ID A0A3B4XUP9_SERLL Unreviewed; 948 AA.
AC A0A3B4XUP9;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase {ECO:0000256|RuleBase:RU366025};
DE EC=3.4.19.12 {ECO:0000256|RuleBase:RU366025};
OS Seriola lalandi dorsalis.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Carangiformes; Carangidae; Seriola.
OX NCBI_TaxID=1841481 {ECO:0000313|Ensembl:ENSSLDP00000019375.1, ECO:0000313|Proteomes:UP000261360};
RN [1] {ECO:0000313|Ensembl:ENSSLDP00000019375.1}
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; A0A3B4XUP9; -.
DR STRING; 1841481.ENSSLDP00000019375; -.
DR Ensembl; ENSSLDT00000020024.1; ENSSLDP00000019375.1; ENSSLDG00000015169.1.
DR GeneTree; ENSGT00940000158829; -.
DR OrthoDB; 227085at2759; -.
DR Proteomes; UP000261360; 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:0021551; P:central nervous system morphogenesis; IEA:Ensembl.
DR GO; GO:1904888; P:cranial skeletal system development; IEA:Ensembl.
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; 2.
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:SF13; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 20; 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 5..109
FT /note="UBP-type"
FT /evidence="ECO:0000259|PROSITE:PS50271"
FT DOMAIN 149..721
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT DOMAIN 723..816
FT /note="DUSP"
FT /evidence="ECO:0000259|PROSITE:PS51283"
FT DOMAIN 825..927
FT /note="DUSP"
FT /evidence="ECO:0000259|PROSITE:PS51283"
FT REGION 260..311
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 323..431
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 270..288
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 361..378
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 384..431
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 948 AA; 105296 MW; 0ED8E46B07970A6F CRC64;
MAEQDICPHL DSIGQVTKED LLQKSKGTCQ SCGAGGPNLW ACLQNDCPYV GCGESYSDHS
TLHAQAKKHN LTVNLTTFRI WCYVCEREVF LEHRPALVSV PAAPHHCKAA EQEVAPQPVG
HPLKAVPIAV AEEEGSESEE DELKPRGLTG MKNIGNSCYM NAALQALSNC PPLTQFFLDC
SGLVRTDKKP ALCKSYQKLI SELWHKKRPS YVVPTSLSHG IKLVNPMFRG YAQQVGASTQ
QDTQEFLRCL MDQLHEELKE PLTECSMSGE GSDGEERRDG DRSPSEDEFL SCDSGSSSDR
GEGGGAGDGE LLVQDECDGV RSPAVGMVGV SPGGVISEKE RLKERRVSGS SLRGGSQEMD
EDADVDTAAE EEAPERGEEE ELTPTPNTEV QNQENNQTSN PVQGQGQSSS TSEPDNEASM
TQPQSTPCSP VRTLQELHPK LSSSPPRSSP LRSAGPAYSF KKAQLLLSAR KKKQSHYRSV
ISDIFDGSIL SLVQCLTCDR VSNTVETFQD LSLPIPGKED LAKLHSSIHQ NLPVKTGVCP
DTYGSQGWIS YIMDSIRRFV VSCIPSWFWG PMVTLEDCLA AFFAADELKG DNMYSCERCK
KLRNGVKYCK VLRLPEILCI HLKRFRHEVM YSFKISSHVS FPLEGLDMRP FLAKESPSQV
TTYDLLSVIC HHGTAGSGHY IAYCQNVING QWYEFDDQYV TEVHETVVQN AEAYVLFYRK
SSEESVRERQ KVVALANMKE PSLLQFYISR EWLNKFNTFA EPGPISNHTF LCQHGGIPPN
KYHYIDDLVV IVPQNVWEYL YNSFGGGPAV NHLYMCAICQ VEIEALAKRR KMEIDTFIKL
NKEFQAEEAP TVILCISMQW FREWESFVKG KDNEPPGPID NSKIGVMKGG HIQLKQGADY
GQISEETWQY LLGIYGGGPE IAVRQTVAPA DPDSLHGERK IEAETRAL
//
