ID OTU1_DANRE Reviewed; 301 AA. AC Q567B1; DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot. DT 10-MAY-2005, sequence version 1. DT 27-MAR-2024, entry version 108. DE RecName: Full=Ubiquitin thioesterase OTU1; DE EC=3.4.19.12 {ECO:0000250|UniProtKB:Q5VVQ6}; GN Name=yod1; ORFNames=zgc:112182; OS Danio rerio (Zebrafish) (Brachydanio rerio). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes; OC Danionidae; Danioninae; Danio. OX NCBI_TaxID=7955; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Embryo; RG NIH - Zebrafish Gene Collection (ZGC) project; RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases. 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. Ubiquitin moieties on substrates may present a steric CC impediment to the threading process when the substrate is transferred CC to the VCP pore and threaded through VCP's axial channel. Mediates CC deubiquitination of 'Lys-27'-, 'Lys-29'- and 'Lys-33'-linked CC polyubiquitin chains. Also able to hydrolyze 'Lys-11'-linked ubiquitin CC chains. Cleaves both polyubiquitin and di-ubiquitin. CC {ECO:0000250|UniProtKB:Q5VVQ6}. 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:0000250|UniProtKB:Q5VVQ6}; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q5VVQ6}. CC Note=Recruited to damaged lysosomes decorated with K48-linked ubiquitin CC chains. {ECO:0000250|UniProtKB:Q5VVQ6}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; BC093247; AAH93247.1; -; mRNA. DR RefSeq; NP_001017716.1; NM_001017716.2. DR AlphaFoldDB; Q567B1; -. DR SMR; Q567B1; -. DR BioGRID; 95523; 1. DR STRING; 7955.ENSDARP00000003565; -. DR MEROPS; C85.007; -. DR PaxDb; 7955-ENSDARP00000003565; -. DR GeneID; 550411; -. DR KEGG; dre:550411; -. DR AGR; ZFIN:ZDB-GENE-050417-217; -. DR CTD; 55432; -. DR ZFIN; ZDB-GENE-050417-217; yod1. DR eggNOG; KOG3288; Eukaryota. DR HOGENOM; CLU_049327_1_0_1; -. DR InParanoid; Q567B1; -. DR OMA; TRCILVY; -. DR OrthoDB; 5486835at2759; -. DR PhylomeDB; Q567B1; -. DR TreeFam; TF323700; -. DR Reactome; R-DRE-5689896; Ovarian tumor domain proteases. DR PRO; PR:Q567B1; -. DR Proteomes; UP000000437; Chromosome 11. DR Bgee; ENSDARG00000008542; Expressed in testis and 24 other cell types or tissues. DR ExpressionAtlas; Q567B1; baseline. DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB. DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; ISS:UniProtKB. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0030968; P:endoplasmic reticulum unfolded protein response; ISS:UniProtKB. DR GO; GO:0016236; P:macroautophagy; ISS:UniProtKB. DR GO; GO:0035871; P:protein K11-linked deubiquitination; ISS:UniProtKB. DR GO; GO:1990167; P:protein K27-linked deubiquitination; ISS:UniProtKB. DR GO; GO:0035523; P:protein K29-linked deubiquitination; ISS:UniProtKB. DR GO; GO:1990168; P:protein K33-linked deubiquitination; ISS:UniProtKB. DR GO; GO:0071108; P:protein K48-linked deubiquitination; ISS:UniProtKB. DR GO; GO:0070536; P:protein K63-linked deubiquitination; ISS:UniProtKB. DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; ISS:UniProtKB. 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. DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1. PE 2: Evidence at transcript level; KW Cytoplasm; Hydrolase; Metal-binding; Protease; Reference proteome; KW Thiol protease; Ubl conjugation pathway; Unfolded protein response; Zinc; KW Zinc-finger. FT CHAIN 1..301 FT /note="Ubiquitin thioesterase OTU1" FT /id="PRO_0000282360" FT DOMAIN 102..227 FT /note="OTU" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00139" FT ZN_FING 271..295 FT /note="C2H2-type" FT REGION 5..83 FT /note="UBX-like" FT REGION 107..113 FT /note="Cys-loop" FT /evidence="ECO:0000250|UniProtKB:Q5VVQ6" FT REGION 166..176 FT /note="Variable-loop" FT /evidence="ECO:0000250|UniProtKB:Q5VVQ6" FT REGION 216..220 FT /note="His-loop" FT /evidence="ECO:0000250|UniProtKB:Q5VVQ6" FT REGION 244..249 FT /note="S2 site" FT /evidence="ECO:0000250|UniProtKB:Q5VVQ6" FT ACT_SITE 110 FT /evidence="ECO:0000250|UniProtKB:Q96FW1" FT ACT_SITE 113 FT /note="Nucleophile" FT /evidence="ECO:0000250|UniProtKB:Q5VVQ6" FT ACT_SITE 220 FT /evidence="ECO:0000250|UniProtKB:Q5VVQ6" FT ACT_SITE 295 FT /evidence="ECO:0000250|UniProtKB:Q96FW1" FT BINDING 219 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:Q5VVQ6" SQ SEQUENCE 301 AA; 33486 MW; 70D85A2694B56198 CRC64; MLRLRCKAKN GTHLMQGLTH QSCVQELKDK IEELTGIPCD VQKIMVGYPP SSLDLRNGEA HLKDYPIKSG DTLIVEEEKN KPKPPVQPTV TKGPSFEVTP VVERRVVPAD NSCLFTSVNY VMEGGVYDPA CASEMRGLIA QIVASDPTAY SEAVLGKTNE EYCTWIRRDD TWGGAIEVSI LSKFYQCEIC VVDTQTVRVD RFGEDAGYTK RVLLIYDGIH YDPLQKVLPG SDVPAQTVFS TVDDVILAQA LELADEARRK RQFTDVNRFA LRCMVCQTGL VGQKEAREHA KETGHTNFGE V //