UCHL5_PIG
ID UCHL5_PIG Reviewed; 329 AA.
AC Q06AT3;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase isozyme L5;
DE Short=UCH-L5;
DE EC=3.4.19.12;
DE AltName: Full=Ubiquitin thioesterase L5;
GN Name=UCHL5;
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: Protease that specifically cleaves 'Lys-48'-linked
CC polyubiquitin chains. Deubiquitinating enzyme associated with the 19S
CC regulatory subunit of the 26S proteasome. Putative regulatory component
CC of the INO80 complex; however is inactive in the INO80 complex and is
CC activated by a transient interaction of the INO80 complex with the
CC proteasome via ADRM1 (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;
CC -!- ACTIVITY REGULATION: Activated by ADRM1. Inhibited by interaction with
CC NFRKB (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Component of the 19S (PA700) regulatory complex of the 26S
CC proteasome. Interacts with ADRM1 and NFRKB. Component of the INO80
CC complex; specifically part of a complex module associated with N-
CC terminus of INO80 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC Note=Associates with the proteasome 19S subunit in the cytoplasm.
CC Associates with the INO80 complex in the nucleus (By similarity).
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase C12 family. {ECO:0000305}.
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DR EMBL; DQ917642; ABI97187.1; -; mRNA.
DR RefSeq; NP_001116682.1; NM_001123210.1.
DR RefSeq; XP_013845139.1; XM_013989685.1.
DR AlphaFoldDB; Q06AT3; -.
DR SMR; Q06AT3; -.
DR STRING; 9823.ENSSSCP00000011515; -.
DR PaxDb; Q06AT3; -.
DR PeptideAtlas; Q06AT3; -.
DR Ensembl; ENSSSCT00070023679; ENSSSCP00070019586; ENSSSCG00070012107.
DR GeneID; 100144472; -.
DR KEGG; ssc:100144472; -.
DR CTD; 51377; -.
DR eggNOG; KOG2778; Eukaryota.
DR InParanoid; Q06AT3; -.
DR OrthoDB; 1363547at2759; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Chromosome 10.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0031011; C:Ino80 complex; IEA:InterPro.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0000502; C:proteasome complex; IEA:UniProtKB-KW.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; ISS:UniProtKB.
DR GO; GO:0070628; F:proteasome binding; IEA:InterPro.
DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0016579; P:protein deubiquitination; ISS:UniProtKB.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR CDD; cd02255; Peptidase_C12; 1.
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; IPR017390; Ubiquitinyl_hydrolase_UCH37.
DR InterPro; IPR033837; UCH37.
DR InterPro; IPR041507; UCH_C.
DR PANTHER; PTHR10589; PTHR10589; 1.
DR Pfam; PF01088; Peptidase_C12; 1.
DR Pfam; PF18031; UCH_C; 1.
DR PIRSF; PIRSF038120; Ubiquitinyl_hydrolase_UCH37; 1.
DR PRINTS; PR00707; UBCTHYDRLASE.
DR SUPFAM; SSF54001; SSF54001; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Cytoplasm; DNA damage; DNA recombination; DNA repair;
KW Hydrolase; Nucleus; Protease; Proteasome; Reference proteome;
KW Thiol protease; Transcription; Transcription regulation;
KW Ubl conjugation pathway.
FT CHAIN 1..329
FT /note="Ubiquitin carboxyl-terminal hydrolase isozyme L5"
FT /id="PRO_0000288777"
FT REGION 313..329
FT /note="Interaction with ADRM1"
FT /evidence="ECO:0000250"
FT ACT_SITE 88
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 164
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT SITE 179
FT /note="Important for enzyme activity"
FT /evidence="ECO:0000250"
FT MOD_RES 47
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9WUP7"
FT MOD_RES 158
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y5K5"
FT MOD_RES 289
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9WUP7"
SQ SEQUENCE 329 AA; 37577 MW; EAB066D16BA51EA5 CRC64;
MTGNAGEWCL MESDPGVFTE LIKGFGCRGA QVEEIWSLEP ENFEKLKPVH GLIFLFKWQP
GEEPAGSVVQ DSRLDTIFFA KQVINNACAT QAIVSVLLNC THQDVHLGET LSEFKEFSQS
FDAAMKGLAL SNSDVIRQVH NSFARQQMFE FDAKTSAKEE DAFHFVSYVP VNGRLYELDG
LREGPIDLGA CNQDDWISAV RPVIEKRIQK YSEGEIRFNL MAIVSDRKMI YEQKIAELQR
QLAEEEPMDT DQGSNMLSAI QSEVAKNQML IEEEVQKLKR YKIENIRRKH NYLPFIMELL
KTLAEHQQLI PLVEKAKEKQ NAKKAQETK
