UCHL4_MOUSE
ID UCHL4_MOUSE Reviewed; 233 AA.
AC P58321;
DT 18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT 18-OCT-2001, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase isozyme L4;
DE Short=UCH-L4;
DE EC=3.4.19.12;
DE AltName: Full=Ubiquitin thioesterase L4;
GN Name=Uchl4;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6J;
RX PubMed=11341770; DOI=10.1006/bbrc.2001.4841;
RA Osawa Y., Wang Y.-L., Osaka H., Aoki S., Wada K.;
RT "Cloning, expression, and mapping of a mouse gene, Uchl4, highly homologous
RT to human and mouse Uchl3.";
RL Biochem. Biophys. Res. Commun. 283:627-633(2001).
CC -!- FUNCTION: Ubiquitin-protein hydrolase is involved both in the
CC processing of ubiquitin precursors and of ubiquitinated proteins. This
CC enzyme is a thiol protease that recognizes and hydrolyzes a peptide
CC bond at the C-terminal glycine of ubiquitin.
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;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in various tissues at low level.
CC -!- SIMILARITY: Belongs to the peptidase C12 family. {ECO:0000305}.
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DR EMBL; AB035420; BAB47122.1; -; mRNA.
DR CCDS; CCDS23278.1; -.
DR PIR; JC7689; JC7689.
DR RefSeq; NP_291085.1; NM_033607.1.
DR AlphaFoldDB; P58321; -.
DR SMR; P58321; -.
DR BioGRID; 220315; 1.
DR STRING; 10090.ENSMUSP00000045208; -.
DR MEROPS; C12.007; -.
DR iPTMnet; P58321; -.
DR PhosphoSitePlus; P58321; -.
DR SwissPalm; P58321; -.
DR jPOST; P58321; -.
DR MaxQB; P58321; -.
DR PaxDb; P58321; -.
DR PRIDE; P58321; -.
DR ProteomicsDB; 298466; -.
DR DNASU; 93841; -.
DR Ensembl; ENSMUST00000039011; ENSMUSP00000045208; ENSMUSG00000035337.
DR GeneID; 93841; -.
DR KEGG; mmu:93841; -.
DR UCSC; uc009qbq.1; mouse.
DR CTD; 93841; -.
DR MGI; MGI:1890440; Uchl4.
DR VEuPathDB; HostDB:ENSMUSG00000035337; -.
DR eggNOG; KOG1415; Eukaryota.
DR GeneTree; ENSGT00940000154925; -.
DR HOGENOM; CLU_054406_1_1_1; -.
DR InParanoid; P58321; -.
DR OMA; TCFVQAP; -.
DR OrthoDB; 1013351at2759; -.
DR PhylomeDB; P58321; -.
DR TreeFam; TF316166; -.
DR BioGRID-ORCS; 93841; 2 hits in 70 CRISPR screens.
DR ChiTaRS; Uchl4; mouse.
DR PRO; PR:P58321; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; P58321; protein.
DR Bgee; ENSMUSG00000035337; Expressed in morula and 81 other tissues.
DR ExpressionAtlas; P58321; baseline and differential.
DR Genevisible; P58321; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; ISO:MGI.
DR GO; GO:0008233; F:peptidase activity; ISO:MGI.
DR GO; GO:0043130; F:ubiquitin binding; ISO:MGI.
DR GO; GO:0030163; P:protein catabolic process; ISO:MGI.
DR GO; GO:0016579; P:protein deubiquitination; ISO:MGI.
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 PANTHER; PTHR10589; PTHR10589; 1.
DR Pfam; PF01088; Peptidase_C12; 1.
DR PRINTS; PR00707; UBCTHYDRLASE.
DR SUPFAM; SSF54001; SSF54001; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Hydrolase; Phosphoprotein; Protease; Reference proteome;
KW Thiol protease; Ubl conjugation pathway.
FT CHAIN 1..233
FT /note="Ubiquitin carboxyl-terminal hydrolase isozyme L4"
FT /id="PRO_0000211064"
FT REGION 8..13
FT /note="Interaction with ubiquitin"
FT /evidence="ECO:0000250"
FT REGION 222..227
FT /note="Interaction with ubiquitin"
FT /evidence="ECO:0000250"
FT ACT_SITE 95
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 172
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT SITE 187
FT /note="Important for enzyme activity"
FT /evidence="ECO:0000250"
FT MOD_RES 133
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P15374"
SQ SEQUENCE 233 AA; 26450 MW; 9D7899AD70C27819 CRC64;
MEGQRWLPLE ANPEVTNQFL KQLGLHPNWQ FVDVYGMESE LLSIIPRPVC AVLLLFPITE
KYEVFRTEEE EKIKSQGQDV TSSVYFMKQT ISNACGTIGT IGLIHAIANN KDKVHFESGS
TLKKFLEESV SMSPEERAKY LENYDAIRVT HETSAHEGQT EAPSIDEKVD LHFIALVHVD
GHLYELDGWK PFPINHGKTS DETLLEDVIK VCKKFMERDP DELRFNAIAL SAA
