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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_RAT               Reviewed;         223 AA.
Q00981; Q6P9V8;
01-APR-1993, integrated into UniProtKB/Swiss-Prot.
05-JUL-2005, sequence version 2.
20-JUN-2018, entry version 145.
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;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Brain;
PubMed=1331034;
Kajimoto Y., Hashimoto T., Shirai Y., Nishino N., Kuno T., Tanaka C.;
"cDNA cloning and tissue distribution of a rat ubiquitin carboxyl-
terminal hydrolase PGP9.5.";
J. Biochem. 112:28-32(1992).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Pituitary;
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).
[3]
PROTEIN SEQUENCE OF 20-27; 84-123 AND 132-199, AND IDENTIFICATION BY
MASS SPECTROMETRY.
STRAIN=Sprague-Dawley; TISSUE=Brain, and Spinal cord;
Lubec G., Boddul S., Afjehi-Sadat L., Kang S.U.;
Submitted (JUL-2007) to UniProtKB.
[4]
GLYCOSYLATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=11739622; DOI=10.1046/j.1471-4159.2001.00655.x;
Cole R.N., Hart G.W.;
"Cytosolic O-glycosylation is abundant in nerve terminals.";
J. Neurochem. 79:1080-1089(2001).
[5]
INTERACTION WITH SNCA.
PubMed=12408865; DOI=10.1016/S0092-8674(02)01012-7;
Liu Y., Fallon L., Lashuel H.A., Liu Z., Lansbury P.T. Jr.;
"The UCH-L1 gene encodes two opposing enzymatic activities that affect
alpha-synuclein degradation and Parkinson's disease susceptibility.";
Cell 111:209-218(2002).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-125, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
-!- 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). {ECO:0000250}.
-!- 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: Monomer. Homodimer. Interacts with COPS5 (By similarity).
Interacts with SNCA. {ECO:0000250, ECO:0000269|PubMed:12408865}.
-!- SUBCELLULAR LOCATION: Cytoplasm. Endoplasmic reticulum membrane
{ECO:0000250}; Lipid-anchor {ECO:0000250}.
-!- PTM: O-glycosylated. {ECO:0000269|PubMed:11739622}.
-!- 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; D10699; BAA01541.1; -; mRNA.
EMBL; BC060573; AAH60573.1; -; mRNA.
PIR; JX0222; JX0222.
RefSeq; NP_058933.2; NM_017237.3.
UniGene; Rn.107213; -.
ProteinModelPortal; Q00981; -.
SMR; Q00981; -.
BioGrid; 248179; 2.
IntAct; Q00981; 2.
STRING; 10116.ENSRNOP00000003248; -.
MEROPS; C12.001; -.
iPTMnet; Q00981; -.
PhosphoSitePlus; Q00981; -.
SwissPalm; Q00981; -.
World-2DPAGE; 0004:Q00981; -.
PaxDb; Q00981; -.
PRIDE; Q00981; -.
Ensembl; ENSRNOT00000003248; ENSRNOP00000003248; ENSRNOG00000002343.
GeneID; 29545; -.
KEGG; rno:29545; -.
UCSC; RGD:3928; rat.
CTD; 7345; -.
RGD; 3928; Uchl1.
eggNOG; KOG1415; Eukaryota.
eggNOG; ENOG4111HNA; LUCA.
GeneTree; ENSGT00510000046640; -.
HOGENOM; HOG000182400; -.
HOVERGEN; HBG075483; -.
InParanoid; Q00981; -.
KO; K05611; -.
OMA; AIQEVHN; -.
OrthoDB; EOG091G0LBS; -.
PhylomeDB; Q00981; -.
BRENDA; 3.4.19.12; 5301.
Reactome; R-RNO-5689603; UCH proteinases.
PRO; PR:Q00981; -.
Proteomes; UP000002494; Chromosome 14.
Bgee; ENSRNOG00000002343; -.
Genevisible; Q00981; RN.
GO; GO:1904115; C:axon cytoplasm; IEA:GOC.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0005829; C:cytosol; IEA:Ensembl.
GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
GO; GO:0043209; C:myelin sheath; IEA:Ensembl.
GO; GO:0044306; C:neuron projection terminus; IEA:Ensembl.
GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
GO; GO:0031694; F:alpha-2A adrenergic receptor binding; IEA:Ensembl.
GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:Ensembl.
GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
GO; GO:0008242; F:omega peptidase activity; IEA:Ensembl.
GO; GO:0004843; F:thiol-dependent ubiquitin-specific protease activity; IBA:GO_Central.
GO; GO:0043130; F:ubiquitin binding; IEA:Ensembl.
GO; GO:0031625; F:ubiquitin protein ligase binding; IEA:Ensembl.
GO; GO:0007628; P:adult walking behavior; IEA:Ensembl.
GO; GO:0007412; P:axon target recognition; IEA:Ensembl.
GO; GO:0019896; P:axonal transport of mitochondrion; IEA:Ensembl.
GO; GO:0008283; P:cell proliferation; IEA:Ensembl.
GO; GO:0042755; P:eating behavior; IEA:Ensembl.
GO; GO:0048747; P:muscle fiber development; IEA:Ensembl.
GO; GO:0043407; P:negative regulation of MAP kinase activity; IEA:Ensembl.
GO; GO:0050905; P:neuromuscular process; IEA:Ensembl.
GO; GO:0016579; P:protein deubiquitination; IBA:GO_Central.
GO; GO:0002931; P:response to ischemia; IEA:Ensembl.
GO; GO:0019233; P:sensory perception of pain; IDA:RGD.
GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IDA:RGD.
Gene3D; 3.40.532.10; -; 1.
InterPro; IPR038765; Papain_like_cys_pep_sf.
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.
SUPFAM; SSF54001; SSF54001; 1.
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_0000211060.
PROPEP 221 223 Removed in mature form. {ECO:0000250}.
/FTId=PRO_0000414315.
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:0000255|PROSITE-
ProRule:PRU10091}.
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:0000244|PubMed:22673903}.
LIPID 220 220 S-farnesyl cysteine.
{ECO:0000250|UniProtKB:P09936}.
CONFLICT 38 38 T -> I (in Ref. 1; BAA01541).
{ECO:0000305}.
CONFLICT 96 96 I -> M (in Ref. 1; BAA01541).
{ECO:0000305}.
CONFLICT 105 107 KLE -> NLG (in Ref. 1; BAA01541).
{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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