Q91Y78 (UCHL3_RAT) Reviewed, UniProtKB/Swiss-Prot

Names 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

Name:

Uchl3

Organism

Rattus norvegicus (Rat) [Reference proteome]

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	230 AA.
Sequence status	Complete.
Protein existence	Evidence 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 process	Ubl conjugation pathway
Cellular component	Cytoplasm
Molecular function	Hydrolase Protease Thiol protease
PTM	Phosphoprotein
Technical term	Complete proteome Direct protein sequencing 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 activity Inferred 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_0000211063
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

	Sequence		Length	Mass (Da)
	Q91Y78 [UniParc]. Last modified December 1, 2001. Version 1. Checksum: C793BEFEEB926F10	FASTA	230	26,124
	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

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, MASS SPECTROMETRY. Strain: Sprague-Dawley. Tissue: Hippocampus.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AB043959 mRNA. Translation: BAB47136.1.
IPI	IPI00208286.
RefSeq	NP_001103635.1. NM_001110165.1.
UniGene	Rn.145487.
3D structure databases
ProteinModelPortal	Q91Y78.
SMR	Q91Y78. Positions 2-230.
ModBase	Search...
Protein-protein interaction databases
STRING	10116.ENSRNOP00000012842.
Protein family/group databases
MEROPS	C12.003.
PTM databases
PhosphoSite	Q91Y78.
Proteomic databases
PaxDb	Q91Y78.
PRIDE	Q91Y78.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	498560.
KEGG	rno:498560.
Organism-specific databases
CTD	7347.
RGD	621131. Uchl3.
Phylogenomic databases
eggNOG	NOG327708.
HOGENOM	HOG000182400.
HOVERGEN	HBG075483.
InParanoid	Q91Y78.
KO	K05609.
OMA	QTEAPNI.
Gene expression databases
ArrayExpress	Q91Y78.
Genevestigator	Q91Y78.
GermOnline	ENSRNOG00000006401. Rattus norvegicus.
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	700167.

Entry information

Entry name

UCHL3_RAT

Accession

Primary (citable) accession number: Q91Y78

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 5, 2005
Last sequence update:	December 1, 2001
Last modified:	April 3, 2013
This is version 81 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program