ID M4ATH0_XIPMA Unreviewed; 300 AA.
AC M4ATH0;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE RecName: Full=Ubiquitin thioesterase OTU {ECO:0000256|RuleBase:RU367104};
DE EC=3.4.19.12 {ECO:0000256|RuleBase:RU367104};
OS Xiphophorus maculatus (Southern platyfish) (Platypoecilus maculatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Xiphophorus.
OX NCBI_TaxID=8083 {ECO:0000313|Ensembl:ENSXMAP00000017765.1, ECO:0000313|Proteomes:UP000002852};
RN [1] {ECO:0000313|Proteomes:UP000002852}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JP 163 A {ECO:0000313|Proteomes:UP000002852};
RA Walter R., Schartl M., Warren W.;
RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000002852}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JP 163 A {ECO:0000313|Proteomes:UP000002852};
RX PubMed=23542700; DOI=10.1038/ng.2604;
RA Schartl M., Walter R.B., Shen Y., Garcia T., Catchen J., Amores A.,
RA Braasch I., Chalopin D., Volff J.N., Lesch K.P., Bisazza A., Minx P.,
RA Hillier L., Wilson R.K., Fuerstenberg S., Boore J., Searle S.,
RA Postlethwait J.H., Warren W.C.;
RT "The genome of the platyfish, Xiphophorus maculatus, provides insights into
RT evolutionary adaptation and several complex traits.";
RL Nat. Genet. 45:567-572(2013).
RN [3] {ECO:0000313|Ensembl:ENSXMAP00000017765.1}
RP IDENTIFICATION.
RC STRAIN=JP 163 A {ECO:0000313|Ensembl:ENSXMAP00000017765.1};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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 RefSeq; XP_005802244.1; XM_005802187.1.
DR AlphaFoldDB; M4ATH0; -.
DR STRING; 8083.ENSXMAP00000017765; -.
DR MEROPS; C85.007; -.
DR Ensembl; ENSXMAT00000017790.2; ENSXMAP00000017765.1; ENSXMAG00000017727.2.
DR GeneID; 102217261; -.
DR KEGG; xma:102217261; -.
DR CTD; 55432; -.
DR eggNOG; KOG3288; Eukaryota.
DR GeneTree; ENSGT00390000009989; -.
DR HOGENOM; CLU_049327_1_0_1; -.
DR InParanoid; M4ATH0; -.
DR OMA; TRCILVY; -.
DR OrthoDB; 5486835at2759; -.
DR Proteomes; UP000002852; 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 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:UP000002852};
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..75
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; 33656 MW; 8EF959777E21D81A CRC64;
MLRLRCKTKN GSHIMQGLTH QSCVQELKSK VEELTGIPCN VQKIMVGYPP SSLDLRNLDA
HLKDYPIKSG DTLIVEEEKN KLKPQDHPIV KAPHLELSPV LARRVVPADN SCLFTSVNYV
VEGGVYDPAC APEMRSLIAQ IVSSDPTAYC EAVLGKTNEE YCAWIKRDDT WGGAIEVSIL
SKFYQCEICV VDTQTVRVDR FGEDAGYHKR VLLIYDGIHY DPLQKEVPHS ETPPQTIFST
TDDIILAQAL ELADEARRKR QFTDVNRFAL RCMVCQTGLV GQKEAREHAK ETGHTNFGEV
//
