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TAU_PANTR
ID   TAU_PANTR               Reviewed;         776 AA.
AC   Q5YCW1;
DT   15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 4.
DT   03-AUG-2022, entry version 130.
DE   RecName: Full=Microtubule-associated protein tau;
GN   Name=MAPT;
OS   Pan troglodytes (Chimpanzee).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pan.
OX   NCBI_TaxID=9598;
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-597 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; AY574135; AAS91773.2; -; Genomic_DNA.
DR   EMBL; AY574122; AAS91773.2; JOINED; Genomic_DNA.
DR   EMBL; AY574123; AAS91773.2; JOINED; Genomic_DNA.
DR   EMBL; AY574124; AAS91773.2; JOINED; Genomic_DNA.
DR   EMBL; AY574125; AAS91773.2; JOINED; Genomic_DNA.
DR   EMBL; AY574126; AAS91773.2; JOINED; Genomic_DNA.
DR   EMBL; AY574127; AAS91773.2; JOINED; Genomic_DNA.
DR   EMBL; AY574128; AAS91773.2; JOINED; Genomic_DNA.
DR   EMBL; AY574129; AAS91773.2; JOINED; Genomic_DNA.
DR   EMBL; AY574130; AAS91773.2; JOINED; Genomic_DNA.
DR   EMBL; AY574131; AAS91773.2; JOINED; Genomic_DNA.
DR   EMBL; AY574132; AAS91773.2; JOINED; Genomic_DNA.
DR   EMBL; AY574133; AAS91773.2; JOINED; Genomic_DNA.
DR   EMBL; AY574134; AAS91773.2; JOINED; Genomic_DNA.
DR   AlphaFoldDB; Q5YCW1; -.
DR   SMR; Q5YCW1; -.
DR   STRING; 9598.ENSPTRP00000015840; -.
DR   PaxDb; Q5YCW1; -.
DR   PRIDE; Q5YCW1; -.
DR   Ensembl; ENSPTRT00000017113; ENSPTRP00000015840; ENSPTRG00000009314.
DR   Ensembl; ENSPTRT00000094329; ENSPTRP00000086254; ENSPTRG00000046868.
DR   VGNC; VGNC:12432; MAPT.
DR   eggNOG; KOG2418; Eukaryota.
DR   GeneTree; ENSGT00940000155494; -.
DR   HOGENOM; CLU_021741_2_0_1; -.
DR   InParanoid; Q5YCW1; -.
DR   TreeFam; TF316358; -.
DR   Proteomes; UP000002277; Chromosome 17.
DR   Bgee; ENSPTRG00000009314; Expressed in dorsolateral prefrontal cortex and 19 other tissues.
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:0043005; C:neuron projection; IBA:GO_Central.
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:0031175; P:neuron projection development; IBA:GO_Central.
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   Reference proteome; Repeat; Ubl conjugation.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P10636"
FT   CHAIN           2..776
FT                   /note="Microtubule-associated protein tau"
FT                   /id="PRO_0000072743"
FT   REPEAT          579..609
FT                   /note="Tau/MAP 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00824"
FT   REPEAT          610..640
FT                   /note="Tau/MAP 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00824"
FT   REPEAT          641..671
FT                   /note="Tau/MAP 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00824"
FT   REPEAT          672..703
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   REGION          733..752
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        27..41
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        45..71
FT                   /note="Polar 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        340..354
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        530..546
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        737..752
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         526
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P10637"
FT   MOD_RES         530
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P10637"
FT   MOD_RES         532
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P10636"
FT   MOD_RES         533
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P10636"
FT   MOD_RES         534
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P10636"
FT   MOD_RES         537
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P10636"
FT   MOD_RES         540
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P10636"
FT   MOD_RES         547
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P10636"
FT   MOD_RES         549
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P10636"
FT   MOD_RES         552
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P10636"
FT   MOD_RES         560
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P10637"
FT   MOD_RES         566
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P10636"
FT   MOD_RES         570
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P10636"
FT   MOD_RES         572
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P10636"
FT   MOD_RES         594
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P10637"
FT   MOD_RES         594
FT                   /note="N6-methyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P10637"
FT   MOD_RES         597
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P10636"
FT   MOD_RES         616
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P10637"
FT   MOD_RES         620
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P10636"
FT   MOD_RES         624
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P10636"
FT   MOD_RES         625
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P10637"
FT   MOD_RES         628
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P10636"
FT   MOD_RES         633
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P10637"
FT   MOD_RES         640
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P10636"
FT   MOD_RES         646
FT                   /note="N6,N6-dimethyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P10637"
FT   MOD_RES         646
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P10637"
FT   MOD_RES         652
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P10637"
FT   MOD_RES         656
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P10637"
FT   MOD_RES         659
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P10636"
FT   MOD_RES         666
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P10637"
FT   MOD_RES         678
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P10637"
FT   MOD_RES         682
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P10637"
FT   MOD_RES         684
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0000250|UniProtKB:P10637"
FT   MOD_RES         687
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P10636"
FT   MOD_RES         691
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P10636"
FT   MOD_RES         704
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P10637"
FT   MOD_RES         720
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P10637"
FT   MOD_RES         729
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P10637"
FT   MOD_RES         731
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P10636"
FT   MOD_RES         735
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P10636"
FT   MOD_RES         738
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P10637"
FT   MOD_RES         739
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P10636"
FT   MOD_RES         744
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P10636"
FT   MOD_RES         751
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P10636"
FT   MOD_RES         757
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P10636"
FT   MOD_RES         762
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        589
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000250|UniProtKB:P10636"
FT   CROSSLNK        594
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin); alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P10637"
FT   CROSSLNK        602
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000250|UniProtKB:P10637"
FT   CROSSLNK        616
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin); alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P10637"
FT   CROSSLNK        633
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin); alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P10637"
FT   CROSSLNK        646
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin); alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P10636"
FT   CROSSLNK        652
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin); alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P10637"
FT   CROSSLNK        656
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin); alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P10637"
FT   CROSSLNK        666
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin); alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P10637"
FT   CROSSLNK        678
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin); alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P10637"
FT   CROSSLNK        682
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin); alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P10637"
FT   CROSSLNK        688
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000250|UniProtKB:P10636"
FT   CROSSLNK        704
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin); alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P10637"
FT   CROSSLNK        710
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000250|UniProtKB:P10637"
FT   CROSSLNK        720
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin); alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P10637"
SQ   SEQUENCE   776 AA;  80979 MW;  38A50C3A20A07951 CRC64;
     MAEPRQEFEV MEDHAGTYGL GDRKDQGGYT MHQDQEGDTD AGLKESPLQT PTEDGSEEPG
     SETSDAKSTP TAEDVTAPLV DEGAPGKQAA AQPHTEIPEG TTAEEAGIGD TPSLEDEAAG
     HVTQEPESGK VVQEGFLREP GPPGLSHQLM SGMPGAPLLP EGPREATRQP SGTGPEDTEG
     GRHAPELLKH QLLGDLHQEG PPLKGAGGKE RPGSKEEVDE DRDVDESSLQ DSPPSKASPA
     QDGRPPQTAA REATSIPGFP AEGAIPLPVD FLSKVSTEIP ASEPDGPSAG RAKGQDAHLE
     FTFHVEITPN VQKEQAHSEE HLGRAAFPGA PGEGPEARGP SLGEDTKEAD LPEPSEKQPA
     AAPRGKPVSR VPQLKARMVS KSKDGTGSDD KKAKTSTRSS AKTLKNRPCL SPKHPTPGSS
     DPLIQPSSPA VCPEPPSSPK YVSSVTPRTG SSGAKEMKLK GADGKTKIAT PRGAAPPGQK
     GQANATRIPA KTPPAPKTPP SSATKQVQRR PPPAGPRSER GEPPKSGDRS GYSSPGSPGT
     PGSRSRTPSL PTPPTREPKK VAVVRTPPKS PSSAKSRLQT APVPMPDLKN VKSKIGSTEN
     LKHQPGGGKV QIINKKLDLS NVQSKCGSKD NIKHVPGGGS VQIVYKPVDL SKVTSKCGSL
     GNIHHKPGGG QVEVKSEKLD FKDRVQSKIG SLDNITHVPG GGNKKIETHK LTFRENAKAK
     TDHGAEIVYK SPVVSGDTSP RHLSNVSSTG SIDMVDSPQL ATLADEVSAS LAKQGL
 
 
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