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Q2TBG8 (UCHL3_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 59. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ubiquitin carboxyl-terminal hydrolase isozyme L3

Short name=UCH-L3
EC=3.4.19.12
Alternative name(s):
Ubiquitin thioesterase L3
Gene names
Name:UCHL3
OrganismBos taurus (Bovine) [Reference proteome]
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos

Protein attributes

Sequence length230 AA.
Sequence statusComplete.
Protein existenceEvidence 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 processUbl conjugation pathway
   Cellular componentCytoplasm
   Molecular functionHydrolase
Protease
Thiol protease
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processubiquitin-dependent protein catabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular_componentmitochondrion

Inferred from electronic annotation. Source: Ensembl

nucleus

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionubiquitin-specific protease activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 230230Ubiquitin carboxyl-terminal hydrolase isozyme L3
PRO_0000239741

Regions

Region8 – 136Interaction with ubiquitin By similarity
Region152 – 1598Interaction with ubiquitin By similarity
Region219 – 2246Interaction with ubiquitin By similarity

Sites

Active site951Nucleophile By similarity
Active site1691Proton donor By similarity
Site1841Important for enzyme activity By similarity

Amino acid modifications

Modified residue1301Phosphoserine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q2TBG8 [UniParc].

Last modified January 24, 2006. Version 1.
Checksum: 01D145E4352627BB

FASTA23026,182
        10         20         30         40         50         60 
MEGQRWLPLE ANPEVTNQFL KQLGLHPNWQ FVDVYGMDPE LLSMVPRPVC AVLLLFPITE 

        70         80         90        100        110        120 
KYEVFRTEEE EKIKSQGQDV TSSVYFMKQT ISNACGTIGL IHAIANNKDK MHFESGSTLK 

       130        140        150        160        170        180 
KFLEESASMS PEERARYLEN YDAIRVTHET SAHEGQTEAP NIDEKVDLHF IALVHVDGHL 

       190        200        210        220        230 
YELDGRKPFP INHGETSDET LLEDAIEVCK KFMERDPDEL RFNAIALSAA 

« Hide

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.
RefSeqNP_001035631.1. NM_001040541.2.
UniGeneBt.27926.

3D structure databases

ProteinModelPortalQ2TBG8.
SMRQ2TBG8. Positions 2-230.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9913.ENSBTAP00000035448.

Protein family/group databases

MEROPSC12.003.

Proteomic databases

PRIDEQ2TBG8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSBTAT00000035577; ENSBTAP00000035448; ENSBTAG00000008024.
GeneID520170.
KEGGbta:520170.

Organism-specific databases

CTD7347.

Phylogenomic databases

eggNOGNOG327708.
GeneTreeENSGT00510000046640.
HOGENOMHOG000182400.
HOVERGENHBG075483.
InParanoidQ2TBG8.
KOK05609.
OMAYETFRTE.
OrthoDBEOG7S7SFK.
TreeFamTF316166.

Family and domain databases

Gene3D3.40.532.10. 1 hit.
InterProIPR001578. Peptidase_C12_UCH.
[Graphical view]
PANTHERPTHR10589. PTHR10589. 1 hit.
PfamPF01088. Peptidase_C12. 1 hit.
[Graphical view]
PRINTSPR00707. UBCTHYDRLASE.
PROSITEPS00140. UCH_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio20873040.

Entry information

Entry nameUCHL3_BOVIN
AccessionPrimary (citable) accession number: Q2TBG8
Entry history
Integrated into UniProtKB/Swiss-Prot: June 13, 2006
Last sequence update: January 24, 2006
Last modified: May 14, 2014
This is version 59 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries