UCHL5_BOVIN
ID UCHL5_BOVIN Reviewed; 328 AA.
AC Q9XSJ0; Q3MHN9;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase isozyme L5;
DE Short=UCH-L5;
DE EC=3.4.19.12;
DE AltName: Full=Ubiquitin C-terminal hydrolase UCH37;
DE AltName: Full=Ubiquitin thioesterase L5;
GN Name=UCHL5; Synonyms=UCH37;
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 [MRNA].
RX PubMed=16906146; DOI=10.1038/ncb1460;
RA Yao T., Song L., Xu W., DeMartino G.N., Florens L., Swanson S.K.,
RA Washburn M.P., Conaway R.C., Conaway J.W., Cohen R.E.;
RT "Proteasome recruitment and activation of the Uch37 deubiquitinating enzyme
RT by Adrm1.";
RL Nat. Cell Biol. 8:994-1002(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (SEP-2005) 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; AF148446; AAD31533.1; -; mRNA.
DR EMBL; BC105166; AAI05167.1; -; mRNA.
DR RefSeq; NP_776906.2; NM_174481.3.
DR AlphaFoldDB; Q9XSJ0; -.
DR SMR; Q9XSJ0; -.
DR STRING; 9913.ENSBTAP00000018104; -.
DR MEROPS; C12.005; -.
DR PaxDb; Q9XSJ0; -.
DR PRIDE; Q9XSJ0; -.
DR Ensembl; ENSBTAT00000018104; ENSBTAP00000018104; ENSBTAG00000013620.
DR GeneID; 282110; -.
DR KEGG; bta:282110; -.
DR CTD; 51377; -.
DR VEuPathDB; HostDB:ENSBTAG00000013620; -.
DR VGNC; VGNC:36633; UCHL5.
DR eggNOG; KOG2778; Eukaryota.
DR GeneTree; ENSGT00940000155195; -.
DR HOGENOM; CLU_018316_0_0_1; -.
DR InParanoid; Q9XSJ0; -.
DR OMA; DGAGNWC; -.
DR OrthoDB; 1363547at2759; -.
DR TreeFam; TF313976; -.
DR BRENDA; 3.4.19.12; 908.
DR Proteomes; UP000009136; Chromosome 16.
DR Bgee; ENSBTAG00000013620; Expressed in saliva-secreting gland and 106 other tissues.
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:Ensembl.
DR GO; GO:0005730; C:nucleolus; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
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; IDA:UniProtKB.
DR GO; GO:0004866; F:endopeptidase inhibitor activity; IEA:Ensembl.
DR GO; GO:0070628; F:proteasome binding; IDA:UniProtKB.
DR GO; GO:0006338; P:chromatin remodeling; IEA:Ensembl.
DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0048853; P:forebrain morphogenesis; IEA:Ensembl.
DR GO; GO:0021670; P:lateral ventricle development; IEA:Ensembl.
DR GO; GO:0030901; P:midbrain development; IEA:Ensembl.
DR GO; GO:0032435; P:negative regulation of proteasomal ubiquitin-dependent protein catabolic process; IEA:Ensembl.
DR GO; GO:0045739; P:positive regulation of DNA repair; IEA:Ensembl.
DR GO; GO:0045880; P:positive regulation of smoothened signaling pathway; IEA:Ensembl.
DR GO; GO:1904507; P:positive regulation of telomere maintenance in response to DNA damage; IEA:Ensembl.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IEA:Ensembl.
DR GO; GO:0016579; P:protein deubiquitination; ISS:UniProtKB.
DR GO; GO:0051726; P:regulation of cell cycle; IEA:Ensembl.
DR GO; GO:0006275; P:regulation of DNA replication; IEA:Ensembl.
DR GO; GO:0060382; P:regulation of DNA strand elongation; IEA:Ensembl.
DR GO; GO:0045995; P:regulation of embryonic development; IEA:Ensembl.
DR GO; GO:0000723; P:telomere maintenance; IEA:Ensembl.
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..328
FT /note="Ubiquitin carboxyl-terminal hydrolase isozyme L5"
FT /id="PRO_0000211065"
FT REGION 312..328
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 288
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9WUP7"
FT CONFLICT 306
FT /note="Q -> K (in Ref. 2; AAI05167)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 328 AA; 37432 MW; D6EFE9C71900CBB0 CRC64;
MTGNAGEWCL MESDPGVFTE LIKGFGCRGA QVEEIWSLEP ENFEKLKPVH GLIFLFKWQP
GEEPAGSVVQ DSRLDTIFFA KQVINNACAT QAIVSVLLNC THQDVHLGET LSEFKEFSQS
FDAAMKGLAL SNSDVIRQVH NSFARQQMFE FDAKTAAKEE DAFHFVSYVP VNGRLYELDG
LREGPIDLGA CNQDDWISAV RPVIEKRIQK YSEGEIRFNL MAIVSDRKMI YEQKIAELQR
QLAEEPMDTD QGSNMLSAIQ SEVAKNQMLI EEEVQKLKRY KIENIRRKHN YLPFIMELLK
TLAEHQQLIP LVEKAKEKQN AKKAQETK
