ID   UBP14_CAEEL             Reviewed;         489 AA.
AC   Q17361; O45248;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2002, sequence version 2.
DT   27-MAR-2024, entry version 153.
DE   RecName: Full=Ubiquitin carboxyl-terminal hydrolase 14;
DE            EC=3.4.19.12;
DE   AltName: Full=Deubiquitinating enzyme 14;
DE   AltName: Full=Ubiquitin thioesterase 14;
DE   AltName: Full=Ubiquitin-specific-processing protease 14;
GN   Name=usp-14; Synonyms=tgt-1; ORFNames=C13B4.2;
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 [MRNA].
RC   STRAIN=Bristol N2;
RA   Deshpande K.L., Katze J.R.;
RL   Submitted (AUG-1995) to the EMBL/GenBank/DDBJ databases.
RN   [2]
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).
CC   -!- FUNCTION: Proteasome-associated deubiquitinase which releases ubiquitin
CC       from the proteasome targeted ubiquitinated proteins. Ensures the
CC       regeneration of ubiquitin at the proteasome (By similarity).
CC       {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   -!- SIMILARITY: Belongs to the peptidase C19 family. USP14/UBP6 subfamily.
CC       {ECO:0000305}.
CC   -!- CAUTION: Was originally (Ref.1) thought to be a queuine tRNA-
CC       ribosyltransferase. {ECO:0000305}.
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DR   EMBL; U32223; AAA74956.1; -; mRNA.
DR   EMBL; Z81468; CAB03876.1; -; Genomic_DNA.
DR   EMBL; Z83236; CAB03876.1; JOINED; Genomic_DNA.
DR   PIR; T19227; T19227.
DR   RefSeq; NP_497006.1; NM_064605.8.
DR   AlphaFoldDB; Q17361; -.
DR   SMR; Q17361; -.
DR   BioGRID; 40386; 21.
DR   STRING; 6239.C13B4.2.1; -.
DR   MEROPS; C19.A36; -.
DR   EPD; Q17361; -.
DR   PaxDb; 6239-C13B4-2; -.
DR   PeptideAtlas; Q17361; -.
DR   EnsemblMetazoa; C13B4.2.1; C13B4.2.1; WBGene00006856.
DR   GeneID; 175105; -.
DR   KEGG; cel:CELE_C13B4.2; -.
DR   UCSC; C13B4.2.1; c. elegans.
DR   AGR; WB:WBGene00006856; -.
DR   WormBase; C13B4.2; CE15615; WBGene00006856; usp-14.
DR   eggNOG; KOG1872; Eukaryota.
DR   GeneTree; ENSGT00390000009615; -.
DR   HOGENOM; CLU_017549_2_1_1; -.
DR   InParanoid; Q17361; -.
DR   OMA; FKSDAEY; -.
DR   OrthoDB; 160664at2759; -.
DR   PhylomeDB; Q17361; -.
DR   Reactome; R-CEL-5689880; Ub-specific processing proteases.
DR   PRO; PR:Q17361; -.
DR   Proteomes; UP000001940; Chromosome II.
DR   Bgee; WBGene00006856; Expressed in germ line (C elegans) and 4 other cell types or tissues.
DR   GO; GO:0000502; C:proteasome complex; IEA:UniProtKB-KW.
DR   GO; GO:0004843; F:cysteine-type deubiquitinase activity; IBA:GO_Central.
DR   GO; GO:0070628; F:proteasome binding; IBA:GO_Central.
DR   GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR   GO; GO:0061136; P:regulation of proteasomal protein catabolic process; IBA:GO_Central.
DR   CDD; cd02657; Peptidase_C19A; 1.
DR   CDD; cd16104; Ubl_USP14_like; 1.
DR   Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   InterPro; IPR001394; Peptidase_C19_UCH.
DR   InterPro; IPR000626; Ubiquitin-like_dom.
DR   InterPro; IPR029071; Ubiquitin-like_domsf.
DR   InterPro; IPR044635; UBP14-like.
DR   InterPro; IPR018200; USP_CS.
DR   InterPro; IPR028889; USP_dom.
DR   PANTHER; PTHR43982; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR   PANTHER; PTHR43982:SF1; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 14; 1.
DR   Pfam; PF00443; UCH; 1.
DR   SMART; SM00213; UBQ; 1.
DR   SUPFAM; SSF54001; Cysteine proteinases; 1.
DR   SUPFAM; SSF54236; Ubiquitin-like; 1.
DR   PROSITE; PS00972; USP_1; 1.
DR   PROSITE; PS00973; USP_2; 1.
DR   PROSITE; PS50235; USP_3; 1.
PE   2: Evidence at transcript level;
KW   Hydrolase; Protease; Proteasome; Reference proteome; Thiol protease;
KW   Ubl conjugation pathway.
FT   CHAIN           1..489
FT                   /note="Ubiquitin carboxyl-terminal hydrolase 14"
FT                   /id="PRO_0000080640"
FT   DOMAIN          102..458
FT                   /note="USP"
FT   REGION          467..489
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        111
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT                   ECO:0000255|PROSITE-ProRule:PRU10093"
FT   ACT_SITE        409
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT                   ECO:0000255|PROSITE-ProRule:PRU10093"
FT   CONFLICT        398
FT                   /note="I -> M (in Ref. 1; AAA74956)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   489 AA;  55878 MW;  4433F2CC59703A9B CRC64;
     MPIVNVKWQK EKYVVEVDTS APPMVFKAQL FALTQVVPER QKVVIMGRTL GDDDWEGITI
     KENMTIMMMG SVGEIPKPPT VLEKKQANRD KQAEEISALY PCGLANLGNT CYFNSCVQML
     KEVNELVLKP AEEMRIREHN DRLCHNLATL FNSLRDKDRA LRSKGEPIKP FAAILTLSDS
     FPQFEKFKQQ DANECLVSIM SNVTRIYGLS GWNIESLFRI QTETTMKCLE SDEVSEKKVE
     RNNQLTCYVN QDVRFLQTGI KAGFEEEMTR NSEELNRDAK WQKNTQISRL PKYLTVNINR
     FFYKESTKTN AKILKSVQFP MQLDTYDLCS QELKDKLVAR RADIKLEEDA KLERELRKKV
     LDKEQGDKIF DDGVALPTAF EDDAGSNNSG FYDLKGIITH KGRSSQDGHY VAWMRSSEDG
     KWRLFDDEHV TVVDEEAILK TSGGGDWHSA YVLLYEARVI KQFPELPPAP VPTEVAADTA
     EPMEVSEKQ
//