ID A0A3B4V076_SERDU Unreviewed; 880 AA.
AC A0A3B4V076;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, 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:ENSSDUP00000024099.1};
OS Seriola dumerili (Greater amberjack) (Caranx dumerili).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Carangiformes; Carangidae; Seriola.
OX NCBI_TaxID=41447 {ECO:0000313|Ensembl:ENSSDUP00000024099.1, ECO:0000313|Proteomes:UP000261420};
RN [1] {ECO:0000313|Ensembl:ENSSDUP00000024099.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) 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 -!- SIMILARITY: Belongs to the peptidase C19 family. USP10 subfamily.
CC {ECO:0000256|ARBA:ARBA00005427}.
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DR AlphaFoldDB; A0A3B4V076; -.
DR STRING; 41447.ENSSDUP00000024099; -.
DR Ensembl; ENSSDUT00000024550.1; ENSSDUP00000024099.1; ENSSDUG00000017506.1.
DR GeneTree; ENSGT00550000074994; -.
DR OrthoDB; 55585at2759; -.
DR Proteomes; UP000261420; Unplaced.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-UniRule.
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; 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 3: Inferred from homology;
KW Hydrolase {ECO:0000256|RuleBase:RU366025};
KW Protease {ECO:0000256|RuleBase:RU366025};
KW Thiol protease {ECO:0000256|RuleBase:RU366025};
KW Ubl conjugation pathway {ECO:0000256|RuleBase:RU366025}.
FT DOMAIN 495..877
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 116..196
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 246..398
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 630..676
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 180..196
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 246..321
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 334..348
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 367..382
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 383..398
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 880 AA; 95329 MW; 11CEAD45626716FF CRC64;
MASHSNQYIF GEFSPDEINQ FFVTPRCYVE LPPFNDKVPC VSQSSGSYCT PAVPYIMESM
GLQVCAEDYQ RIEFGVDEVM DSKPVGVNDP LYKVSSTLNP QAPEFILGCQ SAQKAQQTAP
PAADVPDGTH FNSLDGPDSE ASALDNHQAC QDMDGLPGSL GQRERKKKKK RPPGYYNYLD
PATGSNNSSS AADGTPVTAL VNGHALGGPH HSAEDVDGKV LSGAELSTPG PVSTATSTAA
VAAAKFAPSS TANQRTCDSP DDSSLDLTSG AASLSDGNNA TSSSSSSSQS RGMTEGPRTA
DQQPDNLAPQ SPELSDTPHS PRSKSPLPPS AAVATPSVAT SITTTELEGR EVADSGVANG
LAERETPISA DGHKEDCESG EHTQQASPDT AAQPVVTEQG HSSAIPAAPT ANLPKSWASL
FHNSKPLPGG PQAFVEVKNV VEVVSPSLAT PEQPEKVGEV KDGPVHVSED PMAPKLAELI
ENVKLIHKPV SLQPRGLINK GNWCYINATL QALIACPPMY HLMKSIPLHN EAQRPCTSTP
MIDNFVRLVN EFNNMPVPSK AKQQAVGDKV MKDIRPGVPF EPTYIYRLLT LIKSSLSEKG
RQEDAEEYLG FTLNGLHEEM LALKKLISPQ EEKAPTPNGP ESQPGVEEDV ADKEEEGSED
EWEQVGPRNK TSITRQADFV RTPITDIFGG HIRSVVYQQN SKESATLQPF FTLQLDIQSE
KIRTVQEALE TLVARESVQG YTSKTKQEIE ISRRVTLEEL PPVLVLHLKR FVFEKTGGCQ
KLTKNIDYPV DLEISKDLLS SGVRSKVVKG QRTYRLFAVV YHHGNSATGG HYTTDVFHIG
LNGWLRIDDQ AVKVINQYQV VKQTAERTAY LLYYRRVDLL
//
