Q8C1W1 · VASH1_MOUSE
- ProteinTubulinyl-Tyr carboxypeptidase 1
- GeneVash1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids375 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Tyrosine carboxypeptidase that removes the C-terminal tyrosine residue of alpha-tubulin, thereby regulating microtubule dynamics and function (PubMed:29146868).
Acts as an angiogenesis inhibitor: inhibits migration, proliferation and network formation by endothelial cells as well as angiogenesis (PubMed:19204325).
This inhibitory effect is selective to endothelial cells as it does not affect the migration of smooth muscle cells or fibroblasts (By similarity).
Acts as an angiogenesis inhibitor: inhibits migration, proliferation and network formation by endothelial cells as well as angiogenesis (PubMed:19204325).
This inhibitory effect is selective to endothelial cells as it does not affect the migration of smooth muscle cells or fibroblasts (By similarity).
Catalytic activity
- C-terminal L-alpha-aminoacyl-L-glutamyl-L-glutamyl-L-tyrosyl-[tubulin] + H2O = C-terminal L-alpha-aminoacyl-L-glutamyl-L-glutamyl-[tubulin] + L-tyrosine
Features
Showing features for site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Site | 39-40 | Cleavage | ||||
Sequence: KR | ||||||
Site | 86-87 | Cleavage | ||||
Sequence: RM | ||||||
Active site | 179 | |||||
Sequence: C | ||||||
Active site | 214 | |||||
Sequence: H | ||||||
Active site | 231 | |||||
Sequence: S |
GO annotations
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameTubulinyl-Tyr carboxypeptidase 1
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionQ8C1W1
- Secondary accessions
Proteomes
Organism-specific databases
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 179 | Abolished tyrosine carboxypeptidase activity. | ||||
Sequence: C → A |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 11 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000189981 | 1-375 | Tubulinyl-Tyr carboxypeptidase 1 | |||
Sequence: MPGGKKVVPSGSSSASPNAAATTTAAAAAAAAAPHSGTKRLETTEGASAQRDEEPEEEGEEDLRDGGVPFFINRGGLPVDEATWERMWKHVAKIHPDGEKVALRIRGATDLPKIPIPSVPTFQPTTPVPERLEAVQRYIRELQYNHTGTQFFEIKKSRPLTGLMDLAKEMTKEALPIKCLEAVILGIYLTNSMPTLERFPISFKTYFSGNYFRHIVLGVNFGGRYGALGMSRREDLMYKPPAFRTLSELVLDYEAAYGRCWHVLKKVKLGQCVSHDPHSVEQIEWKHSVLDVERLGREDFRKELERHARDMRLKIGKGTGPPSPTKDRKKDVSSPQRAQSSPHRRNSRSERRPSGEKKPAEPKAMPDLSGYQIRV |
Post-translational modification
Ubiquitinated in vitro.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Expressed at low level in proliferating endothelial cells at the sprouting front but highly expressed in nonproliferating endothelial cells in the termination zone.
Gene expression databases
Structure
Family & Domains
Features
Showing features for region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-69 | Disordered | ||||
Sequence: MPGGKKVVPSGSSSASPNAAATTTAAAAAAAAAPHSGTKRLETTEGASAQRDEEPEEEGEEDLRDGGVP | ||||||
Compositional bias | 9-23 | Polar residues | ||||
Sequence: PSGSSSASPNAAATT | ||||||
Region | 309-375 | Disordered | ||||
Sequence: RDMRLKIGKGTGPPSPTKDRKKDVSSPQRAQSSPHRRNSRSERRPSGEKKPAEPKAMPDLSGYQIRV | ||||||
Region | 329-375 | Involved in heparin-binding and antiangiogenic activity | ||||
Sequence: KKDVSSPQRAQSSPHRRNSRSERRPSGEKKPAEPKAMPDLSGYQIRV | ||||||
Compositional bias | 343-363 | Basic and acidic residues | ||||
Sequence: HRRNSRSERRPSGEKKPAEPK |
Sequence similarities
Belongs to the transglutaminase-like superfamily. Vasohibin family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length375
- Mass (Da)41,875
- Last updated2011-07-27 v4
- Checksum82F7348A17B32B6D
Sequence caution
Features
Showing features for sequence conflict, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 2 | in Ref. 1; BAC41121 | ||||
Sequence: P → A | ||||||
Compositional bias | 9-23 | Polar residues | ||||
Sequence: PSGSSSASPNAAATT | ||||||
Sequence conflict | 157 | in Ref. 1; BAC41121 | ||||
Sequence: S → G | ||||||
Compositional bias | 343-363 | Basic and acidic residues | ||||
Sequence: HRRNSRSERRPSGEKKPAEPK |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AK090166 EMBL· GenBank· DDBJ | BAC41121.1 EMBL· GenBank· DDBJ | mRNA | Frameshift | |
AC102689 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. |