Detail Information for IndEnz0002014055
IED ID IndEnz0002014055
Enzyme Type ID protease014055
Protein Name Cytosolic carboxypeptidase 2
EC 3.4.17.-
ATP/GTP-binding protein-like 2
Protein deglutamylase CCP2
Gene Name Agbl2 Ccp2
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 MNVLLEMAFLSQTLPDPYEDFIHHHLQYYGYFKAQKSSLPNSGTHQRVWRNSPRYMLNGSFGERDDFISDSLEKEMLLWPTCLSSTGHAHIDAVNRDSLLLSSPLLRTRQLIFDELDEASPRLREPRELFSCFSSRGPLQAPRWPIECEVIKENIHHIEWVPHQPEYFYQPTGSEKVPEIVGEEQGTVVYQLDSVPAEGTYFTSSRIGGKRGTIKELAVTLQGPDDNTLLFESRFESGNLQKAVRVGIYEYELTLRTDLYTDKHTQWFYFRVQNTRKDATYRFTIVNLLKPKSLYAVGMKPLMYSQLDATIYNIGWRREGREIKYYKNNVDDGQQPLYCLTWTTQFPHDQDTCFFAHFYPYTYTDLQCYLLSVANNPIQSQFCKLRALCRSLAGNTVYLLTITNPSRTPQEAAAKKAVVLSARVHPGESNSSWIMNGFLDFILSNSPDAQLLRDIFVFKVIPMLNPDGVIVGNYRCSLAGRDLNRHYKTVLKDSFPCIWYTKNMIKRLLEEREVLLYCDFHGHSRKNNIFLYGCHSNNRKHWLHERVFPLMLSKNAPDKFSFDSCNFKVQKCKEGTGRVVMWRMGIINSYTMESTFGGSTLGSKRDTHFTIEDLKSLGYHVCDTLLDFCDPDQTKYTQCLQELKELLQQEINKKLNNFGQDMDLEGNWSDIPLSDIESSTSGSDSSLSDGPPIRLLNIVADEPNQKTVLKNPKKKRLQTRKQRNEQYQKSYLMRELKLTENAPGRARFVSTLQKQPTFLKSPESPSPSVRRSENPRLNETQLSGREKGTSLDPPLTSPKNKERIQSKKPGFTASCSPKRSTNSSLGPAPDVKPNWSKTRYSATRKDHATMAVYPSLHIYTYP
Enzyme Length 862
Uniprot Accession Number Q8CDK2
Absorption
Active Site ACT_SITE 475; /note=Nucleophile; /evidence=ECO:0000250|UniProtKB:P00730
Activity Regulation ACTIVITY REGULATION: Inhibited by RARRES1. {ECO:0000250}.
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:25103237};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60005; Evidence={ECO:0000305|PubMed:25103237};
DNA Binding
EC Number 3.4.17.-
Enzyme Function FUNCTION: Metallocarboxypeptidase that mediates deglutamylation of tubulin and non-tubulin target proteins (PubMed:25103237). 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: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:25103237). {ECO:0000269|PubMed:25103237}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (1); Alternative sequence (8); Chain (1); Compositional bias (3); Erroneous gene model prediction (1); Erroneous initiation (6); Metal binding (3); Mutagenesis (1); Region (3); Sequence conflict (4)
Keywords Alternative splicing;Carboxypeptidase;Cell projection;Cytoplasm;Cytoskeleton;Hydrolase;Metal-binding;Metalloprotease;Protease;Reference proteome;Zinc
Interact With
Induction INDUCTION: Up-regulated during ciliogenesis. {ECO:0000269|PubMed:25103237}.
Subcellular Location SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:17244818}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000250|UniProtKB:Q5U5Z8}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000250|UniProtKB:Q5U5Z8}. Note=Colocalizes with gamma-tubulin in the centrioles and with glutamylated tubulin in the basal bodies of ciliated cells. {ECO:0000250|UniProtKB:Q5U5Z8}.
Modified Residue
Post Translational Modification
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID 12466851; 14610273; 16602821; 16919269; 16952463; 17967808; 18799693; 21677750; 26829768; 28794449; 29593216;
Motif
Gene Encoded By
Mass 99,216
Kinetics
Metal Binding METAL 425; /note=Zinc; /evidence=ECO:0000250|UniProtKB:Q09M02; METAL 428; /note=Zinc; /evidence=ECO:0000250|UniProtKB:Q09M02; METAL 521; /note=Zinc; /evidence=ECO:0000250|UniProtKB:P00730
Rhea ID RHEA:60004; RHEA:60005
Cross Reference Brenda