TAU_MOUSE
ID TAU_MOUSE Reviewed; 733 AA.
AC P10637; A2A5Y9; P10638; Q60684; Q60685; Q60686; Q62286; Q91WK4;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 225.
DE RecName: Full=Microtubule-associated protein tau {ECO:0000305};
DE AltName: Full=Neurofibrillary tangle protein;
DE AltName: Full=Paired helical filament-tau;
DE Short=PHF-tau;
GN Name=Mapt {ECO:0000312|MGI:MGI:97180}; Synonyms=Mtapt, Tau;
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] (ISOFORM PNS-TAU).
RC TISSUE=Neuroblastoma;
RX PubMed=1374898; DOI=10.1073/pnas.89.10.4378;
RA Couchie D., Mavilia C., Georgieff I.S., Liem R.K.H., Shelanski M.L.,
RA Nunez J.;
RT "Primary structure of high molecular weight tau present in the peripheral
RT nervous system.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:4378-4381(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS TAU-A; TAU-D AND TAU-E).
RC STRAIN=Him OF1; TISSUE=Brain, Kidney, and Liver;
RX PubMed=7927211; DOI=10.1002/hep.1840200442;
RA Kenner L., el-Shabrawi Y., Hutter H., Forstner M., Zatloukal K.,
RA Hoefler G., Preisegger K.-H., Kurzbauer R., Denk H.;
RT "Expression of three- and four-repeat tau isoforms in mouse liver.";
RL Hepatology 20:1086-1089(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS TAU-B AND TAU-C).
RC TISSUE=Brain;
RX PubMed=3122323; DOI=10.1126/science.3122323;
RA Lee G., Cowan N.J., Kirschner M.;
RT "The primary structure and heterogeneity of tau protein from mouse brain.";
RL Science 239:285-288(1988).
RN [4]
RP PARTIAL NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING
RP (ISOFORM TAU-B).
RC STRAIN=ICR; TISSUE=Brain;
RX PubMed=7877441; DOI=10.1016/0169-328x(94)90191-0;
RA Sawa A., Oyama F., Matsushita M., Ihara Y.;
RT "Molecular diversity at the carboxyl terminus of human and rat tau.";
RL Brain Res. Mol. Brain Res. 27:111-117(1994).
RN [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM TAU-D).
RC TISSUE=Eye;
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 [7]
RP PROTEIN SEQUENCE OF 504-513; 535-546; 591-609 AND 646-661, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=OF1; TISSUE=Hippocampus;
RA Lubec G., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [8]
RP CHARACTERIZATION.
RX PubMed=8402267;
RA Couchie D., Gache Y., Mavilia C., Guilleminot J., Bridoux A.-M.,
RA Nivez M.-P., Nunez J.;
RT "High molecular weight tau proteins and acquisition of neuronal polarity in
RT peripheral nervous system.";
RL C. R. Acad. Sci. III, Sci. Vie 316:404-409(1993).
RN [9]
RP PHOSPHORYLATION AT TYR-18 BY FYN.
RX PubMed=14999081; DOI=10.1523/jneurosci.4162-03.2004;
RA Lee G., Thangavel R., Sharma V.M., Litersky J.M., Bhaskar K., Fang S.M.,
RA Do L.H., Andreadis A., Van Hoesen G., Ksiezak-Reding H.;
RT "Phosphorylation of tau by fyn: implications for Alzheimer's disease.";
RL J. Neurosci. 24:2304-2312(2004).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-701, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic brain;
RX PubMed=15345747; DOI=10.1074/mcp.m400085-mcp200;
RA Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT "Phosphoproteomic analysis of the developing mouse brain.";
RL Mol. Cell. Proteomics 3:1093-1101(2004).
RN [11]
RP INTERACTION WITH PSMC2.
RX PubMed=15953362; DOI=10.1111/j.1471-4159.2005.03181.x;
RA Babu J.R., Geetha T., Wooten M.W.;
RT "Sequestosome 1/p62 shuttles polyubiquitinated tau for proteasomal
RT degradation.";
RL J. Neurochem. 94:192-203(2005).
RN [12]
RP PHOSPHORYLATION AT SER-554.
RX PubMed=15705853; DOI=10.1126/science.1107403;
RA Kishi M., Pan Y.A., Crump J.G., Sanes J.R.;
RT "Mammalian SAD kinases are required for neuronal polarization.";
RL Science 307:929-932(2005).
RN [13]
RP IDENTIFICATION BY 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 [14]
RP PHOSPHORYLATION AT SER-554.
RX PubMed=17482548; DOI=10.1016/j.cell.2007.03.025;
RA Barnes A.P., Lilley B.N., Pan Y.A., Plummer L.J., Powell A.W., Raines A.N.,
RA Sanes J.R., Polleux F.;
RT "LKB1 and SAD kinases define a pathway required for the polarization of
RT cortical neurons.";
RL Cell 129:549-563(2007).
RN [15]
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 [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-494; SER-688; SER-692 AND
RP SER-696, AND IDENTIFICATION BY 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 [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-188; THR-468; SER-470;
RP TYR-489; SER-490; SER-491; SER-494; THR-497; THR-523; TYR-686; SER-688;
RP SER-692; THR-695; SER-696; SER-701; SER-708 AND SER-714, AND IDENTIFICATION
RP BY MASS 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 [18]
RP ACETYLATION AT LYS-455; LYS-517; LYS-551; LYS-573; LYS-582; LYS-590;
RP LYS-603; LYS-609; LYS-613; LYS-623; LYS-635; LYS-639; LYS-661 AND LYS-677,
RP GLYCOSYLATION AT SER-692, METHYLATION AT ARG-115; ARG-447; LYS-455;
RP LYS-551; LYS-603 AND ARG-641, PHOSPHORYLATION AT THR-58; THR-100; SER-451;
RP THR-461; THR-467; SER-470; THR-473; SER-477; SER-483; SER-487; SER-490;
RP SER-491; SER-494; THR-497; THR-504; SER-506; THR-509; THR-523; SER-527;
RP SER-529; SER-531; SER-554; SER-648; TYR-686; SER-688; SER-692 AND SER-708,
RP AND UBIQUITINATION AT LYS-33; LYS-551; LYS-559; LYS-573; LYS-590; LYS-603;
RP LYS-609; LYS-613; LYS-623; LYS-635; LYS-639; LYS-645; LYS-661; LYS-667 AND
RP LYS-677.
RX PubMed=26192747; DOI=10.1038/nn.4067;
RA Morris M., Knudsen G.M., Maeda S., Trinidad J.C., Ioanoviciu A.,
RA Burlingame A.L., Mucke L.;
RT "Tau post-translational modifications in wild-type and human amyloid
RT precursor protein transgenic mice.";
RL Nat. Neurosci. 18:1183-1189(2015).
CC -!- FUNCTION: Promotes microtubule assembly and stability, and might be
CC involved in the establishment and maintenance of neuronal polarity. The
CC C-terminus binds axonal microtubules while the N-terminus binds neural
CC plasma membrane components, suggesting that tau functions as a linker
CC protein between both. Axonal polarity is predetermined by tau
CC localization (in the neuronal cell) in the domain of the cell body
CC defined by the centrosome. The short isoforms allow plasticity of the
CC cytoskeleton whereas the longer isoforms may preferentially play a role
CC in its stabilization.
CC -!- SUBUNIT: Interacts with MARK1, MARK2, MARK3 AND MARK4 (By similarity).
CC Interacts with SQSTM1 when polyubiquitinated (PubMed:15953362).
CC Interacts with PSMC2 through SQSTM1 (PubMed:15953362). Interacts with
CC FKBP4 (By similarity). Binds to CSNK1D (By similarity). Interacts with
CC SGK1 (By similarity). Interacts with EPM2A; the interaction
CC dephosphorylates MAPT at Ser-369 (By similarity). Interacts with PIN1
CC (By similarity). Interacts with LRRK2 (By similarity). Interacts with
CC LRP1, leading to endocytosis; this interaction is reduced in the
CC presence of LRPAP1/RAP (By similarity). {ECO:0000250|UniProtKB:P10636,
CC ECO:0000250|UniProtKB:P19332, ECO:0000269|PubMed:15953362}.
CC -!- INTERACTION:
CC P10637; O08539: Bin1; NbExp=2; IntAct=EBI-774043, EBI-775152;
CC P10637; Q61644: Pacsin1; NbExp=5; IntAct=EBI-774043, EBI-2255561;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:P10636}. Cell membrane
CC {ECO:0000250|UniProtKB:P10636}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P10636}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:P10636}. Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:P10636}. Cell projection, axon
CC {ECO:0000250|UniProtKB:P10636}. Cell projection, dendrite
CC {ECO:0000250|UniProtKB:P10636}. Secreted
CC {ECO:0000250|UniProtKB:P10636}. Note=Mostly found in the axons of
CC neurons, in the cytosol and in association with plasma membrane
CC components. Can be secreted; the secretion is dependent on protein
CC unfolding and facilitated by the cargo receptor TMED10; it results in
CC protein translocation from the cytoplasm into the ERGIC (endoplasmic
CC reticulum-Golgi intermediate compartment) followed by vesicle entry and
CC secretion. {ECO:0000250|UniProtKB:P10636}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Comment=Additional isoforms seem to exist. Isoforms differ from each
CC other by the presence or absence of up to 5 of the 14 exons. One of
CC these optional exons contains the additional tau/MAP repeat. Two
CC different C-termini are obtained either by the retention or the
CC splicing of intron 13/14.;
CC Name=PNS-Tau;
CC IsoId=P10637-1; Sequence=Displayed;
CC Name=Tau-A;
CC IsoId=P10637-2; Sequence=VSP_003187, VSP_003188;
CC Name=Tau-B;
CC IsoId=P10637-3; Sequence=VSP_003185, VSP_003187, VSP_003188,
CC VSP_003189, VSP_003190;
CC Name=Tau-C;
CC IsoId=P10637-4; Sequence=VSP_003185, VSP_003187, VSP_003188,
CC VSP_003189;
CC Name=Tau-D;
CC IsoId=P10637-5; Sequence=VSP_003185, VSP_003187, VSP_003188;
CC Name=Tau-E;
CC IsoId=P10637-6; Sequence=VSP_003185, VSP_003186, VSP_003187,
CC VSP_003188;
CC -!- TISSUE SPECIFICITY: Expressed in neurons and at a lower level in the
CC liver and kidney. Isoform PNS-tau is expressed in the peripheral
CC nervous system while the others are expressed in the central nervous
CC system.
CC -!- DEVELOPMENTAL STAGE: Shorter forms or low molecular weight tau (lMW-
CC tau) are generally expressed at early development stages and longer
CC forms or high molecular weight tau (hMW-tau) in the adult brain.
CC -!- DOMAIN: The tau/MAP repeat binds to tubulin. Type I isoforms contain 3
CC repeats while type II isoforms contain 4 repeats.
CC -!- PTM: Polyubiquitinated. Requires functional TRAF6 and may provoke
CC SQSTM1-dependent degradation by the proteasome (By similarity).
CC {ECO:0000250}.
CC -!- PTM: Phosphorylation at various serine and threonine residues in S-P or
CC T-P motifs by proline-directed protein kinases (PDPK1, CDK1, CDK5,
CC GSK3, MAPK) (a few sites per protein in interphase, more in mitosis),
CC and at serine residues in K-X-G-S motifs by MAP/microtubule affinity-
CC regulating kinase (MARK1, MARK2, MARK3, MARK4), causing detachment from
CC microtubules, and their disassembly (By similarity). Phosphorylated by
CC PHK. Dephosphorylation at several serine and threonine residues by the
CC serine/threonine phosphatase PPP5C. Phosphorylation at Ser-554 by BRSK1
CC and BRSK2 in neurons affects ability to bind microtubules and plays a
CC role in neuron polarization. Phosphorylation at Ser-188 by SGK1
CC mediates microtubule depolymerization and neurite formation in
CC hippocampal neurons (By similarity). {ECO:0000250,
CC ECO:0000250|UniProtKB:P10636}.
CC -!- DISEASE: Note=May be involved in the pathogenesis of cytoplasmic
CC inclusions (as Mallory bodies) in livers of mice chronically
CC intoxicated with Griseofulvin or DDC (3,5-diethoxycarbonyl-2,4-
CC dihydrocollidine), a model for human alcoholic hepatitis. Alteration of
CC Tau (abnormal phosphorylation and cross-linking) could contribute to
CC Mallory bodies formation and disturbance of microtubule function in
CC alcoholic liver disease.
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DR EMBL; U12914; AAA58343.1; -; mRNA.
DR EMBL; U12915; AAA58344.1; -; mRNA.
DR EMBL; U12916; AAA58345.1; -; mRNA.
DR EMBL; Z12133; CAA78121.1; -; mRNA.
DR EMBL; M93266; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; M18775; AAA40165.1; -; mRNA.
DR EMBL; M18776; AAA40166.1; -; mRNA.
DR EMBL; D30627; BAA18878.1; -; Genomic_DNA.
DR EMBL; AL593843; CAM14797.1; -; Genomic_DNA.
DR EMBL; BC014748; AAH14748.1; -; mRNA.
DR CCDS; CCDS25527.1; -. [P10637-2]
DR CCDS; CCDS25528.1; -. [P10637-5]
DR PIR; A28820; A28820.
DR PIR; A45301; A45301.
DR PIR; B28820; B28820.
DR RefSeq; NP_001033698.1; NM_001038609.2. [P10637-2]
DR RefSeq; NP_001272383.1; NM_001285454.1. [P10637-3]
DR RefSeq; NP_001272384.1; NM_001285455.1. [P10637-6]
DR RefSeq; NP_001272385.1; NM_001285456.1. [P10637-4]
DR RefSeq; NP_034968.3; NM_010838.4. [P10637-5]
DR PDB; 6H0E; X-ray; 1.95 A; G/I/J/K=698-721.
DR PDBsum; 6H0E; -.
DR AlphaFoldDB; P10637; -.
DR BMRB; P10637; -.
DR SMR; P10637; -.
DR BioGRID; 201589; 319.
DR IntAct; P10637; 7.
DR MINT; P10637; -.
DR ChEMBL; CHEMBL4296281; -.
DR GlyGen; P10637; 1 site.
DR iPTMnet; P10637; -.
DR PhosphoSitePlus; P10637; -.
DR jPOST; P10637; -.
DR MaxQB; P10637; -.
DR PaxDb; P10637; -.
DR PeptideAtlas; P10637; -.
DR PRIDE; P10637; -.
DR ProteomicsDB; 259354; -. [P10637-1]
DR ProteomicsDB; 259355; -. [P10637-2]
DR ProteomicsDB; 259356; -. [P10637-3]
DR ProteomicsDB; 259357; -. [P10637-4]
DR ProteomicsDB; 259358; -. [P10637-5]
DR ProteomicsDB; 259359; -. [P10637-6]
DR Antibodypedia; 3124; 5572 antibodies from 53 providers.
DR DNASU; 17762; -.
DR Ensembl; ENSMUST00000100347; ENSMUSP00000097919; ENSMUSG00000018411. [P10637-2]
DR Ensembl; ENSMUST00000106992; ENSMUSP00000102605; ENSMUSG00000018411. [P10637-5]
DR GeneID; 17762; -.
DR KEGG; mmu:17762; -.
DR UCSC; uc007lwf.2; mouse. [P10637-3]
DR UCSC; uc007lwg.2; mouse. [P10637-2]
DR UCSC; uc007lwi.2; mouse. [P10637-4]
DR UCSC; uc011yga.2; mouse. [P10637-6]
DR CTD; 4137; -.
DR MGI; MGI:97180; Mapt.
DR VEuPathDB; HostDB:ENSMUSG00000018411; -.
DR eggNOG; KOG2418; Eukaryota.
DR GeneTree; ENSGT00940000155494; -.
DR HOGENOM; CLU_021741_3_1_1; -.
DR InParanoid; P10637; -.
DR OrthoDB; 716848at2759; -.
DR TreeFam; TF316358; -.
DR Reactome; R-MMU-264870; Caspase-mediated cleavage of cytoskeletal proteins.
DR BioGRID-ORCS; 17762; 4 hits in 76 CRISPR screens.
DR ChiTaRS; Mapt; mouse.
DR PRO; PR:P10637; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; P10637; protein.
DR Bgee; ENSMUSG00000018411; Expressed in embryonic brain and 228 other tissues.
DR ExpressionAtlas; P10637; baseline and differential.
DR Genevisible; P10637; MM.
DR GO; GO:0030673; C:axolemma; ISO:MGI.
DR GO; GO:0030424; C:axon; IDA:MGI.
DR GO; GO:0044295; C:axonal growth cone; ISO:MGI.
DR GO; GO:0005930; C:axoneme; IDA:MGI.
DR GO; GO:0044297; C:cell body; IDA:ARUK-UCL.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0036464; C:cytoplasmic ribonucleoprotein granule; ISO:MGI.
DR GO; GO:0009898; C:cytoplasmic side of plasma membrane; ISO:MGI.
DR GO; GO:0005829; C:cytosol; IDA:ParkinsonsUK-UCL.
DR GO; GO:0030425; C:dendrite; ISS:UniProtKB.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0097386; C:glial cell projection; IDA:ARUK-UCL.
DR GO; GO:0030426; C:growth cone; ISS:UniProtKB.
DR GO; GO:0044304; C:main axon; ISO:MGI.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:0045121; C:membrane raft; IDA:ARUK-UCL.
DR GO; GO:0005874; C:microtubule; ISO:MGI.
DR GO; GO:0015630; C:microtubule cytoskeleton; IDA:MGI.
DR GO; GO:0097418; C:neurofibrillary tangle; ISO:MGI.
DR GO; GO:0043005; C:neuron projection; ISO:MGI.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0034399; C:nuclear periphery; ISO:MGI.
DR GO; GO:0016607; C:nuclear speck; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:ParkinsonsUK-UCL.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0014069; C:postsynaptic density; IDA:MGI.
DR GO; GO:0036477; C:somatodendritic compartment; ISO:MGI.
DR GO; GO:0045298; C:tubulin complex; ISS:UniProtKB.
DR GO; GO:0034185; F:apolipoprotein binding; ISO:MGI.
DR GO; GO:0051087; F:chaperone binding; ISO:MGI.
DR GO; GO:0003677; F:DNA binding; IDA:ParkinsonsUK-UCL.
DR GO; GO:0019899; F:enzyme binding; IPI:ARUK-UCL.
DR GO; GO:0031072; F:heat shock protein binding; ISO:MGI.
DR GO; GO:0051879; F:Hsp90 protein binding; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0071813; F:lipoprotein particle binding; ISO:MGI.
DR GO; GO:0008017; F:microtubule binding; IDA:MGI.
DR GO; GO:0099609; F:microtubule lateral binding; ISO:MGI.
DR GO; GO:0019901; F:protein kinase binding; IPI:ARUK-UCL.
DR GO; GO:0051721; F:protein phosphatase 2A binding; ISO:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0017124; F:SH3 domain binding; ISO:MGI.
DR GO; GO:0007628; P:adult walking behavior; IGI:MGI.
DR GO; GO:1990000; P:amyloid fibril formation; ISO:MGI.
DR GO; GO:0006915; P:apoptotic process; ISO:MGI.
DR GO; GO:0008088; P:axo-dendritic transport; IGI:MGI.
DR GO; GO:0048675; P:axon extension; IMP:MGI.
DR GO; GO:0007409; P:axonogenesis; IGI:MGI.
DR GO; GO:0048312; P:intracellular distribution of mitochondria; ISO:MGI.
DR GO; GO:0046907; P:intracellular transport; IMP:MGI.
DR GO; GO:0008631; P:intrinsic apoptotic signaling pathway in response to oxidative stress; ISO:MGI.
DR GO; GO:0007611; P:learning or memory; ISO:MGI.
DR GO; GO:0007613; P:memory; ISO:MGI.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; IMP:MGI.
DR GO; GO:0046785; P:microtubule polymerization; ISO:MGI.
DR GO; GO:0047497; P:mitochondrion transport along microtubule; IMP:MGI.
DR GO; GO:0051028; P:mRNA transport; ISO:MGI.
DR GO; GO:1903748; P:negative regulation of establishment of protein localization to mitochondrion; ISO:MGI.
DR GO; GO:0010629; P:negative regulation of gene expression; ISO:MGI.
DR GO; GO:0032387; P:negative regulation of intracellular transport; IMP:MGI.
DR GO; GO:0033673; P:negative regulation of kinase activity; ISO:MGI.
DR GO; GO:0090258; P:negative regulation of mitochondrial fission; ISO:MGI.
DR GO; GO:0010917; P:negative regulation of mitochondrial membrane potential; ISO:MGI.
DR GO; GO:1904428; P:negative regulation of tubulin deacetylation; IGI:ARUK-UCL.
DR GO; GO:0001764; P:neuron migration; IMP:MGI.
DR GO; GO:0031175; P:neuron projection development; IBA:GO_Central.
DR GO; GO:0045773; P:positive regulation of axon extension; ISS:UniProtKB.
DR GO; GO:1900454; P:positive regulation of long-term synaptic depression; ISO:MGI.
DR GO; GO:0031116; P:positive regulation of microtubule polymerization; ISS:UniProtKB.
DR GO; GO:1901216; P:positive regulation of neuron death; ISO:MGI.
DR GO; GO:0010976; P:positive regulation of neuron projection development; ISO:MGI.
DR GO; GO:1903829; P:positive regulation of protein localization; ISO:MGI.
DR GO; GO:1902474; P:positive regulation of protein localization to synapse; ISO:MGI.
DR GO; GO:0032930; P:positive regulation of superoxide anion generation; ISO:MGI.
DR GO; GO:0051260; P:protein homooligomerization; ISO:MGI.
DR GO; GO:0051258; P:protein polymerization; ISO:MGI.
DR GO; GO:0010506; P:regulation of autophagy; ISO:MGI.
DR GO; GO:0050848; P:regulation of calcium-mediated signaling; ISO:MGI.
DR GO; GO:1900034; P:regulation of cellular response to heat; IMP:ParkinsonsUK-UCL.
DR GO; GO:0070507; P:regulation of microtubule cytoskeleton organization; ISO:MGI.
DR GO; GO:0031110; P:regulation of microtubule polymerization or depolymerization; ISO:MGI.
DR GO; GO:0060632; P:regulation of microtubule-based movement; IDA:MGI.
DR GO; GO:2001020; P:regulation of response to DNA damage stimulus; IMP:ParkinsonsUK-UCL.
DR GO; GO:0010288; P:response to lead ion; ISO:MGI.
DR GO; GO:0007584; P:response to nutrient; ISO:MGI.
DR GO; GO:0010033; P:response to organic substance; ISO:MGI.
DR GO; GO:0097435; P:supramolecular fiber organization; ISO:MGI.
DR GO; GO:0007416; P:synapse assembly; ISO:MGI.
DR GO; GO:0050808; P:synapse organization; ISO:MGI.
DR InterPro; IPR001084; MAP_tubulin-bd_rpt.
DR InterPro; IPR002955; Tau.
DR Pfam; PF00418; Tubulin-binding; 4.
DR PRINTS; PR01261; TAUPROTEIN.
DR PROSITE; PS00229; TAU_MAP_1; 4.
DR PROSITE; PS51491; TAU_MAP_2; 4.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cell membrane;
KW Cell projection; Cytoplasm; Cytoskeleton; Direct protein sequencing;
KW Disulfide bond; Glycoprotein; Isopeptide bond; Membrane; Methylation;
KW Microtubule; Phosphoprotein; Reference proteome; Repeat; Secreted;
KW Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P10636"
FT CHAIN 2..733
FT /note="Microtubule-associated protein tau"
FT /id="PRO_0000072742"
FT REPEAT 536..566
FT /note="Tau/MAP 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00824"
FT REPEAT 567..597
FT /note="Tau/MAP 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00824"
FT REPEAT 598..628
FT /note="Tau/MAP 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00824"
FT REPEAT 629..660
FT /note="Tau/MAP 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00824"
FT REGION 1..548
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 690..709
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..32
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 124..139
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 201..218
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 275..291
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 351..369
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 385..399
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 410..426
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 451..467
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 487..503
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 694..709
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P10636"
FT MOD_RES 18
FT /note="Phosphotyrosine; by FYN"
FT /evidence="ECO:0000269|PubMed:14999081"
FT MOD_RES 35
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19332"
FT MOD_RES 50
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19332"
FT MOD_RES 58
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:26192747"
FT MOD_RES 60
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P19332"
FT MOD_RES 100
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:26192747"
FT MOD_RES 115
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000269|PubMed:26192747"
FT MOD_RES 188
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 369
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10636"
FT MOD_RES 445
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P10636"
FT MOD_RES 447
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000269|PubMed:26192747"
FT MOD_RES 451
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:26192747"
FT MOD_RES 455
FT /note="N6,N6-dimethyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:26192747"
FT MOD_RES 455
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:26192747"
FT MOD_RES 461
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:26192747"
FT MOD_RES 467
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:26192747"
FT MOD_RES 468
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 470
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:26192747,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 473
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:26192747"
FT MOD_RES 477
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:26192747"
FT MOD_RES 483
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:26192747"
FT MOD_RES 487
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:26192747"
FT MOD_RES 489
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 490
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:26192747,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 491
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:26192747,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 494
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:26192747,
FT ECO:0007744|PubMed:17242355, ECO:0007744|PubMed:21183079"
FT MOD_RES 497
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:26192747,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 504
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:26192747"
FT MOD_RES 506
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:26192747"
FT MOD_RES 509
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:26192747"
FT MOD_RES 517
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:26192747"
FT MOD_RES 523
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:26192747,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 527
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:26192747"
FT MOD_RES 529
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:26192747"
FT MOD_RES 531
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:26192747"
FT MOD_RES 551
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:26192747"
FT MOD_RES 551
FT /note="N6-methyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:26192747"
FT MOD_RES 554
FT /note="Phosphoserine; by MARK1, BRSK1, BRSK2 and PHK"
FT /evidence="ECO:0000269|PubMed:15705853,
FT ECO:0000269|PubMed:17482548, ECO:0000269|PubMed:26192747"
FT MOD_RES 573
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:26192747"
FT MOD_RES 577
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10636"
FT MOD_RES 581
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10636"
FT MOD_RES 582
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:26192747"
FT MOD_RES 585
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10636"
FT MOD_RES 590
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:26192747"
FT MOD_RES 597
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10636"
FT MOD_RES 603
FT /note="N6,N6-dimethyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:26192747"
FT MOD_RES 603
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:26192747"
FT MOD_RES 609
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:26192747"
FT MOD_RES 613
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:26192747"
FT MOD_RES 616
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10636"
FT MOD_RES 623
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:26192747"
FT MOD_RES 635
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:26192747"
FT MOD_RES 639
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:26192747"
FT MOD_RES 641
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000269|PubMed:26192747"
FT MOD_RES 644
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10636"
FT MOD_RES 648
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:26192747"
FT MOD_RES 661
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:26192747"
FT MOD_RES 677
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:26192747"
FT MOD_RES 686
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:26192747,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 688
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:26192747,
FT ECO:0007744|PubMed:17242355, ECO:0007744|PubMed:21183079"
FT MOD_RES 692
FT /note="Phosphoserine; alternate"
FT /evidence="ECO:0000269|PubMed:26192747,
FT ECO:0007744|PubMed:17242355, ECO:0007744|PubMed:21183079"
FT MOD_RES 695
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 696
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 701
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15345747,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 708
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:26192747,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 714
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 719
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P10636"
FT CARBOHYD 692
FT /note="O-linked (GlcNAc...) serine; alternate"
FT /evidence="ECO:0000269|PubMed:26192747"
FT DISULFID 583..614
FT /evidence="ECO:0000250"
FT CROSSLNK 33
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:26192747"
FT CROSSLNK 546
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P10636"
FT CROSSLNK 551
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin); alternate"
FT /evidence="ECO:0000269|PubMed:26192747"
FT CROSSLNK 559
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:26192747"
FT CROSSLNK 573
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin); alternate"
FT /evidence="ECO:0000269|PubMed:26192747"
FT CROSSLNK 590
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin); alternate"
FT /evidence="ECO:0000269|PubMed:26192747"
FT CROSSLNK 603
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin); alternate"
FT /evidence="ECO:0000269|PubMed:26192747"
FT CROSSLNK 609
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin); alternate"
FT /evidence="ECO:0000269|PubMed:26192747"
FT CROSSLNK 613
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin); alternate"
FT /evidence="ECO:0000269|PubMed:26192747"
FT CROSSLNK 623
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin); alternate"
FT /evidence="ECO:0000269|PubMed:26192747"
FT CROSSLNK 635
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin); alternate"
FT /evidence="ECO:0000269|PubMed:26192747"
FT CROSSLNK 639
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin); alternate"
FT /evidence="ECO:0000269|PubMed:26192747"
FT CROSSLNK 645
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:26192747"
FT CROSSLNK 661
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin); alternate"
FT /evidence="ECO:0000269|PubMed:26192747"
FT CROSSLNK 667
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:26192747"
FT CROSSLNK 677
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin); alternate"
FT /evidence="ECO:0000269|PubMed:26192747"
FT VAR_SEQ 34..91
FT /note="Missing (in isoform Tau-B, isoform Tau-C, isoform
FT Tau-D and isoform Tau-E)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:3122323, ECO:0000303|PubMed:7927211"
FT /id="VSP_003185"
FT VAR_SEQ 92..113
FT /note="Missing (in isoform Tau-E)"
FT /evidence="ECO:0000303|PubMed:7927211"
FT /id="VSP_003186"
FT VAR_SEQ 114..350
FT /note="Missing (in isoform Tau-A, isoform Tau-B, isoform
FT Tau-C, isoform Tau-D and isoform Tau-E)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:3122323, ECO:0000303|PubMed:7927211"
FT /id="VSP_003187"
FT VAR_SEQ 368..433
FT /note="Missing (in isoform Tau-A, isoform Tau-B, isoform
FT Tau-C, isoform Tau-D and isoform Tau-E)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:3122323, ECO:0000303|PubMed:7927211"
FT /id="VSP_003188"
FT VAR_SEQ 567..597
FT /note="Missing (in isoform Tau-B and isoform Tau-C)"
FT /evidence="ECO:0000303|PubMed:3122323"
FT /id="VSP_003189"
FT VAR_SEQ 733
FT /note="L -> KAALLSSQVWNYSHDLATITDLGL (in isoform Tau-B)"
FT /evidence="ECO:0000303|PubMed:3122323"
FT /id="VSP_003190"
FT CONFLICT 3
FT /note="D -> N (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 9
FT /note="D -> N (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 405
FT /note="S -> C (in Ref. 5; CAM14797)"
FT /evidence="ECO:0000305"
FT CONFLICT 528
FT /note="P -> T (in Ref. 2; CAA78121)"
FT /evidence="ECO:0000305"
FT CONFLICT 549
FT /note="R -> G (in Ref. 6; AAH14748)"
FT /evidence="ECO:0000305"
FT CONFLICT 672
FT /note="E -> Q (in Ref. 1)"
FT /evidence="ECO:0000305"
FT HELIX 714..716
FT /evidence="ECO:0007829|PDB:6H0E"
SQ SEQUENCE 733 AA; 76243 MW; 80C0D50AC5F64E6F CRC64;
MADPRQEFDT MEDHAGDYTL LQDQEGDMDH GLKESPPQPP ADDGAEEPGS ETSDAKSTPT
AEDVTAPLVD ERAPDKQAAA QPHTEIPEGI TAEEAGIGDT PNQEDQAAGH VTQGRREGQA
PDLGTSDWTR QQVSSMSGAP LLPQGLREAT CQPSGTRPED IEKSHPASEL LRRGPPQKEG
WGQDRLGSEE EVDEDLTVDE SSQDSPPSQA SLTPGRAAPQ AGSGSVCGET ASVPGLPTEG
SVPLPADFFS KVSAETQASQ PEGPGTGPME EGHEAAPEFT FHVEIKASTP KEQDLEGATV
VGVPGEEQKA QTQGPSVGKG TKEASLQEPP GKQPAAGLPG RPVSRVPQLK ARVASKDRTG
NDEKKAKTST PSCAKAPSHR PCLSPTRPTL GSSDPLIKPS SPAVSPEPAT SPKHVSSVTP
RNGSPGTKQM KLKGADGKTG AKIATPRGAA SPAQKGTSNA TRIPAKTTPS PKTPPGSGEP
PKSGERSGYS SPGSPGTPGS RSRTPSLPTP PTREPKKVAV VRTPPKSPSA SKSRLQTAPV
PMPDLKNVRS KIGSTENLKH QPGGGKVQII NKKLDLSNVQ SKCGSKDNIK HVPGGGSVQI
VYKPVDLSKV TSKCGSLGNI HHKPGGGQVE VKSEKLDFKD RVQSKIGSLD NITHVPGGGN
KKIETHKLTF RENAKAKTDH GAEIVYKSPV VSGDTSPRHL SNVSSTGSID MVDSPQLATL
ADEVSASLAK QGL
