PLEC_MOUSE
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 03-AUG-2022, entry version 202.
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, Pancreas,
RC 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}.
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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; 29.
DR CORUM; Q9QXS1; -.
DR DIP; DIP-32004N; -.
DR IntAct; Q9QXS1; 16.
DR MINT; Q9QXS1; -.
DR STRING; 10090.ENSMUSP00000075772; -.
DR iPTMnet; Q9QXS1; -.
DR PhosphoSitePlus; Q9QXS1; -.
DR SwissPalm; Q9QXS1; -.
DR EPD; Q9QXS1; -.
DR jPOST; Q9QXS1; -.
DR MaxQB; Q9QXS1; -.
DR PaxDb; Q9QXS1; -.
DR PeptideAtlas; Q9QXS1; -.
DR PRIDE; 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 Antibodypedia; 3549; 209 antibodies from 32 providers.
DR DNASU; 18810; -.
DR Ensembl; ENSMUST00000023226; ENSMUSP00000023226; ENSMUSG00000022565. [Q9QXS1-3]
DR Ensembl; ENSMUST00000054449; ENSMUSP00000057158; ENSMUSG00000022565. [Q9QXS1-4]
DR Ensembl; ENSMUST00000071869; ENSMUSP00000071765; ENSMUSG00000022565. [Q9QXS1-12]
DR Ensembl; ENSMUST00000072692; ENSMUSP00000072478; ENSMUSG00000022565. [Q9QXS1-14]
DR Ensembl; ENSMUST00000073418; ENSMUSP00000073124; ENSMUSG00000022565. [Q9QXS1-1]
DR Ensembl; ENSMUST00000074834; ENSMUSP00000074383; ENSMUSG00000022565. [Q9QXS1-13]
DR Ensembl; ENSMUST00000076442; ENSMUSP00000075772; ENSMUSG00000022565. [Q9QXS1-2]
DR Ensembl; ENSMUST00000089610; ENSMUSP00000087037; ENSMUSG00000022565. [Q9QXS1-8]
DR Ensembl; ENSMUST00000169108; ENSMUSP00000126068; ENSMUSG00000022565. [Q9QXS1-10]
DR Ensembl; ENSMUST00000169714; ENSMUSP00000126526; ENSMUSG00000022565. [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 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; REERWVY; -.
DR OrthoDB; 2464at2759; -.
DR PhylomeDB; Q9QXS1; -.
DR Reactome; R-MMU-2022090; Assembly of collagen fibrils and other multimeric structures.
DR Reactome; R-MMU-264870; Caspase-mediated cleavage of cytoskeletal proteins.
DR Reactome; R-MMU-446107; Type I hemidesmosome assembly.
DR BioGRID-ORCS; 18810; 4 hits in 74 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 243 other tissues.
DR ExpressionAtlas; Q9QXS1; baseline and differential.
DR Genevisible; Q9QXS1; MM.
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:0016020; C:membrane; IBA:GO_Central.
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:0047485; F:protein N-terminus binding; ISO: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:0005198; F:structural molecule activity; IBA:GO_Central.
DR GO; GO:0030036; P:actin cytoskeleton organization; IMP:MGI.
DR GO; GO:0031532; P:actin cytoskeleton reorganization; 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:0070584; P:mitochondrion morphogenesis; 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:0006469; P:negative regulation of protein kinase activity; 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:2000983; P:regulation of ATP citrate synthase activity; 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; cd00014; CH; 2.
DR CDD; cd00176; SPEC; 2.
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; 18.
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; 35.
DR SMART; SM00150; SPEC; 6.
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; 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 PLEC-
FT 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 PLEC-
FT 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 PLEC-
FT 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
