Detail Information for IndEnz0002018928
IED ID IndEnz0002018928
Enzyme Type ID protease018928
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 Rattus norvegicus (Rat)
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 Rattus Rattus norvegicus (Rat)
Enzyme Sequence MELRCGGLLFSSRFDSGNLAHVEKVETVPSDGEGVGGAATAPTSGSASSPDYEFNVWTRPDCAETEYENGNRSWFYFSVRGGTPGKLIKINIMNMNKQSKLYSQGMAPFVRTLPSRPRWERIRERPTFEMTETQFVLSFVHRFVEGRGATTFFAFCYPFSYSDCQDLLSQLDQRFPENYSAHSSPLDSIYYHRELLCYSLDGLRVDLLTITSCHGLRDDREPRLEQLFPDVGTPRPFRFTGKRIFFLSSRVHPGETPSSFVFNGFLDFILRPDDPRAQTLRRLFVFKLIPMLNPDGVVRGHYRTDSRGVNLNRQYLKPDAVLHPAIYGAKAVLLYHHVHSRLNSKNPSNQQPSSLHLPPEVPLSDLEKANNLHNELHLGQSPDGENHDRWTETEPTEEKTDPVWIMPQPIPELEEPAPDAIPPKESGVAYYVDLHGHASKRGCFMYGNSFSDESTQVENMLYPKLISLNSAHFDFQGCNFSEKNMYARDRRDGQSKEGSGRVAIYKASGIIHSYTLECNYNTGRSVNSIPAACHDNGRASPPPPPTFPSRYTVELFEQVGRALAIAALDMAECNPWPRIVLSEHSSLTNLRAWMLKHVRNSRGLTSTANVGLNKKRGSRTPPKSNNGLPVSCSENALSRARSFSTGTSTGGSSSQQNSPQMKNSPSFPFHGSRPAGLPGLGSSTQKVSHRVLGPVREPRCPDRRRRQQQQQQQQQQQQQQQQQPLNQRSTTSSLAPSPTLASASPTSSRNMGSCLLPNSLSLSGSSCPFSSSGDKPEAVMVIGKSLLGAGARIPCIRTRLQTCQRRVSARRGPGFPRLGPGWAGAHRRLAEG
Enzyme Length 832
Uniprot Accession Number B2GV17
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); Chain (1); Compositional bias (5); Metal binding (3); Region (4)
Keywords Carboxypeptidase;Cytoplasm;Cytoskeleton;Hydrolase;Metal-binding;Metalloprotease;Nucleus;Protease;Reference proteome;Zinc
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q09M02}. Nucleus {ECO:0000250|UniProtKB:Q09M02}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:Q8NDL9}. Midbody {ECO:0000250|UniProtKB:Q8NDL9}. Note=Mainly cytoplasmic. Slight accumulation in the nucleus is observed. Colocalizes with alpha-tubulin in the mitotic spindle and with midbody microtubules in the intercellular bridges formed during cytokinesis. {ECO:0000250|UniProtKB:Q09M02, ECO:0000250|UniProtKB:Q8NDL9}.
Modified Residue
Post Translational Modification
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 92,554
Kinetics
Metal Binding METAL 252; /note=Zinc; /evidence=ECO:0000250|UniProtKB:Q09M02; METAL 255; /note=Zinc; /evidence=ECO:0000250|UniProtKB:Q09M02; METAL 435; /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