UCHL3_BOVIN
ID UCHL3_BOVIN Reviewed; 230 AA.
AC Q2TBG8;
DT 13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase isozyme L3;
DE Short=UCH-L3;
DE EC=3.4.19.12 {ECO:0000250|UniProtKB:P15374};
DE AltName: Full=Ubiquitin thioesterase L3;
GN Name=UCHL3;
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 (NOV-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Deubiquitinating enzyme (DUB) that controls levels of
CC cellular ubiquitin through processing of ubiquitin precursors and
CC ubiquitinated proteins. Thiol protease that recognizes and hydrolyzes a
CC peptide bond at the C-terminal glycine of either ubiquitin or NEDD8.
CC Has a 10-fold preference for Arg and Lys at position P3''.
CC Deubiquitinates ENAC in apical compartments, thereby regulating apical
CC membrane recycling. Indirectly increases the phosphorylation of IGFIR,
CC AKT and FOXO1 and promotes insulin-signaling and insulin-induced
CC adipogenesis. Required for stress-response retinal, skeletal muscle and
CC germ cell maintenance. May be involved in working memory. Can hydrolyze
CC UBB(+1), a mutated form of ubiquitin which is not effectively degraded
CC by the proteasome (By similarity). {ECO:0000250}.
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:P15374};
CC -!- ACTIVITY REGULATION: Inhibited by monoubiquitin and diubiquitin.
CC {ECO:0000250}.
CC -!- SUBUNIT: Preferentially binds diubiquitin; the interaction does not
CC hydrolyze diubiquitin but, in vitro, inhibits the hydrolyzing activity
CC on other substrates. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase C12 family. {ECO:0000305}.
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DR EMBL; BC110247; AAI10248.1; -; mRNA.
DR RefSeq; NP_001035631.1; NM_001040541.2.
DR AlphaFoldDB; Q2TBG8; -.
DR BMRB; Q2TBG8; -.
DR SMR; Q2TBG8; -.
DR IntAct; Q2TBG8; 1.
DR STRING; 9913.ENSBTAP00000035448; -.
DR MEROPS; C12.003; -.
DR PaxDb; Q2TBG8; -.
DR PeptideAtlas; Q2TBG8; -.
DR PRIDE; Q2TBG8; -.
DR Ensembl; ENSBTAT00000071781; ENSBTAP00000057147; ENSBTAG00000008024.
DR GeneID; 520170; -.
DR KEGG; bta:520170; -.
DR CTD; 7347; -.
DR VEuPathDB; HostDB:ENSBTAG00000008024; -.
DR VGNC; VGNC:36632; UCHL3.
DR eggNOG; KOG1415; Eukaryota.
DR GeneTree; ENSGT00940000154925; -.
DR HOGENOM; CLU_054406_1_1_1; -.
DR InParanoid; Q2TBG8; -.
DR OMA; YVCFVKG; -.
DR OrthoDB; 1013351at2759; -.
DR TreeFam; TF316166; -.
DR Proteomes; UP000009136; Chromosome 12.
DR Bgee; ENSBTAG00000008024; Expressed in oocyte and 105 other tissues.
DR ExpressionAtlas; Q2TBG8; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IBA:GO_Central.
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 PANTHER; PTHR10589; PTHR10589; 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; Hydrolase; Phosphoprotein; Protease; Reference proteome;
KW Thiol protease; Ubl conjugation pathway.
FT CHAIN 1..230
FT /note="Ubiquitin carboxyl-terminal hydrolase isozyme L3"
FT /id="PRO_0000239741"
FT REGION 8..13
FT /note="Interaction with ubiquitin"
FT /evidence="ECO:0000250|UniProtKB:P15374"
FT REGION 152..159
FT /note="Interaction with ubiquitin. Crossover loop which
FT restricts access of large ubiquitin adducts to the active
FT site"
FT /evidence="ECO:0000250|UniProtKB:P15374"
FT REGION 219..224
FT /note="Interaction with ubiquitin"
FT /evidence="ECO:0000250|UniProtKB:P15374"
FT ACT_SITE 95
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10091"
FT ACT_SITE 169
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10091"
FT SITE 184
FT /note="Important for enzyme activity"
FT /evidence="ECO:0000250|UniProtKB:P09936"
FT MOD_RES 130
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P15374"
SQ SEQUENCE 230 AA; 26182 MW; 01D145E4352627BB CRC64;
MEGQRWLPLE ANPEVTNQFL KQLGLHPNWQ FVDVYGMDPE LLSMVPRPVC AVLLLFPITE
KYEVFRTEEE EKIKSQGQDV TSSVYFMKQT ISNACGTIGL IHAIANNKDK MHFESGSTLK
KFLEESASMS PEERARYLEN YDAIRVTHET SAHEGQTEAP NIDEKVDLHF IALVHVDGHL
YELDGRKPFP INHGETSDET LLEDAIEVCK KFMERDPDEL RFNAIALSAA
