UBH4_CAEEL
ID UBH4_CAEEL Reviewed; 321 AA.
AC Q09444;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 2.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase ubh-4 {ECO:0000305};
DE EC=3.4.19.12 {ECO:0000305|PubMed:23770237};
DE AltName: Full=Ubiquitin C-terminal hydrolase family 1 member 4 {ECO:0000312|WormBase:C08B11.7};
DE AltName: Full=Ubiquitin thioesterase 4 {ECO:0000305};
GN Name=ubh-4 {ECO:0000312|WormBase:C08B11.7};
GN ORFNames=C08B11.7 {ECO:0000312|WormBase:C08B11.7};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH RPN-13, TISSUE SPECIFICITY,
RP INDUCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=23770237; DOI=10.1016/j.celrep.2013.05.012;
RA Matilainen O., Arpalahti L., Rantanen V., Hautaniemi S., Holmberg C.I.;
RT "Insulin/IGF-1 signaling regulates proteasome activity through the
RT deubiquitinating enzyme UBH-4.";
RL Cell Rep. 3:1980-1995(2013).
CC -!- FUNCTION: Ubiquitin-protein hydrolase involved both in the processing
CC of ubiquitin precursors and of ubiquitinated proteins. This enzyme is a
CC thiol protease that recognizes and hydrolyzes a peptide bond at the C-
CC terminal glycine of ubiquitin. {ECO:0000305|PubMed:23770237}.
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:0000305|PubMed:23770237};
CC -!- SUBUNIT: Interacts with proteasome 19S subunit rpn-13.
CC {ECO:0000269|PubMed:23770237}.
CC -!- TISSUE SPECIFICITY: Highly expressed in intestine and to a lesser
CC extent in other tissues including muscles and neurons.
CC {ECO:0000269|PubMed:23770237}.
CC -!- INDUCTION: Expression decreases with age.
CC {ECO:0000269|PubMed:23770237}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown causes a slight decrease
CC in lifespan and in brood size. Enhanced proteasome activity,
CC specifically in the intestine. {ECO:0000269|PubMed:23770237}.
CC -!- SIMILARITY: Belongs to the peptidase C12 family. {ECO:0000305}.
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DR EMBL; Z46676; CAA86665.2; -; Genomic_DNA.
DR PIR; T19070; T19070.
DR RefSeq; NP_495684.2; NM_063283.4.
DR AlphaFoldDB; Q09444; -.
DR SMR; Q09444; -.
DR BioGRID; 39621; 6.
DR DIP; DIP-26660N; -.
DR IntAct; Q09444; 1.
DR STRING; 6239.C08B11.7; -.
DR MEROPS; C12.005; -.
DR EPD; Q09444; -.
DR PaxDb; Q09444; -.
DR PeptideAtlas; Q09444; -.
DR EnsemblMetazoa; C08B11.7.1; C08B11.7.1; WBGene00006724.
DR EnsemblMetazoa; C08B11.7.2; C08B11.7.2; WBGene00006724.
DR GeneID; 174289; -.
DR UCSC; C08B11.7; c. elegans.
DR CTD; 174289; -.
DR WormBase; C08B11.7; CE36913; WBGene00006724; ubh-4.
DR eggNOG; KOG2778; Eukaryota.
DR GeneTree; ENSGT00940000155195; -.
DR HOGENOM; CLU_018316_0_1_1; -.
DR InParanoid; Q09444; -.
DR OMA; DGAGNWC; -.
DR OrthoDB; 1363547at2759; -.
DR PhylomeDB; Q09444; -.
DR Reactome; R-CEL-5689603; UCH proteinases.
DR PRO; PR:Q09444; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00006724; Expressed in germ line (C elegans) and 4 other tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IMP:UniProtKB.
DR GO; GO:0032435; P:negative regulation of proteasomal ubiquitin-dependent protein catabolic process; IMP:UniProtKB.
DR GO; GO:0016579; P:protein deubiquitination; IMP:UniProtKB.
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 InterPro; IPR017390; Ubiquitinyl_hydrolase_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 1: Evidence at protein level;
KW Hydrolase; Protease; Reference proteome; Thiol protease;
KW Ubl conjugation pathway.
FT CHAIN 1..321
FT /note="Ubiquitin carboxyl-terminal hydrolase ubh-4"
FT /id="PRO_0000211071"
FT ACT_SITE 83
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P09936"
FT ACT_SITE 158
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P09936"
FT SITE 173
FT /note="Important for enzyme activity"
FT /evidence="ECO:0000250|UniProtKB:P09936"
SQ SEQUENCE 321 AA; 37120 MW; F6A658161FC13AD5 CRC64;
MTDAGSWCLI ESDPGVFTEM LRGFGVDGLQ VEELYSLDDD KAMTRPTYGL IFLFKWRQGD
ETTGIPSDKQ NIFFAHQTIQ NACATQALIN LLMNVEDTDV KLGNILNQYK EFAIDLDPNT
RGHCLSNSEE IRTVHNSFSR QTLFELDIKG GESEDNYHFV TYVPIGNKVY ELDGLRELPL
EVAEFQKEQD WIEAIKPVIQ QRMQKYSEGE ITFNLMALVP NRKQKLQEMM ENLIQANENN
ELEEQIADLN KAIADEDYKM EMYRKENNRR RHNYTPFVIE LMKILAKEGK LVGLVDNAYQ
AAKEKSKLNT DITKLELKRK Q
