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Q91Y78 (UCHL3_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 88. 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
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

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

Inferred from electronic annotation. Source: InterPro

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   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_0000211063

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
Q91Y78 [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: C793BEFEEB926F10

FASTA23026,124
        10         20         30         40         50         60 
MEGQRWLPLE ANPEVTNQFL KQLGLHPNWQ FVDVYGMEPE LLSMVPRPVC AVLLLFPITE 

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

       130        140        150        160        170        180 
KFLEESVAMS PEERARHLEN YDAIRVTHET SAHEGQTEAP SIDEKVDLHF IALVHVDGHL 

       190        200        210        220        230 
YELDGRKPFP INHGKTSDET LLEDAIEVCK KFMERDPDEL RFNAIALSAA 

« Hide

References

[1]"Cloning of rat UCHL3."
Osawa Y.
Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Wistar.
Tissue: Brain and Liver.
[2]Lubec G., Chen W.-Q.
Submitted (APR-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 166-186, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: Sprague-Dawley.
Tissue: Hippocampus.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB043959 mRNA. Translation: BAB47136.1.
RefSeqNP_001103635.1. NM_001110165.1.
UniGeneRn.145487.

3D structure databases

ProteinModelPortalQ91Y78.
SMRQ91Y78. Positions 2-230.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10116.ENSRNOP00000012842.

Protein family/group databases

MEROPSC12.003.

PTM databases

PhosphoSiteQ91Y78.

Proteomic databases

PaxDbQ91Y78.
PRIDEQ91Y78.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID498560.
KEGGrno:498560.

Organism-specific databases

CTD7347.
RGD621131. Uchl3.

Phylogenomic databases

eggNOGNOG327708.
HOGENOMHOG000182400.
HOVERGENHBG075483.
InParanoidQ91Y78.
KOK05609.
PhylomeDBQ91Y78.

Gene expression databases

GenevestigatorQ91Y78.

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

NextBio700167.

Entry information

Entry nameUCHL3_RAT
AccessionPrimary (citable) accession number: Q91Y78
Entry history
Integrated into UniProtKB/Swiss-Prot: July 5, 2005
Last sequence update: December 1, 2001
Last modified: April 16, 2014
This is version 88 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