Microtubule-associated protein tau - Spermophilus citellus (European suslik)

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Q6TS35 (TAU_SPECI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 56. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Microtubule-associated protein tau

Gene names

Name:

MAPT

Organism

Spermophilus citellus (European suslik) (Citellus citellus)

Taxonomic identifier

9997 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Sciuridae › Xerinae › Marmotini › Spermophilus

Protein attributes

Sequence length	430 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Promotes microtubule assembly and stability, and might be involved in the establishment and maintenance of neuronal polarity. The C-terminus binds axonal microtubules while the N-terminus binds neural plasma membrane components, suggesting that tau functions as a linker protein between both. Axonal polarity is predetermined by tau localization (in the neuronal cell) in the domain of the cell body defined by the centrosome. The short isoforms allow plasticity of the cytoskeleton whereas the longer isoforms may preferentially play a role in its stabilization. Ref.1
Subunit structure	Interacts with SQSTM1 when polyubiquitinated. Interacts with PSMC2 through SQSTM1 By similarity. Interacts with FKBP4. Binds to CSNK1D By similarity.
Subcellular location	Cytoplasm › cytosol By similarity. Cell membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasm › cytoskeleton. Cell projection › axon. Note: Mostly found in the axons of neurons, in the cytosol and in association with plasma membrane components By similarity.
Domain	The tau/MAP repeat binds to tubulin By similarity.
Post-translational modification	Polyubiquitinated. Requires functional TRAF6 and may provoke SQSTM1-dependent degradation by the proteasome By similarity. Phosphorylation at various serine and threonine residues in S-P or T-P motifs by proline-directed protein kinases (PDPK1: CDK1, CDK5, GSK3, MAPK) (a few sites per protein in interphase, more in mitosis), and at serine residues in K-X-G-S motifs by MAP/microtubule affinity-regulating kinase (MARK1 or MARK2), causing detachment from microtubules, and their disassembly. Phosphorylation at Ser-345 by BRSK1 and BRSK2 in neurons affects ability to bind microtubules and plays a role in neuron polarization. Phosphorylated by PHK By similarity. Ref.1 Hyperphosphorylated (in particular at Thr-170, Ser-191, Thr-194, Ser-251, and Ser-345) during hibernation. Phosphorylation is fully reversible after arousal. Highly phosphorylated tau contains a number of paired helical filaments (PHFs)-like epitopes. PHF-like phosphorylation is not associated with fibril formation. Distribution of PHF-like tau is more intense in the entorhinal cortex, hippocampus and isocortical areas. PHF-like phosphorylation-dephosphorylation during hibernation cycle is synchronized with regression-re-establishment of afferentation. It may reflect a protective mechanism in a unfavorable environment. Ref.1
Sequence similarities	Contains 4 Tau/MAP repeats.

Ontologies

Keywords
Biological process	Hibernation
Cellular component	Cell membrane Cell projection Cytoplasm Cytoskeleton Membrane Microtubule
Coding sequence diversity	Alternative splicing
Domain	Repeat
PTM	Acetylation Disulfide bond Phosphoprotein Ubl conjugation
Gene Ontology (GO)
Biological_process	hibernation Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	axon Inferred from electronic annotation. Source: UniProtKB-SubCell cytosol Inferred from electronic annotation. Source: UniProtKB-SubCell microtubule Inferred from electronic annotation. Source: UniProtKB-KW plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Complete GO annotation...

Alternative products

This entry describes 1 isoform produced by alternative splicing. [Select] Note: A number of isoforms are produced. 6 isoforms have been detected in the adult brain. The pattern of isoforms and their relative expression levels are unaffected during hibernation cycle.

Isoform 1 (identifier: Q6TS35-1) This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed By similarity

Chain

2 – 430

429

Microtubule-associated protein tau

PRO_0000232454

Regions

Repeat

233 – 263

Tau/MAP 1

Repeat

264 – 294

Tau/MAP 2

Repeat

295 – 325

Tau/MAP 3

Repeat

326 – 357

Tau/MAP 4

Amino acid modifications

Modified residue

N-acetylalanine By similarity

Modified residue

Phosphotyrosine; by FYN By similarity

Modified residue

Phosphoserine By similarity

Modified residue

Phosphothreonine By similarity

Modified residue

Phosphothreonine By similarity

Modified residue

142

Phosphothreonine By similarity

Modified residue

154

Phosphothreonine By similarity

Modified residue

164

Phosphothreonine By similarity

Modified residue

167

Phosphoserine By similarity

Modified residue

170

Phosphothreonine

Modified residue

186

Phosphotyrosine By similarity

Modified residue

187

Phosphoserine

Modified residue

188

Phosphoserine

Modified residue

191

Phosphoserine; by CK1, PDPK1 and TTBK1

Modified residue

194

Phosphothreonine; by CK1 and PDPK1

Modified residue

199

Phosphoserine Probable

Modified residue

201

Phosphothreonine; by BRSK1, BRSK2, DYRK2 and PDPK1 By similarity

Modified residue

203

Phosphoserine By similarity

Modified residue

206

Phosphothreonine By similarity

Modified residue

220

Phosphothreonine; by GSK3-beta and PDPK1 By similarity

Modified residue

224

Phosphoserine By similarity

Modified residue

226

Phosphoserine; by PHK By similarity

Modified residue

251

Phosphoserine; also in form PHF-tau-like found during hibernation; by MARK1, BRSK1, BRSK2 and PHK Probable

Modified residue

274

Phosphoserine; by PHK By similarity

Modified residue

278

Phosphoserine; by PHK By similarity

Modified residue

282

Phosphoserine By similarity

Modified residue

294

Phosphoserine By similarity

Modified residue

313

Phosphoserine By similarity

Modified residue

341

Phosphoserine; by PHK By similarity

Modified residue

345

Phosphoserine; in form PHF-tau-like found during hibernation Probable

Modified residue

385

Phosphoserine; by CK1 and PDPK1

Modified residue

389

Phosphoserine By similarity

Modified residue

392

Phosphothreonine By similarity

Modified residue

393

Phosphoserine; by CK1 and PDPK1

Modified residue

398

Phosphoserine By similarity

Modified residue

401

Phosphoserine By similarity

Modified residue

403

Phosphothreonine By similarity

Modified residue

405

Phosphoserine By similarity

Modified residue

411

Phosphoserine By similarity

Modified residue

416

Phosphothreonine By similarity

Disulfide bond

280 ↔ 311

By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

Isoform 1 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 5ED2B0EB0DFADAF0
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FASTA

430

44,803

        10         20         30         40         50         60 
MAEPRQEFDT AEDHAEGYAL LQDQEGEHGL KASPLQTPAD DGPEEPVSET SDAKSTPTAE 

        70         80         90        100        110        120 
DVTAPLVDER TPGEQAATQP PTDIPEGTTA EEAGIGDTPN MEDQAAGHVT QARMVSKGKE 

       130        140        150        160        170        180 
GTGSEDRKAK GADSKTGTKI ATPRGTAPPG QKGTANATRI PAKTTPSPKT PPGTGEPAKS 

       190        200        210        220        230        240 
GDRSGYSSPG SPGTPGSRSR TPSLPTPPTR EPKKVAVVRT PPKSPSSTKS RLQTAPVPMP 

       250        260        270        280        290        300 
DLKNVRSKIG STENLKHQPG GGKVQIINKK LDLSNVQSKC GSKDNIKHVP GGGSVQIVYK 

       310        320        330        340        350        360 
PVDLSKVTSK CGSLGNIHHK PGGGQVEVKS EKLDFKDRVQ SKIGSLDNIT HVPGGGNKKI 

       370        380        390        400        410        420 
ETHKLTFREN AKAKTDHGAE IVYKSPVVSG DTSPRHLSNV SSTGSINMVD SPQLATLADE 

       430 
VSASLAKQGL

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References

[1]

"Reversible paired helical filament-like phosphorylation of tau is an adaptive process associated with neuronal plasticity in hibernating animals."
Arendt T., Stieler J., Strijkstra A.M., Hut R.A., Ruediger J., Van der Zee E.A., Harkany T., Holzer M., Haertig W.
J. Neurosci. 23:6972-6981(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], ALTERNATIVE SPLICING, PHOSPHORYLATION, FUNCTION DURING HIBERNATION.

Web resources

Protein Spotlight

Vita minima - Issue 68 of March 2006

Cross-references

Sequence databases
EMBL GenBank DDBJ	AY388477 mRNA. Translation: AAQ92319.1.
3D structure databases
ModBase	Search...
Proteomic databases
PRIDE	Q6TS35.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Phylogenomic databases
HOVERGEN	HBG000991.
Family and domain databases
InterPro	IPR027324. MAP2/MAP4/Tau. IPR001084. Tau/MAP_tubulin-bd_rpt. IPR002955. Tau_protein. [Graphical view]
PANTHER	PTHR11501. PTHR11501. 1 hit.
Pfam	PF00418. Tubulin-binding. 4 hits. [Graphical view]
PRINTS	PR01261. TAUPROTEIN.
PROSITE	PS00229. TAU_MAP_1. 4 hits. PS51491. TAU_MAP_2. 4 hits. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

TAU_SPECI

Accession

Primary (citable) accession number: Q6TS35

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 18, 2006
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 56 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Protein Spotlight

Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries

Names·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Alternative products

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Sequences

References

Web resources

Cross-references

Sequence databases

3D structure databases

Proteomic databases

Protocols and materials databases

Phylogenomic databases

Family and domain databases

Entry information

Relevant documents