| IED ID | IndEnz0002009834 |
| Enzyme Type ID | protease009834 |
| Protein Name |
Tubulinyl-Tyr carboxypeptidase 2 EC 3.4.17.17 Vasohibin-2 Vasohibin-like protein |
| Gene Name | VASH2 VASHL |
| Organism | Homo sapiens (Human) |
| 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 Primates Haplorrhini Simiiformes Catarrhini Hominoidea (apes) Hominidae (great apes) Homininae Homo Homo sapiens (Human) |
| Enzyme Sequence | MTGSAADTHRCPHPKGAKGTRSRSSHARPVSLATSGGSEEEDKDGGVLFHVNKSGFPIDSHTWERMWMHVAKVHPKGGEMVGAIRNAAFLAKPSIPQVPNYRLSMTIPDWLQAIQNYMKTLQYNHTGTQFFEIRKMRPLSGLMETAKEMTRESLPIKCLEAVILGIYLTNGQPSIERFPISFKTYFSGNYFHHVVLGIYCNGRYGSLGMSRRAELMDKPLTFRTLSDLIFDFEDSYKKYLHTVKKVKIGLYVPHEPHSFQPIEWKQLVLNVSKMLRADIRKELEKYARDMRMKILKPASAHSPTQVRSRGKSLSPRRRQASPPRRLGRREKSPALPEKKVADLSTLNEVGYQIRI |
| Enzyme Length | 355 |
| Uniprot Accession Number | Q86V25 |
| Absorption | |
| Active Site | ACT_SITE 158; /evidence="ECO:0000269|PubMed:29146869, ECO:0000305|PubMed:26794318"; ACT_SITE 193; /evidence="ECO:0000305|PubMed:26794318"; ACT_SITE 210; /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:29146869, ECO:0000269|PubMed:31235911}; |
| 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:29146869). Critical for spindle function and accurate chromosome segregation during mitosis since microtuble detyronisation regulates mitotic spindle length and postioning (PubMed:31171830). Acts as an activator of angiogenesis: expressed in infiltrating mononuclear cells in the sprouting front to promote angiogenesis (PubMed:19204325). Plays a role in axon formation (PubMed:31235911). {ECO:0000269|PubMed:19204325, ECO:0000269|PubMed:29146869, ECO:0000269|PubMed:31235911}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Alternative sequence (8); Beta strand (8); Chain (1); Helix (8); Modified residue (1); Mutagenesis (12); Region (2); Turn (1) |
| Keywords | 3D-structure;Alternative splicing;Carboxypeptidase;Cytoplasm;Cytoskeleton;Hydrolase;Phosphoprotein;Protease;Reference proteome;Secreted |
| Interact With | |
| Induction | INDUCTION: By VEGF. {ECO:0000269|PubMed:16528006}. |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19204325}. Secreted {ECO:0000269|PubMed:20736312}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:31235911}. Note=Mainly localizes in the cytoplasm (PubMed:19204325). Some fraction is secreted via a non-canonical secretion system; interaction with SVBP promotes secretion (PubMed:20736312). Associates with microtubules (PubMed:31235911). {ECO:0000269|PubMed:19204325, ECO:0000269|PubMed:20736312, ECO:0000269|PubMed:31235911}. |
| Modified Residue | MOD_RES 302; /note=Phosphoserine; /evidence=ECO:0007744|PubMed:21406692 |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (6) |
| Cross Reference PDB | 6J4O; 6J4P; 6J4Q; 6J4S; 6J4V; 6QBY; |
| Mapped Pubmed ID | 22438034; 22614011; 22826464; 23100270; 23615928; 24510904; 24595063; 25184477; 25269476; 25468068; 25916042; 25957412; 26177649; 27702660; 27879017; 28064471; 28327155; 28882646; 28960674; 29039601; 29042694; 29146868; 30318866; 30940294; 31074083; 32494966; 7452228; |
| Motif | |
| Gene Encoded By | |
| Mass | 40,450 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | RHEA:57444 |
| Cross Reference Brenda |