IED ID | IndEnz0002018927 |
Enzyme Type ID | protease018927 |
Protein Name |
Cytosolic carboxypeptidase 6 EC 3.4.17.- EC 3.4.17.24 ATP/GTP-binding protein-like 4 Protein deglutamylase CCP6 |
Gene Name | Agbl4 Ccp6 |
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 | MAERSQTAPEAGNDTGNEDAIGGNVNKYIVLPNGYSGQPKKGHLTFDACFESGNLGRVEQVSDFEYDLFIRPDTCNPRFRVWFNFTVENVKELQRVIFNIVNFSKTKSLYRDGMAPMVKSTSRPKWQRLPPKNVYYYRCPDHRKNYVMSFAFCFDREDDIYQFAYCYPYTYTRFQHYLDSLQKKNMDYFFREQLGQSVQQRQLDLLTITSPENLREGSEKKVIFITGRVHPGETPSSFVCQGIIDFLVSQHPIARVLREHLVFKIAPMLNPDGVYLGNYRCSLMGFDLNRHWLDPSPWAHPTLHGVKQLIIKMYNDPKTSLEFYIDIHAHSTMMNGFMYGNIFEDEERFQRQSIFPKLLCQNAEDFSYTSTSFNRDAVKAGTGRRFLGGLLDHSSYCYTLEVSFYSYIIGGTTAAVPYTEEAYMKLGRNVARTFLDYYRLNSLVEKIAVPMPRLRSKEERRLGWEHPSCLRAEQPLEVLGIPMCSGKALNEHLGNDIQWHLDCGSSTLPLGLISCSPSSSASWNDMAMSNSILLPDHSFH |
Enzyme Length | 540 |
Uniprot Accession Number | Q09LZ8 |
Absorption | |
Active Site | ACT_SITE 280; /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:0000269|PubMed:21074048, ECO:0000269|PubMed:25103237, ECO:0000269|PubMed:26829768, ECO:0000269|PubMed:29593216};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60005; Evidence={ECO:0000305|PubMed:21074048, ECO:0000305|PubMed:25103237, ECO:0000305|PubMed:26829768, ECO:0000305|PubMed:29593216}; 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:0000269|PubMed:21074048};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63793; Evidence={ECO:0000305|PubMed:21074048}; |
DNA Binding | |
EC Number | 3.4.17.-; 3.4.17.24 |
Enzyme Function | FUNCTION: Metallocarboxypeptidase that mediates protein deglutamylation of tubulin and non-tubulin target proteins (PubMed:21074048, PubMed:25103237, PubMed:26829768, PubMed:29593216). Catalyzes the removal of polyglutamate side chains present on the gamma-carboxyl group of glutamate residues within the C-terminal tail of tubulin protein (PubMed:21074048, PubMed:25103237). Specifically cleaves tubulin long-side-chains, while it is not able to remove the branching point glutamate (PubMed:25103237). Also catalyzes the removal of polyglutamate residues from the carboxy-terminus of non-tubulin proteins such as MYLK (PubMed:21074048). Mediates the deglutamylation of nucleotidyltransferase CGAS, leading to CGAS antiviral defense response activation (PubMed:26829768). Involved in KLF4 deglutamylation which promotes KLF4 proteasome-mediated degradation, thereby negatively regulating cell pluripotency maintenance and embryogenesis (PubMed:29593216). {ECO:0000269|PubMed:21074048, ECO:0000269|PubMed:25103237, ECO:0000269|PubMed:26829768, ECO:0000269|PubMed:29593216}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Active site (1); Alternative sequence (2); Chain (1); Erroneous gene model prediction (8); Metal binding (3); Mutagenesis (2) |
Keywords | Alternative splicing;Carboxypeptidase;Cell projection;Cytoplasm;Cytoskeleton;Golgi apparatus;Hydrolase;Metal-binding;Metalloprotease;Protease;Reference proteome;Zinc |
Interact With | |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:17244818}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000250|UniProtKB:Q5VU57}. Golgi apparatus {ECO:0000250|UniProtKB:Q5VU57}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000250|UniProtKB:Q5VU57}. Note=Colocalizes with gamma-tubulin in the centrioles at interphase and dividing cells and with glutamylated tubulin in basal bodies of ciliated cells. {ECO:0000250|UniProtKB:Q5VU57}. |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | 11217851; 12466851; 16096065; 21267068; 25332286; 28794449; 30420556; |
Motif | |
Gene Encoded By | |
Mass | 62,210 |
Kinetics | |
Metal Binding | METAL 230; /note=Zinc; /evidence=ECO:0000305|PubMed:21074048; METAL 233; /note=Zinc; /evidence=ECO:0000305|PubMed:21074048; METAL 328; /note=Zinc; /evidence=ECO:0000250|UniProtKB:P00730 |
Rhea ID | RHEA:60004; RHEA:60005; RHEA:63792; RHEA:63793 |
Cross Reference Brenda |