidney, CC liver, uterus, spleen and salivary gland (PubMed:10556294). CC {ECO:0000269|PubMed:10556294, ECO:0000269|PubMed:21745462}. 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. Isoform PLEC-1A is phosphorylated on Ser-21. CC Isoform PLEC-1A is phosphorylated on Tyr-26. CC -!- SIMILARITY: Belongs to the plakin or cytolinker family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AY480033; AAR95666.1; -; mRNA. DR EMBL; AY480038; AAR95671.1; -; mRNA. DR EMBL; AY480043; AAR95676.1; -; mRNA. DR EMBL; AC110211; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AF188006; AAF18066.1; -; mRNA. DR EMBL; AF188007; AAF18067.1; -; mRNA. DR EMBL; AF188008; AAF18068.1; -; mRNA. DR EMBL; AF188009; AAF18069.1; -; mRNA. DR EMBL; AF188010; AAF18070.1; -; mRNA. DR EMBL; AF188011; AAF18071.1; -; mRNA. DR EMBL; AF188012; AAF18072.1; -; mRNA. DR EMBL; AF188013; AAF18073.1; -; mRNA. DR EMBL; AF188014; AAF18074.1; -; mRNA. DR EMBL; AF188015; AAF18075.1; -; mRNA. DR EMBL; AF188016; AAF18076.1; -; mRNA. DR EMBL; AF188017; AAF18077.1; -; mRNA. DR EMBL; AF188018; AAF18078.1; -; mRNA. DR EMBL; AF188019; AAF18079.1; -; mRNA. DR EMBL; AF188020; AAF18080.1; -; mRNA. DR EMBL; AF188021; AAF18081.1; -; mRNA. DR EMBL; AF188022; AAF18082.1; -; mRNA. DR EMBL; AF188023; AAF18083.1; -; mRNA. DR EMBL; AK017743; -; NOT_ANNOTATED_CDS; mRNA. DR CCDS; CCDS37113.1; -. [Q9QXS1-13] DR CCDS; CCDS37114.1; -. [Q9QXS1-2] DR CCDS; CCDS37115.1; -. [Q9QXS1-14] DR CCDS; CCDS37116.1; -. [Q9QXS1-3] DR CCDS; CCDS49644.1; -. [Q9QXS1-5] DR CCDS; CCDS49645.1; -. [Q9QXS1-4] DR CCDS; CCDS49646.1; -. [Q9QXS1-10] DR CCDS; CCDS49647.1; -. [Q9QXS1-1] DR CCDS; CCDS49648.1; -. [Q9QXS1-12] DR CCDS; CCDS49649.1; -. [Q9QXS1-8] DR PIR; D59404; D59404. DR RefSeq; NP_001157012.1; NM_001163540.1. [Q9QXS1-1] DR RefSeq; NP_001157014.1; NM_001163542.1. [Q9QXS1-8] DR RefSeq; NP_001157021.1; NM_001163549.1. [Q9QXS1-4] DR RefSeq; NP_001157675.1; NM_001164203.1. DR RefSeq; NP_035247.2; NM_011117.2. [Q9QXS1-6] DR RefSeq; NP_958791.2; NM_201389.2. [Q9QXS1-2] DR RefSeq; NP_958796.2; NM_201394.2. [Q9QXS1-3] DR PDB; 1SH5; X-ray; 2.00 A; A/B=181-417. DR PDB; 1SH6; X-ray; 2.00 A; A=181-417. DR PDB; 4Q57; X-ray; 1.80 A; B=181-411. DR PDBsum; 1SH5; -. DR PDBsum; 1SH6; -. DR PDBsum; 4Q57; -. DR SMR; Q9QXS1; -. DR BioGRID; 202243; 36. DR CORUM; Q9QXS1; -. DR DIP; DIP-32004N; -. DR IntAct; Q9QXS1; 16. DR MINT; Q9QXS1; -. DR STRING; 10090.ENSMUSP00000073124; -. DR GlyGen; Q9QXS1; 4 sites, 1 O-linked glycan (4 sites). DR iPTMnet; Q9QXS1; -. DR PhosphoSitePlus; Q9QXS1; -. DR SwissPalm; Q9QXS1; -. DR EPD; Q9QXS1; -. DR jPOST; Q9QXS1; -. DR MaxQB; Q9QXS1; -. DR PaxDb; 10090-ENSMUSP00000075772; -. DR PeptideAtlas; Q9QXS1; -. DR ProteomicsDB; 288234; -. [Q9QXS1-1] DR ProteomicsDB; 288235; -. [Q9QXS1-2] DR ProteomicsDB; 288236; -. [Q9QXS1-3] DR ProteomicsDB; 288237; -. [Q9QXS1-4] DR ProteomicsDB; 288238; -. [Q9QXS1-5] DR ProteomicsDB; 288239; -. [Q9QXS1-6] DR ProteomicsDB; 288240; -. [Q9QXS1-7] DR ProteomicsDB; 288241; -. [Q9QXS1-8] DR ProteomicsDB; 288242; -. [Q9QXS1-9] DR ProteomicsDB; 288243; -. [Q9QXS1-10] DR ProteomicsDB; 288244; -. [Q9QXS1-11] DR ProteomicsDB; 288245; -. [Q9QXS1-12] DR ProteomicsDB; 288246; -. [Q9QXS1-13] DR ProteomicsDB; 288247; -. [Q9QXS1-14] DR ProteomicsDB; 288248; -. [Q9QXS1-15] DR ProteomicsDB; 288249; -. [Q9QXS1-16] DR Pumba; Q9QXS1; -. DR Antibodypedia; 3549; 240 antibodies from 32 providers. DR DNASU; 18810; -. DR Ensembl; ENSMUST00000023226.13; ENSMUSP00000023226.7; ENSMUSG00000022565.16. [Q9QXS1-3] DR Ensembl; ENSMUST00000054449.14; ENSMUSP00000057158.8; ENSMUSG00000022565.16. [Q9QXS1-4] DR Ensembl; ENSMUST00000071869.12; ENSMUSP00000071765.6; ENSMUSG00000022565.16. [Q9QXS1-12] DR Ensembl; ENSMUST00000072692.11; ENSMUSP00000072478.5; ENSMUSG00000022565.16. [Q9QXS1-14] DR Ensembl; ENSMUST00000073418.13; ENSMUSP00000073124.7; ENSMUSG00000022565.16. [Q9QXS1-1] DR Ensembl; ENSMUST00000074834.12; ENSMUSP00000074383.6; ENSMUSG00000022565.16. [Q9QXS1-13] DR Ensembl; ENSMUST00000076442.12; ENSMUSP00000075772.6; ENSMUSG00000022565.16. [Q9QXS1-2] DR Ensembl; ENSMUST00000089610.10; ENSMUSP00000087037.4; ENSMUSG00000022565.16. [Q9QXS1-8] DR Ensembl; ENSMUST00000169108.8; ENSMUSP00000126068.2; ENSMUSG00000022565.16. [Q9QXS1-10] DR Ensembl; ENSMUST00000169714.8; ENSMUSP00000126526.2; ENSMUSG00000022565.16. [Q9QXS1-5] DR GeneID; 18810; -. DR KEGG; mmu:18810; -. DR UCSC; uc007wir.2; mouse. [Q9QXS1-3] DR UCSC; uc007wis.2; mouse. [Q9QXS1-14] DR UCSC; uc007wit.2; mouse. [Q9QXS1-1] DR UCSC; uc007wiu.2; mouse. [Q9QXS1-5] DR UCSC; uc007wiv.2; mouse. [Q9QXS1-10] DR UCSC; uc007wiw.2; mouse. [Q9QXS1-2] DR UCSC; uc007wiz.2; mouse. [Q9QXS1-12] DR UCSC; uc007wja.2; mouse. [Q9QXS1-13] DR UCSC; uc007wjb.2; mouse. [Q9QXS1-6] DR UCSC; uc007wjd.2; mouse. [Q9QXS1-4] DR UCSC; uc011zuq.1; mouse. [Q9QXS1-8] DR AGR; MGI:1277961; -. DR CTD; 5339; -. DR MGI; MGI:1277961; Plec. DR VEuPathDB; HostDB:ENSMUSG00000022565; -. DR eggNOG; KOG0516; Eukaryota. DR eggNOG; KOG3344; Eukaryota. DR GeneTree; ENSGT00940000159045; -. DR HOGENOM; CLU_000132_0_0_1; -. DR InParanoid; Q9QXS1; -. DR OMA; GDECQLL; -. DR OrthoDB; 5321591at2759; -. DR PhylomeDB; Q9QXS1; -. DR Reactome; R-MMU-264870; Caspase-mediated cleavage of cytoskeletal proteins. DR Reactome; R-MMU-446107; Type I hemidesmosome assembly. DR BioGRID-ORCS; 18810; 5 hits in 79 CRISPR screens. DR ChiTaRS; Plec; mouse. DR EvolutionaryTrace; Q9QXS1; -. DR PRO; PR:Q9QXS1; -. DR Proteomes; UP000000589; Chromosome 15. DR RNAct; Q9QXS1; Protein. DR Bgee; ENSMUSG00000022565; Expressed in tarsal region and 245 other cell types or tissues. DR ExpressionAtlas; Q9QXS1; baseline and differential. DR GO; GO:0016324; C:apical plasma membrane; ISO:MGI. DR GO; GO:0030424; C:axon; IDA:MGI. DR GO; GO:0009925; C:basal plasma membrane; ISO:MGI. DR GO; GO:0005903; C:brush border; IDA:UniProtKB. DR GO; GO:0071944; C:cell periphery; IDA:MGI. DR GO; GO:0043292; C:contractile fiber; IDA:MGI. DR GO; GO:0005737; C:cytoplasm; IDA:MGI. DR GO; GO:0005829; C:cytosol; ISO:MGI. DR GO; GO:0030425; C:dendrite; IDA:MGI. DR GO; GO:0005925; C:focal adhesion; ISO:MGI. DR GO; GO:0030056; C:hemidesmosome; IDA:MGI. DR GO; GO:0045111; C:intermediate filament cytoskeleton; ISO:MGI. DR GO; GO:0005741; C:mitochondrial outer membrane; IMP:MGI. DR GO; GO:0043209; C:myelin sheath; IDA:MGI. DR GO; GO:0030016; C:myofibril; IDA:MGI. DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI. DR GO; GO:0042383; C:sarcolemma; IDA:MGI. DR GO; GO:0016528; C:sarcoplasm; ISO:MGI. DR GO; GO:0030018; C:Z disc; IDA:MGI. DR GO; GO:0003779; F:actin binding; IDA:MGI. DR GO; GO:0051015; F:actin filament binding; IDA:MGI. DR GO; GO:0030506; F:ankyrin binding; ISO:MGI. DR GO; GO:0008092; F:cytoskeletal protein binding; ISO:MGI. DR GO; GO:0002162; F:dystroglycan binding; IDA:MGI. DR GO; GO:0043621; F:protein self-association; IDA:MGI. DR GO; GO:0005200; F:structural constituent of cytoskeleton; ISO:MGI. DR GO; GO:0008307; F:structural constituent of muscle; ISO:MGI. DR GO; GO:0030036; P:actin cytoskeleton organization; IMP:MGI. DR GO; GO:0007015; P:actin filament organization; IMP:MGI. DR GO; GO:2000689; P:actomyosin contractile ring assembly actin filament organization; IMP:MGI. DR GO; GO:0034332; P:adherens junction organization; IMP:MGI. DR GO; GO:0055013; P:cardiac muscle cell development; IMP:MGI. DR GO; GO:0000902; P:cell morphogenesis; IMP:MGI. DR GO; GO:0048870; P:cell motility; IMP:MGI. DR GO; GO:0031668; P:cellular response to extracellular stimulus; IMP:MGI. DR GO; GO:0071498; P:cellular response to fluid shear stress; IMP:MGI. DR GO; GO:0071464; P:cellular response to hydrostatic pressure; IMP:MGI. DR GO; GO:0071260; P:cellular response to mechanical stimulus; IMP:MGI. DR GO; GO:0061436; P:establishment of skin barrier; IMP:MGI. DR GO; GO:0010761; P:fibroblast migration; IMP:MGI. DR GO; GO:0010467; P:gene expression; IMP:MGI. DR GO; GO:0031581; P:hemidesmosome assembly; ISS:UniProtKB. DR GO; GO:0045104; P:intermediate filament cytoskeleton organization; IMP:MGI. DR GO; GO:0045109; P:intermediate filament organization; IMP:MGI. DR GO; GO:0003334; P:keratinocyte development; IMP:MGI. DR GO; GO:0030216; P:keratinocyte differentiation; IMP:MGI. DR GO; GO:0002522; P:leukocyte migration involved in immune response; IMP:MGI. DR GO; GO:0007005; P:mitochondrion organization; IMP:MGI. DR GO; GO:0035264; P:multicellular organism growth; IMP:MGI. DR GO; GO:0022011; P:myelination in peripheral nervous system; IMP:MGI. DR GO; GO:0045445; P:myoblast differentiation; IMP:MGI. DR GO; GO:0006997; P:nucleus organization; IMP:MGI. DR GO; GO:0032287; P:peripheral nervous system myelin maintenance; IMP:MGI. DR GO; GO:0008104; P:protein localization; IMP:MGI. DR GO; GO:0043933; P:protein-containing complex organization; IMP:MGI. DR GO; GO:0043114; P:regulation of vascular permeability; IMP:MGI. DR GO; GO:0022904; P:respiratory electron transport chain; IMP:MGI. DR GO; GO:0032094; P:response to food; IMP:MGI. DR GO; GO:0007584; P:response to nutrient; ISO:MGI. DR GO; GO:0045214; P:sarcomere organization; IMP:MGI. DR GO; GO:0048741; P:skeletal muscle fiber development; IMP:MGI. DR GO; GO:0007519; P:skeletal muscle tissue development; IMP:MGI. DR GO; GO:0014866; P:skeletal myofibril assembly; IMP:MGI. DR GO; GO:0043588; P:skin development; IMP:MGI. DR GO; GO:0010818; P:T cell chemotaxis; IMP:MGI. DR GO; GO:0120193; P:tight junction organization; IMP:MGI. DR GO; GO:0019226; P:transmission of nerve impulse; IMP:MGI. DR GO; GO:0042060; P:wound healing; IBA:GO_Central. DR CDD; cd21188; CH_PLEC-like_rpt1; 1. DR CDD; cd21238; CH_PLEC_rpt2; 1. DR CDD; cd00176; SPEC; 2. DR Gene3D; 1.20.58.1060; -; 1. DR Gene3D; 1.20.58.60; -; 5. DR Gene3D; 3.30.160.780; -; 1. DR Gene3D; 1.10.418.10; Calponin-like domain; 2. DR Gene3D; 3.90.1290.10; Plakin repeat; 6. DR Gene3D; 2.30.30.40; SH3 Domains; 1. DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1. DR InterPro; IPR001589; Actinin_actin-bd_CS. DR InterPro; IPR001715; CH_dom. DR InterPro; IPR036872; CH_dom_sf. DR InterPro; IPR041615; Desmoplakin_SH3. DR InterPro; IPR041573; Desmoplakin_Spectrin-like. DR InterPro; IPR049538; PCN-like_spectrin-like_rpt. DR InterPro; IPR043197; Plakin. DR InterPro; IPR035915; Plakin_repeat_sf. DR InterPro; IPR005326; Plectin_eS10_N. DR InterPro; IPR001101; Plectin_repeat. DR InterPro; IPR001452; SH3_domain. DR InterPro; IPR018159; Spectrin/alpha-actinin. DR InterPro; IPR036388; WH-like_DNA-bd_sf. DR PANTHER; PTHR23169; ENVOPLAKIN; 1. DR PANTHER; PTHR23169:SF20; PLECTIN; 1. DR Pfam; PF00307; CH; 2. DR Pfam; PF00681; Plectin; 19. DR Pfam; PF03501; S10_plectin; 1. DR Pfam; PF17902; SH3_10; 1. DR Pfam; PF18373; Spectrin_2; 1. DR Pfam; PF21019; Spectrin_3; 1. DR Pfam; PF21020; Spectrin_4; 1. DR Pfam; PF21097; SR_plectin_7; 1. DR SMART; SM00033; CH; 2. DR SMART; SM00250; PLEC; 35. DR SMART; SM00150; SPEC; 6. DR SUPFAM; SSF47576; Calponin-homology domain, CH-domain; 1. DR SUPFAM; SSF75399; Plakin repeat; 7. DR SUPFAM; SSF46966; Spectrin repeat; 4. DR PROSITE; PS00019; ACTININ_1; 1. DR PROSITE; PS00020; ACTININ_2; 1. DR PROSITE; PS50021; CH; 2. DR PROSITE; PS50002; SH3; 1. DR Genevisible; Q9QXS1; MM. 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; Methylation; Phosphoprotein; Reference proteome; KW Repeat; SH3 domain. FT CHAIN 1..4691 FT /note="Plectin" FT /id="PRO_0000078136" FT DOMAIN 185..293 FT /note="Calponin-homology (CH) 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044" FT DOMAIN 306..411 FT /note="Calponin-homology (CH) 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044" FT REPEAT 653..727 FT /note="Spectrin 1" FT REPEAT 748..832 FT /note="Spectrin 2" FT REPEAT 845..938 FT /note="Spectrin 3" FT DOMAIN 949..1006 FT /note="SH3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192" FT REPEAT 1323..1423 FT /note="Spectrin 4" FT REPEAT 2795..2832 FT /note="Plectin 1" FT REPEAT 2833..2870 FT /note="Plectin 2" FT REPEAT 2871..2908 FT /note="Plectin 3" FT REPEAT 2909..2946 FT /note="Plectin 4" FT REPEAT 2947..2984 FT /note="Plectin 5" FT REPEAT 2988..3022 FT /note="Plectin 6" FT REPEAT 3123..3160 FT /note="Plectin 7" FT REPEAT 3161..3198 FT /note="Plectin 8" FT REPEAT 3199..3236 FT /note="Plectin 9" FT REPEAT 3237..3274 FT /note="Plectin 10" FT REPEAT 3275..3312 FT /note="Plectin 11" FT REPEAT 3315..3350 FT /note="Plectin 12" FT REPEAT 3492..3529 FT /note="Plectin 13" FT REPEAT 3530..3567 FT /note="Plectin 14" FT REPEAT 3568..3605 FT /note="Plectin 15" FT REPEAT 3606..3643 FT /note="Plectin 16" FT REPEAT 3647..3681 FT /note="Plectin 17" FT REPEAT 3827..3864 FT /note="Plectin 18" FT REPEAT 3865..3902 FT /note="Plectin 19" FT REPEAT 3903..3940 FT /note="Plectin 20" FT REPEAT 3941..3978 FT /note="Plectin 21" FT REPEAT 3982..4015 FT /note="Plectin 22" FT REPEAT 4070..4107 FT /note="Plectin 23" FT REPEAT 4108..4145 FT /note="Plectin 24" FT REPEAT 4146..4183 FT /note="Plectin 25" FT REPEAT 4184..4221 FT /note="Plectin 26" FT REPEAT 4225..4259 FT /note="Plectin 27" FT REPEAT 4272..4312 FT /note="Plectin 28" FT REPEAT 4415..4452 FT /note="Plectin 29" FT REPEAT 4453..4490 FT /note="Plectin 30" FT REPEAT 4491..4528 FT /note="Plectin 31" FT REPEAT 4529..4566 FT /note="Plectin 32" FT REPEAT 4567..4604 FT /note="Plectin 33" FT REGION 1..1478 FT /note="Globular 1" FT /evidence="ECO:0000250" FT REGION 113..161 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 167..186 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 181..411 FT /note="Actin-binding" FT REGION 1479..2762 FT /note="Central fibrous rod domain" FT /evidence="ECO:0000250" FT REGION 1626..1653 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1801..1835 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 2100..2141 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 2223..2317 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 2675..2728 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 2763..4691 FT /note="Globular 2" FT /evidence="ECO:0000250" FT REGION 3312..3338 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 4257..4307 FT /note="Binding to intermediate filaments" FT /evidence="ECO:0000250" FT REGION 4387..4420 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 4618..4691 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 4632..4647 FT /note="4 X 4 AA tandem repeats of G-S-R-X" FT COILED 1477..1697 FT /evidence="ECO:0000255" FT COILED 1729..2764 FT /evidence="ECO:0000255" FT COMPBIAS 134..156 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1805..1835 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 2223..2265 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 2692..2728 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 3313..3327 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 4387..4417 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 4618..4675 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 728 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:16452087, FT ECO:0007744|PubMed:21183079" FT MOD_RES 823 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:17208939" FT MOD_RES 1055 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 1443 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q15149" FT MOD_RES 1729 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q15149" FT MOD_RES 1733 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:23806337" FT MOD_RES 2639 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q15149" FT MOD_RES 2644 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:23806337" FT MOD_RES 2781 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P30427" FT MOD_RES 2788 FT /note="Phosphotyrosine" FT /evidence="ECO:0007744|PubMed:17947660" FT MOD_RES 2809 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q15149" FT MOD_RES 2893 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:Q15149" FT MOD_RES 3040 FT /note="Phosphotyrosine" FT /evidence="ECO:0007744|PubMed:17947660" FT MOD_RES 3060 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:23806337" FT MOD_RES 3098 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q15149" FT MOD_RES 3369 FT /note="Phosphotyrosine" FT /evidence="ECO:0007744|PubMed:17947660" FT MOD_RES 3427 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q15149" FT MOD_RES 3792 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:Q15149" FT MOD_RES 3797 FT /note="Phosphotyrosine" FT /evidence="ECO:0007744|PubMed:17947660" FT MOD_RES 4037 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 4061 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q15149" FT MOD_RES 4389 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19131326, FT ECO:0007744|PubMed:21183079" FT MOD_RES 4391 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 4392 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 4393 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19131326, FT ECO:0007744|PubMed:19144319, ECO:0007744|PubMed:21183079" FT MOD_RES 4396 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19144319, FT ECO:0007744|PubMed:21183079" FT MOD_RES 4397 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q15149" FT MOD_RES 4398 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q15149" FT MOD_RES 4399 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q15149" FT MOD_RES 4400 FT /note="Phosphotyrosine" FT /evidence="ECO:0000250|UniProtKB:Q15149" FT MOD_RES 4403 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q15149" FT MOD_RES 4413 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P30427" FT MOD_RES 4418 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:Q15149" FT MOD_RES 4546 FT /note="Phosphothreonine; by CDK1" FT /evidence="ECO:0000250|UniProtKB:Q9JI55" FT MOD_RES 4614 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q15149" FT MOD_RES 4620 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 4622 FT /note="Phosphotyrosine" FT /evidence="ECO:0007744|PubMed:17947660" FT MOD_RES 4623 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q15149" FT MOD_RES 4625 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 4629 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 4630 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 4633 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17242355, FT ECO:0007744|PubMed:21183079" FT MOD_RES 4634 FT /note="Omega-N-methylarginine" FT /evidence="ECO:0007744|PubMed:24129315" FT MOD_RES 4647 FT /note="Omega-N-methylarginine" FT /evidence="ECO:0007744|PubMed:24129315" FT MOD_RES 4649 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 4682 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q15149" FT VAR_SEQ 1..242 FT /note="Missing (in isoform PLEC-1H)" FT /evidence="ECO:0000305" FT /id="VSP_005040" FT VAR_SEQ 1..66 FT /note="MVAGMLMPLDRLRAIYEVLFREGVMVAKKDRRPRSLHPHVPGVTNLQVMRAM FT ASLKARGLVRETFA -> MSGEDSEVRPVAVAEGSSNGSSGSPSPGDTLPWNLGKTQRS FT RRSGGGSVGNGSVLDPAERAVIRIA (in isoform PLEC-0,1C, isoform FT PLEC-0,1C,2A,3A and isoform PLEC-0,1C,2A)" FT /evidence="ECO:0000305" FT /id="VSP_005039" FT VAR_SEQ 1..44 FT /note="MVAGMLMPLDRLRAIYEVLFREGVMVAKKDRRPRSLHPHVPGVT -> MAGT FT WAAKGVFTSQREVLLERPCWLDGGCEQVRRGYLYGQLCCV (in isoform FT PLEC-1G)" FT /evidence="ECO:0000305" FT /id="VSP_005038" FT VAR_SEQ 1..37 FT /note="MVAGMLMPLDRLRAIYEVLFREGVMVAKKDRRPRSLH -> MSQHRLRVPEP FT EGLGSKRTSSEDNLYLAVLRASEGKK (in isoform PLEC-1A)" FT /evidence="ECO:0000305" FT /id="VSP_005036" FT VAR_SEQ 1..37 FT /note="MVAGMLMPLDRLRAIYEVLFREGVMVAKKDRRPRSLH -> MEPSGSLFPSL FT VVVGHVVTLAAVWHWRKGHRQAKDEQ (in isoform PLEC-1B and isoform FT PLEC-1B,2A)" FT /evidence="ECO:0000305" FT /id="VSP_005037" FT VAR_SEQ 1..33 FT /note="MVAGMLMPLDRLRAIYEVLFREGVMVAKKDRRP -> MNETVCRRKLSPSGS FT TNTLSRLRGTSVTCTKTS (in isoform PLEC-1I)" FT /evidence="ECO:0000305" FT /id="VSP_005035" FT VAR_SEQ 1..28 FT /note="MVAGMLMPLDRLRAIYEVLFREGVMVAK -> MAHLLTSGPPPDEQDFIQAY FT EEVREKYK (in isoform PLEC-1F)" FT /evidence="ECO:0000305" FT /id="VSP_005034" FT VAR_SEQ 1..15 FT /note="MVAGMLMPLDRLRAI -> MDPSRAIQHEISSLK (in isoform FT PLEC-1E and isoform PLEC-1E,2A)" FT /evidence="ECO:0000305" FT /id="VSP_005033" FT VAR_SEQ 1..5 FT /note="MVAGM -> MKIVP (in isoform PLEC-1D and isoform FT PLEC-1D,2A)" FT /evidence="ECO:0000305" FT /id="VSP_005032" FT VAR_SEQ 6..180 FT /note="Missing (in isoform PLEC-1D and isoform PLEC-1D,2A)" FT /evidence="ECO:0000305" FT /id="VSP_005041" FT VAR_SEQ 16..180 FT /note="Missing (in isoform PLEC-1E and isoform PLEC-1E,2A)" FT /evidence="ECO:0000305" FT /id="VSP_005042" FT VAR_SEQ 29..180 FT /note="Missing (in isoform PLEC-1F)" FT /evidence="ECO:0000305" FT /id="VSP_005043" FT VAR_SEQ 34..180 FT /note="Missing (in isoform PLEC-1I)" FT /evidence="ECO:0000305" FT /id="VSP_005044" FT VAR_SEQ 38..180 FT /note="Missing (in isoform PLEC-1A, isoform PLEC-1B and FT isoform PLEC-1B,2A)" FT /evidence="ECO:0000305" FT /id="VSP_005045" FT VAR_SEQ 45..180 FT /note="Missing (in isoform PLEC-1G)" FT /evidence="ECO:0000305" FT /id="VSP_005046" FT VAR_SEQ 67..180 FT /note="Missing (in isoform PLEC-0,1C, isoform PLEC-0,1C,2A FT and isoform PLEC-0,1C,2A,3A)" FT /evidence="ECO:0000305" FT /id="VSP_005047" FT VAR_SEQ 202..206 FT /note="Missing (in isoform PLEC-1, isoform PLEC-1A, isoform FT PLEC-1B, isoform PLEC-1D, isoform PLEC-1E, isoform PLEC-1G, FT isoform PLEC-1F and isoform PLEC-0,1C)" FT /evidence="ECO:0000305" FT /id="VSP_005048" FT VAR_SEQ 239 FT /note="E -> ERDVIRSVRLPRE (in isoform PLEC-0,1C,2A,3A)" FT /evidence="ECO:0000305" FT /id="VSP_005049" FT CONFLICT 2535 FT /note="A -> V (in Ref. 1; AAR95666/AAR95671/AAR95676)" FT /evidence="ECO:0000305" FT HELIX 181..199 FT /evidence="ECO:0007829|PDB:4Q57" FT HELIX 205..207 FT /evidence="ECO:0007829|PDB:1SH5" FT TURN 214..220 FT /evidence="ECO:0007829|PDB:4Q57" FT HELIX 222..232 FT /evidence="ECO:0007829|PDB:4Q57" FT HELIX 244..260 FT /evidence="ECO:0007829|PDB:4Q57" FT HELIX 270..274 FT /evidence="ECO:0007829|PDB:4Q57" FT HELIX 278..292 FT /evidence="ECO:0007829|PDB:4Q57" FT HELIX 294..296 FT /evidence="ECO:0007829|PDB:4Q57" FT HELIX 308..319 FT /evidence="ECO:0007829|PDB:4Q57" FT TURN 320..322 FT /evidence="ECO:0007829|PDB:4Q57" FT HELIX 333..335 FT /evidence="ECO:0007829|PDB:4Q57" FT HELIX 339..348 FT /evidence="ECO:0007829|PDB:4Q57" FT HELIX 350..352 FT /evidence="ECO:0007829|PDB:4Q57" FT HELIX 355..360 FT /evidence="ECO:0007829|PDB:4Q57" FT HELIX 363..378 FT /evidence="ECO:0007829|PDB:4Q57" FT HELIX 386..389 FT /evidence="ECO:0007829|PDB:4Q57" FT STRAND 390..393 FT /evidence="ECO:0007829|PDB:4Q57" FT HELIX 396..408 FT /evidence="ECO:0007829|PDB:4Q57" FT MOD_RES Q9QXS1-3:21 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19131326, FT ECO:0007744|PubMed:19144319, ECO:0007744|PubMed:21183079" FT MOD_RES Q9QXS1-3:26 FT /note="Phosphotyrosine" FT /evidence="ECO:0007744|PubMed:17947660" FT REGION Q9QXS1-6:963..4572 FT /note="Required for interaction with intermediate filament FT proteins" FT /evidence="ECO:0000250|UniProtKB:Q15149" FT REGION Q9QXS1-6:3954..4291 FT /note="Required for interaction with type2 keratins, DES FT and VIM" FT /evidence="ECO:0000269|PubMed:24940650" FT REGION Q9QXS1-6:4503..4572 FT /note="Required for efficient interaction with KRT5 and FT KRT14 heterodimers" FT /evidence="ECO:0000269|PubMed:24940650" SQ SEQUENCE 4691 AA; 534188 MW; 91A09EC8181137D1 CRC64; MVAGMLMPLD RLRAIYEVLF REGVMVAKKD RRPRSLHPHV PGVTNLQVMR AMASLKARGL VRETFAWCHF YWYLTNEGID HLRQYLHLPP EIVPASLQRV RRPVAMVIPA RRRSPHVQTM QGPLGCPPKR GPLPAEDPAR EERQVYRRKE REEGAPETPV VSATTVGTLA RPGPEPAPAT DERDRVQKKT FTKWVNKHLI KHWRAEAQRH ISDLYEDLRD GHNLISLLEV LSGDSLPREK GRMRFHKLQN VQIALDYLRH RQVKLVNIRN DDIADGNPKL TLGLIWTIIL HFQISDIQVS GQSEDMTAKE KLLLWSQRMV EGYQGLRCDN FTTSWRDGRL FNAIIHRHKP MLIDMNKVYR QTNLENLDQA FSVAERDLGV TRLLDPEDVD VPQPDEKSII TYVSSLYDAM PRVPGAQDGV RANELQLRWQ EYRELVLLLL QWIRHHTAAF EERKFPSSFE EIEILWCQFL KFKETELPAK EADKNRSKVI YQSLEGAVQA GQLKIPPGYH PLDVEKEWGK LHVAILEREK QLRSEFERLE CLQRIVSKLQ MEAGLCEEQL NQADALLQSD IRLLASGKVA QRAGEVERDL DKADGMIRLL FNDVQTLKDG RHPQGEQMYR RVYRLHERLV AIRTEYNLRL KAGVGAPVTQ VTLQSTQRRP ELEDSTLRYL QDLLAWVEEN QRRIDSAEWG VDLPSVEAQL GSHRGMHQSI EEFRAKIERA RNDESQLSPA TRGAYRDCLG RLDLQYAKLL NSSKARLRSL ESLHGFVAAA TKELMWLNEK EEEEVGFDWS DRNTNMAAKK ESYSALMREL EMKEKKIKEI QNTGDRLLRE DHPARPTVES FQAALQTQWS WMLQLCCCIE AHLKENTAYF QFFSDVREAE EQLQKLQETL RRKYSCDRTI TVTRLEDLLQ DAQDEKEQLN EYKGHLSGLA KRAKAIVQLK PRNPAHPVRG HVPLIAVCDY KQVEVTVHKG DQCQLVGPAQ PSHWKVLSGS SSEAAVPSVC FLVPPPNQEA QEAVARLEAQ HQALVTLWHQ LHVDMKSLLA WQSLSRDIQL IRSWSLVTFR TLKPEEQRQA LRNLELHYQA FLRDSQDAGG FGPEDRLVAE REYGSCSRHY QQLLQSLEQG EQEESRCQRC ISELKDIRLQ LEACETRTVH RLRLPLDKDP ARECAQRIAE QQKAQAEVEG LGKGVARLSA EAEKVLALPE PSPAAPTLRS ELELTLGKLE QVRSLSAIYL EKLKTISLVI RSTQGAEEVL KTHEEQLKEA QAVPATLQEL EATKASLKKL RAQAEAQQPV FNTLRDELRG AQEVGERLQQ RHGERDVEVE RWRERVTQLL ERWQAVLAQT DVRQRELEQL GRQLRYYRES ADPLSAWLQD AKRRQEQIQA VPIANCQAAR EQLRQEKALL EEIERHGEKV EECQKFAKQY INAIKDYELQ LITYKAQLEP VASPAKKPKV QSGSESVIQE YVDLRTRYSE LTTLTSQYIK FISETLRRME EEERLAEQQR AEERERLAEV EAALEKQRQL AEAHAQAKAQ AELEAQELQR RMQEEVARRE EAAVDAQQQK RSIQEELQHL RQSSEAEIQA KAQQVEAAER SRMRIEEEIR VVRLQLETTE RQRGGAEGEL QALRARAEEA EAQKRQAQEE AERLRRQVQD ESQRKRQAEA ELALRVKAEA EAAREKQRAL QALDELRLQA EEAERRLRQA EAERARQVQV ALETAQRSAE VELQSKRASF AEKTAQLERT LQEEHVTVAQ LREEAERRAQ QQAEAERARE EAERELERWQ LKANEALRLR LQAEEVAQQK SLAQADAEKQ KEEAEREARR RGKAEEQAVR QRELAEQELE KQRQLAEGTA QQRLAAEQEL IRLRAETEQG EQQRQLLEEE LARLQHEATA ATQKRQELEA ELAKVRAEME VLLASKARAE EESRSTSEKS KQRLEAEAGR FRELAEEAAR LRALAEEAKR QRQLAEEDAA RQRAEAERVL TEKLAAISEA TRLKTEAEIA LKEKEAENER LRRLAEDEAF QRRRLEEQAA LHKADIEERL AQLRKASESE LERQKGLVED TLRQRRQVEE EIMALKVSFE KAAAGKAELE LELGRIRSNA EDTMRSKEQA ELEAARQRQL AAEEEQRRRE AEERVQRSLA AEEEAARQRK VALEEVERLK AKVEEARRLR ERAEQESARQ LQLAQEAAQK RLQAEEKAHA FVVQQREEEL QQTLQQEQNM LDRLRSEAEA ARRAAEEAEE AREQAEREAA QSRKQVEEAE RLKQSAEEQA QAQAQAQAAA EKLRKEAEQE AARRAQAEQA ALKQKQAADA EMEKHKKFAE QTLRQKAQVE QELTTLRLQL EETDHQKSIL DEELQRLKAE VTEAARQRSQ VEEELFSVRV QMEELGKLKA RIEAENRALI LRDKDNTQRF LEEEAEKMKQ VAEEAARLSV AAQEAARLRQ LAEEDLAQQR ALAEKMLKEK MQAVQEATRL KAEAELLQQQ KELAQEQARR LQEDKEQMAQ QLVEETQGFQ RTLEAERQRQ LEMSAEAERL KLRMAEMSRA QARAEEDAQR FRKQAEEIGE KLHRTELATQ EKVTLVQTLE IQRQQSDHDA ERLREAIAEL EREKEKLKQE AKLLQLKSEE MQTVQQEQIL QETQALQKSF LSEKDSLLQR ERFIEQEKAK LEQLFQDEVA KAKQLREEQQ RQQQQMEQEK QELMASMEEA RRRQREAEEG VRRKQEELQH LEQQRQQQEK LLAEENQRLR ERLQRLEEEH RAALAHSEIA TTQAASTKAL PNGRDAPDGP SVEAEPEYTF EGLRQKVPAQ QLQEAGILSQ EELQRLAQGH TTVAELTQRE DVYRYLKGRS SIAGLLLKPT NEKLSVYTAL QRQLLSPGTA LILLEAQAAS GFLLDPVRNR RLTVNEAVKE GVVGPELHHK LLSAERAVTG YKDPYTGEQI SLFQAMKKDL IVRDHGVRLL EAQIATGGII DPVHSHRVPV DVAYKRGYFD EEMNRILSDP SDDTKGFFDP NTHENLTYLQ LLERCVEDPE TGLRLLPLTD KAAKGGELVY TDTEARDVFE KATVSAPFGK FQGRTVTIWE IINSEYFTAE QRRDLLQQFR TGHITVEKII KIVITVVEEH ERKGQLCFEG LRALVPAAEL LDSGVISHEL YQQLQRGERS VREVAEADSV RQALRGTNVI AGVWLEEAGQ KLSIYEALKK DLLQPEVAVA LLEAQAGTGH IIDPATSARL TVDEAVRAGL VGPELHEKLL SAEKAVTGYR DPYSGQSVSL FQALKKGLIP REQGLRLLDA QLSTGGIVDP SKSHRVPLDV AYARGYLDKE TNRALTSPRD DARVYHDPST QEPVTYSQLQ QRCRSDQLTG LSLLPLSEKA VRARQEEVYS ELQARETLEQ AKVEVPVGSF KGRAMTVWEL ISSEYFTEEQ RQELLRQFRT GKVTVEKVIK IVITIVEEVE TRRQERLSFS GLRAPVPASE LLDAKILSRA QFDQLKDGKT SVKELSEVGS VRTLLQGSGC LAGIYLEDSK EKVTIYEAMR RGLLRPSTAT LLLEAQAATG FLVDPVRNQR LYVHEAVKAG VVGPELHEKL LSAEKAVTGY KDPYSGNTIS LFQAMKKGLV LRDHAIRLLE AQVATGGIID PVHSHRLPVD VAYQRGYFDE EMNRVLADPS DDTKGFFDPN THENLTYLQL LERCVEDPET GLRLLPLKGA EKTEVVETTQ VYTEEETRRA FEETQIDIPG GGSHGGSSMS LWEVMQSNMI PEDQRARLMA DFQAGRVTKE RMIIIIIEII EKTEIIRQQN LASYDYVRRR LTAEDLYEAR IISLETYNLF REGTKNLREV LEMESAWRYL YGTGAVAGVY LPGSRQTLTI YQALKKGLLS AEVARLLLEA QAATGFLLDP VKGERLTVDE AVRKGLVGPE LHDRLLSAER AVTGYRDPYT EQTISLFQAM KKELIPAEEA LRLLDAQLAT GGIVDPRLGF HLPLEVAYQR GYLNKDTHDQ LSEPSEVRSY VDPSTDERLS YTQLLKRCRR DDPSGQMLLL LSDARKLTFR GLRKQITVEE LVRSQVMDEA TALQLQEGLT SIEEVTKNLQ KFLEGTSCIA GVFVDATKER LSVYQAMKKG IIRPGTAFEL LEAQAATGYV IDPIKGLKLT VEEAVRMGIV GPEFKDKLLS AERAVTGYKD PYSGKLISLF QAMKKGLILK DHGIRLLEAQ IATGGIIDPE ESHRLPVEVA YKRGLFDEEM NEILTDPSDD TKGFFDPNTE ENLTYLQLME RCITDPQTGL CLLPLKEKKR ERKTSSKSSV RKRRVVIVDP ETGKEMSVYE AYRKGLIDHQ TYLELSEQEC EWEEITISSS DGVVKSMIID RRSGRQYDID DAITKNLIDR SALDQYRAGT LSITEFADML SGNAGGFRSR SSSVGSSSSY PISSAGPRTQ LASWSDPTEE TGPVAGILDT ETLEKVSITE AMHRNLVDNI TGQRLLEAQA CTGGIIDPST GERFPVTEAV NKGLVDKIMV DRINLAQKAF CGFEDPRTKT KMSAAQALKK GWLYYEAGQR FLEVQYLTGG LIEPDTPGRV SLDEALQRGT VDARTAQKLR DVSAYSKYLT CPKTKLKISY KDALDRSMVE EGTGLRLLEA AAQSSKGYYS PYSVSGSGST AGSRTGSRTG SRAGSRRGSF DATGSGFSMT FSSSSYSSSG YGRRYASGPS ASLGGPESAV A //