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Ubiquitin carboxyl-terminal hydrolase isozyme L3 (UCH-L3) (EC 3.4.19.12) (Ubiquitin thioesterase L3)

 UCHL3_MOUSE             Reviewed;         230 AA.
Q9JKB1; Q9EQX7;
26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
26-SEP-2001, sequence version 2.
20-JUN-2018, entry version 146.
RecName: Full=Ubiquitin carboxyl-terminal hydrolase isozyme L3;
Short=UCH-L3;
EC=3.4.19.12;
AltName: Full=Ubiquitin thioesterase L3;
Name=Uchl3;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA], DEVELOPMENTAL STAGE, AND TISSUE
SPECIFICITY.
STRAIN=Swiss Webster / NIH;
PubMed=10713173; DOI=10.1128/MCB.20.7.2498-2504.2000;
Kurihara L.J., Semenova E., Levorse J.M., Tilghman S.M.;
"Expression and functional analysis of Uch-L3 during mouse
development.";
Mol. Cell. Biol. 20:2498-2504(2000).
[2]
NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND TISSUE
SPECIFICITY.
STRAIN=C57BL/6J; TISSUE=Kidney, and Liver;
PubMed=11341770; DOI=10.1006/bbrc.2001.4841;
Osawa Y., Wang Y.-L., Osaka H., Aoki S., Wada K.;
"Cloning, expression, and mapping of a mouse gene, Uchl4, highly
homologous to human and mouse Uchl3.";
Biochem. Biophys. Res. Commun. 283:627-633(2001).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Testis;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
DEVELOPMENTAL STAGE.
PubMed=9790970; DOI=10.1006/bbrc.1998.9532;
Wada H., Kito K., Caskey L.S., Yeh E.T.H., Kamitani T.;
"Cleavage of the C-terminus of NEDD8 by UCH-L3.";
Biochem. Biophys. Res. Commun. 251:688-692(1998).
[5]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=15884048; DOI=10.1002/hipo.20082;
Wood M.A., Kaplan M.P., Brensinger C.M., Guo W., Abel T.;
"Ubiquitin C-terminal hydrolase L3 (Uchl3) is involved in working
memory.";
Hippocampus 15:610-621(2005).
[6]
DISRUPTION PHENOTYPE, FUNCTION, AND TISSUE SPECIFICITY.
PubMed=16816367; DOI=10.2353/ajpath.2006.060085;
Sano Y., Furuta A., Setsuie R., Kikuchi H., Wang Y.L., Sakurai M.,
Kwon J., Noda M., Wada K.;
"Photoreceptor cell apoptosis in the retinal degeneration of Uchl3-
deficient mice.";
Am. J. Pathol. 169:132-141(2006).
[7]
DISRUPTION PHENOTYPE, FUNCTION, AND TISSUE SPECIFICITY.
PubMed=17460351; DOI=10.1538/expanim.56.71;
Kwon J.;
"The new function of two ubiquitin C-terminal hydrolase isozymes as
reciprocal modulators of germ cell apoptosis.";
Exp. Anim. 56:71-77(2007).
[8]
FUNCTION IN ENAC RECYCLING, AND SUBCELLULAR LOCATION.
PubMed=17967898; DOI=10.1074/jbc.M707989200;
Butterworth M.B., Edinger R.S., Ovaa H., Burg D., Johnson J.P.,
Frizzell R.A.;
"The deubiquitinating enzyme UCH-L3 regulates the apical membrane
recycling of the epithelial sodium channel.";
J. Biol. Chem. 282:37885-37893(2007).
[9]
DISRUPTION PHENOTYPE, FUNCTION IN ADIPOGENESIS AND INSULIN SIGNALING,
AND MUTAGENESIS OF CYS-95.
PubMed=19837878; DOI=10.1210/en.2009-0332;
Suzuki M., Setsuie R., Wada K.;
"Ubiquitin carboxyl-terminal hydrolase l3 promotes insulin signaling
and adipogenesis.";
Endocrinology 150:5230-5239(2009).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
Pancreas, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[11]
DISRUPTION PHENOTYPE.
PubMed=20380862; DOI=10.1016/j.neuint.2010.03.021;
Setsuie R., Suzuki M., Tsuchiya Y., Wada K.;
"Skeletal muscles of Uchl3 knockout mice show polyubiquitinated
protein accumulation and stress responses.";
Neurochem. Int. 56:911-918(2010).
[12]
FUNCTION.
PubMed=21762696; DOI=10.1016/j.febslet.2011.06.037;
Dennissen F.J., Kholod N., Hermes D.J., Kemmerling N.,
Steinbusch H.W., Dantuma N.P., van Leeuwen F.W.;
"Mutant ubiquitin (UBB(+1)) associated with neurodegenerative
disorders is hydrolyzed by ubiquitin C-terminal hydrolase L3 (UCH-
L3).";
FEBS Lett. 585:2568-2574(2011).
-!- 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. {ECO:0000269|PubMed:15884048,
ECO:0000269|PubMed:16816367, ECO:0000269|PubMed:17460351,
ECO:0000269|PubMed:17967898, ECO:0000269|PubMed:19837878,
ECO:0000269|PubMed:21762696}.
-!- 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.
{ECO:0000250}.
-!- SUBUNIT: Preferentially binds diubiquitin; the interaction does
not hydrolyze diubiquitin but, in vitro, inhibits the hydrolyzing
activity on other substrates. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11341770,
ECO:0000269|PubMed:17967898}.
-!- TISSUE SPECIFICITY: Ubiquitously expressed, with highest levels in
brain, liver, heart, thymus, kidney and testis. Highly expressed
in the cauda epididymidis, in meiotic pachytene spermatocytes and
post-meiotic spematids. In the retina, enriched in the
photoreceptor inner segment. {ECO:0000269|PubMed:10713173,
ECO:0000269|PubMed:11341770, ECO:0000269|PubMed:16816367,
ECO:0000269|PubMed:17460351}.
-!- DEVELOPMENTAL STAGE: Expressed at E8.5 in structures required for
skeletal patterning. Highly expressed at E11, and decreases
markedly from E15. {ECO:0000269|PubMed:10713173,
ECO:0000269|PubMed:9790970}.
-!- DISRUPTION PHENOTYPE: Mice have no developmental defects, are
fertile, and show normal T-cell differentiation. They have normal
anxiety, locomotor behavior, motor function and synaptic
transmission, but show defects in spatial learning and working
memory. Exhibit stress-related effects with profound apoptosis-
mediated germ cell loss and also, prominent retinal degeneration
with photoreceptor cell apoptosis and mitochondrial oxidative
stress. Mice show reduced capacity for adipocyte differentiation
and impaired insulin responses. {ECO:0000269|PubMed:15884048,
ECO:0000269|PubMed:16816367, ECO:0000269|PubMed:17460351,
ECO:0000269|PubMed:19837878, ECO:0000269|PubMed:20380862}.
-!- SIMILARITY: Belongs to the peptidase C12 family. {ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; AF247358; AAF64193.1; -; mRNA.
EMBL; AB033370; BAB20094.1; -; mRNA.
EMBL; BC048481; AAH48481.1; -; mRNA.
CCDS; CCDS27313.1; -.
PIR; JC7688; JC7688.
RefSeq; NP_057932.2; NM_016723.2.
UniGene; Mm.275970; -.
ProteinModelPortal; Q9JKB1; -.
SMR; Q9JKB1; -.
BioGrid; 206165; 2.
IntAct; Q9JKB1; 2.
MINT; Q9JKB1; -.
STRING; 10090.ENSMUSP00000002289; -.
BindingDB; Q9JKB1; -.
MEROPS; C12.003; -.
iPTMnet; Q9JKB1; -.
PhosphoSitePlus; Q9JKB1; -.
SwissPalm; Q9JKB1; -.
REPRODUCTION-2DPAGE; IPI00311369; -.
REPRODUCTION-2DPAGE; Q9JKB1; -.
EPD; Q9JKB1; -.
MaxQB; Q9JKB1; -.
PaxDb; Q9JKB1; -.
PeptideAtlas; Q9JKB1; -.
PRIDE; Q9JKB1; -.
Ensembl; ENSMUST00000002289; ENSMUSP00000002289; ENSMUSG00000022111.
GeneID; 50933; -.
KEGG; mmu:50933; -.
UCSC; uc007uvw.1; mouse.
CTD; 7347; -.
MGI; MGI:1355274; Uchl3.
eggNOG; KOG1415; Eukaryota.
eggNOG; ENOG4111HNA; LUCA.
GeneTree; ENSGT00510000046640; -.
HOGENOM; HOG000182400; -.
HOVERGEN; HBG075483; -.
InParanoid; Q9JKB1; -.
KO; K05609; -.
OMA; VYGMEPE; -.
OrthoDB; EOG091G0LBS; -.
PhylomeDB; Q9JKB1; -.
TreeFam; TF316166; -.
BRENDA; 3.4.19.12; 3474.
Reactome; R-MMU-5689603; UCH proteinases.
Reactome; R-MMU-8866652; Synthesis of active ubiquitin: roles of E1 and E2 enzymes.
Reactome; R-MMU-8951664; Neddylation.
PRO; PR:Q9JKB1; -.
Proteomes; UP000000589; Chromosome 14.
Bgee; ENSMUSG00000022111; -.
Genevisible; Q9JKB1; MM.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0005634; C:nucleus; ISO:MGI.
GO; GO:0008233; F:peptidase activity; IDA:UniProtKB.
GO; GO:0004843; F:thiol-dependent ubiquitin-specific protease activity; ISO:MGI.
GO; GO:0043130; F:ubiquitin binding; ISO:MGI.
GO; GO:0101005; F:ubiquitinyl hydrolase activity; IDA:MGI.
GO; GO:0007628; P:adult walking behavior; IGI:MGI.
GO; GO:0032869; P:cellular response to insulin stimulus; IDA:UniProtKB.
GO; GO:0042755; P:eating behavior; IGI:MGI.
GO; GO:0045600; P:positive regulation of fat cell differentiation; IDA:UniProtKB.
GO; GO:0030163; P:protein catabolic process; IDA:UniProtKB.
GO; GO:0016579; P:protein deubiquitination; IDA:MGI.
GO; GO:0060041; P:retina development in camera-type eye; IMP:MGI.
GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
Gene3D; 3.40.532.10; -; 1.
InterPro; IPR038765; Papain_like_cys_pep_sf.
InterPro; IPR001578; Peptidase_C12_UCH.
InterPro; IPR036959; Peptidase_C12_UCH_sf.
PANTHER; PTHR10589; PTHR10589; 1.
Pfam; PF01088; Peptidase_C12; 1.
PRINTS; PR00707; UBCTHYDRLASE.
SUPFAM; SSF54001; SSF54001; 1.
PROSITE; PS00140; UCH_1; 1.
1: Evidence at protein level;
Complete proteome; Cytoplasm; Hydrolase; Phosphoprotein; Protease;
Reference proteome; Thiol protease; Ubl conjugation pathway.
CHAIN 1 230 Ubiquitin carboxyl-terminal hydrolase
isozyme L3.
/FTId=PRO_0000211062.
REGION 8 13 Interaction with ubiquitin.
{ECO:0000250|UniProtKB:P15374}.
REGION 152 159 Interaction with ubiquitin.
{ECO:0000250|UniProtKB:P15374}.
REGION 219 224 Interaction with ubiquitin.
{ECO:0000250|UniProtKB:P15374}.
ACT_SITE 95 95 Nucleophile. {ECO:0000255|PROSITE-
ProRule:PRU10091}.
ACT_SITE 169 169 Proton donor. {ECO:0000255|PROSITE-
ProRule:PRU10091}.
SITE 184 184 Important for enzyme activity.
{ECO:0000250}.
MOD_RES 130 130 Phosphoserine.
{ECO:0000250|UniProtKB:P15374}.
MUTAGEN 95 95 C->S: No increase in phosphorylation of
AKT1, FOXO1 and INSR. No increased
expression of SLC2A1, FABP4 nor ADIPOQ.
Impaired formation of large lipid
droplets. {ECO:0000269|PubMed:19837878}.
CONFLICT 205 207 AIE -> VIK (in Ref. 1; AAF64193).
{ECO:0000305}.
SEQUENCE 230 AA; 26152 MW; F147991F3ED69AC3 CRC64;
MEGQRWLPLE ANPEVTNQFL KQLGLHPNWQ FVDVYGMEPE LLSMVPRPVC AVLLLFPITE
KYEVFRTEEE EKIKSQGQDV TSSVYFMKQT ISNACGTIGL IHAIANNKDK MHFESGSTLK
KFLEESVSMS PEERAKFLEN YDAIRVTHET SAHEGQTEAP SIDEKVDLHF IALVHVDGHL
YELDGRKPFP INHGKTSDET LLEDAIEVCK KFMERDPDEL RFNAIALSAA


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