ID A0A2Y9KCK3_ENHLU Unreviewed; 798 AA.
AC A0A2Y9KCK3;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase {ECO:0000256|RuleBase:RU366025};
DE EC=3.4.19.12 {ECO:0000256|RuleBase:RU366025};
GN Name=LOC111152789 {ECO:0000313|RefSeq:XP_022367135.1};
OS Enhydra lutris kenyoni (northern sea otter).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC Lutrinae; Enhydra.
OX NCBI_TaxID=391180 {ECO:0000313|Proteomes:UP000248482, ECO:0000313|RefSeq:XP_022367135.1};
RN [1] {ECO:0000313|RefSeq:XP_022367135.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_022367135.1};
RG RefSeq;
RL Submitted (NOV-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 RefSeq; XP_022367135.1; XM_022511427.1.
DR AlphaFoldDB; A0A2Y9KCK3; -.
DR STRING; 391180.A0A2Y9KCK3; -.
DR KEGG; elk:111152789; -.
DR OrthoDB; 55585at2759; -.
DR Proteomes; UP000248482; Unplaced.
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 ECO:0000313|RefSeq:XP_022367135.1};
KW Protease {ECO:0000256|RuleBase:RU366025};
KW Reference proteome {ECO:0000313|Proteomes:UP000248482};
KW Thiol protease {ECO:0000256|RuleBase:RU366025};
KW Ubl conjugation pathway {ECO:0000256|RuleBase:RU366025}.
FT DOMAIN 415..795
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 226..245
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 309..372
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 551..594
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 330..372
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 798 AA; 86721 MW; D0EA31A2D69478EF CRC64;
MALRNPQYIF GDFSPDEFNQ FFVTPRSSVE LPPYSGTVLC GPQDPDELPD GQEYQRIEFG
VNEVIEPSDA LPRAPSYSIS STLNPQAPEF ILSCTTSKKT PDDPDKEATY GAVDCQYPGS
ALALDGSSGA EVEVLESDGV AGGLGQRERK KKKKRPPGYY SYLKDGGEGG LPTEALVNGH
ANPAVPHSVG SEDAEFVGDV PLSGTPRTCD SPQDSTDFVS DAVPGGPFPG ALDGDARTAG
QPEGCHGADL EQSCLSAEAG RDSLLRTAVA QPYMGTHTTE NLGVANGQIL ESSGEGSAAN
GAALHTVESV DSGPTKAESA SPASDAPASA AGTAPTSQPK SWASLFHDSK PSSSSPVASV
ETKYSPPATS PLVSEKQIEV KEGLVPVSED PVAIKIAELL ENVTLIHKPV SLQPRGLINK
GNWCYINATL QALVACPPMY HLMKFIPLYS KVQRPCTSTP MIDSFVRLMN EFTNMPVPPK
PRQALGDRIV RDIRPGAAFE PTYIYRLLTV IKSSLSEKGR QEDAEEYLGF ILNGLHEEML
NLKKLLSPNN EKLPISNGPK SHSVNEDEQE EPGEGSEDEW EQVGPRNKTS VTRQAEFVQT
PITGIFGGHI RSVVYQQSSK ESATLQPFFT LQLDIQSDRI RTVQDALESL VAREAVQGYT
TKTKQEVEIS RRVTLEKLPP VLVLHLKRFV YEKTGGCQKL VKNIDYPVDL EISKELLSPG
VKNKNFKCHR TYRLFAVVYH HGSSATGGHY TTDVFQIGLN GWLRIDDQAV KVVSQYQVVK
PTAERTAYLL YYRRVDLL
//
