ID   UBP10_XENTR             Reviewed;         805 AA.
AC   Q6DIJ4;
DT   23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   27-MAR-2024, entry version 100.
DE   RecName: Full=Ubiquitin carboxyl-terminal hydrolase 10;
DE            EC=3.4.19.12 {ECO:0000250|UniProtKB:Q14694};
DE   AltName: Full=Deubiquitinating enzyme 10;
DE   AltName: Full=Ubiquitin thioesterase 10;
DE   AltName: Full=Ubiquitin-specific-processing protease 10;
GN   Name=usp10; ORFNames=TGas137m11.1;
OS   Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX   NCBI_TaxID=8364;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Gastrula;
RG   Sanger Xenopus tropicalis EST/cDNA project;
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Hydrolase that can remove conjugated ubiquitin from target
CC       proteins such as p53/tp53, rps2/us5, rps3/us3, rps10/eS10, becn1, snx3
CC       and cftr. Acts as an essential regulator of p53/tp53 stability: in
CC       unstressed cells, specifically deubiquitinates p53/tp53 in the
CC       cytoplasm, leading to counteracts MDM2 action and stabilize p53/tp53.
CC       Following DNA damage, translocates to the nucleus and deubiquitinates
CC       p53/tp53, leading to regulate the p53/TP53-dependent DNA damage
CC       response. Component of a regulatory loop that controls autophagy and
CC       p53/tp53 levels. Plays a key role in 40S ribosome subunit recycling
CC       when a ribosome has stalled during translation: acts both by inhibiting
CC       formation of stress granules, which store stalled translation pre-
CC       initiation complexes, and mediating deubiquitination of 40S ribosome
CC       subunits. Deubiquitinates cftr in early endosomes, enhancing its
CC       endocytic recycling. {ECO:0000250|UniProtKB:Q14694}.
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:Q14694};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q14694}. Nucleus
CC       {ECO:0000250|UniProtKB:Q14694}.
CC   -!- SIMILARITY: Belongs to the peptidase C19 family. USP10 subfamily.
CC       {ECO:0000305}.
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DR   EMBL; CR855702; CAJ83514.1; -; mRNA.
DR   EMBL; BC075544; AAH75544.1; -; mRNA.
DR   RefSeq; NP_001006761.1; NM_001006760.1.
DR   AlphaFoldDB; Q6DIJ4; -.
DR   SMR; Q6DIJ4; -.
DR   STRING; 8364.ENSXETP00000016806; -.
DR   MEROPS; C19.018; -.
DR   DNASU; 448441; -.
DR   GeneID; 448441; -.
DR   KEGG; xtr:448441; -.
DR   AGR; Xenbase:XB-GENE-966184; -.
DR   CTD; 9100; -.
DR   Xenbase; XB-GENE-966184; usp10.
DR   InParanoid; Q6DIJ4; -.
DR   OMA; RTCGSPQ; -.
DR   OrthoDB; 55585at2759; -.
DR   Proteomes; UP000008143; Chromosome 4.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005769; C:early endosome; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0004843; F:cysteine-type deubiquitinase activity; ISS:UniProtKB.
DR   GO; GO:0004197; F:cysteine-type endopeptidase activity; ISS:UniProtKB.
DR   GO; GO:0002039; F:p53 binding; ISS:UniProtKB.
DR   GO; GO:0044325; F:transmembrane transporter binding; ISS:UniProtKB.
DR   GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
DR   GO; GO:0071347; P:cellular response to interleukin-1; ISS:UniProtKB.
DR   GO; GO:0006974; P:DNA damage response; ISS:UniProtKB.
DR   GO; GO:0030330; P:DNA damage response, signal transduction by p53 class mediator; ISS:UniProtKB.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   GO; GO:0043124; P:negative regulation of canonical NF-kappaB signal transduction; ISS:UniProtKB.
DR   GO; GO:0062030; P:negative regulation of stress granule assembly; ISS:UniProtKB.
DR   GO; GO:0016579; P:protein deubiquitination; ISS:UniProtKB.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   GO; GO:0010506; P:regulation of autophagy; ISS:UniProtKB.
DR   GO; GO:0072344; P:rescue of stalled ribosome; ISS:UniProtKB.
DR   CDD; cd02257; Peptidase_C19; 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; IPR018200; USP_CS.
DR   InterPro; IPR028889; USP_dom.
DR   PANTHER; PTHR24006; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR   PANTHER; PTHR24006:SF687; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 10; 1.
DR   Pfam; PF00443; UCH; 1.
DR   SUPFAM; SSF54001; Cysteine proteinases; 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   Autophagy; Cytoplasm; DNA damage; DNA repair; Hydrolase; Nucleus; Protease;
KW   Reference proteome; Thiol protease; Ubl conjugation pathway.
FT   CHAIN           1..805
FT                   /note="Ubiquitin carboxyl-terminal hydrolase 10"
FT                   /id="PRO_0000393004"
FT   DOMAIN          422..802
FT                   /note="USP"
FT   REGION          139..170
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          561..593
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        431
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT                   ECO:0000255|PROSITE-ProRule:PRU10093"
FT   ACT_SITE        756
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT                   ECO:0000255|PROSITE-ProRule:PRU10093"
SQ   SEQUENCE   805 AA;  88936 MW;  F95A8A2A4FB60DD1 CRC64;
     MASPSGQYIF GEFSDDEFKQ FFVTARCTVE LPPYNEHFFP CGPQSSGDFQ DDMHLKFSEV
     IHGISGEDCP RIEFGIEEVI DHSTALPNNT DYSISSNLNP QAPEFILTCS SSPKTSNNVL
     HENNFDAINC QFSECAIPDG SGNADSDGTS GTGQRERKKK KKRPPGYYSY LEGVGDVPSE
     TLVNGHANST GLNSISTDDP DLAEDIPIST TSPRTCNSPD NFVDLNNEAL SNDASMHNAL
     DNARTAGQPE ECSVTSSEQS CIPSDNGRES PVRTAVVQPF AGTDTTENLG VTNGQTLESS
     EEGTASNGVV LLPEVSSLSE EAKPEETSTA QAVVHLPGSA SANPPAKSWA SLFHNSKPSS
     TTQVAYVETK NATPVTSPQV TEKQVEIKEG PVPVSEDPVA IKIAELLEEV KLVHKPVSLQ
     PRGLINKGNW CYINATLQAL VACPPMYHLM KSIPVYTKAQ RPCTSTPMID SFVRLMNEFT
     NMPILPKAKQ ASGEKVIRDI RPGAPFEPAY IYRLLTVFKS SLSEKGRQED AEEYLGFILN
     GLHEEMLSLK KLLLPQNDKI HINNGPDPVS EKEEINKDEQ EGSDEEWEQV GPRHKSSVTR
     QADFVQTPIT DIFGGHMRSV VYQQSSKESA TLQPFFTLQL DIQSEKIRTV QDALESLVAR
     ESVQGYTTKT KQEVEICRRV TLEELPPVLV LHLKRFVFEK TGGCQKLIKN IEYPVDLEIS
     KDLLSPGVKS KIFKGQRTYR LFAVVYHHGN SATGGHYTTD VFQIGLNGWL RIDDQTVKVI
     NQYQVVKQTV ERTAYLLYYR RVDLL
//