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Ubiquitin carboxyl-terminal hydrolase isozyme L1 (UCH-L1) (EC 3.4.19.12) (EC 6.-.-.-) (Neuron cytoplasmic protein 9.5) (PGP 9.5) (PGP9.5) (Ubiquitin thioesterase L1)

 UCHL1_MOUSE             Reviewed;         223 AA.
Q9R0P9; Q9R122;
26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
01-MAY-2000, sequence version 1.
25-OCT-2017, entry version 153.
RecName: Full=Ubiquitin carboxyl-terminal hydrolase isozyme L1;
Short=UCH-L1;
EC=3.4.19.12;
EC=6.-.-.-;
AltName: Full=Neuron cytoplasmic protein 9.5;
AltName: Full=PGP 9.5;
Short=PGP9.5;
AltName: Full=Ubiquitin thioesterase L1;
Flags: Precursor;
Name=Uchl1;
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], TISSUE SPECIFICITY, AND DISRUPTION
PHENOTYPE.
TISSUE=Brain;
PubMed=10471497; DOI=10.1038/12647;
Saigoh K., Wang Y.-L., Suh J.G., Yamanishi T., Sakai Y., Kiyosawa H.,
Harada T., Ichihara N., Wakana S., Kikuchi T., Wada K.;
"Intragenic deletion in the gene encoding ubiquitin carboxy-terminal
hydrolase in gad mice.";
Nat. Genet. 23:47-51(1999).
[2]
NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 1-10, AND TISSUE
SPECIFICITY.
STRAIN=C57BL/6J; TISSUE=Pituitary;
PubMed=12559414; DOI=10.1016/S0531-5565(02)00117-1;
Marzban G., Grillari J., Reisinger E., Hemetsberger T., Grabherr R.,
Katinger H.;
"Age-related alterations in the protein expression profile of C57BL/6J
mouse pituitaries.";
Exp. Gerontol. 37:1451-1460(2002).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Hippocampus;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Retina;
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).
[5]
PROTEIN SEQUENCE OF 20-27; 66-78; 116-123; 136-153 AND 158-199, AND
IDENTIFICATION BY MASS SPECTROMETRY.
STRAIN=C57BL/6J; TISSUE=Brain, and Hippocampus;
Lubec G., Kang S.U., Klug S., Yang J.W., Zigmond M.;
Submitted (JUL-2007) to UniProtKB.
[6]
BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF ASP-30 AND CYS-90,
SUBCELLULAR LOCATION, TISSUE SPECIFICITY, FUNCTION, AND DISRUPTION
PHENOTYPE.
PubMed=12913066; DOI=10.1093/hmg/ddg211;
Osaka H., Wang Y.-L., Takada K., Takizawa S., Setsuie R., Li H.,
Sato Y., Nishikawa K., Sun Y.-J., Sakurai M., Harada T., Hara Y.,
Kimura I., Chiba S., Namikawa K., Kiyama H., Noda M., Aoki S.,
Wada K.;
"Ubiquitin carboxy-terminal hydrolase L1 binds to and stabilizes
monoubiquitin in neuron.";
Hum. Mol. Genet. 12:1945-1958(2003).
[7]
TISSUE SPECIFICITY.
PubMed=14695319; DOI=10.1016/S0002-9440(10)63096-9;
Harada T., Harada C., Wang Y.-L., Osaka H., Amanai K., Tanaka K.,
Takizawa S., Setsuie R., Sakurai M., Sato Y., Noda M., Wada K.;
"Role of ubiquitin carboxy terminal hydrolase-L1 in neural cell
apoptosis induced by ischemic retinal injury in vivo.";
Am. J. Pathol. 164:59-64(2004).
[8]
TISSUE SPECIFICITY.
PubMed=15911766; DOI=10.1073/pnas.0503239102;
Lombardino A.J., Li X.-C., Hertel M., Nottebohm F.;
"Replaceable neurons and neurodegenerative disease share depressed
UCHL1 levels.";
Proc. Natl. Acad. Sci. U.S.A. 102:8036-8041(2005).
[9]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Liver, Lung, 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).
-!- 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.
{ECO:0000269|PubMed:12913066}.
-!- 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).
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=116 nM for Ub-AMC {ECO:0000269|PubMed:12913066};
-!- SUBUNIT: Monomer. Homodimer. Interacts with COPS5 and SNCA (By
similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12913066}.
Endoplasmic reticulum membrane {ECO:0000250}; Lipid-anchor
{ECO:0000250}.
-!- TISSUE SPECIFICITY: Expressed in brain, where it is found in
neurons but not in oligodendrocytes or astrocytes. Found in the
ganglion cell layer and the inner nuclear layer of the retina (at
protein level). Expressed in brain and testis. In the brain,
expression is at its lowest in replaceable neurons of hippocampus
and olfactory bulb. Highly expressed in senescent pituitary.
{ECO:0000269|PubMed:10471497, ECO:0000269|PubMed:12559414,
ECO:0000269|PubMed:12913066, ECO:0000269|PubMed:14695319,
ECO:0000269|PubMed:15911766}.
-!- PTM: O-glycosylated. {ECO:0000250}.
-!- DISRUPTION PHENOTYPE: Mice show sensory ataxia at an early stage,
followed by motor ataxia at a later stage. They have reduced
levels of monoubiquitin in the nervous system, and increased
resistance to retinal ischemia. {ECO:0000269|PubMed:10471497,
ECO:0000269|PubMed:12913066}.
-!- MISCELLANEOUS: In contrast to UCHL3, does not hydrolyze a peptide
bond at the C-terminal glycine of NEDD8. {ECO:0000250}.
-!- SIMILARITY: Belongs to the peptidase C12 family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AB025313; BAA84083.1; -; mRNA.
EMBL; AF172334; AAD51029.1; -; mRNA.
EMBL; AK013729; BAB28976.1; -; mRNA.
EMBL; BC039177; AAH39177.1; -; mRNA.
CCDS; CCDS19315.1; -.
RefSeq; NP_035800.2; NM_011670.2.
UniGene; Mm.29807; -.
ProteinModelPortal; Q9R0P9; -.
SMR; Q9R0P9; -.
BioGrid; 204423; 9.
IntAct; Q9R0P9; 6.
MINT; MINT-4139420; -.
STRING; 10090.ENSMUSP00000031131; -.
BindingDB; Q9R0P9; -.
MEROPS; C12.001; -.
iPTMnet; Q9R0P9; -.
PhosphoSitePlus; Q9R0P9; -.
SwissPalm; Q9R0P9; -.
REPRODUCTION-2DPAGE; IPI00313962; -.
REPRODUCTION-2DPAGE; Q9R0P9; -.
UCD-2DPAGE; Q9R0P9; -.
EPD; Q9R0P9; -.
MaxQB; Q9R0P9; -.
PaxDb; Q9R0P9; -.
PeptideAtlas; Q9R0P9; -.
PRIDE; Q9R0P9; -.
Ensembl; ENSMUST00000031131; ENSMUSP00000031131; ENSMUSG00000029223.
GeneID; 22223; -.
KEGG; mmu:22223; -.
UCSC; uc008xpf.2; mouse.
CTD; 7345; -.
MGI; MGI:103149; Uchl1.
eggNOG; KOG1415; Eukaryota.
eggNOG; ENOG4111HNA; LUCA.
GeneTree; ENSGT00510000046640; -.
HOVERGEN; HBG075483; -.
InParanoid; Q9R0P9; -.
KO; K05611; -.
OMA; AIQEVHN; -.
OrthoDB; EOG091G0LBS; -.
PhylomeDB; Q9R0P9; -.
TreeFam; TF316166; -.
BRENDA; 3.4.19.12; 3474.
Reactome; R-MMU-5689603; UCH proteinases.
ChiTaRS; Uchl1; mouse.
PRO; PR:Q9R0P9; -.
Proteomes; UP000000589; Chromosome 5.
Bgee; ENSMUSG00000029223; -.
CleanEx; MM_UCHL1; -.
Genevisible; Q9R0P9; MM.
GO; GO:0030424; C:axon; IDA:MGI.
GO; GO:1904115; C:axon cytoplasm; IEA:GOC.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:MGI.
GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
GO; GO:0070062; C:extracellular exosome; ISO:MGI.
GO; GO:0043209; C:myelin sheath; IDA:UniProtKB.
GO; GO:0044306; C:neuron projection terminus; IDA:MGI.
GO; GO:0043025; C:neuronal cell body; IDA:MGI.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
GO; GO:0031694; F:alpha-2A adrenergic receptor binding; ISO:MGI.
GO; GO:0004197; F:cysteine-type endopeptidase activity; ISS:UniProtKB.
GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
GO; GO:0008242; F:omega peptidase activity; ISS:UniProtKB.
GO; GO:0004843; F:thiol-dependent ubiquitin-specific protease activity; IDA:MGI.
GO; GO:0043130; F:ubiquitin binding; IDA:MGI.
GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:MGI.
GO; GO:0007628; P:adult walking behavior; IMP:MGI.
GO; GO:0007412; P:axon target recognition; IMP:MGI.
GO; GO:0019896; P:axonal transport of mitochondrion; IMP:MGI.
GO; GO:0007409; P:axonogenesis; IMP:MGI.
GO; GO:0008283; P:cell proliferation; IMP:MGI.
GO; GO:0042755; P:eating behavior; IGI:MGI.
GO; GO:0048747; P:muscle fiber development; IGI:MGI.
GO; GO:0043407; P:negative regulation of MAP kinase activity; ISO:MGI.
GO; GO:0050905; P:neuromuscular process; IMP:MGI.
GO; GO:0016579; P:protein deubiquitination; ISS:UniProtKB.
GO; GO:0002931; P:response to ischemia; IMP:MGI.
GO; GO:0019233; P:sensory perception of pain; IEA:Ensembl.
GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:Ensembl.
Gene3D; 3.40.532.10; -; 1.
InterPro; IPR001578; Peptidase_C12_UCH.
InterPro; IPR036959; Peptidase_C12_UCH_sf.
InterPro; IPR030297; UCHL1.
PANTHER; PTHR10589; PTHR10589; 1.
PANTHER; PTHR10589:SF19; PTHR10589:SF19; 1.
Pfam; PF01088; Peptidase_C12; 1.
PRINTS; PR00707; UBCTHYDRLASE.
PROSITE; PS00140; UCH_1; 1.
1: Evidence at protein level;
Complete proteome; Cytoplasm; Direct protein sequencing;
Endoplasmic reticulum; Glycoprotein; Hydrolase; Ligase; Lipoprotein;
Membrane; Phosphoprotein; Prenylation; Protease; Reference proteome;
Thiol protease; Ubl conjugation pathway.
CHAIN 1 220 Ubiquitin carboxyl-terminal hydrolase
isozyme L1.
/FTId=PRO_0000211058.
PROPEP 221 223 Removed in mature form. {ECO:0000250}.
/FTId=PRO_0000414313.
REGION 5 10 Interaction with ubiquitin.
{ECO:0000250|UniProtKB:P09936}.
REGION 211 216 Interaction with ubiquitin.
{ECO:0000250|UniProtKB:P09936}.
ACT_SITE 90 90 Nucleophile. {ECO:0000305}.
ACT_SITE 161 161 Proton donor. {ECO:0000255|PROSITE-
ProRule:PRU10091}.
SITE 176 176 Important for enzyme activity.
{ECO:0000250}.
MOD_RES 125 125 Phosphoserine.
{ECO:0000250|UniProtKB:Q00981}.
LIPID 220 220 S-farnesyl cysteine.
{ECO:0000250|UniProtKB:P09936}.
MUTAGEN 30 30 D->K: Abolishes enzymatic activity and
ubiquitin binding.
{ECO:0000269|PubMed:12913066}.
MUTAGEN 90 90 C->S: Abolishes enzymatic activity, but
does not affect ubiquitin binding.
{ECO:0000269|PubMed:12913066}.
CONFLICT 149 149 E -> K (in Ref. 2; AAD51029).
{ECO:0000305}.
SEQUENCE 223 AA; 24838 MW; F1402BF7B0C077EA CRC64;
MQLKPMEINP EMLNKVLAKL GVAGQWRFAD VLGLEEETLG SVPSPACALL LLFPLTAQHE
NFRKKQIEEL KGQEVSPKVY FMKQTIGNSC GTIGLIHAVA NNQDKLEFED GSVLKQFLSE
TEKLSPEDRA KCFEKNEAIQ AAHDSVAQEG QCRVDDKVNF HFILFNNVDG HLYELDGRMP
FPVNHGASSE DSLLQDAAKV CREFTEREQG EVRFSAVALC KAA


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