Detail Information for IndEnz0002009835
IED ID IndEnz0002009835
Enzyme Type ID protease009835
Protein Name Tubulinyl-Tyr carboxypeptidase 2
EC 3.4.17.17
Vasohibin-2
Vasohibin-like protein
Gene Name Vash2 Vashl
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 MTGSAADTHRCPHPKITKGTRSRSSHARPVSLATSGGSEEEDKDGGVLFHVNKSGFPIDSHTWERMWLHVAKVHPRGGEMVGAIRNAAFLAKPSIPQVPNYRLSMTIPDWLQAIQNYMKTLQYNHTGTQFFEIRKMRPLSGLMETAKEMTRESLPIKCLEAVILGIYLTNGQPSIERFPISFKTYFSGNYFHHVVLGIYCNGYYGSLGMSRRAELMDKPLTFRTLSDLVFDFEDSYKKYLHTVKKVKIGLYVPHEPHSFQPIEWKQLVLNVSKMLRADIRKELEKYARDMRMKILKPASAHSPTQVRSRGKSLSPRRRQASPPRRLGRRDKSPALTEKKVADLGTLNEVGYQIRI
Enzyme Length 355
Uniprot Accession Number Q8C5G2
Absorption
Active Site ACT_SITE 158; /evidence="ECO:0000269|PubMed:29146868, 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:29146868, ECO:0000269|PubMed:31324789};
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 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:29146868, ECO:0000269|PubMed:31235911}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (3); Beta strand (7); Chain (1); Erroneous initiation (1); Helix (9); Modified residue (1); Mutagenesis (13); Region (2); Sequence conflict (1); Turn (2)
Keywords 3D-structure;Carboxypeptidase;Cytoplasm;Cytoskeleton;Hydrolase;Phosphoprotein;Protease;Reference proteome;Secreted
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q86V25}. Secreted {ECO:0000250|UniProtKB:Q86V25}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q86V25}. Note=Mainly localizes in the cytoplasm. Some fraction is secreted via a non-canonical secretion system; interaction with SVBP promotes secretion. Associates with microtubules (By similarity). {ECO:0000250|UniProtKB:Q86V25}.
Modified Residue MOD_RES 302; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:Q86V25
Post Translational Modification
Signal Peptide
Structure 3D X-ray crystallography (3)
Cross Reference PDB 6JZC; 6JZD; 6JZE;
Mapped Pubmed ID 12466851; 16919269; 22826464; 22967998; 24885408; 25184477; 27867016; 28960674; 29641565; 32604722;
Motif
Gene Encoded By
Mass 40,499
Kinetics
Metal Binding
Rhea ID RHEA:57444
Cross Reference Brenda