UCHL1_HORSE
ID UCHL1_HORSE Reviewed; 223 AA.
AC Q9GM50; O62662;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 2.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase isozyme L1;
DE Short=UCH-L1;
DE EC=3.4.19.12 {ECO:0000250|UniProtKB:P09936};
DE AltName: Full=Neuron cytoplasmic protein 9.5;
DE AltName: Full=PGP 9.5;
DE Short=PGP9.5;
DE AltName: Full=Ubiquitin thioesterase L1;
DE Flags: Precursor;
GN Name=UCHL1;
OS Equus caballus (Horse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus.
OX NCBI_TaxID=9796;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Sato F., Harigai N., Iwanaga T., Hasegawa T., Ishida N.;
RT "cDNA cloning of equine ubiquitin C-terminal hydrolase (PGP9.5).";
RL Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 50-188.
RC TISSUE=Brain;
RA Yanase H., Kitamura H., Iwanaga T., Kanehira K., Okita K.;
RL Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Ubiquitin-protein hydrolase involved both in the processing
CC of ubiquitin precursors and of ubiquitinated proteins. This enzyme is a
CC thiol protease that recognizes and hydrolyzes a peptide bond at the C-
CC terminal glycine of ubiquitin (By similarity). Also binds to free
CC monoubiquitin and may prevent its degradation in lysosomes (By
CC similarity). The homodimer may have ATP-independent ubiquitin ligase
CC activity (By similarity). {ECO:0000250|UniProtKB:P09936,
CC ECO:0000250|UniProtKB:Q9R0P9}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Thiol-dependent hydrolysis of ester, thioester, amide, peptide
CC and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-
CC residue protein attached to proteins as an intracellular targeting
CC signal).; EC=3.4.19.12; Evidence={ECO:0000250|UniProtKB:P09936};
CC -!- SUBUNIT: Monomer. Homodimer. Interacts with COPS5 and SNCA (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Endoplasmic reticulum
CC membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}.
CC -!- PTM: O-glycosylated. {ECO:0000250}.
CC -!- MISCELLANEOUS: In contrast to UCHL3, does not hydrolyze a peptide bond
CC at the C-terminal glycine of NEDD8. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase C12 family. {ECO:0000305}.
CC -!- CAUTION: The homodimer may have ATP-independent ubiquitin ligase
CC activity. However, in another study, UCHL1 was shown to lack ubiquitin
CC ligase activity. {ECO:0000250|UniProtKB:P09936}.
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DR EMBL; AB049188; BAB13757.1; -; mRNA.
DR EMBL; AB013344; BAA28214.1; -; mRNA.
DR RefSeq; NP_001075289.1; NM_001081820.1.
DR AlphaFoldDB; Q9GM50; -.
DR BMRB; Q9GM50; -.
DR SMR; Q9GM50; -.
DR STRING; 9796.ENSECAP00000024797; -.
DR MEROPS; C12.001; -.
DR PaxDb; Q9GM50; -.
DR PeptideAtlas; Q9GM50; -.
DR PRIDE; Q9GM50; -.
DR GeneID; 100033838; -.
DR KEGG; ecb:100033838; -.
DR CTD; 7345; -.
DR InParanoid; Q9GM50; -.
DR OrthoDB; 1013351at2759; -.
DR Proteomes; UP000002281; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IBA:GO_Central.
DR GO; GO:0016874; F:ligase activity; IEA:InterPro.
DR GO; GO:0016579; P:protein deubiquitination; IBA:GO_Central.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR Gene3D; 3.40.532.10; -; 1.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR001578; Peptidase_C12_UCH.
DR InterPro; IPR036959; Peptidase_C12_UCH_sf.
DR InterPro; IPR030297; UCHL1.
DR PANTHER; PTHR10589; PTHR10589; 1.
DR PANTHER; PTHR10589:SF19; PTHR10589:SF19; 1.
DR Pfam; PF01088; Peptidase_C12; 1.
DR PRINTS; PR00707; UBCTHYDRLASE.
DR SUPFAM; SSF54001; SSF54001; 1.
DR PROSITE; PS00140; UCH_1; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Endoplasmic reticulum; Glycoprotein; Hydrolase; Lipoprotein;
KW Membrane; Phosphoprotein; Prenylation; Protease; Reference proteome;
KW Thiol protease; Ubl conjugation pathway.
FT CHAIN 1..220
FT /note="Ubiquitin carboxyl-terminal hydrolase isozyme L1"
FT /id="PRO_0000211054"
FT PROPEP 221..223
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000414310"
FT REGION 5..10
FT /note="Interaction with ubiquitin"
FT /evidence="ECO:0000250|UniProtKB:P09936"
FT REGION 211..216
FT /note="Interaction with ubiquitin"
FT /evidence="ECO:0000250|UniProtKB:P09936"
FT ACT_SITE 90
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10091"
FT ACT_SITE 161
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10091"
FT SITE 176
FT /note="Important for enzyme activity"
FT /evidence="ECO:0000250"
FT MOD_RES 125
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q00981"
FT LIPID 220
FT /note="S-farnesyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:P09936"
FT CONFLICT 187
FT /note="A -> T (in Ref. 1; BAB13757)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 223 AA; 24888 MW; A32AFE7D1721CAD6 CRC64;
MQLKPMEINP EMLNKVLARL GVAGQWRFVD VLGLEEETLG SVPAPACALL LLFPLTAQHE
NFRKKQIEEL KGQEVSPKVY FMKQTIGNSC GTIGLIHAVA NNQDKLEFED GSVLKQFLSE
TEKLSPEDRA KCFEKNEAIQ AAHDAVAQEG QCRVDDKVNF HFILFNNVDG HLYELDGRMP
FPVNHGASSE DLLLQDAAKV CREFTEREQG EVRFSAVALC KAA
