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Q00981 (UCHL1_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 118. 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 L1

Short name=UCH-L1
EC=3.4.19.12
EC=6.-.-.-
Alternative name(s):
Neuron cytoplasmic protein 9.5
PGP 9.5
Short name=PGP9.5
Ubiquitin thioesterase L1
Gene names
Name:Uchl1
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length223 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Ubiquitin-protein hydrolase involved both in the processing of ubiquitin precursors and of ubiquitinated proteins. This enzyme is a thiol protease that recognizes and hydrolyzes a peptide bond at the C-terminal glycine of ubiquitin. Also binds to free monoubiquitin and may prevent its degradation in lysosomes. The homodimer may have ATP-independent ubiquitin ligase activity 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).

Subunit structure

Monomer. Homodimer. Interacts with COPS5 By similarity. Interacts with SNCA. Ref.5

Subcellular location

Cytoplasm. Endoplasmic reticulum membrane; Lipid-anchor By similarity.

Post-translational modification

O-glycosylated. Ref.4

Miscellaneous

In contrast to UCHL3, does not hydrolyze a peptide bond at the C-terminal glycine of NEDD8 By similarity.

Sequence similarities

Belongs to the peptidase C12 family.

Ontologies

Keywords
   Biological processUbl conjugation pathway
   Cellular componentCytoplasm
Endoplasmic reticulum
Membrane
   Molecular functionHydrolase
Ligase
Protease
Thiol protease
   PTMGlycoprotein
Lipoprotein
Oxidation
Prenylation
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processadult walking behavior

Inferred from electronic annotation. Source: Ensembl

axon target recognition

Inferred from electronic annotation. Source: Ensembl

axon transport of mitochondrion

Inferred from electronic annotation. Source: Ensembl

cell proliferation

Inferred from electronic annotation. Source: Ensembl

eating behavior

Inferred from electronic annotation. Source: Ensembl

muscle fiber development

Inferred from electronic annotation. Source: Ensembl

negative regulation of MAP kinase activity

Inferred from electronic annotation. Source: Ensembl

neuromuscular process

Inferred from electronic annotation. Source: Ensembl

protein deubiquitination

Inferred from electronic annotation. Source: Ensembl

response to ischemia

Inferred from electronic annotation. Source: Ensembl

sensory perception of pain

Inferred from direct assay PubMed 11850463. Source: RGD

ubiquitin-dependent protein catabolic process

Inferred from direct assay PubMed 11850463. Source: RGD

   Cellular_componentaxon

Inferred from electronic annotation. Source: Ensembl

cytosol

Inferred from electronic annotation. Source: Ensembl

endoplasmic reticulum membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

neuronal cell body

Inferred from electronic annotation. Source: Ensembl

nucleus

Inferred from electronic annotation. Source: Ensembl

plasma membrane

Inferred from electronic annotation. Source: Ensembl

   Molecular_functioncysteine-type endopeptidase activity

Inferred from electronic annotation. Source: Ensembl

ligase activity

Inferred from electronic annotation. Source: UniProtKB-KW

omega peptidase activity

Inferred from electronic annotation. Source: Ensembl

ubiquitin thiolesterase activity

Inferred from electronic annotation. Source: Ensembl

ubiquitin-specific protease activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 220220Ubiquitin carboxyl-terminal hydrolase isozyme L1
PRO_0000211060
Propeptide221 – 2233Removed in mature form By similarity
PRO_0000414315

Regions

Region5 – 106Interaction with ubiquitin By similarity
Region151 – 1566Interaction with ubiquitin By similarity
Region211 – 2166Interaction with ubiquitin By similarity

Sites

Active site901Nucleophile By similarity
Active site1611Proton donor By similarity
Site11Susceptible to oxidation By similarity
Site61Susceptible to oxidation By similarity
Site121Susceptible to oxidation By similarity
Site1761Important for enzyme activity By similarity
Site1791Susceptible to oxidation By similarity
Site2201Susceptible to oxidation By similarity

Amino acid modifications

Lipidation2201S-farnesyl cysteine By similarity

Experimental info

Sequence conflict381T → I in BAA01541. Ref.1
Sequence conflict961I → M in BAA01541. Ref.1
Sequence conflict105 – 1073KLE → NLG in BAA01541. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q00981 [UniParc].

Last modified July 5, 2005. Version 2.
Checksum: F1402BF7B0C077EA

FASTA22324,838
        10         20         30         40         50         60 
MQLKPMEINP EMLNKVLAKL GVAGQWRFAD VLGLEEETLG SVPSPACALL LLFPLTAQHE 

        70         80         90        100        110        120 
NFRKKQIEEL KGQEVSPKVY FMKQTIGNSC GTIGLIHAVA NNQDKLEFED GSVLKQFLSE 

       130        140        150        160        170        180 
TEKLSPEDRA KCFEKNEAIQ AAHDSVAQEG QCRVDDKVNF HFILFNNVDG HLYELDGRMP 

       190        200        210        220 
FPVNHGASSE DSLLQDAAKV CREFTEREQG EVRFSAVALC KAA 

« Hide

References

« Hide 'large scale' references
[1]"cDNA cloning and tissue distribution of a rat ubiquitin carboxyl-terminal hydrolase PGP9.5."
Kajimoto Y., Hashimoto T., Shirai Y., Nishino N., Kuno T., Tanaka C.
J. Biochem. 112:28-32(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Brain.
[2]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Pituitary.
[3]Lubec G., Boddul S., Afjehi-Sadat L., Kang S.U.
Submitted (JUL-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 20-27; 84-123 AND 132-199, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: Sprague-Dawley.
Tissue: Brain and Spinal cord.
[4]"Cytosolic O-glycosylation is abundant in nerve terminals."
Cole R.N., Hart G.W.
J. Neurochem. 79:1080-1089(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION, IDENTIFICATION BY MASS SPECTROMETRY.
[5]"The UCH-L1 gene encodes two opposing enzymatic activities that affect alpha-synuclein degradation and Parkinson's disease susceptibility."
Liu Y., Fallon L., Lashuel H.A., Liu Z., Lansbury P.T. Jr.
Cell 111:209-218(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SNCA.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D10699 mRNA. Translation: BAA01541.1.
BC060573 mRNA. Translation: AAH60573.1.
PIRJX0222.
RefSeqNP_058933.2. NM_017237.3.
UniGeneRn.107213.

3D structure databases

ProteinModelPortalQ00981.
SMRQ00981. Positions 1-223.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid248179. 1 interaction.
IntActQ00981. 1 interaction.
STRING10116.ENSRNOP00000056108.

Chemistry

BindingDBQ00981.

Protein family/group databases

MEROPSC12.001.

PTM databases

PhosphoSiteQ00981.

2D gel databases

World-2DPAGE0004:Q00981.

Proteomic databases

PaxDbQ00981.
PRIDEQ00981.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000003248; ENSRNOP00000003248; ENSRNOG00000002343.
GeneID29545.
KEGGrno:29545.
UCSCRGD:3928. rat.

Organism-specific databases

CTD7345.
RGD3928. Uchl1.

Phylogenomic databases

eggNOGNOG327708.
GeneTreeENSGT00510000046640.
HOGENOMHOG000182400.
HOVERGENHBG075483.
KOK05611.
OMAKSHENGH.
OrthoDBEOG7S7SFK.
PhylomeDBQ00981.

Enzyme and pathway databases

BRENDA3.4.19.12. 5301.

Gene expression databases

GenevestigatorQ00981.

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

NextBio609557.
PROQ00981.

Entry information

Entry nameUCHL1_RAT
AccessionPrimary (citable) accession number: Q00981
Secondary accession number(s): Q6P9V8
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: July 5, 2005
Last modified: May 14, 2014
This is version 118 of the entry and version 2 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