| IED ID | IndEnz0002005873 |
| Enzyme Type ID | protease005873 |
| Protein Name |
Cytosolic carboxypeptidase 6 EC 3.4.17.- ATP/GTP-binding protein-like 4 homolog CeAGBL4 |
| Gene Name | ccpp-6 Nnac2 EEED8.6 |
| Organism | Caenorhabditis elegans |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Protostomia Ecdysozoa Nematoda (roundworms) Chromadorea Rhabditida Rhabditina Rhabditomorpha Rhabditoidea Rhabditidae Peloderinae Caenorhabditis Caenorhabditis elegans |
| Enzyme Sequence | MGYVGNVSYPDTIPGQGNLVFEASFESGNLGRVDKVSCSEYDLFIRPDTLNNKYRVWFYFECKNASENQRAIFNIVNFSKQRTLFEMGIAAPVVKSNAQNSWARIPSRHIYYYRSSQHNDRWILSFAFIFESPDPVQFAYCIPYTYGQMQIWLNELESRKYPFFHRDLLVQTVQKRRVDLITIDATPDTFQGSKKMIFLTARVHPGESPSSHVMHGIIEFLVSKDDRAQKLRKVYCFKIIPMLNPDGVFLGNYRCSLMGHDLNRMWRTPSDWAHPSIYAVKNLLTQYDNNPQAQTVIYVDLHAHSQKPNCFLYGNVNMSAVEEKSTFRQLWLPHLLADLSEDYSLEFTQFNTDVEKAGTGRRTMGDLLSCLCYTLEVSFFSYRHTDSSGNGIQHCTPYLQYKYEALGEAFCRALLNFYEADCGLREIVLERPFKTFLPARAQKTLKKQARKVIQTVMMK |
| Enzyme Length | 459 |
| Uniprot Accession Number | Q09296 |
| Absorption | |
| Active Site | ACT_SITE 254; /note=Nucleophile; /evidence=ECO:0000250|UniProtKB:P00730 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | 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:0000305|PubMed:20519502}; |
| DNA Binding | |
| EC Number | 3.4.17.- |
| Enzyme Function | FUNCTION: Metallocarboxypeptidase that catalyzes the removing of polyglutamate side chains that are present on the gamma-carboxyl group of glutamate residues of tubulin in sensory cilia (PubMed:17244817, PubMed:20519502). Probably via the deglutamylation of tubulin, promotes microtubule stability required for axon regrowth after injury (PubMed:23000142). Also regulates microtubule dynamics in uterine muscle cells (PubMed:24780738). {ECO:0000269|PubMed:17244817, ECO:0000269|PubMed:20519502, ECO:0000269|PubMed:23000142, ECO:0000269|PubMed:24780738}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (1); Metal binding (3) |
| Keywords | Carboxypeptidase;Cytoplasm;Hydrolase;Metal-binding;Metalloprotease;Protease;Reference proteome;Zinc |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q09LZ8}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 15338614; 17486083; 17850180; 21085631; 22560298; 23800452; 25487147; 26657059; 27638466; |
| Motif | |
| Gene Encoded By | |
| Mass | 53,241 |
| Kinetics | |
| Metal Binding | METAL 204; /note=Zinc; /evidence=ECO:0000250|UniProtKB:P00730; METAL 207; /note=Zinc; /evidence=ECO:0000250|UniProtKB:P00730; METAL 302; /note=Zinc; /evidence=ECO:0000250|UniProtKB:P00730 |
| Rhea ID | RHEA:60004 |
| Cross Reference Brenda | 3.4.17.24; |