EPIPL_MOUSE
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 03-AUG-2022, entry version 117.
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}.
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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 iPTMnet; Q8R0W0; -.
DR PhosphoSitePlus; Q8R0W0; -.
DR SwissPalm; Q8R0W0; -.
DR EPD; Q8R0W0; -.
DR jPOST; Q8R0W0; -.
DR MaxQB; Q8R0W0; -.
DR PeptideAtlas; Q8R0W0; -.
DR PRIDE; Q8R0W0; -.
DR ProteomicsDB; 277890; -.
DR DNASU; 223650; -.
DR GeneID; 223650; -.
DR KEGG; mmu:223650; -.
DR UCSC; uc007wio.1; mouse.
DR CTD; 83481; -.
DR MGI; MGI:2386306; Eppk1.
DR InParanoid; Q8R0W0; -.
DR OrthoDB; 2464at2759; -.
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:0045104; P:intermediate filament cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0045109; P:intermediate filament organization; IDA:UniProtKB.
DR GO; GO:0030336; P:negative regulation of cell migration; 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; -; 16.
DR InterPro; IPR043197; Plakin.
DR InterPro; IPR035915; Plakin_repeat_sf.
DR InterPro; IPR001101; Plectin_repeat.
DR PANTHER; PTHR23169; PTHR23169; 29.
DR Pfam; PF00681; Plectin; 45.
DR SMART; SM00250; PLEC; 77.
DR SUPFAM; SSF75399; SSF75399; 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
