UniProt ID: A0A0R4IYD6 |
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:0000256|ARBA:ARBA00029302}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60005; Evidence={ECO:0000256|ARBA:ARBA00029302}; SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000256|ARBA:ARBA00004514}. SIMILARITY: Belongs to the peptidase M14 family. {ECO:0000256|ARBA:ARBA00005988}. |
UniProt ID: A0A8M6Z500 |
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:0000256|ARBA:ARBA00029302}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60005; Evidence={ECO:0000256|ARBA:ARBA00029302}; SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000256|ARBA:ARBA00004514}. SIMILARITY: Belongs to the peptidase M14 family. {ECO:0000256|ARBA:ARBA00005988}. |
UniProt ID: A6H8T7 |
FUNCTION: Metallocarboxypeptidase that mediates deglutamylation of target proteins. Catalyzes the deglutamylation of polyglutamate side chains generated by post-translational polyglutamylation in proteins such as tubulins. Also removes gene-encoded polyglutamates from the carboxy-terminus of target proteins such as MYLK. Does not show detyrosinase or deglycylase activities from the carboxy-terminus of tubulin. {ECO:0000250|UniProtKB:Q8CDK2}. 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. {ECO:0000250|UniProtKB:Q8CDK2}. 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}; COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; Note=Binds 1 zinc ion per subunit. {ECO:0000250}; SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q8CDK2}. 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}. SIMILARITY: Belongs to the peptidase M14 family. {ECO:0000305}. CAUTION: Was originally thought to have detyrosinating activity from C- terminal positions on tubulin. {ECO:0000250|UniProtKB:Q5U5Z8}. |
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