Q8C1W1 · VASH1_MOUSE

  • Protein
    Tubulinyl-Tyr carboxypeptidase 1
  • Gene
    Vash1
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

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).

Features

Showing features for site, active site.

137550100150200250300350
TypeIDPosition(s)Description
Site39-40Cleavage
Site86-87Cleavage
Active site179
Active site214
Active site231

GO annotations

AspectTerm
Cellular Componentapical part of cell
Cellular Componentcytoplasm
Cellular Componentendoplasmic reticulum
Cellular Componentextracellular space
Molecular Functionactin binding
Molecular Functionmetallocarboxypeptidase activity
Molecular Functiontubulin-tyrosine carboxypeptidase
Biological Processangiogenesis
Biological Processlabyrinthine layer blood vessel development
Biological Processnegative regulation of angiogenesis
Biological Processnegative regulation of blood vessel endothelial cell migration
Biological Processnegative regulation of endothelial cell migration
Biological Processnegative regulation of endothelial cell proliferation
Biological Processnegative regulation of lymphangiogenesis
Biological Processplacenta blood vessel development
Biological Processpositive regulation of gene expression
Biological Processproteolysis
Biological Processregulation of angiogenesis
Biological Processregulation of cell cycle
Biological Processregulation of cellular senescence
Biological Processresponse to wounding

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Tubulinyl-Tyr carboxypeptidase 1
  • EC number
  • Alternative names
    • Tyrosine carboxypeptidase 1
      (TTCP 1
      )
    • Vasohibin-1

Gene names

    • Name
      Vash1
    • Synonyms
      Vash

Organism names

  • Taxonomic identifier
  • Strain
    • C57BL/6J
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus

Accessions

  • Primary accession
    Q8C1W1
  • Secondary accessions
    • E9QKT9
    • Q8C394

Proteomes

Organism-specific databases

Subcellular Location

Cytoplasm
Secreted
Note: Mainly localizes in the cytoplasm. Some fraction is secreted via a non-canonical secretion system; interaction with SVBP promotes secretion.

Keywords

Phenotypes & Variants

Features

Showing features for mutagenesis.

TypeIDPosition(s)Description
Mutagenesis179Abolished tyrosine carboxypeptidase activity.

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.

Go to variant viewer

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00001899811-375Tubulinyl-Tyr carboxypeptidase 1

Post-translational modification

Ubiquitinated in vitro.

Keywords

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

Interaction

Subunit

Interacts with SVBP; interaction enhances VASH1 tyrosine carboxypeptidase activity.

Protein-protein interaction databases

Miscellaneous

Structure

Family & Domains

Features

Showing features for region, compositional bias.

TypeIDPosition(s)Description
Region1-69Disordered
Compositional bias9-23Polar residues
Region309-375Disordered
Region329-375Involved in heparin-binding and antiangiogenic activity
Compositional bias343-363Basic and acidic residues

Sequence similarities

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    375
  • Mass (Da)
    41,875
  • Last updated
    2011-07-27 v4
  • Checksum
    82F7348A17B32B6D
MPGGKKVVPSGSSSASPNAAATTTAAAAAAAAAPHSGTKRLETTEGASAQRDEEPEEEGEEDLRDGGVPFFINRGGLPVDEATWERMWKHVAKIHPDGEKVALRIRGATDLPKIPIPSVPTFQPTTPVPERLEAVQRYIRELQYNHTGTQFFEIKKSRPLTGLMDLAKEMTKEALPIKCLEAVILGIYLTNSMPTLERFPISFKTYFSGNYFRHIVLGVNFGGRYGALGMSRREDLMYKPPAFRTLSELVLDYEAAYGRCWHVLKKVKLGQCVSHDPHSVEQIEWKHSVLDVERLGREDFRKELERHARDMRLKIGKGTGPPSPTKDRKKDVSSPQRAQSSPHRRNSRSERRPSGEKKPAEPKAMPDLSGYQIRV

Sequence caution

The sequence BAC41121.1 differs from that shown. Reason: Frameshift

Features

Showing features for sequence conflict, compositional bias.

TypeIDPosition(s)Description
Sequence conflict2in Ref. 1; BAC41121
Compositional bias9-23Polar residues
Sequence conflict157in Ref. 1; BAC41121
Compositional bias343-363Basic and acidic residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AK090166
EMBL· GenBank· DDBJ
BAC41121.1
EMBL· GenBank· DDBJ
mRNA Frameshift
AC102689
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.

Genome annotation databases

Similar Proteins

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