ID A0A3B3DN58_ORYME Unreviewed; 300 AA.
AC A0A3B3DN58;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=Ubiquitin thioesterase OTU {ECO:0000256|RuleBase:RU367104};
DE EC=3.4.19.12 {ECO:0000256|RuleBase:RU367104};
GN ORFNames=FQA47_024504 {ECO:0000313|EMBL:KAF6736223.1};
OS Oryzias melastigma (Marine medaka).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Beloniformes; Adrianichthyidae; Oryziinae;
OC Oryzias.
OX NCBI_TaxID=30732 {ECO:0000313|Ensembl:ENSOMEP00000031371.1, ECO:0000313|Proteomes:UP000261560};
RN [1] {ECO:0000313|Ensembl:ENSOMEP00000031371.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
RN [2] {ECO:0000313|EMBL:KAF6736223.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Bigg-433 {ECO:0000313|EMBL:KAF6736223.1};
RX PubMed=32938378;
RA Liang P., Saqib H.S.A., Ni X., Shen Y.;
RT "Long-read sequencing and de novo genome assembly of marine medaka (Oryzias
RT melastigma).";
RL BMC Genomics 21:0-0(0).
CC -!- FUNCTION: Hydrolase that can remove conjugated ubiquitin from proteins
CC and participates in endoplasmic reticulum-associated degradation (ERAD)
CC for misfolded lumenal proteins. May act by triming the ubiquitin chain
CC on the associated substrate to facilitate their threading through the
CC VCP/p97 pore. Cleaves both polyubiquitin and di-ubiquitin.
CC {ECO:0000256|RuleBase:RU367104}.
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:RU367104};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU367104}.
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DR EMBL; WKFB01000094; KAF6736223.1; -; Genomic_DNA.
DR STRING; 30732.ENSOMEP00000031371; -.
DR PaxDb; 30732-ENSOMEP00000031371; -.
DR Ensembl; ENSOMET00000033600.1; ENSOMEP00000031371.1; ENSOMEG00000016065.1.
DR GeneTree; ENSGT00390000009989; -.
DR OMA; TRCILVY; -.
DR OrthoDB; 5486835at2759; -.
DR Proteomes; UP000261560; Unplaced.
DR Proteomes; UP000646548; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006986; P:response to unfolded protein; IEA:UniProtKB-KW.
DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IEA:UniProtKB-UniRule.
DR CDD; cd22745; OTU_OTU1; 1.
DR CDD; cd17059; Ubl_OTU1; 1.
DR Gene3D; 3.90.70.80; -; 1.
DR InterPro; IPR048857; OTU1_Ubl.
DR InterPro; IPR003323; OTU_dom.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR000626; Ubiquitin-like_dom.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR PANTHER; PTHR13312; HIV-INDUCED PROTEIN-7-LIKE PROTEASE; 1.
DR PANTHER; PTHR13312:SF0; UBIQUITIN THIOESTERASE OTU1; 1.
DR Pfam; PF02338; OTU; 1.
DR Pfam; PF21403; OTU1_UBXL; 1.
DR SMART; SM00213; UBQ; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR SUPFAM; SSF54236; Ubiquitin-like; 1.
DR PROSITE; PS50802; OTU; 1.
DR PROSITE; PS50053; UBIQUITIN_2; 1.
PE 4: Predicted;
KW Cytoplasm {ECO:0000256|RuleBase:RU367104};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU367104};
KW Protease {ECO:0000256|RuleBase:RU367104};
KW Reference proteome {ECO:0000313|Proteomes:UP000646548};
KW Thiol protease {ECO:0000256|RuleBase:RU367104};
KW Ubl conjugation pathway {ECO:0000256|RuleBase:RU367104};
KW Unfolded protein response {ECO:0000256|ARBA:ARBA00023230}.
FT DOMAIN 2..82
FT /note="Ubiquitin-like"
FT /evidence="ECO:0000259|PROSITE:PS50053"
FT DOMAIN 101..226
FT /note="OTU"
FT /evidence="ECO:0000259|PROSITE:PS50802"
SQ SEQUENCE 300 AA; 33322 MW; 9EF478856619BBCA CRC64;
MLRLRCKTKN GSHIMHGLTH QSCVQELKSK VEELTGIPCD VQKIMVGYPP SSLDLRNGDA
HLKDYPIKSG DTLIVEEEKN KPKPLDQPAV KAPPLEASPV LARRVVPADN SCLFTSVYYV
VEGGVYDPAC APEMRGLIAQ IVSSDPAAYC EAVLGKTNED YCAWIRRDDT WGGAIEVSIL
SKFYQCEICV VDTQTVRVDR FGEDAGYHKR VLLIYDGIHY DPLHKEVPGS DSPPQTVFST
TDDVILAQAL ELADEARRKR QFTDVNRFAL RCMVCQTGLV GQKEAREHAK ETGHTNFGEV
//
