ID EPIPL_MOUSE Reviewed; 6548 AA. AC Q8R0W0; DT 15-AUG-2003, integrated into UniProtKB/Swiss-Prot. DT 15-AUG-2003, sequence version 2. DT 24-JAN-2024, entry version 124. DE RecName: Full=Epiplakin {ECO:0000303|PubMed:12791695}; GN Name=Eppk1 {ECO:0000312|MGI:MGI:2386306}; Synonyms=EPPK; 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 {ECO:0000312|EMBL:AAP70316.1}; RN [1] {ECO:0000305} RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY. RC STRAIN=C57BL/6J {ECO:0000312|EMBL:AAP70316.1}; RC TISSUE=Skin {ECO:0000269|PubMed:12791695}; RX PubMed=12791695; DOI=10.1074/jbc.m303055200; RA Spazierer D., Fuchs P., Proell V., Janda L., Oehler S., Fischer I., RA Hauptmann R., Wiche G.; RT "Epiplakin gene analysis in mouse reveals a single exon encoding a 725-kDa RT protein with expression restricted to epithelial tissues."; RL J. Biol. Chem. 278:31657-31666(2003). RN [2] {ECO:0000305} RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 6318-6548. RC TISSUE=Salivary gland {ECO:0000312|EMBL:AAH26387.1}; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [3] RP DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, AND FUNCTION. RX PubMed=16382146; DOI=10.1128/mcb.26.2.548-558.2006; RA Goto M., Sumiyoshi H., Sakai T., Faessler R., Ohashi S., Adachi E., RA Yoshioka H., Fujiwara S.; RT "Elimination of epiplakin by gene targeting results in acceleration of RT keratinocyte migration in mice."; RL Mol. Cell. Biol. 26:548-558(2006). RN [4] RP INTERACTION WITH KRT5 AND KRT14, TISSUE SPECIFICITY, AND FUNCTION. RX PubMed=18285451; DOI=10.1242/jcs.013755; RA Spazierer D., Raberger J., Gross K., Fuchs P., Wiche G.; RT "Stress-induced recruitment of epiplakin to keratin networks increases RT their resistance to hyperphosphorylation-induced disruption."; RL J. Cell Sci. 121:825-833(2008). RN [5] RP SUBCELLULAR LOCATION, AND FUNCTION. RX PubMed=20926261; DOI=10.1016/j.jdermsci.2010.08.011; RA Ishikawa K., Sumiyoshi H., Matsuo N., Takeo N., Goto M., Okamoto O., RA Tatsukawa S., Kitamura H., Fujikura Y., Yoshioka H., Fujiwara S.; RT "Epiplakin accelerates the lateral organization of keratin filaments during RT wound healing."; RL J. Dermatol. Sci. 60:95-104(2010). RN [6] RP SUBCELLULAR LOCATION, AND FUNCTION. RX PubMed=23599337; DOI=10.1167/iovs.12-11077; RA Kokado M., Okada Y., Goto M., Ishikawa K., Miyamoto T., Yamanaka O., RA Fujiwara S., Saika S.; RT "Increased fragility, impaired differentiation, and acceleration of RT migration of corneal epithelium of epiplakin-null mice."; RL Invest. Ophthalmol. Vis. Sci. 54:3780-3789(2013). RN [7] RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND FUNCTION. RX PubMed=25232867; DOI=10.1371/journal.pone.0108323; RA Woegenstein K.L., Szabo S., Lunova M., Wiche G., Haybaeck J., Strnad P., RA Boor P., Wagner M., Fuchs P.; RT "Epiplakin deficiency aggravates murine caerulein-induced acute RT pancreatitis and favors the formation of acinar keratin granules."; RL PLoS ONE 9:E108323-E108323(2014). RN [8] RP TISSUE SPECIFICITY, INDUCTION, INTERACTION WITH KRT8 AND KRT18, FUNCTION, RP AND SUBCELLULAR LOCATION. RX PubMed=25617501; DOI=10.1016/j.jhep.2015.01.007; RA Szabo S., Woegenstein K.L., Oesterreicher C.H., Guldiken N., Chen Y., RA Doler C., Wiche G., Boor P., Haybaeck J., Strnad P., Fuchs P.; RT "Epiplakin attenuates experimental mouse liver injury by chaperoning RT keratin reorganization."; RL J. Hepatol. 62:1357-1366(2015). CC -!- FUNCTION: Cytoskeletal linker protein that connects to intermediate CC filaments and controls their reorganization in response to stress CC (PubMed:16382146, PubMed:20926261, PubMed:18285451, PubMed:25232867, CC PubMed:25617501, PubMed:23599337). In response to mechanical stress CC like wound healing, is associated with the machinery for cellular CC motility by slowing down keratinocyte migration and proliferation and CC accelerating keratin bundling in proliferating keratinocytes thus CC contributing to tissue architecture (PubMed:16382146, PubMed:20926261). CC However in wound healing in corneal epithelium also positively CC regulates cell differentiation and proliferation and negatively CC regulates migration thereby controlling corneal epithelium CC morphogenesis and integrity (PubMed:23599337). In response to cellular CC stress, plays a role in keratin filament reorganization, probably by CC protecting keratin filaments against disruption (PubMed:18285451). CC During liver and pancreas injuries, plays a protective role by CC chaperoning disease-induced intermediate filament reorganization CC (PubMed:25232867, PubMed:25617501). {ECO:0000269|PubMed:16382146, CC ECO:0000269|PubMed:18285451, ECO:0000269|PubMed:20926261, CC ECO:0000269|PubMed:23599337, ECO:0000269|PubMed:25232867, CC ECO:0000269|PubMed:25617501}. CC -!- SUBUNIT: Interacts with KRT5, KRT14 and KRT5/KRT14 heterotetramer; CC interacts preferentially with assembled filaments rather than keratin CC monomers (PubMed:18285451). Interacts with KRT8 and KRT18 and CC KRT8/KRT18 heterotetramer; interacts preferentially with assembled CC filaments rather than keratin monomers (PubMed:25617501). Interacts CC with KRT1, VIM and DES; interaction is stronger with KRT1 than with VIM CC or DES; interaction is dependent of higher-order structure of CC intermediate filament (By similarity). {ECO:0000250|UniProtKB:P58107, CC ECO:0000269|PubMed:18285451, ECO:0000269|PubMed:25617501}. CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton CC {ECO:0000269|PubMed:20926261, ECO:0000269|PubMed:25617501}. CC Apicolateral cell membrane {ECO:0000269|PubMed:25232867}. Basolateral CC cell membrane {ECO:0000269|PubMed:23599337}. Cell junction CC {ECO:0000269|PubMed:23599337}. Cell junction, hemidesmosome CC {ECO:0000250|UniProtKB:P58107}. Cell junction, tight junction CC {ECO:0000250|UniProtKB:P58107}. Cell projection CC {ECO:0000250|UniProtKB:P58107}. Note=Apicolateral cell membrane CC localization is keratin filaments-dependent (PubMed:25232867). May move CC dynamically from bundling intermediate filaments in the cytoplasm or at CC the cell periphery and reinforcing them. Decorates the keratin CC intermediate filaments (IF) network and partially that of vimentin (By CC similarity). {ECO:0000250|UniProtKB:P58107, CC ECO:0000269|PubMed:25232867}. CC -!- TISSUE SPECIFICITY: High levels in skin, small intestine and salivary CC gland. Lower levels in lung, uterus and liver. Not detected in brain, CC kidney, muscle, heart or spleen. In skin, expressed in all epidermal CC layers but not in the dermis. In intestine, expressed exclusively in CC the epithelial cell layer of the villi. In liver, expressed at CC hepatocyte margins. Around the region of the wound, expressed in the CC upper half of the epidermis. Weakly expressed on the basilar side of CC the suprabasal layer of the epidermis at the wound's edge. Expressed CC strongly in the upper layer of the epidermis, especially in larger CC keratinocytes (PubMed:16382146). Expressed in undifferentiated primary CC keratinocytes (PubMed:18285451). Strongly expressed in ductal cells, CC and also expressed in acinar cells (PubMed:25232867). Expressed in CC hepatocytes and cholangiocytes (PubMed:25617501). CC {ECO:0000269|PubMed:12791695, ECO:0000269|PubMed:16382146, CC ECO:0000269|PubMed:18285451, ECO:0000269|PubMed:25232867, CC ECO:0000269|PubMed:25617501}. CC -!- INDUCTION: Up-regulated upon calcium-mediated keratinocyte CC differentiation (PubMed:18285451). Up-regulated in hepatocytes during CC liver stress (PubMed:25617501). {ECO:0000269|PubMed:18285451, CC ECO:0000269|PubMed:25617501}. CC -!- DOMAIN: Plectin repeats are important for the binding to keratin and CC VIM and controls intermediate filament networks organization. CC {ECO:0000250|UniProtKB:P58107}. CC -!- DISRUPTION PHENOTYPE: Homozygous knockout mice develop normally and are CC healthy and fertile. Skin of homozygous knockout mice reveal no CC blistering and fragility. Exhibit slightly enhanced wound closure. CC {ECO:0000269|PubMed:16382146}. 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; AY312170; AAP70316.1; -; mRNA. DR EMBL; BC026387; AAH26387.1; -; mRNA. DR RefSeq; NP_659097.2; NM_144848.2. DR BioGRID; 230168; 5. DR IntAct; Q8R0W0; 1. DR STRING; 10090.ENSMUSP00000154609; -. DR GlyGen; Q8R0W0; 2 sites, 1 O-linked glycan (2 sites). DR iPTMnet; Q8R0W0; -. DR PhosphoSitePlus; Q8R0W0; -. DR SwissPalm; Q8R0W0; -. DR EPD; Q8R0W0; -. DR jPOST; Q8R0W0; -. DR MaxQB; Q8R0W0; -. DR PeptideAtlas; Q8R0W0; -. DR ProteomicsDB; 277890; -. DR Pumba; Q8R0W0; -. DR DNASU; 223650; -. DR GeneID; 223650; -. DR KEGG; mmu:223650; -. DR UCSC; uc007wio.1; mouse. DR AGR; MGI:2386306; -. DR CTD; 83481; -. DR MGI; MGI:2386306; Eppk1. DR InParanoid; Q8R0W0; -. DR OrthoDB; 5321591at2759; -. DR BioGRID-ORCS; 223650; 2 hits in 17 CRISPR screens. DR PRO; PR:Q8R0W0; -. DR Proteomes; UP000000589; Unplaced. DR RNAct; Q8R0W0; Protein. DR GO; GO:0016327; C:apicolateral plasma membrane; IDA:UniProtKB. DR GO; GO:0045178; C:basal part of cell; IDA:UniProtKB. DR GO; GO:0016323; C:basolateral plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005923; C:bicellular tight junction; ISO:MGI. DR GO; GO:0030054; C:cell junction; IBA:GO_Central. DR GO; GO:0071944; C:cell periphery; ISO:MGI. DR GO; GO:0042995; C:cell projection; IEA:UniProtKB-SubCell. DR GO; GO:0005911; C:cell-cell junction; IDA:UniProtKB. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0005856; C:cytoskeleton; IDA:UniProtKB. DR GO; GO:0030056; C:hemidesmosome; ISO:MGI. DR GO; GO:0045111; C:intermediate filament cytoskeleton; ISO:MGI. DR GO; GO:0045095; C:keratin filament; ISO:MGI. DR GO; GO:0016020; C:membrane; IBA:GO_Central. DR GO; GO:0097356; C:perinucleolar compartment; ISO:MGI. DR GO; GO:0019215; F:intermediate filament binding; ISO:MGI. DR GO; GO:1990254; F:keratin filament binding; IPI:UniProtKB. DR GO; GO:0005198; F:structural molecule activity; IBA:GO_Central. DR GO; GO:0007010; P:cytoskeleton organization; IMP:UniProtKB. DR GO; GO:0045110; P:intermediate filament bundle assembly; IMP:UniProtKB. DR GO; GO:0045109; P:intermediate filament organization; IDA:UniProtKB. DR GO; GO:0030336; P:negative regulation of cell migration; ISO:MGI. DR GO; GO:0050680; P:negative regulation of epithelial cell proliferation; ISO:MGI. DR GO; GO:0051548; P:negative regulation of keratinocyte migration; IMP:UniProtKB. DR GO; GO:0010839; P:negative regulation of keratinocyte proliferation; IMP:UniProtKB. DR GO; GO:0061045; P:negative regulation of wound healing; IMP:UniProtKB. DR GO; GO:0060054; P:positive regulation of epithelial cell proliferation involved in wound healing; IMP:UniProtKB. DR GO; GO:0030856; P:regulation of epithelial cell differentiation; IMP:UniProtKB. DR GO; GO:1905041; P:regulation of epithelium regeneration; IMP:UniProtKB. DR GO; GO:0042060; P:wound healing; ISO:MGI. DR Gene3D; 3.90.1290.10; Plakin repeat; 16. DR InterPro; IPR043197; Plakin. DR InterPro; IPR035915; Plakin_repeat_sf. DR InterPro; IPR001101; Plectin_repeat. DR PANTHER; PTHR23169; ENVOPLAKIN; 1. DR PANTHER; PTHR23169:SF21; EPIPLAKIN; 1. DR Pfam; PF00681; Plectin; 36. DR SMART; SM00250; PLEC; 77. DR SUPFAM; SSF75399; Plakin repeat; 16. PE 1: Evidence at protein level; KW Cell junction; Cell membrane; Cell projection; Coiled coil; Cytoplasm; KW Cytoskeleton; Membrane; Phosphoprotein; Reference proteome; Repeat; KW Tight junction. FT CHAIN 1..6548 FT /note="Epiplakin" FT /id="PRO_0000078146" FT REPEAT 41..78 FT /note="Plectin 1" FT REPEAT 79..116 FT /note="Plectin 2" FT REPEAT 117..154 FT /note="Plectin 3" FT REPEAT 155..192 FT /note="Plectin 4" FT REPEAT 285..322 FT /note="Plectin 5" FT REPEAT 323..360 FT /note="Plectin 6" FT REPEAT 362..398 FT /note="Plectin 7" FT REPEAT 399..436 FT /note="Plectin 8" FT REPEAT 437..470 FT /note="Plectin 9" FT REPEAT 611..648 FT /note="Plectin 10" FT REPEAT 649..686 FT /note="Plectin 11" FT REPEAT 687..724 FT /note="Plectin 12" FT REPEAT 725..762 FT /note="Plectin 13" FT REPEAT 766..800 FT /note="Plectin 14" FT REPEAT 931..968 FT /note="Plectin 15" FT REPEAT 969..1006 FT /note="Plectin 16" FT REPEAT 1007..1044 FT /note="Plectin 17" FT REPEAT 1224..1284 FT /note="Plectin 18" FT REPEAT 1285..1322 FT /note="Plectin 19" FT REPEAT 1323..1360 FT /note="Plectin 20" FT REPEAT 1361..1398 FT /note="Plectin 21" FT REPEAT 1402..1436 FT /note="Plectin 22" FT REPEAT 1572..1609 FT /note="Plectin 23" FT REPEAT 1610..1647 FT /note="Plectin 24" FT REPEAT 1648..1685 FT /note="Plectin 25" FT REPEAT 1686..1723 FT /note="Plectin 26" FT REPEAT 1727..1761 FT /note="Plectin 27" FT REPEAT 1898..1935 FT /note="Plectin 28" FT REPEAT 1936..1973 FT /note="Plectin 29" FT REPEAT 1974..2011 FT /note="Plectin 30" FT REPEAT 2012..2049 FT /note="Plectin 31" FT REPEAT 2225..2267 FT /note="Plectin 32" FT REPEAT 2268..2305 FT /note="Plectin 33" FT REPEAT 2306..2343 FT /note="Plectin 34" FT REPEAT 2344..2381 FT /note="Plectin 35" FT REPEAT 2385..2419 FT /note="Plectin 36" FT REPEAT 2740..2782 FT /note="Plectin 37" FT REPEAT 2783..2820 FT /note="Plectin 38" FT REPEAT 2821..2858 FT /note="Plectin 39" FT REPEAT 2859..2896 FT /note="Plectin 40" FT REPEAT 2900..2934 FT /note="Plectin 41" FT REPEAT 3255..3297 FT /note="Plectin 42" FT REPEAT 3298..3335 FT /note="Plectin 43" FT REPEAT 3336..3373 FT /note="Plectin 44" FT REPEAT 3374..3411 FT /note="Plectin 45" FT REPEAT 3415..3449 FT /note="Plectin 46" FT REPEAT 3770..3812 FT /note="Plectin 47" FT REPEAT 3813..3850 FT /note="Plectin 48" FT REPEAT 3851..3888 FT /note="Plectin 49" FT REPEAT 3889..3926 FT /note="Plectin 50" FT REPEAT 3930..3964 FT /note="Plectin 51" FT REPEAT 4285..4327 FT /note="Plectin 52" FT REPEAT 4328..4365 FT /note="Plectin 53" FT REPEAT 4366..4403 FT /note="Plectin 54" FT REPEAT 4404..4441 FT /note="Plectin 55" FT REPEAT 4445..4479 FT /note="Plectin 56" FT REPEAT 4800..4842 FT /note="Plectin 57" FT REPEAT 4843..4880 FT /note="Plectin 58" FT REPEAT 4881..4918 FT /note="Plectin 59" FT REPEAT 4919..4956 FT /note="Plectin 60" FT REPEAT 4960..4994 FT /note="Plectin 61" FT REPEAT 5315..5357 FT /note="Plectin 62" FT REPEAT 5358..5395 FT /note="Plectin 63" FT REPEAT 5396..5433 FT /note="Plectin 64" FT REPEAT 5434..5471 FT /note="Plectin 65" FT REPEAT 5475..5509 FT /note="Plectin 66" FT REPEAT 5830..5872 FT /note="Plectin 67" FT REPEAT 5873..5910 FT /note="Plectin 68" FT REPEAT 5911..5948 FT /note="Plectin 69" FT REPEAT 5949..5986 FT /note="Plectin 70" FT REPEAT 5990..6024 FT /note="Plectin 71" FT REPEAT 6345..6387 FT /note="Plectin 72" FT REPEAT 6388..6425 FT /note="Plectin 73" FT REPEAT 6426..6463 FT /note="Plectin 74" FT REPEAT 6464..6501 FT /note="Plectin 75" FT REPEAT 6505..6539 FT /note="Plectin 76" FT REGION 49..1123 FT /note="Interaction with KRT5" FT /evidence="ECO:0000269|PubMed:18285451" FT REGION 1580..6545 FT /note="Interaction with KRT5" FT /evidence="ECO:0000269|PubMed:18285451" FT REGION 2575..2626 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 2748..2940 FT /note="Interaction with KRT14" FT /evidence="ECO:0000269|PubMed:18285451" FT REGION 3090..3146 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 3605..3661 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 4120..4176 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 4635..4691 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 5150..5206 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 5665..5721 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 6180..6234 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 545..565 FT /evidence="ECO:0000255" FT COILED 851..886 FT /evidence="ECO:0000255" FT COILED 1819..1851 FT /evidence="ECO:0000255" FT COMPBIAS 2575..2594 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 2596..2626 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 3090..3109 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 3111..3146 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 3605..3624 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 3626..3661 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 4120..4139 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 4141..4176 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 4635..4654 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 4656..4691 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 5150..5169 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 5171..5206 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 5665..5684 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 5686..5721 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 6180..6199 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 6201..6234 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 33 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:P58107" FT MOD_RES 1551 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:P58107" FT MOD_RES 2430 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P58107" FT MOD_RES 2508 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P58107" FT MOD_RES 3220 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P58107" FT MOD_RES 3460 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P58107" FT MOD_RES 3538 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P58107" FT MOD_RES 3735 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P58107" FT MOD_RES 3975 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P58107" FT MOD_RES 4053 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P58107" FT MOD_RES 4765 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P58107" FT MOD_RES 5005 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P58107" FT MOD_RES 5083 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P58107" FT MOD_RES 5795 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P58107" FT MOD_RES 6035 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P58107" FT MOD_RES 6113 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P58107" FT MOD_RES 6310 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P58107" SQ SEQUENCE 6548 AA; 724646 MW; 9162C07AFCA157B6 CRC64; MNGQAPPHDV VVANGTEKFI VPKIKKNQLG ASTPSRPQAE AALPTTARSI AGVYVEASGQ TQSIYAAIKQ GLLPTGLGLT LLEAQAATGG LVDLAQGQLL PVSEALRRGL VGLELKEKLL AAERAVTGYP DPYGGEKLSL FQAIKKEVVD RTLGWRLLEA QLATGGLVDP TQGVQVAPEL ACQQGLLDKE TWLSLVESEP SMGTPGFSDP NTLEQLPYSV LLGRCVQDPS SGLPLLPLKT TFHTLAGAAS ASMLLEAGVL NEEMVRDLQE GMLVVSDVGT RPEVRRYLEG TGGLAGVVLL PGGHKKSFFQ ATVEHLVSKG IALQLLEAQA ATRTLVHPTT GQRLWVEEAV KAGLVGPELH EQLLVAEQAV TGYYDPFSSS RIPVFQAMKK GLVDQPLALR LLDAQLATGG LICPARRFRL PLEAALRFGC LDEETRQRLS QAMGFSDPTT HDRLGYEQLL ALSVTDPETG LAFLPLPGMS HANEPQGPTF IDHCTRQALS KATTSISVGR YQGRPVSLWE LLFSESVPVK KRAMLAQRHQ EGALSVEELA AELKNIVEQA AATAKVTFAG LRDTVTPGEL LKAEIINQDL FEQLERGQTS AQDVGSLDSV QRYLQGTGSI AGLLLPDSQE RLSIYEARSK GLLRPGTALI LLEAQAATGF IIDPKENKRY SVEEALRAGV IGPDVYAKLL SAEHAVTGYT DPYSGEQISL FQAMQRDLIV RDHGIRLLEA QIATGGVIDP VHSHRVPVDV AYQRGYFDQI LNSILLDPSD DTKGFFDPNT HENLTYLQLL ERCVHDSETG LHLLPLSSTR PQLVDSSTRQ AFQKLLLSVK YGRFRGQRVS AWELVNSEYF TEDRRRQLLQ RYRQRKITLE QVTQLLEKEM RRWTDITLPA LQGQVTAYQL LEAHIINQEL LDQVLTGTIS PDALLQVGDV HRYLRGSGTV GGVLLKPSNQ RISLYQAMKQ KLLPPSTALA LLEAQAATGT ITDPCSMETL SVDEAVCRGV VGAEVYGKLK RAEHSITGYR DPFSGKKVSL FRAMKKGLVP VEQATRLLEA QVSTGGVVDP TTHLHLPMPV AVQRGCIDRE MEAALSRSPE TFPTPDGRGH TSYAQLLEHC LQDKASGLHL LPLTEDAPNV PTDTQIQETL QASAGTEDGL SLWDLLTSCH FTEEQRRGYL EDVKVGKISV PQLQNTVRSW VHSAKLLARA RITVPGPRGE VPATWLRDAG IITQETLEAL AQGMQSPDEV AKQPTVKVCL WGTGCVAGVL LQPSGTKLSI AQAVRDGLLP TGLGQQLLEA QVASGFLVNP LTNQRLSVEG AVKAGLVGME QSEHLRQVEK AVTGYSDPFS GGSLSLWQAM EKGLVTQSEA FPLLQVQLAT GGVVDPVHGV HLPQEVAYKL GLLDEQTSRV LTATGKENKL FFDPNSREKV TYQQLRELCV LDADTGLWLL PLPQGTVLEV DDHTAVALRA MKVPINMGRF QGHSVSLWDL LHSEYVGAEK RRELVALCCS GRAAALRQVI GMLTTLVEAA EKQPSQATFK GLRKQVSAGD LFRSQLITKQ TLDELNQGKR TVQEVTEMDS VRRSLEGGNF IAGVLIQDTK EKMSIPEALR RHILRPGTAL VLLEAQAATG FIIDPVENRK LTVEQAFQAG MFGKETYMKL LSAERAVTGY TDPYTGEQIS LFQAMQRDLI VRDHGIRLLE AQIATGGIID PVHSHRVPVD VAYQRGYFNE EMNRILSDPS DDTKGFFDPN THENLTYLQL LERCVEDPET GLYMLEIVKK GETYTYIDEA TRQALTSRTV KMYVGKFAGQ TVSVWDLLSS QYFTEGRRRK LLREYRAQNI GLENLLEVIT STVEETEKQS QIFKVPGIHG DVTAAELFNS GILNKKTLDA LRSGDRGFQD LRWLEDVRVY LEGSNYIAGV IAPLTQKVMS FYEASREELI PAGFAAQMLE AQAATGYLMD PCTNQRLCVD EAIAAGLVGE DLRERLVNAE MAAKGYKDPA TGETIPLYQA MERKLVGREE ALRLLEVQVA TGGVIDPRHH HRVPLDTACQ RGCMCDDSLV LIADQKHMRK RFVDPNTQEK VTYQELQDRC QREEKSGWAL FPVVKDKKDI EYVDEATKRA LEAEQVEVTV GRYRGQRRSV WELLNSEYVS EEKKMELVRL YKEDTTRALQ KVVELILQMI ADKERRSRQL WFRGLRTQVT AEELLRSEVI TKQTLEDLEE GRTTVDQIER KEDVKRYLKG TSCIAGVLVP VQGEPGRQEK MSIYQAMWKG VLRPGTALVL LEAQAATGFI IDPVNNRRLS VEEAVAAGVV GGEIQEKLLS AERAVTGYTD PYTGDQISLF QAMQRDLIVR DHGIRLLEAQ IATGGVIDPV HSHRVPVDVA YQRGYFDEDM NSILADPGDD TKGFFDPNTH ENLTYLQLLR RCVRDPETGF YMLQLAGKGS SVHHLSEELR RALREARVTP GTGDFQGQSI SVWELLFYRE VPESLRQDLL RCYQAGGLTV HDVTTTLTSL LARAKDGSPR GDPQGALGKA TMEVKRGHLR GHEVPVWDIL TSNYVSRDTR KELLAQFSSG SLTLPMLKRR LTTIIEEAEE TQESKPKPRD ASLKQQDTGA RGSGTSPDEG DAQDSSESAR QQQEQTLRAT TMQVHRGQFR DQQVSVWKVL FSSYLSETRR EELLAQHLAG KLGVMELVSL LTQIIEETEE RLSKVSFPGL RRQVSASELC TSGILDRDTM RELAQGTKTI HEVTEMDSVK RYLGGSSCIA GVLVPVQGEP GRQEKMSIYQ AMWKGVLRPG TALVLLEAQA ATGFIIDPVN NRRLSVEEAV AAGVVGGEIQ EKLLSAERAV TGYTDPYTGD QISLFQAMQR DLIVRDHGIR LLEAQIATGG VIDPVHSHRV PVDVAYQRGY FDEDMNSILA DPGDDTKGFF DPNTHENLTY LQLLRRCVRD PETGFYMLQL AGKGSSVHHL SEELRRALRE ARVTPGTGDF QGQSISVWEL LFYREVPESL RQDLLRRYQA GGLTVHDVTT TLTSLLARAK DGSPRXDPQG ALGKATMEVK RGHLRGHXVP VWDILTSNYV SRDTRKELLA QFSSGSLTLP MLKRRLTTII EEAEETQESK PKPRDASLKQ QDTGARGSGT SPDEGDAQDS SESARQQQEQ TLRATTMQVH RGQFRDQQVS VWKVLFSSYL SETRREELLA QHLAGKLGVM ELVSLLTQII EETEERLSKV SFPGLRRQVS ASELCTSGIL DRDTMRELAQ GTKTIHEVTE MDSVKRYLGG SSCIAGVLVP VQGEPGRQEK MSIYQAMWKG VLRPGTALVL LEAQAATGFI IDPVNNRRLS VEEAVAAGVV GGEIQEKLLS AERAVTGYTD PYTGDQISLF QAMQRDLIVR DHGIRLLEAQ IATGGVIDPV HSHRVPVDVA YQRGYFDEDM NSILADPGDD TKGFFDPNTH ENLTYLQLLR RCVRDPETGF YMLQLAGKGS SVHHLSEELR RALREARVTP GTGDFQGQSI SVWELLFYRE VPESLRQDLL RRYQAGGLTV HDVTTTLTSL LARAKDGSPR XDPQGALGKA TMEVKRGHLR GHXVPVWDIL TSNYVSRDTR KELLAQFSSG SLTLPMLKRR LTTIIEEAEE TQESKPKPRD ASLKQQDTGA RGSGTSPDEG DAQDSSESAR QQQEQTLRAT TMQVHRGQFR DQQVSVWKVL FSSYLSETRR EELLAQHLAG KLGVMELVSL LTQIIEETEE RLSKVSFPGL RRQVSASELC TSGILDRDTM RELAQGTKTI HEVTEMDSVK RYLGGSSCIA GVLVPVQGEP GRQEKMSIYQ AMWKGVLRPG TALVLLEAQA ATGFIIDPVN NRRLSVEEAV AAGVVGGEIQ EKLLSAERAV TGYTDPYTGD QISLFQAMQR DLIVRDHGIR LLEAQIATGG VIDPVHSHRV PVDVAYQRGY FDEDMNSILA DPGDDTKGFF DPNTHENLTY LQLLRRCVRD PETGFYMLQL AGKGSSVHHL SEELRRALRE ARVTPGTGDF QGQSISVWEL LFYREVPESL RQDLLRRYQA GGLTVHDVTT TLTSLLARAK DGSPRXDPQG ALGKATMEVK RGHLRGHXVP VWDILTSNYV SRDTRKELLA QFSSGSLTLP MLKRRLTTII EEAEETQESK PKPRDASLKQ QDTGARGSGT SPDEGDAQDS SESARQQQEQ TLRATTMQVH RGQFRDQQVS VWKVLFSSYL SETRREELLA QHLAGKLGVM ELVSLLTQII EETEERLSKV SFPGLRRQVS ASELCTSGIL DRDTMRELAQ GTKTIHEVTE MDSVKRYLGG SSCIAGVLVP VQGEPGRQEK MSIYQAMWKG VLRPGTALVL LEAQAATGFI IDPVNNRRLS VEEAVAAGVV GGEIQEKLLS AERAVTGYTD PYTGDQISLF QAMQRDLIVR DHGIRLLEAQ IATGGVIDPV HSHRVPVDVA YQRGYFDEDM NSILADPGDD TKGFFDPNTH ENLTYLQLLR RCVRDPETGF YMLQLAGKGS SVHHLSEELR RALREARVTP GTGDFQGQSI SVWELLFYRE VPESLRQDLL RRYQAGGLTV HDVTTTLTSL LARAKDGSPR XDPQGALGKA TMEVKRGHLR GHXVPVWDIL TSNYVSRDTR KELLAQFSSG SLTLPMLKRR LTTIIEEAEE TQESKPKPRD ASLKQQDTGA RGSGTSPDEG DAQDSSESAR QQQEQTLRAT TMQVHRGQFR DQQVSVWKVL FSSYLSETRR EELLAQHLAG KLGVMELVSL LTQIIEETEE RLSKVSFPGL RRQVSASELC TSGILDRDTM RELAQGTKTI HEVTEMDSVK RYLGGSSCIA GVLVPVQGEP GRQEKMSIYQ AMWKGVLRPG TALVLLEAQA ATGFIIDPVN NRRLSVEEAV AAGVVGGEIQ EKLLSAERAV TGYTDPYTGD QISLFQAMQR DLIVRDHGIR LLEAQIATGG VIDPVHSHRV PVDVAYQRGY FDEDMNSILA DPGDDTKGFF DPNTHENLTY LQLLRRCVRD PETGFYMLQL AGKGSSVHHL SEELRRALRE ARVTPGTGDF QGQSISVWEL LFYREVPESL RQDLLRRYQA GGLTVHDVTT TLTSLLARAK DGSPRXDPQG ALGKATMEVK RGHLRGHXVP VWDILTSNYV SRDTRKELLA QFSSGSLTLP MLKRRLTTII EEAEETQESK PKPRDASLKQ QDTGARGSGT SPDEGDAQDS SESARQQQEQ TLRATTMQVH RGQFRDQQVS VWKVLFSSYL SETRREELLA QHLAGKLGVM ELVSLLTQII EETEERLSKV SFPGLRRQVS ASELCTSGIL DRDTMRELAQ GTKTIHEVTE MDSVKRYLGG SSCIAGVLVP VQGEPGRQEK MSIYQAMWKG VLRPGTALVL LEAQAATGFI IDPVNNRRLS VEEAVAAGVV GGEIQEKLLS AERAVTGYTD PYTGDQISLF QAMQRDLIVR DHGIRLLEAQ IATGGVIDPV HSHRVPVDVA YQRGYFDEDM NSILADPGDD TKGFFDPNTH ENLTYLQLLR RCVRDPETGF YMLQLAGKGS SVHHLSEELR RALREARVTP GTGDFQGQSI SVWELLFYRE VPESLRQDLL RRYQAGGLTV HDVTTTLTSL LARAKDGSPR XDPQGALGKA TMEVKRGHLR GHXVPVWDIL TSNYVSRDTR KELLAQFSSG SLTLPMLKRR LTTIIEEAEE TQESKPKPRD ASLKQQDTGA RGSGTSPDEG DAQDSSESAR QQQEQTLRAT TMQVHRGQFR DQQVSVWKVL FSSYLSETRR EELLAQHLAG KLGVMELVSL LTQIIEETEE RLSKVSFPGL RRQVSASELC TSGILDRDTM RELAQGTKTI HEVTEMDSVK RYLGGSSCIA GVLVPVQGEP GRQEKMSIYQ AMWKGVLRPG TALVLLEAQA ATGFIIDPVN NRRLSVEEAV AAGVVGGEIQ EKLLSAERAV TGYTDPYTGD QISLFQAMQR DLIVRDHGIR LLEAQIATGG VIDPVHSHRV PVDVAYQRGY FDEDMNSILA DPGDDTKGFF DPNTHENLTY LQLLRRCVRD PETGFYMLQL AGKGSSVHHL SEELRRALRE ARVTPGTGDF QGQSISVWEL LFYREVPESL RQDLLRRYQA GGLTVHDVTT TLTSLLARAK DGSPREDPQG ALGKATMEVK RGHLRGHVVP VWDILTSNYV SRDTRKELLA QFSSGSLTLP MLKRRLTTII EEAEETQESK PKPRDASLKQ QDTGARGSGT SPDEGDAQDS SESARQQQEQ TLRATTMQVH RGQFRDQQVS VWKVLFSSYL SETRREELLA QHLAGKLGVM ELVSLLTQII EETEERLSKV SFPGLRRQVS ASELCTSGIL DRDTMRELAQ GTKTIHEVTE MDSVKRYLGG SSCIAGVLVP VQGEPGRQEK MSIYQAMWKG VLRPGTALVL LEAQAATGFI IDPVNNRRLS VEEAVAAGVV GGEIQEKLLS AERAVTGYTD PYTGDQISLF QAMQRDLIVK NHGIRLLEAQ IATGGVIDPV HSHRVPVDVA YQRGYFDQEM NSILADPGDD TKGFFDPNTH ENLTYLQLLQ RATIDPETGL LFLSLSKG //