| IED ID | IndEnz0002009725 |
| Enzyme Type ID | protease009725 |
| Protein Name |
AMSH-like protease sst2 EC 3.4.19.- Suppressor of ste12 deletion protein 2 |
| Gene Name | sst2 SPAC19B12.10 |
| Organism | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota Taphrinomycotina Schizosaccharomycetes Schizosaccharomycetales Schizosaccharomycetaceae Schizosaccharomyces Schizosaccharomyces pombe (Fission yeast) Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
| Enzyme Sequence | MNILQGSEAPLSYEEIASRAGAFDFNKNIPLKNWLRTSTTISKQAHVYVSEHDYSNGVFLLFRYCELFMKCQKHPDAAAYKKELFDYYQGVRNALEEIELIKPIVKEQYEQYQCQKNDLDDLKKLSMKDSQPSLEKPVSYVDEPILEQWALSDLQILPPSSTDLLSPDSQKLSKSSSDLPQFDYPSLNSSPTFNSNLPISSSRFEKTSLSDSKLVSPEPLDDNKDIQFIKKPIYTRTSEPRPKPAGTFKIHAYTEGGKPLRTIYLPKLLKKVFLDVVKPNTKKNLETCGILCGKLRQNAFFITHLVIPLQEATSDTCGTTDEASLFEFQDKHNLLTLGWIHTHPTQTCFMSSVDLHTHCSYQLMLPEAIAIVMAPSKNTSGIFRLLDPEGLQTIVKCRKPGLFHPHEGKVYTMVAQPGHVREINSKLQVVDLRVK |
| Enzyme Length | 435 |
| Uniprot Accession Number | Q9P371 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.19.- |
| Enzyme Function | FUNCTION: Zinc metalloprotease that specifically cleaves 'Lys-63'-linked polyubiquitin chains. Does not cleave 'Lys-48'-linked polyubiquitin chains (By similarity). Plays a role in the multivesicular body (MVB) sorting pathway. Required for ubiquitin-dependent sorting of proteins into the endosome and subsequent trafficking to the vacuole. May regulate MVB sorting through deubiquitination of ubiquitinated ESCRT proteins. {ECO:0000250, ECO:0000269|PubMed:17660439}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Beta strand (13); Chain (1); Domain (1); Helix (4); Metal binding (7); Modified residue (1); Motif (1); Region (1); Site (1); Turn (2) |
| Keywords | 3D-structure;Cytoplasm;Endosome;Hydrolase;Metal-binding;Metalloprotease;Phosphoprotein;Protease;Reference proteome;Ubl conjugation pathway;Zinc |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Endosome {ECO:0000269|PubMed:16823372}. |
| Modified Residue | MOD_RES 192; /note=Phosphothreonine; /evidence=ECO:0000269|PubMed:18257517 |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (14) |
| Cross Reference PDB | 4JXE; 4K1R; 4MS7; 4MSD; 4MSJ; 4MSM; 4MSQ; 4NQL; 4PQT; 4ZD4; 4ZD5; 4ZFR; 4ZFT; 7LM3; |
| Mapped Pubmed ID | 17951524; 18684775; 19264558; 20473289; 21182284; 21712547; 21850271; 22194353; 23093943; 23697806; 24787148; 25720772; 26365378; 26368668; 26412298; 30726745; 34100774; 34250083; |
| Motif | MOTIF 341..354; /note=JAMM motif; /evidence=ECO:0000255|PROSITE-ProRule:PRU01182 |
| Gene Encoded By | |
| Mass | 49,349 |
| Kinetics | |
| Metal Binding | METAL 341; /note=Zinc 1; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU01182; METAL 343; /note=Zinc 1; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU01182; METAL 354; /note=Zinc 1; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU01182; METAL 356; /note=Zinc 2; /evidence=ECO:0000250; METAL 397; /note=Zinc 2; /evidence=ECO:0000250; METAL 404; /note=Zinc 2; /evidence=ECO:0000250; METAL 406; /note=Zinc 2; /evidence=ECO:0000250 |
| Rhea ID | |
| Cross Reference Brenda |