ID A0A452QFS1_URSAM Unreviewed; 793 AA.
AC A0A452QFS1;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 24.
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:ENSUAMP00000003730.1};
OS Ursus americanus (American black bear) (Euarctos americanus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Ursidae; Ursus.
OX NCBI_TaxID=9643 {ECO:0000313|Ensembl:ENSUAMP00000003730.1, ECO:0000313|Proteomes:UP000291022};
RN [1] {ECO:0000313|Proteomes:UP000291022}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Korstanje R., Srivastava A., Sarsani V.K., Sheehan S.M., Seger R.L.,
RA Barter M.E., Lindqvist C., Brody L.C., Mullikin J.C.;
RT "De novo assembly and RNA-Seq shows season-dependent expression and editing
RT in black bear kidneys.";
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSUAMP00000003730.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- FUNCTION: Deubiquitinating enzyme that removes conjugated ubiquitin
CC from specific proteins to regulate different cellular processes.
CC {ECO:0000256|RuleBase:RU366025}.
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 -!- SIMILARITY: Belongs to the peptidase C19 family. USP10 subfamily.
CC {ECO:0000256|ARBA:ARBA00005427}.
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DR AlphaFoldDB; A0A452QFS1; -.
DR Ensembl; ENSUAMT00000004249.1; ENSUAMP00000003730.1; ENSUAMG00000003075.1.
DR GeneTree; ENSGT00550000074994; -.
DR Proteomes; UP000291022; Unassembled WGS sequence.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd02257; Peptidase_C19; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR InterPro; IPR009818; Ataxin-2_C.
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; 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 DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW Hydrolase {ECO:0000256|RuleBase:RU366025};
KW Protease {ECO:0000256|RuleBase:RU366025};
KW Reference proteome {ECO:0000313|Proteomes:UP000291022};
KW Thiol protease {ECO:0000256|RuleBase:RU366025};
KW Ubl conjugation pathway {ECO:0000256|RuleBase:RU366025}.
FT DOMAIN 414..790
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 136..165
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 224..252
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 307..361
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 548..587
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 330..361
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 793 AA; 86237 MW; B7EBEAC2B0DDE6BD CRC64;
RLTHNPEMKS NFSPDEFNQF FVTPRSSVEL PPYSGAVVCG PPATDELPDG QEYQRIEFGV
NEVIEPNDTL PRTPNYSISS TLNPQAPEFI LSCTTSKKTP DDLDKEATYS SVDCQYPGSS
LALDGSSSTE VEVLESDGVT GGLGQRERKK KKKRPPGYYS YLKDGGEGSI PTEALVNGHA
NPAVPNSVGS EDAELVGDMP PSGTPRTCNS PQDSTDFVSD AVPAGPFPGA LDDDSRTAGQ
PEGCPGADSV QSCLPAEAGR DSLLRTAVAQ PYTGTHTTEN LGVANGQILE SSGEGSAANG
VELHTVESAD SDPAKAGSAP PAADALAAAT GTAPTSQPKS WASLFHDSKP SPSSPVASVE
TKYSPPATSA LASEKQIEVK EGLVPVSEDP VAVKIAELLE NVTLIHKPVS LQPRGLINKG
NWCYINATLQ ALVACPPMYH LMKFIPLYSK VQRPCTSTPM IDSLLHFRYE NLCPVSIAAL
GDKIVRDIRP GAAFEPTYIY RLLTVIKSSL SEKGRQEDAE EYLGFILNGL HEEMLNLKKL
LSPNNTKLTI SNGPKSHSVN EDEQEEPGEG SEDEWEQVGP RNKTSVTRQA EFVQTPITGI
FGGHIRSVVY QQSSKESATL QPFFTLQLDI QSDRIRTVQD ALESLVARES VQGYTTKTKQ
EVEISRRVTL EKLPPVLVLH LKRFVYEKTG GCQKLIKNIE YPVDLEISKE LLSPGVKNKN
FKCHRTYRLF AVVYHHGSSA TGGHYTTDVF QIGLNGWLRI DDQAVKVINQ YQVVKPTAER
TAYLLYYRRV DLL
//
