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 04-NOV-2026, entry version 245. 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, RC Pancreas, Spleen, and Testis; RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001; RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R., RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.; RT "A tissue-specific atlas of mouse protein phosphorylation and expression."; RL Cell 143:1174-1189(2010). RN [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 P10637; P52479: Usp10; NbExp=3; IntAct=EBI-774043, EBI-8327299; 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. 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; 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_001038609.3. [P10637-2] DR RefSeq; NP_001272383.1; NM_001285454.2. [P10637-3] DR RefSeq; NP_001272384.1; NM_001285455.2. [P10637-6] DR RefSeq; NP_001272385.1; NM_001285456.2. [P10637-4] DR RefSeq; NP_001390940.1; NM_001404011.1. [P10637-5] DR RefSeq; NP_001390941.1; NM_001404012.1. [P10637-4] DR RefSeq; NP_001390943.1; NM_001404014.1. [P10637-4] DR RefSeq; NP_001390944.1; NM_001404015.1. [P10637-4] DR RefSeq; NP_001390945.1; NM_001404016.1. [P10637-4] DR RefSeq; NP_034968.3; NM_010838.5. [P10637-5] DR PDB; 29OS; EM; 3.60 A; A/B/C/D/E/F=1-733. DR PDB; 29OU; EM; 3.40 A; A/B/C=1-733. DR PDB; 6H0E; X-ray; 1.95 A; G/I/J/K=698-721. DR PDB; 8Q96; EM; 3.09 A; A/D/G/J=566-621. DR BMRB; P10637; -. DR SMR; P10637; -. DR BioGRID; 201589; 335. DR CORUM; P10637; -. DR IntAct; P10637; 7. DR ChEMBL; CHEMBL4296281; -. DR GlyCosmos; P10637; 8 sites, 3 glycans. DR GlyGen; P10637; 9 sites, 2 N-linked glycans (2 sites), 1 O-linked glycan (4 sites). DR iPTMnet; P10637; -. DR PhosphoSitePlus; P10637; -. DR SwissPalm; P10637; -. DR PeptideAtlas; 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 jPOST; P10637; -. DR DNASU; 17762; -. DR Ensembl; ENSMPUT00000008186; ENSMPUP00000008060; ENSMPUG00000008117. DR Ensembl; ENSMUST00000100347.11; ENSMUSP00000097919.5; ENSMUSG00000018411.18. [P10637-2] DR Ensembl; ENSMUST00000106992.10; ENSMUSP00000102605.4; ENSMUSG00000018411.18. [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 VEuPathDB; HostDB:ENSMUSG00000018411; -. DR AGR; MGI:97180; -. DR MGI; MGI:97180; Mapt. DR eggNOG; KOG2418; Eukaryota. DR GeneTree; ENSGT00940000155494; -. DR HOGENOM; CLU_021741_3_1_1; -. DR InParanoid; P10637; -. DR Reactome; R-MMU-264870; Caspase-mediated cleavage of cytoskeletal proteins. DR Reactome; R-MMU-9833482; PKR-mediated signaling. DR PRO; PR:P10637; -. DR Bgee; ENSMUSG00000018411; Expressed in embryonic brain and 231 other cell types or tissues. DR ExpressionAtlas; P10637; baseline and differential. DR InterPro; IPR027324; MAP2/MAP4/Tau. DR InterPro; IPR001084; MAP_tubulin-bd_rpt. DR InterPro; IPR002955; Tau. DR PANTHER; PTHR11501; MICROTUBULE-ASSOCIATED PROTEIN; 1. DR PANTHER; PTHR11501:SF14; MICROTUBULE-ASSOCIATED PROTEIN TAU; 1. DR Pfam; PF00418; Tubulin-binding; 4. DR PRINTS; PR01261; TAUPROTEIN. DR PROSITE; PS00229; TAU_MAP_1; 4. DR PROSITE; PS51491; TAU_MAP_2; 4. DR GO; GO:0030673; C:axolemma; ISO:GO_Central. DR GO; GO:0030424; C:axon; IDA:MGI. DR GO; GO:0044295; C:axonal growth cone; ISO:GO_Central. 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:GO_Central. DR GO; GO:0009898; C:cytoplasmic side of plasma membrane; ISO:GO_Central. DR GO; GO:0005829; C:cytosol; IDA:ParkinsonsUK-UCL. DR GO; GO:0030425; C:dendrite; ISS:UniProtKB. DR GO; GO:0005576; C:extracellular region; ISS:UniProtKB. 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:GO_Central. DR GO; GO:0045121; C:membrane raft; IDA:ARUK-UCL. DR GO; GO:0005874; C:microtubule; ISO:GO_Central. DR GO; GO:0015630; C:microtubule cytoskeleton; IDA:MGI. DR GO; GO:0097418; C:neurofibrillary tangle; ISO:GO_Central. DR GO; GO:0043025; C:neuronal cell body; ISO:GO_Central. DR GO; GO:0034399; C:nuclear periphery; ISO:GO_Central. 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:GO_Central. DR GO; GO:0045298; C:tubulin complex; ISS:UniProtKB. DR GO; GO:0034185; F:apolipoprotein binding; ISO:GO_Central. DR GO; GO:0003677; F:DNA binding; IDA:ParkinsonsUK-UCL. DR GO; GO:0019899; F:enzyme binding; IPI:ARUK-UCL. DR GO; GO:0004857; F:enzyme inhibitor activity; IDA:ARUK-UCL. DR GO; GO:0031072; F:heat shock protein binding; ISO:GO_Central. DR GO; GO:0051879; F:Hsp90 protein binding; ISO:GO_Central. DR GO; GO:0042802; F:identical protein binding; ISO:GO_Central. DR GO; GO:0071813; F:lipoprotein particle binding; ISO:GO_Central. DR GO; GO:0008017; F:microtubule binding; IDA:MGI. DR GO; GO:0099609; F:microtubule lateral binding; ISO:GO_Central. DR GO; GO:0140778; F:microtubule stabilizing activity; IBA:GO_Central. DR GO; GO:0019901; F:protein kinase binding; IPI:ARUK-UCL. DR GO; GO:0051721; F:protein phosphatase 2A binding; ISO:GO_Central. DR GO; GO:0044877; F:protein-containing complex binding; ISO:GO_Central. DR GO; GO:0051087; F:protein-folding chaperone binding; ISO:GO_Central. DR GO; GO:0017124; F:SH3 domain binding; ISO:GO_Central. DR GO; GO:0007628; P:adult walking behavior; IGI:MGI. DR GO; GO:1990000; P:amyloid fibril formation; ISO:GO_Central. 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:0071277; P:cellular response to calcium ion; ISO:GO_Central. DR GO; GO:0006974; P:DNA damage response; IMP:ParkinsonsUK-UCL. DR GO; GO:0048312; P:intracellular distribution of mitochondria; ISO:GO_Central. DR GO; GO:0008631; P:intrinsic apoptotic signaling pathway in response to oxidative stress; ISO:GO_Central. DR GO; GO:0007611; P:learning or memory; ISO:GO_Central. DR GO; GO:0007613; P:memory; ISO:GO_Central. DR GO; GO:0000226; P:microtubule cytoskeleton organization; IMP:MGI. DR GO; GO:0046785; P:microtubule polymerization; ISO:GO_Central. DR GO; GO:0047497; P:mitochondrion transport along microtubule; IMP:MGI. DR GO; GO:0051028; P:mRNA transport; ISO:GO_Central. DR GO; GO:0010629; P:negative regulation of gene expression; ISO:GO_Central. DR GO; GO:0032387; P:negative regulation of intracellular transport; IMP:MGI. DR GO; GO:0090258; P:negative regulation of mitochondrial fission; ISO:GO_Central. DR GO; GO:0010917; P:negative regulation of mitochondrial membrane potential; ISO:GO_Central. DR GO; GO:1903748; P:negative regulation of protein localization to mitochondrion; ISO:GO_Central. DR GO; GO:1904428; P:negative regulation of tubulin deacetylation; ISO:GO_Central. 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:GO_Central. DR GO; GO:1905322; P:positive regulation of mesenchymal stem cell migration; ISO:GO_Central. DR GO; GO:0031116; P:positive regulation of microtubule polymerization; ISS:UniProtKB. DR GO; GO:0010918; P:positive regulation of mitochondrial membrane potential; ISO:GO_Central. DR GO; GO:0010976; P:positive regulation of neuron projection development; ISO:GO_Central. DR GO; GO:1903829; P:positive regulation of protein localization; ISO:GO_Central. DR GO; GO:1902474; P:positive regulation of protein localization to synapse; ISO:GO_Central. DR GO; GO:0032930; P:positive regulation of superoxide anion generation; ISO:GO_Central. DR GO; GO:0051260; P:protein homooligomerization; ISO:GO_Central. DR GO; GO:0051258; P:protein polymerization; ISO:GO_Central. DR GO; GO:0010506; P:regulation of autophagy; ISO:MGI. DR GO; GO:0050848; P:regulation of calcium-mediated signaling; ISO:GO_Central. 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:GO_Central. DR GO; GO:0031110; P:regulation of microtubule polymerization or depolymerization; ISO:GO_Central. DR GO; GO:0060632; P:regulation of microtubule-based movement; IDA:MGI. DR GO; GO:0046685; P:response to arsenic-containing substance; ISO:GO_Central. DR GO; GO:0055093; P:response to hyperoxia; ISO:GO_Central. DR GO; GO:0010288; P:response to lead ion; ISO:GO_Central. DR GO; GO:0007584; P:response to nutrient; ISO:GO_Central. DR GO; GO:0097435; P:supramolecular fiber organization; ISO:GO_Central. DR GO; GO:0007416; P:synapse assembly; ISO:GO_Central. DR GO; GO:0050808; P:synapse organization; ISO:GO_Central. DR Proteomes; UP000000589; Chromosome 11. DR Antibodypedia; 3124; 6446 antibodies from 58 providers. DR RNAct; P10637; protein. DR BioGRID-ORCS; 17762; 4 hits in 81 CRISPR screens. DR AlphaFoldDB; P10637; -. DR EMDB; EMD-18269; -. DR EMDB; EMD-37445; -. DR EMDB; EMD-57273; -. DR EMDB; EMD-57275; -. DR CD-CODE; CE726F99; Postsynaptic density. DR CD-CODE; E94C8F89; Tau inclusion. DR FunCoup; P10637; 590. 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..16 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 50..60 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 126..137 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 157..172 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 189..202 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 203..212 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 270..294 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 354..366 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 413..427 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 479..506 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 693..708 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 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 STRAND 567..575 FT /evidence="ECO:0007829|PDB:8Q96" FT STRAND 584..596 FT /evidence="ECO:0007829|PDB:8Q96" FT STRAND 598..603 FT /evidence="ECO:0007829|PDB:8Q96" FT STRAND 615..619 FT /evidence="ECO:0007829|PDB:8Q96" 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 //