UCHL3_PIG
ID UCHL3_PIG Reviewed; 230 AA.
AC Q06AB3;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 64.
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 Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Liu G.Y.;
RL Submitted (AUG-2006) 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, and exhibits a
CC preference towards 'Lys-48'-linked ubiquitin chains. Deubiquitinates
CC ENAC in apical compartments, thereby regulating apical membrane
CC recycling. Indirectly increases the phosphorylation of IGFIR, AKT and
CC FOXO1 and promotes insulin-signaling and insulin-induced adipogenesis.
CC Required for stress-response retinal, skeletal muscle and germ cell
CC maintenance. May be involved in working memory. Can hydrolyze UBB(+1),
CC a mutated form of ubiquitin which is not effectively degraded by the
CC 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; DQ972951; ABI96187.1; -; mRNA.
DR RefSeq; NP_001070695.1; NM_001077227.1.
DR AlphaFoldDB; Q06AB3; -.
DR BMRB; Q06AB3; -.
DR SMR; Q06AB3; -.
DR STRING; 9823.ENSSSCP00000010107; -.
DR MEROPS; C12.003; -.
DR PaxDb; Q06AB3; -.
DR PeptideAtlas; Q06AB3; -.
DR PRIDE; Q06AB3; -.
DR GeneID; 768115; -.
DR KEGG; ssc:768115; -.
DR CTD; 7347; -.
DR eggNOG; KOG1415; Eukaryota.
DR InParanoid; Q06AB3; -.
DR OrthoDB; 1013351at2759; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
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_0000289800"
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; 26090 MW; 1C12B99BAA02E427 CRC64;
MEGQRWLPLE ANPEVTNQFL KQLGLHPNWQ FVDVYGMDPE LLSMVPRPVC AVLLLFPITE
KYEVFRTEEE EKIKSQGQDV TPSVYFMKQT ISNACGTIGL IHAIANNKNK MHFESGSTLK
KFLEESASMS PDERARYLES YDAIPVTHET SAHEGQTEAP NIDEKVDLHF IALVHVDGHL
YELDGRKPFP INHGETSDET LLEDAIEVCK KFMERDPDEL RFNAIALSAA
