| IED ID | IndEnz0002009833 |
| Enzyme Type ID | protease009833 |
| Protein Name |
Tubulinyl-Tyr carboxypeptidase 1 EC 3.4.17.17 Tyrosine carboxypeptidase 1 TTCP 1 Vasohibin-1 |
| Gene Name | Vash1 Vash |
| Organism | Mus musculus (Mouse) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Glires (Rodents and rabbits) Rodentia Myomorpha (mice and others) Muroidea Muridae Murinae Mus Mus Mus musculus (Mouse) |
| Enzyme Sequence | MPGGKKVVPSGSSSASPNAAATTTAAAAAAAAAPHSGTKRLETTEGASAQRDEEPEEEGEEDLRDGGVPFFINRGGLPVDEATWERMWKHVAKIHPDGEKVALRIRGATDLPKIPIPSVPTFQPTTPVPERLEAVQRYIRELQYNHTGTQFFEIKKSRPLTGLMDLAKEMTKEALPIKCLEAVILGIYLTNSMPTLERFPISFKTYFSGNYFRHIVLGVNFGGRYGALGMSRREDLMYKPPAFRTLSELVLDYEAAYGRCWHVLKKVKLGQCVSHDPHSVEQIEWKHSVLDVERLGREDFRKELERHARDMRLKIGKGTGPPSPTKDRKKDVSSPQRAQSSPHRRNSRSERRPSGEKKPAEPKAMPDLSGYQIRV |
| Enzyme Length | 375 |
| Uniprot Accession Number | Q8C1W1 |
| Absorption | |
| Active Site | ACT_SITE 179; /evidence="ECO:0000269|PubMed:29146868, ECO:0000305|PubMed:26794318"; ACT_SITE 214; /evidence="ECO:0000305|PubMed:26794318"; ACT_SITE 231; /evidence="ECO:0000305|PubMed:26794318" |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=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; Xref=Rhea:RHEA:57444, Rhea:RHEA-COMP:16434, Rhea:RHEA-COMP:16435, ChEBI:CHEBI:15377, ChEBI:CHEBI:58315, ChEBI:CHEBI:149554, ChEBI:CHEBI:149555; EC=3.4.17.17; Evidence={ECO:0000269|PubMed:29146868}; |
| DNA Binding | |
| EC Number | 3.4.17.17 |
| Enzyme 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). {ECO:0000250|UniProtKB:Q7L8A9, ECO:0000269|PubMed:19204325, ECO:0000269|PubMed:29146868}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (1); Compositional bias (2); Frameshift (1); Mutagenesis (1); Region (3); Sequence conflict (2); Site (2) |
| Keywords | Carboxypeptidase;Cell cycle;Cytoplasm;Growth arrest;Hydrolase;Protease;Reference proteome;Secreted;Ubl conjugation |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q7L8A9}. Secreted {ECO:0000250|UniProtKB:Q7L8A9}. Note=Mainly localizes in the cytoplasm. Some fraction is secreted via a non-canonical secretion system; interaction with SVBP promotes secretion. {ECO:0000250|UniProtKB:Q7L8A9}. |
| Modified Residue | |
| Post Translational Modification | PTM: Ubiquitinated in vitro. {ECO:0000250|UniProtKB:Q7L8A9}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 12466851; 15226823; 15467828; 16473886; 16707096; 19179360; 19498005; 19682397; 20133819; 20884873; 21228103; 21267068; 21677750; 23056314; 24066086; 25184477; 25255225; 26025651; 27169581; 27325558; 31091125; 31815666; 33441910; |
| Motif | |
| Gene Encoded By | |
| Mass | 41,875 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | RHEA:57444 |
| Cross Reference Brenda |