UCHL1_BOVIN
ID UCHL1_BOVIN Reviewed; 252 AA.
AC P23356; Q2NKZ2;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2006, sequence version 2.
DT 03-AUG-2022, entry version 155.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PROTEIN SEQUENCE OF 1-25.
RC TISSUE=Brain;
RX PubMed=1833240; DOI=10.1016/0014-5793(91)81242-z;
RA Giambanco I., Bianchi R., Ceccarelli P., Pula G., Sorci G., Antonioli S.,
RA Bocchini V., Donato R.;
RT "'Neuron-specific' protein gene product 9.5 (PGP 9.5) is also expressed in
RT glioma cell lines and its expression depends on cellular growth state.";
RL FEBS Lett. 290:131-134(1991).
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. Endoplasmic reticulum membrane
CC {ECO:0000250}; Lipid-anchor {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Neurons and cells of the diffuse neuroendocrine
CC system and their tumors.
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; BC111330; AAI11331.1; -; mRNA.
DR PIR; S17561; S17561.
DR RefSeq; NP_001039637.1; NM_001046172.2.
DR AlphaFoldDB; P23356; -.
DR SMR; P23356; -.
DR STRING; 9913.ENSBTAP00000044075; -.
DR MEROPS; C12.001; -.
DR PaxDb; P23356; -.
DR PeptideAtlas; P23356; -.
DR PRIDE; P23356; -.
DR Ensembl; ENSBTAT00000046823; ENSBTAP00000044075; ENSBTAG00000005078.
DR GeneID; 514394; -.
DR KEGG; bta:514394; -.
DR CTD; 7345; -.
DR VEuPathDB; HostDB:ENSBTAG00000005078; -.
DR VGNC; VGNC:36631; UCHL1.
DR eggNOG; KOG1415; Eukaryota.
DR GeneTree; ENSGT00940000157306; -.
DR HOGENOM; CLU_054406_2_0_1; -.
DR InParanoid; P23356; -.
DR OMA; HACGLIA; -.
DR OrthoDB; 1013351at2759; -.
DR TreeFam; TF316166; -.
DR Proteomes; UP000009136; Chromosome 6.
DR Bgee; ENSBTAG00000005078; Expressed in Ammon's horn and 105 other tissues.
DR ExpressionAtlas; P23356; baseline and differential.
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 1: Evidence at protein level;
KW Cytoplasm; Direct protein sequencing; Endoplasmic reticulum; Glycoprotein;
KW Hydrolase; Lipoprotein; Membrane; Phosphoprotein; Prenylation; Protease;
KW Reference proteome; Thiol protease; Ubl conjugation pathway.
FT CHAIN 1..249
FT /note="Ubiquitin carboxyl-terminal hydrolase isozyme L1"
FT /id="PRO_0000211053"
FT PROPEP 250..252
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000414309"
FT REGION 5..10
FT /note="Interaction with ubiquitin"
FT /evidence="ECO:0000250|UniProtKB:P09936"
FT REGION 240..245
FT /note="Interaction with ubiquitin"
FT /evidence="ECO:0000250|UniProtKB:P09936"
FT ACT_SITE 119
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10091"
FT ACT_SITE 190
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10091"
FT SITE 205
FT /note="Important for enzyme activity"
FT MOD_RES 154
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q00981"
FT LIPID 249
FT /note="S-farnesyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:P09936"
FT CONFLICT 9
FT /note="N -> D (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 252 AA; 28335 MW; 9D62A458590188B7 CRC64;
MQLKPMEINP EMLNKVLTRL GVAGQWRFED VLGLEEESLG SVPAPACALL LLFPLTAQRC
FKLGREAASR FHHPDYPGRL FILLVSQHEN FRKKQIEELK GQEVSPKVYF MKQTIGNSCG
TIGLIHAVAN NQDKLEFEDG SVLKQFLSET EKLSPEDRAK CFEKNEAIQA AHDAVAQEGQ
CRVDDKVNFH FILFNNVDGH LYELDGRMPF PVNHGTSSED SLLQDAAKVC REFTEREQGE
VRFSAVALCK AA
