| IED ID | IndEnz0002016583 |
| Enzyme Type ID | protease016583 |
| Protein Name |
Cytosolic carboxypeptidase 3 EC 3.4.17.- ATP/GTP-binding protein-like 3 Protein deglutamylase CCP3 |
| Gene Name | AGBL3 CCP3 |
| 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 | MSEDSEKEDYSDRTISDEDESDEDMFMKFVSEDLHRCALLTADSFGDPFFPRTTQILLEYQLGRWVPRLREPRDLYGVSSSGPLSPTRWPYHCEVIDEKVQHIDWTPSCPEPVYIPTGLETEPLYPDSKEATVVYLAEDAYKEPCFVYSRVGGNRTPLKQPVDYRDNTLMFEARFESGNLQKVVKVAEYEYQLTVRPDLFTNKHTQWYYFQVTNMRAGIVYRFTIVNFTKPASLYSRGMRPLFYSEKEAKAHHIGWQRIGDQIKYYRNNPGQDGRHYFSLTWTFQFPHNKDTCYFAHCYPYTYTNLQEYLSGINNDPVRSKFCKIRVLCHTLARNMVYILTITTPLKNSDSRKRKAVILTARVHPGETNSSWIMKGFLDYILGNSSDAQLLRDTFVFKVVPMLNPDGVIVGNYRCSLAGRDLNRNYTSLLKESFPSVWYTRNMVHRLMEKREVILYCDLHGHSRKENIFMYGCDGSDRSKTLYLQQRIFPLMLSKNCPDKFSFSACKFNVQKSKEGTGRVVMWKMGIRNSFTMEATFCGSTLGNKRGTHFSTKDLESMGYHFCDSLLDYCDPDRTKYYRCLKELEEMERHITLEKVFEDSDTPVIDITLDVESSSRGSDSSESIDSLTYLLKLTSQKKHLKTKKERNSTIASHQNARGQEVYDRGHLLQRHTQSNSDVKDTRPNEPDDYMVDYFRRQLPNQGLAHCKLRLPGSRHSPASASRVAGTTGTRHHTWLIFVFLVEMGKKIPLKGTDLYGNCFKVTSLQSPMGKQTSTWTEKTRIPTEDLHHNLKSKIKECISFQSKKTGINWTDDEKRSYKDKGIVQTQEILQYLLPIVHSTKNMQTTQIKQLFNPRTNFQIQHQLNPATCRNIKKYSTSWTAPRNHPFVIQGDVMANSSEWVQSKPHRSLESLSPLKGPKKNKHSQIWAIKNEDIKPLSSKWETASSSFGMDANVLKYKSLQAEETNQQSSKHTALHLTKNKDEQANKNDGQPTLYLKFQRES |
| Enzyme Length | 1001 |
| Uniprot Accession Number | Q8NEM8 |
| Absorption | |
| Active Site | ACT_SITE 414; /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:0000250|UniProtKB:Q8CDP0};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60005; Evidence={ECO:0000250|UniProtKB:Q8CDP0}; |
| DNA Binding | |
| EC Number | 3.4.17.- |
| 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 tubulin protein. Specifically cleaves tubulin long-side-chains, while it is not able to remove the branching point glutamate. Also catalyzes the removal of polyglutamate residues from the carboxy-terminus of non-tubulin proteins such as MYLK. May catalyze the hydrolysis of aspartate from the carboxy-terminus of target proteins. Does not show detyrosinase or deglycylase activities from the carboxy-terminus of target proteins. {ECO:0000250|UniProtKB:Q8CDP0}.; FUNCTION: [Isoform 2]: Metallocarboxypeptidase that mediates tubulin deglutamylation. {ECO:0000269|PubMed:25103237}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Alternative sequence (5); Chain (1); Metal binding (3); Natural variant (3); Region (2); Sequence conflict (2) |
| Keywords | Alternative splicing;Carboxypeptidase;Cytoplasm;Hydrolase;Metal-binding;Metalloprotease;Protease;Reference proteome;Zinc |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q8CDP0}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 17244818; 20379614; 20519502; 21074048; |
| Motif | |
| Gene Encoded By | |
| Mass | 116,011 |
| Kinetics | |
| Metal Binding | METAL 364; /note=Zinc; /evidence=ECO:0000250|UniProtKB:Q09M02; METAL 367; /note=Zinc; /evidence=ECO:0000250|UniProtKB:Q09M02; METAL 460; /note=Zinc; /evidence=ECO:0000250|UniProtKB:P00730 |
| Rhea ID | RHEA:60004; RHEA:60005 |
| Cross Reference Brenda |