ID A0A3Q2W0L5_HAPBU Unreviewed; 392 AA.
AC A0A3Q2W0L5;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase {ECO:0000256|RuleBase:RU366025};
DE EC=3.4.19.12 {ECO:0000256|RuleBase:RU366025};
OS Haplochromis burtoni (Burton's mouthbrooder) (Chromis burtoni).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Haplochromini; Haplochromis.
OX NCBI_TaxID=8153 {ECO:0000313|Ensembl:ENSHBUP00000018106.1, ECO:0000313|Proteomes:UP000264840};
RN [1] {ECO:0000313|Ensembl:ENSHBUP00000018106.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-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|RuleBase:RU366025};
CC -!- SIMILARITY: Belongs to the peptidase C19 family.
CC {ECO:0000256|RuleBase:RU366025}.
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DR RefSeq; XP_005946917.1; XM_005946855.1.
DR AlphaFoldDB; A0A3Q2W0L5; -.
DR STRING; 8153.ENSHBUP00000018106; -.
DR Ensembl; ENSHBUT00000027053.1; ENSHBUP00000018106.1; ENSHBUG00000020195.1.
DR GeneID; 102310935; -.
DR CTD; 559878; -.
DR GeneTree; ENSGT00940000153284; -.
DR OMA; AVTEHTH; -.
DR OrthoDB; 227085at2759; -.
DR Proteomes; UP000264840; Unplaced.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd02663; Peptidase_C19G; 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:SF860; USP DOMAIN-CONTAINING PROTEIN; 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 Reference proteome {ECO:0000313|Proteomes:UP000264840};
KW Thiol protease {ECO:0000256|RuleBase:RU366025};
KW Ubl conjugation pathway {ECO:0000256|RuleBase:RU366025}.
FT DOMAIN 39..391
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 147..187
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 392 AA; 44245 MW; 28FE3320867776F5 CRC64;
MEILMTVRKI ASICTMGANA SALEKEIGPE QFPVNEHYFG LVNFGNTCYC NSVLQALYFC
RPFREKVLAY KVQPRRKESL LTCLADLFNS IATQKKKVGV IPPKKFISRL RKENELFDNY
MQQDAHEFLN YLLNTIADLL QEEKSQERQQ NGKLVQNGGG GVGGGGGGVG GGSSESGGGG
GEVEGGKETQ QTWVHEIFQG TLTNETRCLN CEAVSSKDED FLDLSVDVEQ NTSITHCLRG
FSNTETLCSE YKYYCEQCRS KQEAQKRMRV KKLPMILALH LKRFKYMDQL HRYTKLSYRV
VFPLELRLFN TSGDATNPDR LYDLVAVVVH CGSGPNRGHY ITIVKSHGFW LLFDDDIVEK
IDAQAIEEFY GLTSDISKNS ESGYILFYQS RD
//
