Q2TBG8 (UCHL3_BOVIN) Reviewed, UniProtKB/Swiss-Prot
Last modified
April 3, 2013.
Version 51.
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 |
| ||
| Organism | Bos taurus (Bovine) [Reference proteome] | ||
| Taxonomic identifier | 9913 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos![]() |
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". 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 | mitochondrion Inferred from electronic annotation. Source: Compara nucleusInferred from electronic annotation. Source: Compara |
| 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_0000239741 | |||||
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] | NIH - Mammalian Gene Collection (MGC) project Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Crossbred X Angus. Tissue: Liver. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | BC110247 mRNA. Translation: AAI10248.1. |
| IPI | IPI00705749. |
| RefSeq | NP_001035631.1. NM_001040541.2. |
| UniGene | Bt.27926. |
3D structure databases | |
| ProteinModelPortal | Q2TBG8. |
| SMR | Q2TBG8. Positions 2-230. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 9913.ENSBTAP00000035448. |
Proteomic databases | |
| PRIDE | Q2TBG8. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| Ensembl | ENSBTAT00000035577; ENSBTAP00000035448; ENSBTAG00000008024. |
| GeneID | 520170. |
| KEGG | bta:520170. |
Organism-specific databases | |
| CTD | 7347. |
Phylogenomic databases | |
| eggNOG | NOG327708. |
| GeneTree | ENSGT00510000046640. |
| HOGENOM | HOG000182400. |
| HOVERGEN | HBG075483. |
| InParanoid | Q2TBG8. |
| KO | K05609. |
| OMA | QTEAPNI. |
| OrthoDB | EOG4HX51V. |
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... |
Other | |
| NextBio | 20873040. |
Entry information
| Entry name | UCHL3_BOVIN | ||||||||
| Accession | Primary (citable) accession number: Q2TBG8 | ||||||||
| 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
