Q06AB3 (UCHL3_PIG) Reviewed, UniProtKB/Swiss-Prot
Last modified
March 6, 2013.
Version 33.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Ubiquitin carboxyl-terminal hydrolase isozyme L3 Short name=UCH-L3 EC=3.4.19.12 Alternative name(s): Ubiquitin thioesterase L3 | ||
| Gene names |
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| Organism | Sus scrofa (Pig) [Reference proteome] | ||
| Taxonomic identifier | 9823 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Suina › Suidae › Sus![]() |
Protein attributes
| Sequence length | 230 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at transcript level |
General annotation (Comments)
| Function | Deubiquitinating enzyme (DUB) that controls levels of cellular ubiquitin through processing of ubiquitin precursors and ubiquitinated proteins. Thiol protease that recognizes and hydrolyzes a peptide bond at the C-terminal glycine of either ubiquitin or NEDD8. Has a 10-fold preference for Arg and Lys at position P3, and exhibits a preference towards 'Lys-48'-linked Ubiquitin chains". Deubiquitinates ENAC in apical compartments, thereby regulating apical membrane recycling. Indirectly increases the phosphorylation of IGFIR, AKT and FOXO1 and promotes insulin-signaling and insulin-induced adipogenesis. Required for stress-response retinal, skeletal muscle and germ cell maintenance. May be involved in working memory. Can hydrolyze UBB(+1), a mutated form of ubiquitin which is not effectively degraded by the proteasome By similarity. |
| Catalytic activity | Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal). |
| Enzyme regulation | Inhibited by monoubiquitin and diubiquitin By similarity. |
| Subunit structure | Preferentially binds diubiquitin; the interaction does not hydrolyze diubiquitin but, in vitro, inhibits the hydrolyzing activity on other substrates By similarity. |
| Subcellular location | Cytoplasm By similarity. |
| Sequence similarities | Belongs to the peptidase C12 family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Ubl conjugation pathway |
| Cellular component | Cytoplasm |
| Molecular function | Hydrolase Protease Thiol protease |
| PTM | Phosphoprotein |
| Technical term | Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological_process | ubiquitin-dependent protein catabolic process Inferred from electronic annotation. Source: InterPro |
| Cellular_component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular_function | cysteine-type peptidase activity Inferred from electronic annotation. Source: UniProtKB-KW ubiquitin thiolesterase activityInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 230 | 230 | Ubiquitin carboxyl-terminal hydrolase isozyme L3 | PRO_0000289800 | |||||
Regions | |||||||||
| Region | 8 – 13 | 6 | Interaction with ubiquitin By similarity | ||||||
| Region | 152 – 159 | 8 | Interaction with ubiquitin By similarity | ||||||
| Region | 219 – 224 | 6 | Interaction with ubiquitin By similarity | ||||||
Sites | |||||||||
| Active site | 95 | 1 | Nucleophile By similarity | ||||||
| Active site | 169 | 1 | Proton donor By similarity | ||||||
| Site | 184 | 1 | Important for enzyme activity By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 130 | 1 | Phosphoserine By similarity | ||||||
Sequences
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References
| [1] | Liu G.Y. Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | DQ972951 mRNA. Translation: ABI96187.1. |
| RefSeq | NP_001070695.1. NM_001077227.1. |
| UniGene | Ssc.13668. |
3D structure databases | |
| ProteinModelPortal | Q06AB3. |
| SMR | Q06AB3. Positions 2-230. |
| ModBase | Search... |
Protein family/group databases | |
| MEROPS | C12.003. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 768115. |
| KEGG | ssc:768115. |
Organism-specific databases | |
| CTD | 7347. |
Phylogenomic databases | |
| HOVERGEN | HBG075483. |
| KO | K05609. |
Enzyme and pathway databases | |
| BRENDA | 3.4.19.12. 6170. |
Family and domain databases | |
| Gene3D | 3.40.532.10. 1 hit. |
| InterPro | IPR001578. Peptidase_C12. [Graphical view] |
| PANTHER | PTHR10589. PTHR10589. 1 hit. |
| Pfam | PF01088. Peptidase_C12. 1 hit. [Graphical view] |
| PRINTS | PR00707. UBCTHYDRLASE. |
| PROSITE | PS00140. UCH_1. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | UCHL3_PIG | ||||||||
| Accession | Primary (citable) accession number: Q06AB3 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
Relevant documents
| Peptidase families Classification of peptidase families and list of entries |
| SIMILARITY comments Index of protein domains and families |

Clusters with
