| IED ID | IndEnz0002016601 |
| Enzyme Type ID | protease016601 |
| Protein Name |
Cytosolic carboxypeptidase-like protein 5 EC 3.4.17.- EC 3.4.17.24 ATP/GTP-binding protein-like 5 Protein deglutamylase CCP5 |
| Gene Name | agbl5 ccp5 zgc:91997 |
| Organism | Danio rerio (Zebrafish) (Brachydanio rerio) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Actinopterygii Actinopteri Neopterygii Teleostei Osteoglossocephalai Clupeocephala Otomorpha Ostariophysi Otophysi Cypriniphysae Cypriniformes (carps and others) Cyprinoidei Danionidae Danioninae Danio Danio rerio (Zebrafish) (Brachydanio rerio) |
| Enzyme Sequence | MEIRVGSAVFSSRFDSGNLARVERVEASEAAGESSRSASVPQPDYEFNVWTRPDCASTEFENGNRSWFYFSVRGLLPGKLLKINMMNMNKQSKLYTQGMAPFVRTLPVKTRWERVRDRPTFEMSDSQFILSFVHRLLDVRGVTTYFSFCYPFSYAECQDMMLQLDHKFLSSTSTHTACSPPESIYYHRELLCHSLDGHRVDLITVSSCHGLLEEREPRLDKLFPDLSTARSHRFTGKRVFFVSSRVHPGETPSSFVFNGFLNFILSQEDPRAQTLRRMFVFKLIPMLNPDGVVRGHYRTDSRGVNLNRQYVNPSPDLHPSIYGAKSLLLYHHIHNRLGHASGSALKTSNQSNTSPPVATPTERERCMNLRNEAERGEGPTFDLSEIPMQLEESWEKSGVQREAEHSDENESAQSRGETNSAPSEQVPPQESGVAYYIDLHGHASKRGCFMYGNNLTEESQQVENMLYAKLISLNCAHFDFLGCNFSEKNMYARDKRDGQSKEGSGRVAIHKAIGLVHSYTLECNYNTGRSVNTIPPACHDNGRATPPPPPAFPPKYTPEVYEQVGRAVAVAALDMAECNPWPRLVLSEHSSLLNLRASILKHVRNSTGLTSNNRRNTHCKTSSSPPKPVSLSTSASENSLNRTRSTTNVQGSRQTPQLKSSPSFTFGTTAHRPSHRSLGPVRECKAQEKRRPPPPPLPHHHHQQHQRLSVRLSAPVRAPLSPSSSSSSSSSSPSSSSSAPGPGSISLAGNSCPEFRPANQIKELRGGRGKGGRSGPAYCHSSQQRTALTTKEPLQDSLDILTSIEYSRCELQPRPSRIPVRRELQSSVIPLSSTETPTMRVWKLIKPGLKKHLAGVSGKDRLSTKALLKNSSRQTDQHIHRSLPT |
| Enzyme Length | 885 |
| Uniprot Accession Number | Q68EI3 |
| Absorption | |
| Active Site | ACT_SITE 298; /note=Nucleophile; /evidence=ECO:0000250|UniProtKB:P00730 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=gamma-L-glutamyl-L-glutamyl-[protein] + H2O = L-glutamate + L-glutamyl-[protein]; Xref=Rhea:RHEA:60152, Rhea:RHEA-COMP:10208, Rhea:RHEA-COMP:15517, ChEBI:CHEBI:15377, ChEBI:CHEBI:29973, ChEBI:CHEBI:29985, ChEBI:CHEBI:143622; Evidence={ECO:0000250|UniProtKB:Q09M02};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60153; Evidence={ECO:0000250|UniProtKB:Q09M02}; CATALYTIC ACTIVITY: Reaction=(L-glutamyl)(n+1)-gamma-L-glutamyl-L-glutamyl-[protein] + H2O = (L-glutamyl)(n)-gamma-L-glutamyl-L-glutamyl-[protein] + L-glutamate; Xref=Rhea:RHEA:60004, Rhea:RHEA-COMP:15519, Rhea:RHEA-COMP:15675, ChEBI:CHEBI:15377, ChEBI:CHEBI:29985, ChEBI:CHEBI:143623; Evidence={ECO:0000250|UniProtKB:Q09M02};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60005; Evidence={ECO:0000250|UniProtKB:Q09M02}; CATALYTIC ACTIVITY: Reaction=C-terminal L-alpha-aminoacyl-L-glutamyl-[tubulin] + H2O = C-terminal L-alpha-aminoacyl-[tubulin] + L-glutamate; Xref=Rhea:RHEA:63796, Rhea:RHEA-COMP:16436, Rhea:RHEA-COMP:16437, ChEBI:CHEBI:15377, ChEBI:CHEBI:29985, ChEBI:CHEBI:90782, ChEBI:CHEBI:149556; EC=3.4.17.24; Evidence={ECO:0000250|UniProtKB:Q09M02};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63797; Evidence={ECO:0000250|UniProtKB:Q09M02}; CATALYTIC ACTIVITY: Reaction=C-terminal L-alpha-aminoacyl-L-glutamyl-L-glutamyl-[tubulin] + H2O = C-terminal L-alpha-aminoacyl-L-glutamyl-[tubulin] + L-glutamate; Xref=Rhea:RHEA:63792, Rhea:RHEA-COMP:16435, Rhea:RHEA-COMP:16436, ChEBI:CHEBI:15377, ChEBI:CHEBI:29985, ChEBI:CHEBI:149555, ChEBI:CHEBI:149556; EC=3.4.17.24; Evidence={ECO:0000250|UniProtKB:Q09M02};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63793; Evidence={ECO:0000250|UniProtKB:Q09M02}; |
| DNA Binding | |
| EC Number | 3.4.17.-; 3.4.17.24 |
| Enzyme Function | FUNCTION: Metallocarboxypeptidase that mediates deglutamylation of tubulin and non-tubulin target proteins. Catalyzes the removal of polyglutamate side chains present on the gamma-carboxyl group of glutamate residues within the C-terminal tail of alpha- and beta-tubulin. Cleaves alpha- and gamma-linked polyglutamate tubulin side-chain, as well as the branching point glutamate. Also catalyzes the removal of alpha-linked glutamate residues from the carboxy-terminus of alpha-tubulin. {ECO:0000250|UniProtKB:Q09M02}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (1); Compositional bias (6); Metal binding (3); Region (4) |
| Keywords | Carboxypeptidase;Cytoplasm;Cytoskeleton;Hydrolase;Metal-binding;Metalloprotease;Nucleus;Protease;Reference proteome;Zinc |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q09M02}. Nucleus {ECO:0000250|UniProtKB:Q09M02}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:Q8NDL9}. Midbody {ECO:0000250|UniProtKB:Q8NDL9}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 24022483; 24743595; |
| Motif | |
| Gene Encoded By | |
| Mass | 98,709 |
| Kinetics | |
| Metal Binding | METAL 247; /note=Zinc; /evidence=ECO:0000250|UniProtKB:Q09M02; METAL 250; /note=Zinc; /evidence=ECO:0000250|UniProtKB:Q09M02; METAL 440; /note=Zinc; /evidence=ECO:0000250|UniProtKB:P00730 |
| Rhea ID | RHEA:60152; RHEA:60153; RHEA:60004; RHEA:60005; RHEA:63796; RHEA:63797; RHEA:63792; RHEA:63793 |
| Cross Reference Brenda | 3.4.17.24; |