UB10A_XENLA
ID UB10A_XENLA Reviewed; 791 AA.
AC Q2NL57;
DT 23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 07-FEB-2006, sequence version 1.
DT 03-AUG-2022, entry version 70.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase 10-A;
DE EC=3.4.19.12 {ECO:0000250|UniProtKB:Q14694};
DE AltName: Full=Deubiquitinating enzyme 10-A;
DE AltName: Full=Ubiquitin thioesterase 10-A;
DE AltName: Full=Ubiquitin-specific-processing protease 10-A;
GN Name=usp10-a;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Eye;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Hydrolase that can remove conjugated ubiquitin from target
CC proteins such as p53/tp53. Acts as an essential regulator of p53/tp53
CC stability: in unstressed cells, specifically deubiquitinates p53/tp53
CC in the cytoplasm, leading to counteracts MDM2 action and stabilize
CC p53/tp53. Following DNA damage, translocates to the nucleus and
CC deubiquitinates p53/tp53, leading to regulate the p53/TP53-dependent
CC DNA damage response. Component of a regulatory loop that controls
CC autophagy and p53/tp53 levels (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; 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; BC110953; AAI10954.1; -; mRNA.
DR RefSeq; NP_001090293.1; NM_001096824.1.
DR AlphaFoldDB; Q2NL57; -.
DR SMR; Q2NL57; -.
DR MEROPS; C19.018; -.
DR DNASU; 779202; -.
DR GeneID; 779202; -.
DR KEGG; xla:779202; -.
DR CTD; 779202; -.
DR Xenbase; XB-GENE-966190; usp10.S.
DR OMA; TPRTCDS; -.
DR Proteomes; UP000186698; Chromosome 4S.
DR Bgee; 779202; Expressed in gastrula and 19 other tissues.
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:0006974; P:cellular response to DNA damage stimulus; ISS:UniProtKB.
DR GO; GO:0071347; P:cellular response to interleukin-1; 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 I-kappaB kinase/NF-kappaB signaling; ISS:UniProtKB.
DR GO; GO:0016579; P:protein deubiquitination; ISS:UniProtKB.
DR GO; GO:0010506; P:regulation of autophagy; ISS:UniProtKB.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR028767; USP10.
DR InterPro; IPR018200; USP_CS.
DR InterPro; IPR028889; USP_dom.
DR PANTHER; PTHR13328:SF5; PTHR13328:SF5; 1.
DR Pfam; PF00443; UCH; 1.
DR SUPFAM; SSF54001; SSF54001; 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..791
FT /note="Ubiquitin carboxyl-terminal hydrolase 10-A"
FT /id="PRO_0000393002"
FT DOMAIN 408..788
FT /note="USP"
FT REGION 118..156
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 270..291
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 560..580
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 118..136
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 270..289
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 417
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT ECO:0000255|PROSITE-ProRule:PRU10093"
FT ACT_SITE 742
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT ECO:0000255|PROSITE-ProRule:PRU10093"
SQ SEQUENCE 791 AA; 87563 MW; 650D8F74F5A047F9 CRC64;
MASPSEQYIF GEFSDDEFKQ FFVTARCTVE LPPYNEHFFP CGPQSSGDFQ DGEECPRIEF
GIEEVIDHNT TLPNNTDYSI SSNLNPQAPE FILTCSSSPK DSNNVLHENN FDAIDCQFSE
SSIPDGSGNA DSDGTSGTGQ RERKKKKKRP PGYYSYLEGV GDVPSETLLN GHANSAGLNS
ISTDDPDLAE DIPISTTSPR TCTSPDNFVD LNNEALSDDA SMHNVLDNTR TAGQPEECSV
TSSEQSCIPS DNGRESPVRT AVVQPFAGTD TTENLGVTNG QTLESPEEDT ASNGVVLHPE
VISLSEEAKA EEISTAQAVI HLPGSASANA PAKSWASLFH NSKPSSTPQV AYVETKNTPP
VTSLQVTEKQ VEIKEGPVPV SEDPVAIKIA ELLEEVKLVH KPVSLQPRGL INKGNWCYIN
ATLQALVACP PMYHLMKSIP VYTKAQKPCT STPMIDSFVR LMNEFTNMPI LPKAKQAPGE
KVVRDIRPGA PFEPAYIYRL LTVFKSSLSE KGRQEDAEEY LGFILNGLHE EMLALKKLLL
PQNDKIHINN GPDPVFATEE VNKEEQEGSD EEWEQVGPRN KSSVTRQADF VQTPITDIFG
GHMRSVVYQQ SSKESATLQP FFTLQLDIQS EKIRTVQDAL ESLVARESVQ GYTTKTKQEV
EICRRVTLEE LPPVLVLHLK RFVFEKTGGC QKLIKNIEYP VDLEISKDLL SPGVKSKIFK
GQRTYRLFAV VYHHGNSATG GHYTTDVFQI GLNGWLRIDD QTVKVINQYQ VVKQTVERTA
YLLYYRRVDL L
