ID A0A663DYT0_AQUCH Unreviewed; 789 AA.
AC A0A663DYT0;
DT 17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 1.
DT 18-JUN-2025, entry version 26.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase {ECO:0000256|RuleBase:RU366025};
DE EC=3.4.19.12 {ECO:0000256|RuleBase:RU366025};
GN Name=USP10 {ECO:0000313|Ensembl:ENSACCP00020005082.1};
OS Aquila chrysaetos chrysaetos.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Neoaves; Telluraves; Accipitrimorphae;
OC Accipitriformes; Accipitridae; Accipitrinae; Aquila.
OX NCBI_TaxID=223781 {ECO:0000313|Ensembl:ENSACCP00020005082.1, ECO:0000313|Proteomes:UP000472275};
RN [1] {ECO:0000313|Ensembl:ENSACCP00020005082.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (MAR-2025) to UniProtKB.
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:0000256|ARBA:ARBA00000707,
CC ECO:0000256|RuleBase:RU366025};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the peptidase C19 family. USP10 subfamily.
CC {ECO:0000256|ARBA:ARBA00005427}.
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DR RefSeq; XP_029881445.1; XM_030025585.2.
DR AlphaFoldDB; A0A663DYT0; -.
DR FunCoup; A0A663DYT0; 425.
DR Ensembl; ENSACCT00020005298.1; ENSACCP00020005082.1; ENSACCG00020003492.1.
DR GeneID; 115345994; -.
DR GeneTree; ENSGT00550000074994; -.
DR InParanoid; A0A663DYT0; -.
DR OrthoDB; 429671at2759; -.
DR Proteomes; UP000472275; Chromosome 9.
DR GO; GO:0022626; C:cytosolic ribosome; IEA:Ensembl.
DR GO; GO:0005769; C:early endosome; IEA:Ensembl.
DR GO; GO:0045111; C:intermediate filament cytoskeleton; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0032991; C:protein-containing complex; IEA:Ensembl.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:Ensembl.
DR GO; GO:0140678; F:molecular function inhibitor activity; IEA:Ensembl.
DR GO; GO:0002039; F:p53 binding; IEA:Ensembl.
DR GO; GO:0044325; F:transmembrane transporter binding; IEA:Ensembl.
DR GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
DR GO; GO:0071347; P:cellular response to interleukin-1; IEA:Ensembl.
DR GO; GO:0030330; P:DNA damage response, signal transduction by p53 class mediator; IEA:Ensembl.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0035520; P:monoubiquitinated protein deubiquitination; IEA:Ensembl.
DR GO; GO:0043124; P:negative regulation of canonical NF-kappaB signal transduction; IEA:Ensembl.
DR GO; GO:0062030; P:negative regulation of stress granule assembly; IEA:Ensembl.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0010506; P:regulation of autophagy; IEA:Ensembl.
DR GO; GO:0072344; P:rescue of stalled ribosome; IEA:Ensembl.
DR CDD; cd02257; Peptidase_C19; 1.
DR FunFam; 3.90.70.10:FF:000015; Ubiquitin specific peptidase 10; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR InterPro; IPR009818; PAM2_motif.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR050164; Peptidase_C19.
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; PF07145; PAM2; 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 3: Inferred from homology;
KW Autophagy {ECO:0000256|ARBA:ARBA00023006};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU366025};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU366025};
KW Reference proteome {ECO:0000313|Proteomes:UP000472275};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807,
KW ECO:0000256|RuleBase:RU366025};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|RuleBase:RU366025}.
FT DOMAIN 405..786
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 119..148
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 296..315
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 541..585
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 296..308
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 556..572
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 789 AA; 86927 MW; 426D1207E2634999 CRC64;
MAVNSAQYIF GEFSPDEFNQ FFVTPRCSVE LPPYNETVSC GIKSTGEEYQ RIEFGVNEVI
ETQSSVLNNT DYSISSTLNP QAPEFILSCA PAQKTPDDTL GETNYNSIDC QFTDPTLALD
SGSNAENDGL SGGLGQRERK KKKKRPPGYY SYLEDVSDGI APTEALVNGH ANSSGLNSIS
TEDTELTGDI PSLATPRTCN SPDNSVDFVN EAVSDDSVSS TLDNTRTAGQ PEVCRVTNSE
QFCIPSETGR DSPLRTAVVQ SYAGTDTTEN LGVTNGQTLE SSGEDTAANG VELHTVESTD
SDQAKPEEAS PTTEATVPVA GSVPVNQPAK SWASLFHNSK PSASTSVVYV ETKYTPPATS
TLVPEKQVEV KEGPVPVSED PVAIKIAEIL ENVRLIHKPV SLQPRGLINK GNWCYINATL
QALVACPPMY HLMKSIPMYS KSQRPCTSTP MIDSFVRLMN EFTNMPVPPK AKQALGDKIV
RDIRPGAAFE PTYIYRLLTV IKSSLSEKGR QEDAEEYLGF ILNGLHEEML TLKKLLSPHN
EKLSVSNGPE AQTVHEEEEQ DEQGEGSEDE WEQVGPRNKS SVTRQADFVQ TPITDIFGGH
IRSVVYQQSS KESATLQPFF TLQLDIQSDK IRTVQDALES LVARESVQGY TTKTKQEVEI
SRRVTLEELP PVLVLHLKRF VYEKTGGCQK LIKNIEYPVD LEISKELLSP GVKSKIFKGQ
RTYRLFAVVY HHGNSATGGH YTTDVFQIGL NGWLRIDDQA VKVINQYQVV KPSAERTAYL
LYYRRVDLL
//
