| IED ID | IndEnz0002018919 |
| Enzyme Type ID | protease018919 |
| Protein Name |
Cytosolic carboxypeptidase 1 EC 3.4.17.- EC 3.4.17.24 ATP/GTP-binding protein 1 Protein deglutamylase CCP1 |
| Gene Name | agtpbp1 ccp1 |
| Organism | Xenopus laevis (African clawed frog) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amphibia Batrachia Anura Pipoidea Pipidae Xenopodinae Xenopus Xenopus Xenopus laevis (African clawed frog) |
| Enzyme Sequence | MSKVKATAEKCQLNISRIQSLLSQLEKVNAESLLFDTDNTRYVTAKIFHLAQTQEKTRKEMTAKGSTGIEVILCTLENTRDLQTILNILNILNELASTAGGRRINALISKGGARILLQLLLSASKESPSNEELMIVLHSLLAKLGPKDKKFGVKARVSGALNISLNLVKQNLQNPRLILPCLQVLRVCCMNSVNSAYLGKNGAVEILFKIIGPFTRRNTGLIKVSLDTLAALLKSRTNARKAVDRAYVQTLISTYMDWHRHDTRHRHMLIRKGILQCLKSITNIKIGRKAFIDANGMKTLYNTSQECQAVRTLDPLVNTSSLIMRKCFPKNRLPLPTIKSAFQFQLPFMPTSGPVALLYSMPPEVDDVVDESDDNEDTDAETEAEAENEDSDQICKNDDIETDITKLIPGQELGRTLEDLKMYERFFPELTEDFQEFDLVSNEPKPGAKLGPIIVPTAGEEQPEVPNNFMKNLARRSCNISLEDESNQRPTFLDMSKNVTNKGNSLDQKVHVDKDGSCYYYSNDIVRDLEKLSLHKASGNHPCRNGCVSAKDKPNFLPHPCNKSTSSSISCSNSLFEKHSMHLGPLCCSGIAPDDDESSPLDEQVMREMTDFDSILPLHDPDLYIEIVKNTKSVPEYTEVAYPDYFGHVPPFFKERLLERPYGVQRSKIFQDIERMIHPNDIIDRVIYDLDNPSCSAHDEIDILKFNSKFESGNLRKVIQIRKNEYDLILNSDINSNHYHQWFYFEVSGMRTGVAYRFNIINCEKSNSQFNYGMQPLMYSVQEALASRPWWYRVGTDICYYKNHFSRSSLATGGQKGKSYYTITFTVTFPHKDDVCYFAYHYPYTYSTLKMHLQKLESLHSPQQIYFRQEVLCETLGGNGCPVITITAMPESNYYEHVYQFRNRPYIFLTSRVHPGETNASWVMKGTLEFLMGSSATAQSLRESYIFKIVPMLNPDGVINGNHRCSLSGEDLNRQWQNPNSDLHPTIYHTKGLLQYLSAIKRVPLVYCDYHGHSRKKNVFMYGCSIKETVWHTNANAASCDMVEESGYKTLPKVLNQIAPAFSMSSCSFVVEKSKESTARVVVWKEIGVQRSYTMESTLCGCDQGKYKDLQIGTKELEEMGAKFCVGLLRLKRLTSPMELTLPPSLIDIENELIESSCKVASPTTYVLEDDEPRFIEEVDYSAESNDDVDPDLPENIGDFETSTLEEESFSDSEITRTHMSGQST |
| Enzyme Length | 1225 |
| Uniprot Accession Number | Q6DD21 |
| Absorption | |
| Active Site | ACT_SITE 964; /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:Q641K1};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60005; Evidence={ECO:0000250|UniProtKB:Q641K1}; 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:Q641K1};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63793; Evidence={ECO:0000250|UniProtKB:Q641K1}; |
| 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. 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. 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 alpha-tubulin as well as non-tubulin proteins. {ECO:0000250|UniProtKB:Q641K1}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (1); Compositional bias (2); Metal binding (3); Region (2) |
| Keywords | Carboxypeptidase;Cytoplasm;Hydrolase;Metal-binding;Metalloprotease;Mitochondrion;Nucleus;Protease;Zinc |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9UPW5}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q641K1}. Nucleus {ECO:0000250|UniProtKB:Q641K1}. Mitochondrion {ECO:0000250|UniProtKB:Q641K1}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 138,782 |
| Kinetics | |
| Metal Binding | METAL 914; /note=Zinc; /evidence=ECO:0000250|UniProtKB:Q09M02; METAL 917; /note=Zinc; /evidence=ECO:0000250|UniProtKB:Q09M02; METAL 1011; /note=Zinc; /evidence=ECO:0000250|UniProtKB:P00730 |
| Rhea ID | RHEA:60004; RHEA:60005; RHEA:63792; RHEA:63793 |
| Cross Reference Brenda |