Detail Information for IndEnz0002005862
IED ID IndEnz0002005862
Enzyme Type ID protease005862
Protein Name Cytosolic carboxypeptidase 2
EC 3.4.17.-
ATP/GTP-binding protein-like 2
Protein deglutamylase CCP2
Gene Name AGBL2 CCP2
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 MFPALETHLKQTIPDPYEDFMYRHLQYYGYFKAQRGSLPNSATHQHVRKNNPQCLLNGSLGEKDDLIPDTLQKEKLLWPISLSSAVHRQIEAINRDFHSCLGWMQWRGLSSLQPPPPRFKDSPASAFRVAGITDSHMLSLPHLRSRQLLYDELDEVNPRLREPQELFSILSTKRPLQAPRWPIECEVIKENIHHIEWAPPQPEYFYQPKGNEKVPEIVGEKKGTVVYQLDSVPIEGSYFTSSRVGGKRGIVKELAVTLQGPEDNTLLFESRFESGNLQKAVRVDTYEYELTLRTDLYTNKHTQWFYFRVQNTRKDATYRFTIVNLLKPKSLYTVGMKPLLYSQLDANTRNIGWRREGNEIKYYKNNTDDGQQPFYCLTWTIQFPYDQDTCFFAHFYPYTYTDLQCYLLSVANNPIQSQFCKLQTLCRSLAGNTVYLLTITNPSQTPQEAAAKKAVVLSARVHPGESNGSWVMKGFLDFILSNSPDAQLLRDIFVFKVLPMLNPDGVIVGNYRCSLAGRDLNRHYKTILKESFPCIWYTRNMIKRLLEEREVLLYCDFHGHSRKNNIFLYGCNNNNRKYWLHERVFPLMLCKNAPDKFSFHSCNFKVQKCKEGTGRVVMWRMGILNSYTMESTFGGSTLGNKRDTHFTIEDLKSLGYHVCDTLLDFCDPDQMKFTQCLAELKELLRQEIHKKFHELGQDVDLEGSWSDISLSDIESSTSGSDSSLSDGLPVHLANIADELTQKKKMFKKKKKKSLQTRKQRNEQYQKKNLMQKLKLTEDTSEKAGFASTLQKQPTFFKNSENSSFLPMKNENPRLNETNLNRRDKDTPLDPSMATLILPKNKGRMQNKKPGFTVSCSPKRTINSSQEPAPGMKPNWPRSRYPATKRGCAAMAAYPSLHIYTYP
Enzyme Length 902
Uniprot Accession Number Q5U5Z8
Absorption
Active Site ACT_SITE 512; /note=Nucleophile; /evidence=ECO:0000250|UniProtKB:P00730
Activity Regulation ACTIVITY REGULATION: Inhibited by RARRES1. {ECO:0000269|PubMed:21303978}.
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:Q8CDK2};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60005; Evidence={ECO:0000250|UniProtKB:Q8CDK2};
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. {ECO:0000250|UniProtKB:Q8CDK2}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (1); Alternative sequence (2); Chain (1); Compositional bias (2); Erroneous initiation (2); Erroneous termination (1); Metal binding (3); Natural variant (5); Region (2)
Keywords Alternative splicing;Carboxypeptidase;Cell projection;Cytoplasm;Cytoskeleton;Hydrolase;Metal-binding;Metalloprotease;Protease;Reference proteome;Zinc
Interact With Q8NHQ1; P17568
Induction
Subcellular Location SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q8CDK2}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000269|PubMed:23085998}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000269|PubMed:23085998}. Note=Colocalizes with gamma-tubulin in the centrioles and with glutamylated tubulin in the basal bodies of ciliated cells. {ECO:0000269|PubMed:23085998}.
Modified Residue
Post Translational Modification
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID 17244817; 17244818; 20519502; 21074048; 24884516; 25103237; 25916089; 29126912; 32307444;
Motif
Gene Encoded By
Mass 104,194
Kinetics
Metal Binding METAL 462; /note=Zinc; /evidence=ECO:0000250|UniProtKB:Q09M02; METAL 465; /note=Zinc; /evidence=ECO:0000250|UniProtKB:Q09M02; METAL 558; /note=Zinc; /evidence=ECO:0000250|UniProtKB:P00730
Rhea ID RHEA:60004; RHEA:60005
Cross Reference Brenda