| IED ID | IndEnz0002005866 |
| Enzyme Type ID | protease005866 |
| Protein Name |
Cytosolic carboxypeptidase-like protein 5 EC 3.4.17.- EC 3.4.17.24 ATP/GTP-binding protein-like 5 Protein deglutamylase CCP5 |
| Gene Name | AGBL5 CCP5 |
| 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 | MELRCGGLLFSSRFDSGNLAHVEKVESLSSDGEGVGGGASALTSGIASSPDYEFNVWTRPDCAETEFENGNRSWFYFSVRGGMPGKLIKINIMNMNKQSKLYSQGMAPFVRTLPTRPRWERIRDRPTFEMTETQFVLSFVHRFVEGRGATTFFAFCYPFSYSDCQELLNQLDQRFPENHPTHSSPLDTIYYHRELLCYSLDGLRVDLLTITSCHGLREDREPRLEQLFPDTSTPRPFRFAGKRIFFLSSRVHPGETPSSFVFNGFLDFILRPDDPRAQTLRRLFVFKLIPMLNPDGVVRGHYRTDSRGVNLNRQYLKPDAVLHPAIYGAKAVLLYHHVHSRLNSQSSSEHQPSSCLPPDAPVSDLEKANNLQNEAQCGHSADRHNAEAWKQTEPAEQKLNSVWIMPQQSAGLEESAPDTIPPKESGVAYYVDLHGHASKRGCFMYGNSFSDESTQVENMLYPKLISLNSAHFDFQGCNFSEKNMYARDRRDGQSKEGSGRVAIYKASGIIHSYTLECNYNTGRSVNSIPAACHDNGRASPPPPPAFPSRYTVELFEQVGRAMAIAALDMAECNPWPRIVLSEHSSLTNLRAWMLKHVRNSRGLSSTLNVGVNKKRGLRTPPKSHNGLPVSCSENTLSRARSFSTGTSAGGSSSSQQNSPQMKNSPSFPFHGSRPAGLPGLGSSTQKVTHRVLGPVREPRSQDRRRQQQPLNHRPAGSLAPSPAPTSSGPASSHKLGSCLLPDSFNIPGSSCSLLSSGDKPEAVMVIGKGLLGTGARMPCIKTRLQARPRLGRGSPPTRRGMKGSSGPTSPTPRTRESSELELGSCSATPGLPQARPPRPRSAPAFSPISCSLSDSPSWNCYSRGPLGQPEVCFVPKSPPLTVSPRV |
| Enzyme Length | 886 |
| Uniprot Accession Number | Q8NDL9 |
| Absorption | |
| Active Site | ACT_SITE 303; /note=Nucleophile; /evidence=ECO:0000250|UniProtKB:P00730 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=gamma-L-glutamyl-L-glutamyl-[protein] + H2O = L-glutamate + L-glutamyl-[protein]; Xref=Rhea:RHEA:60152, Rhea:RHEA-COMP:10208, Rhea:RHEA-COMP:15517, ChEBI:CHEBI:15377, ChEBI:CHEBI:29973, ChEBI:CHEBI:29985, ChEBI:CHEBI:143622; Evidence={ECO:0000250|UniProtKB:Q09M02};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60153; Evidence={ECO:0000250|UniProtKB:Q09M02}; 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:Q09M02};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60005; Evidence={ECO:0000250|UniProtKB:Q09M02}; CATALYTIC ACTIVITY: Reaction=C-terminal L-alpha-aminoacyl-L-glutamyl-[tubulin] + H2O = C-terminal L-alpha-aminoacyl-[tubulin] + L-glutamate; Xref=Rhea:RHEA:63796, Rhea:RHEA-COMP:16436, Rhea:RHEA-COMP:16437, ChEBI:CHEBI:15377, ChEBI:CHEBI:29985, ChEBI:CHEBI:90782, ChEBI:CHEBI:149556; EC=3.4.17.24; Evidence={ECO:0000250|UniProtKB:Q09M02};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63797; Evidence={ECO:0000250|UniProtKB:Q09M02}; 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:Q09M02};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63793; Evidence={ECO:0000250|UniProtKB:Q09M02}; |
| DNA Binding | |
| EC Number | 3.4.17.-; 3.4.17.24 |
| 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 alpha- and beta-tubulin. Cleaves alpha- and gamma-linked polyglutamate tubulin side-chain, as well as the branching point glutamate. Also catalyzes the removal of alpha-linked glutamate residues from the carboxy-terminus of alpha-tubulin. Mediates deglutamylation of nucleotidyltransferase CGAS, leading to CGAS antiviral defense response activation. {ECO:0000250|UniProtKB:Q09M02}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Alternative sequence (4); Chain (1); Compositional bias (4); Erroneous gene model prediction (2); Erroneous initiation (1); Metal binding (3); Modified residue (1); Natural variant (8); Region (3); Sequence conflict (4) |
| Keywords | Alternative splicing;Carboxypeptidase;Cytoplasm;Cytoskeleton;Disease variant;Hydrolase;Metal-binding;Metalloprotease;Nucleus;Phosphoprotein;Protease;Reference proteome;Retinitis pigmentosa;Zinc |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q09M02}. Nucleus {ECO:0000269|PubMed:23085998}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:23085998}. Midbody {ECO:0000269|PubMed:23085998}. Note=Mainly cytoplasmic. Slight accumulation in the nucleus is observed (By similarity). Colocalizes with alpha-tubulin in the mitotic spindle and with midbody microtubules in the intercellular bridges formed during cytokinesis. {ECO:0000250|UniProtKB:Q09M02, ECO:0000269|PubMed:23085998}. |
| Modified Residue | MOD_RES 841; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:Q09M02 |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 17244817; 17244818; 19913121; 20467438; 20519502; 20628086; 21074048; 25103237; 30925032; |
| Motif | |
| Gene Encoded By | |
| Mass | 97,534 |
| Kinetics | |
| Metal Binding | METAL 252; /note=Zinc; /evidence=ECO:0000250|UniProtKB:Q09M02; METAL 255; /note=Zinc; /evidence=ECO:0000250|UniProtKB:Q09M02; METAL 434; /note=Zinc; /evidence=ECO:0000250|UniProtKB:P00730 |
| Rhea ID | RHEA:60152; RHEA:60153; RHEA:60004; RHEA:60005; RHEA:63796; RHEA:63797; RHEA:63792; RHEA:63793 |
| Cross Reference Brenda | 3.4.17.24; |