IED ID | IndEnz0002014208 |
Enzyme Type ID | protease014208 |
Protein Name |
AMSH-like ubiquitin thioesterase 3 EC 3.4.19.- Deubiquitinating enzyme AMSH3 |
Gene Name | AMSH3 At4g16144 FCAALL |
Organism | Arabidopsis thaliana (Mouse-ear cress) |
Taxonomic Lineage | cellular organisms Eukaryota Viridiplantae Streptophyta Streptophytina Embryophyta Tracheophyta Euphyllophyta Spermatophyta Magnoliopsida Mesangiospermae eudicotyledons Gunneridae Pentapetalae rosids malvids Brassicales Brassicaceae Camelineae Arabidopsis Arabidopsis thaliana (Mouse-ear cress) |
Enzyme Sequence | MKIDLNKVAREIEVDNRIPLRNYYRIADNLLRQASIYREEKNVVDLYIMLLRYSSLISETIPFHRDYQASLPQERLGSRKRLRAVINELESLKPEFNQLVDKLNRVEDESRQDGSDLPVVSYSSDAVEWPPAHKASYSRPDINKPLPTSQPSWTYNNNLTSSSNRTQIDQQFQKLSFDFLPPNQATLSRHSFLGPNGLKRQMVAPKSEIKVQYPSNTDWGSADNSGLIEAGPSSSSASLNGDSQEVSTLNSVLSLDDGRWQRHSEAVNSQFISDATEDPFQFVGMKQPSPPPVLAQVHQELAQICPSKVADPRPGPAIPSLEGKEGSNSYQHLHVPVRIMDDFLRLARSNTERNLETCGVLAGSLKNRVFHITTLIIPKQESTSDSCQTLNEEEIFEVQDRLSLFPLGWIHTHPTQTCFMSSVDLHTHYSYQIMLPEAVAIVMAPTDESTPHGIFHLSDPSGVSVIRNCQQRGFHPHEESEDGNPIYEHCSHVFLNAKLKYEVLDLR |
Enzyme Length | 507 |
Uniprot Accession Number | Q5PNU3 |
Absorption | |
Active Site | |
Activity Regulation | |
Binding Site | |
Calcium Binding | |
catalytic Activity | |
DNA Binding | |
EC Number | 3.4.19.- |
Enzyme Function | FUNCTION: Zinc metalloprotease that cleaves 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains, but is not implicated in protein degradation by the 26S proteasome, deneddylation, or desumoylation. Required for intracellular trafficking (e.g. trafficking from the Golgi to the vacuole and the vacuolar trafficking of endocytosed cargo), endocytosis and vacuole biogenesis. {ECO:0000269|PubMed:20543027}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Chain (1); Coiled coil (1); Compositional bias (1); Domain (1); Frameshift (2); Metal binding (7); Motif (1); Mutagenesis (1); Region (2); Sequence conflict (2); Site (1) |
Keywords | Coiled coil;Cytoplasm;Endocytosis;Endosome;Hydrolase;Membrane;Metal-binding;Metalloprotease;Protease;Protein transport;Reference proteome;Transport;Ubl conjugation pathway;Vacuole;Zinc |
Interact With | |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:20543027}; Peripheral membrane protein {ECO:0000269|PubMed:20543027}. Cytoplasm {ECO:0000269|PubMed:26324913, ECO:0000305|PubMed:20543027}. Vacuole membrane {ECO:0000305|PubMed:20543027}; Peripheral membrane protein {ECO:0000305|PubMed:20543027}. Late endosome {ECO:0000269|PubMed:26324913}. Note=Localized in late endosome when associated with BRO1/ALIX. {ECO:0000269|PubMed:26324913}. |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | 21810997; 23800962; 24486765; 28784794; 30018157; 30485803; 30690193; |
Motif | MOTIF 411..424; /note=JAMM motif; /evidence=ECO:0000255|PROSITE-ProRule:PRU01182 |
Gene Encoded By | |
Mass | 57,268 |
Kinetics | |
Metal Binding | METAL 411; /note=Zinc 1; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU01182; METAL 413; /note=Zinc 1; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU01182; METAL 424; /note=Zinc 1; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU01182; METAL 426; /note=Zinc 2; /evidence=ECO:0000250; METAL 469; /note=Zinc 2; /evidence=ECO:0000250; METAL 475; /note=Zinc 2; /evidence=ECO:0000250; METAL 477; /note=Zinc 2; /evidence=ECO:0000250 |
Rhea ID | |
Cross Reference Brenda |