Q8IKM8 · UCHL3_PLAF7
- ProteinUbiquitin carboxyl-terminal hydrolase UCHL3
- GeneUCHL3
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids232 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Thiol protease that recognizes and hydrolyzes a peptide bond at the C-terminal glycine of either ubiquitin or NEDD8 (PubMed:17371404, PubMed:20042598, PubMed:31658303).
Essential for parasite blood stage survival (PubMed:20042598).
Essential for parasite blood stage survival (PubMed:20042598).
Catalytic activity
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
301 nM | ubiquitin-AMC |
kcat is 3.2 sec-1 with ubiquitin-AMC as substrate.
Features
Showing features for site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Site | 33 | Interaction with ubiquitin | ||||
Sequence: D | ||||||
Site | 86 | Transition state stabilizer | ||||
Sequence: Q | ||||||
Active site | 92 | Nucleophile | ||||
Sequence: C | ||||||
Site | 157 | Interaction with ubiquitin | ||||
Sequence: D | ||||||
Active site | 164 | Proton donor | ||||
Sequence: H | ||||||
Site | 179 | Important for enzyme activity | ||||
Sequence: D | ||||||
Site | 219 | Interaction with ubiquitin | ||||
Sequence: S |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | ubiquitin ligase complex | |
Molecular Function | cysteine-type deubiquitinase activity | |
Molecular Function | deNEDDylase activity | |
Molecular Function | ubiquitin binding | |
Biological Process | protein deneddylation | |
Biological Process | protein deubiquitination | |
Biological Process | ubiquitin-dependent protein catabolic process |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameUbiquitin carboxyl-terminal hydrolase UCHL3
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Sar > Alveolata > Apicomplexa > Aconoidasida > Haemosporida > Plasmodiidae > Plasmodium > Plasmodium (Laverania)
Accessions
- Primary accessionQ8IKM8
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 13 | Small increase in deubiquitinating and deneddylating activities. Small reduction in deubiquitinating and deneddylating activities; when associated with E-33. | ||||
Sequence: N → D | ||||||
Mutagenesis | 33 | Small reduction in deubiquitinating and deneddylating activities. Small reduction in deubiquitinating and deneddylating activities; when associated with D-13. | ||||
Sequence: D → E | ||||||
Mutagenesis | 92 | Complete loss of deubiquitinating and deneddylating activities. | ||||
Sequence: C → A |
PTM/Processing
Features
Showing features for chain, modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000451572 | 1-232 | UniProt | Ubiquitin carboxyl-terminal hydrolase UCHL3 | |||
Sequence: MAKNDIWTPLESNPDSLYLYSCKLGQSKLKFVDIYGFNNDLLDMIPQPVQAVIFLYPVNDNIVSENNTNDKHNLKENFDNVWFIKQYIPNSCGTIALLHLYGNLRNKFELDKDSVLDDFFNKVNEMSAEKRGQELKNNKSIENLHHEFCGQVENRDDILDVDTHFIVFVQIEGKIIELDGRKDHPTVHCFTNGDNFLYDTGKIIQDKFIEKCKDDLRFSALAVIPNDNFDII | |||||||
Modified residue (large scale data) | 114 | PTMeXchange | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 127 | PTMeXchange | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 140 | PTMeXchange | Phosphoserine | ||||
Sequence: S |
Proteomic databases
Expression
Developmental stage
Expressed during the parasite blood stage, in schizonts (at protein level).
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 6-225 | UCH catalytic | ||||
Sequence: IWTPLESNPDSLYLYSCKLGQSKLKFVDIYGFNNDLLDMIPQPVQAVIFLYPVNDNIVSENNTNDKHNLKENFDNVWFIKQYIPNSCGTIALLHLYGNLRNKFELDKDSVLDDFFNKVNEMSAEKRGQELKNNKSIENLHHEFCGQVENRDDILDVDTHFIVFVQIEGKIIELDGRKDHPTVHCFTNGDNFLYDTGKIIQDKFIEKCKDDLRFSALAVIP | ||||||
Region | 10-14 | Interaction with ubiquitin | ||||
Sequence: LESNP | ||||||
Region | 151-159 | Crossover loop which restricts access of large ubiquitin adducts to the active site | ||||
Sequence: QVENRDDIL | ||||||
Region | 163-165 | Interaction with ubiquitin | ||||
Sequence: THF |
Sequence similarities
Belongs to the peptidase C12 family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length232
- Mass (Da)26,899
- Last updated2009-09-22 v2
- Checksum8B2720342B644DFF
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
LN999946 EMBL· GenBank· DDBJ | CZU00300.1 EMBL· GenBank· DDBJ | Genomic DNA |