TAU_PONPY
ID TAU_PONPY Reviewed; 758 AA.
AC Q5S6V2;
DT 15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 02-JUN-2021, entry version 95.
DE RecName: Full=Microtubule-associated protein tau;
GN Name=MAPT;
OS Pongo pygmaeus (Bornean orangutan).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9600;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=15474313; DOI=10.1016/j.gene.2004.07.013;
RA Holzer M., Craxton M., Jakes R., Arendt T., Goedert M.;
RT "Tau gene (MAPT) sequence variation among primates.";
RL Gene 341:313-322(2004).
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 (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with MARK1, MARK2, MARK3 AND MARK4 (By similarity).
CC Interacts with SQSTM1 when polyubiquitinated (By similarity). Interacts
CC with PSMC2 through SQSTM1 (By similarity). Interacts with FKBP4 (By
CC similarity). Binds to CSNK1D (By similarity). Interacts with SGK1 (By
CC similarity). Interacts with EPM2A; the interaction dephosphorylates
CC MAPT at Ser-396 (By similarity). Interacts with PIN1 (By similarity).
CC Interacts with LRRK2 (By similarity). Interacts with LRP1, leading to
CC endocytosis; this interaction is reduced in the presence of LRPAP1/RAP
CC (By similarity). {ECO:0000250|UniProtKB:P10636,
CC ECO:0000250|UniProtKB:P10637, ECO:0000250|UniProtKB:P19332}.
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}. Note=Mostly found in the axons of
CC neurons, in the cytosol and in association with plasma membrane
CC components. {ECO:0000250|UniProtKB:P10636}.
CC -!- DOMAIN: The tau/MAP repeat binds to tubulin. {ECO:0000250}.
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 or MARK4), causing detachment
CC from microtubules, and their disassembly (By similarity).
CC Phosphorylation at Ser-579 by BRSK1 and BRSK2 in neurons affects
CC ability to bind microtubules and plays a role in neuron polarization.
CC Phosphorylated by PHK. Dephosphorylation at several serine and
CC threonine residues by the serine/threonine phosphatase PPP5C (By
CC similarity). Phosphorylation at Ser-214 by SGK1 mediates microtubule
CC depolymerization and neurite formation in hippocampal neurons (By
CC similarity). {ECO:0000250, ECO:0000250|UniProtKB:P10636}.
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DR EMBL; AY769109; AAV52386.1; -; Genomic_DNA.
DR EMBL; AY769097; AAV52386.1; JOINED; Genomic_DNA.
DR EMBL; AY769098; AAV52386.1; JOINED; Genomic_DNA.
DR EMBL; AY769099; AAV52386.1; JOINED; Genomic_DNA.
DR EMBL; AY769102; AAV52386.1; JOINED; Genomic_DNA.
DR EMBL; AY769101; AAV52386.1; JOINED; Genomic_DNA.
DR EMBL; AY769100; AAV52386.1; JOINED; Genomic_DNA.
DR EMBL; AY769103; AAV52386.1; JOINED; Genomic_DNA.
DR EMBL; AY769105; AAV52386.1; JOINED; Genomic_DNA.
DR EMBL; AY769107; AAV52386.1; JOINED; Genomic_DNA.
DR EMBL; AY769108; AAV52386.1; JOINED; Genomic_DNA.
DR EMBL; AY769106; AAV52386.1; JOINED; Genomic_DNA.
DR EMBL; AY769104; AAV52386.1; JOINED; Genomic_DNA.
DR BMRB; Q5S6V2; -.
DR GO; GO:0030424; C:axon; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0030425; C:dendrite; ISS:UniProtKB.
DR GO; GO:0030426; C:growth cone; ISS:UniProtKB.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0045298; C:tubulin complex; ISS:UniProtKB.
DR GO; GO:0008017; F:microtubule binding; ISS:UniProtKB.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; ISS:UniProtKB.
DR GO; GO:0045773; P:positive regulation of axon extension; ISS:UniProtKB.
DR GO; GO:0031116; P:positive regulation of microtubule polymerization; ISS:UniProtKB.
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 3: Inferred from homology;
KW Acetylation; Cell membrane; Cell projection; Cytoplasm; Cytoskeleton;
KW Isopeptide bond; Membrane; Methylation; Microtubule; Phosphoprotein;
KW Repeat; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P10636"
FT CHAIN 2..758
FT /note="Microtubule-associated protein tau"
FT /id="PRO_0000072745"
FT REPEAT 561..591
FT /note="Tau/MAP 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00824"
FT REPEAT 592..622
FT /note="Tau/MAP 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00824"
FT REPEAT 623..653
FT /note="Tau/MAP 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00824"
FT REPEAT 654..685
FT /note="Tau/MAP 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00824"
FT REGION 1..591
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..20
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 179..193
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 382..397
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 508..528
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"
FT /evidence="ECO:0000250|UniProtKB:P10636"
FT MOD_RES 29
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P10637"
FT MOD_RES 46
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19332"
FT MOD_RES 61
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19332"
FT MOD_RES 69
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P10637"
FT MOD_RES 71
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P19332"
FT MOD_RES 111
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P10637"
FT MOD_RES 214
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10636"
FT MOD_RES 396
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10636"
FT MOD_RES 470
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P10636"
FT MOD_RES 472
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:P10637"
FT MOD_RES 480
FT /note="N6,N6-dimethyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P10637"
FT MOD_RES 480
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P10637"
FT MOD_RES 486
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P10637"
FT MOD_RES 492
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P10637"
FT MOD_RES 498
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P10636"
FT MOD_RES 502
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10637"
FT MOD_RES 508
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10637"
FT MOD_RES 512
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10637"
FT MOD_RES 514
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P10636"
FT MOD_RES 515
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10636"
FT MOD_RES 516
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10636"
FT MOD_RES 519
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10636"
FT MOD_RES 522
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P10636"
FT MOD_RES 529
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P10636"
FT MOD_RES 531
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10636"
FT MOD_RES 534
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P10636"
FT MOD_RES 542
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P10637"
FT MOD_RES 548
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P10636"
FT MOD_RES 552
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10636"
FT MOD_RES 554
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10636"
FT MOD_RES 576
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P10637"
FT MOD_RES 576
FT /note="N6-methyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P10637"
FT MOD_RES 579
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10636"
FT MOD_RES 598
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P10637"
FT MOD_RES 602
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10636"
FT MOD_RES 606
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10636"
FT MOD_RES 607
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P10637"
FT MOD_RES 610
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10636"
FT MOD_RES 615
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P10637"
FT MOD_RES 622
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10636"
FT MOD_RES 628
FT /note="N6,N6-dimethyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P10637"
FT MOD_RES 628
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P10637"
FT MOD_RES 634
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P10637"
FT MOD_RES 638
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P10637"
FT MOD_RES 641
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10636"
FT MOD_RES 648
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P10637"
FT MOD_RES 660
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P10637"
FT MOD_RES 664
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P10637"
FT MOD_RES 666
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:P10637"
FT MOD_RES 669
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10636"
FT MOD_RES 673
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10636"
FT MOD_RES 686
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P10637"
FT MOD_RES 702
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P10637"
FT MOD_RES 711
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P10637"
FT MOD_RES 713
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10636"
FT MOD_RES 717
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10636"
FT MOD_RES 720
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P10637"
FT MOD_RES 721
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10636"
FT MOD_RES 726
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10636"
FT MOD_RES 733
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10636"
FT MOD_RES 739
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10636"
FT MOD_RES 744
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P10636"
FT CROSSLNK 44
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P10637"
FT CROSSLNK 571
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P10636"
FT CROSSLNK 576
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin); alternate"
FT /evidence="ECO:0000250|UniProtKB:P10637"
FT CROSSLNK 584
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P10637"
FT CROSSLNK 598
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin); alternate"
FT /evidence="ECO:0000250|UniProtKB:P10637"
FT CROSSLNK 615
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin); alternate"
FT /evidence="ECO:0000250|UniProtKB:P10637"
FT CROSSLNK 628
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin); alternate"
FT /evidence="ECO:0000250|UniProtKB:P10636"
FT CROSSLNK 634
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin); alternate"
FT /evidence="ECO:0000250|UniProtKB:P10637"
FT CROSSLNK 638
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin); alternate"
FT /evidence="ECO:0000250|UniProtKB:P10637"
FT CROSSLNK 648
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin); alternate"
FT /evidence="ECO:0000250|UniProtKB:P10637"
FT CROSSLNK 660
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin); alternate"
FT /evidence="ECO:0000250|UniProtKB:P10637"
FT CROSSLNK 664
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin); alternate"
FT /evidence="ECO:0000250|UniProtKB:P10637"
FT CROSSLNK 670
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P10636"
FT CROSSLNK 686
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin); alternate"
FT /evidence="ECO:0000250|UniProtKB:P10637"
FT CROSSLNK 692
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P10637"
FT CROSSLNK 702
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin); alternate"
FT /evidence="ECO:0000250|UniProtKB:P10637"
SQ SEQUENCE 758 AA; 78905 MW; 013F0B0C73AE1086 CRC64;
MAEPHQEFDV TEDHAGTYGL GDRKDQGGYT MLQDQEGDTD AGLKESPLQT PAEDGSEEPG
SETSDAKSTP TAEDVTAPLV DERAPGEQAA AQPHMEIPXG TTAEEAGIGD TPSLEDEAAG
HVTQEPESGK VVREGFLGEP GPPGLSHQLV SGMPGAPLLP EGPREATRQP SGIGPEDTEG
GRHAPELLKH QLLGDLHQEG PPLKGAGGKE RPGSKEEVDE DRDVDESSPQ DSPPSKVSPA
QDGWPPQAAA REATSIPGFP AEGAIPLPVD FLSKVSTEIP ASEPDRPSAG GAEGQDAPPE
FTFHVEITPN VQKEQAHSEE HLRRAAFPGA PGEGPEAQGP SLGEDAKEAD LPEPSEKQPA
AAPRGKPISR VPQLKARMVS KSKDGTGSDD KKAKTSTRSS AKTLKNRPCL SPKHPTPGSS
DPLIQPSSPA VCPEPPSSPK YVSSVTPRTG SSGAKEMKLK GADGKTKIAT PRGAAPPGQK
GQANATRIPA KTPPAPKTPP SSGEPPKSGD RSGYSSPGSP GTPGSRSRTP SLPTPPTREP
KKVAVVRTPP KSPSSAKSRL QTAPVPMPDL KNVKSKIGST ENLKHQPGGG KVQIINKKLD
LSNVQSKCGS KDNIKHVPGG GSVQIVYKPV DLSKVTSKCG SLGNIHHKPG GGQVEVKSEK
LDFKDRVQSK IGSLDNITHV PGGGHKKIET HKLTFRENAK AKTDHGAEIV YKSPVVSGDT
SPRHLSNVSS TGSIDMVDSP QLATLADEVS ASLAKQGL
