Detail Information for IndEnz0002018919
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