ID A0A3B4TW76_SERDU Unreviewed; 830 AA.
AC A0A3B4TW76;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase {ECO:0000256|RuleBase:RU366025};
DE EC=3.4.19.12 {ECO:0000256|RuleBase:RU366025};
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:ENSSDUP00000009980.1, ECO:0000313|Proteomes:UP000261420};
RN [1] {ECO:0000313|Ensembl:ENSSDUP00000009980.1}
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 -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome {ECO:0000256|ARBA:ARBA00004300}. Cytoplasm,
CC perinuclear region {ECO:0000256|ARBA:ARBA00004556}.
CC -!- SIMILARITY: Belongs to the peptidase C19 family. USP20/USP33 subfamily.
CC {ECO:0000256|ARBA:ARBA00008269}.
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DR AlphaFoldDB; A0A3B4TW76; -.
DR STRING; 41447.ENSSDUP00000009980; -.
DR Ensembl; ENSSDUT00000010172.1; ENSSDUP00000009980.1; ENSSDUG00000007306.1.
DR GeneTree; ENSGT00940000157311; -.
DR OMA; LCSVICH; -.
DR Proteomes; UP000261420; Unplaced.
DR GO; GO:0005813; C:centrosome; IEA:UniProtKB-SubCell.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd02674; Peptidase_C19R; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR Gene3D; 3.30.2230.10; DUSP-like; 2.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR035927; DUSP-like_sf.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR006615; Pept_C19_DUSP.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR018200; USP_CS.
DR InterPro; IPR028889; USP_dom.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR001607; Znf_UBP.
DR PANTHER; PTHR21646; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR PANTHER; PTHR21646:SF32; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 33; 1.
DR Pfam; PF06337; DUSP; 2.
DR Pfam; PF00443; UCH; 1.
DR Pfam; PF02148; zf-UBP; 1.
DR SMART; SM00695; DUSP; 2.
DR SMART; SM00290; ZnF_UBP; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR SUPFAM; SSF143791; DUSP-like; 2.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS51283; DUSP; 2.
DR PROSITE; PS00972; USP_1; 1.
DR PROSITE; PS00973; USP_2; 1.
DR PROSITE; PS50235; USP_3; 1.
DR PROSITE; PS50271; ZF_UBP; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW Endocytosis {ECO:0000256|ARBA:ARBA00022583};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU366025};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Protease {ECO:0000256|RuleBase:RU366025};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Thiol protease {ECO:0000256|RuleBase:RU366025};
KW Ubl conjugation pathway {ECO:0000256|RuleBase:RU366025};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00502}.
FT DOMAIN 7..108
FT /note="UBP-type"
FT /evidence="ECO:0000259|PROSITE:PS50271"
FT DOMAIN 123..603
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT DOMAIN 605..698
FT /note="DUSP"
FT /evidence="ECO:0000259|PROSITE:PS51283"
FT DOMAIN 707..809
FT /note="DUSP"
FT /evidence="ECO:0000259|PROSITE:PS51283"
FT REGION 227..278
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 810..830
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 255..272
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 815..830
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 830 AA; 93588 MW; 4F246C7DF8C256CF CRC64;
MPLVSSCDCP HLDCVGEITK EELIQKSHGQ CQDCKVGGPN LWACLENGCA YVGCGESHTD
HSTVHSQETR HNLTVNLTTL RVWCYACGKE VFLERKLGPH SPHANSKPLP SSQSAGQVKA
GLTGLKNIGN TCYMNAALQA LSNCPPLTQF FLECGGMVRT DKKPALCKSY QKLVSDLWHK
NRPSYVVPTN LFQGIKAINP MFRGYSQQDS QEFLRCLMDQ LHEELKEPLP EPYDQSNGIT
VDEGPEEDNR SQSDNDFQSC ESCGSSERAD NEVQGGNVRM DDTNEAEMLI PEQDEIQKGK
IIRGRHIQIE CLKSQDFSRL VITVIYLCRR TVKHILFSLC LPTAVTTFSP PKNKRQKKYR
SVISDVFDGT IVSSVQCLTC DRVSVTLENF QDISLPIPGK EDLAKLHSST HQTSMVKAGS
CGEAYAPQGW IAFVMEYIKR CVCVCVCVWF WGPVVTLQDC LAAFFARDEL KGDNMYSCEK
CKKLRNGVKF CKMQSLPEIL CIHLKRFRHE LMFSTKISTH VSFPLEGLDL QPFLAKDSSA
QTTNYDLLSV ICHHGTASSG HYIAYCRNDA NNLWYEFDDQ SVTEVSESCV QNAEAYVLFY
KKSNEDAVKE RRRVSGLFSM MEPSLLQFYI SRQWLNKFKT FAEPGPISND DFLCSHGGVP
PNKATFIDDL VIMLPQNVWD HLYSRYGGGP AVNHLYVCHT CQIEIEKLEK RRKSELDMFV
RLNKAFQEEE SPVVIYCISM QWFREWEGFV KGKDNDPPGP IDNSKITVNK NGHLTLKQGA
DSGQISEETW NFLHSIYGGG PLVTVRPNIS HQEAESSQSE EKIEVETRSL
//
