ID OTU1_XENLA Reviewed; 304 AA. AC Q0IH43; DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot. DT 03-OCT-2006, sequence version 1. DT 27-MAR-2024, entry version 77. DE RecName: Full=Ubiquitin thioesterase OTU1; DE EC=3.4.19.12 {ECO:0000250|UniProtKB:Q5VVQ6}; GN Name=yod1; OS Xenopus laevis (African clawed frog). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia; OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus. OX NCBI_TaxID=8355; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Ovary; RG NIH - Xenopus Gene Collection (XGC) project; RL Submitted (SEP-2006) 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 --------------------------------------------------------------------------- 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; BC123321; AAI23322.1; -; mRNA. DR RefSeq; NP_001090389.1; NM_001096920.1. DR AlphaFoldDB; Q0IH43; -. DR SMR; Q0IH43; -. DR MEROPS; C85.007; -. DR MaxQB; Q0IH43; -. DR DNASU; 779300; -. DR GeneID; 779300; -. DR KEGG; xla:779300; -. DR AGR; Xenbase:XB-GENE-998963; -. DR CTD; 779300; -. DR Xenbase; XB-GENE-998963; yod1.L. DR OMA; TRCILVY; -. DR OrthoDB; 5486835at2759; -. DR Proteomes; UP000186698; Chromosome 2L. DR Bgee; 779300; Expressed in blastula and 19 other cell types or tissues. 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; IPR029071; Ubiquitin-like_domsf. DR InterPro; IPR013087; Znf_C2H2_type. 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; 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..304 FT /note="Ubiquitin thioesterase OTU1" FT /id="PRO_0000282361" FT DOMAIN 105..230 FT /note="OTU" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00139" FT ZN_FING 274..298 FT /note="C2H2-type" FT REGION 5..83 FT /note="UBX-like" FT REGION 110..116 FT /note="Cys-loop" FT /evidence="ECO:0000250|UniProtKB:Q5VVQ6" FT REGION 169..179 FT /note="Variable-loop" FT /evidence="ECO:0000250|UniProtKB:Q5VVQ6" FT REGION 219..223 FT /note="His-loop" FT /evidence="ECO:0000250|UniProtKB:Q5VVQ6" FT REGION 247..252 FT /note="S2 site" FT /evidence="ECO:0000250|UniProtKB:Q5VVQ6" FT ACT_SITE 113 FT /evidence="ECO:0000250|UniProtKB:Q96FW1" FT ACT_SITE 116 FT /note="Nucleophile" FT /evidence="ECO:0000250|UniProtKB:Q5VVQ6" FT ACT_SITE 223 FT /evidence="ECO:0000250|UniProtKB:Q5VVQ6" FT ACT_SITE 298 FT /evidence="ECO:0000250|UniProtKB:Q96FW1" FT BINDING 222 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:Q5VVQ6" SQ SEQUENCE 304 AA; 33807 MW; 4A0FEDC19A47E0DE CRC64; MLRLRCKTRE GTQLLQGLTD RSSIRELQER IAGVTGISGP LQRVMVGFPP LSLDLSDEEA TLKNMSIKSG DTLIVEEDKS KLRSATPPVS KTDIGNWNAP AQPTIVRRVV PADNSCLFTS IYYVVEGGVY DPACALEMRS LIAEIVASDQ SAYCDAVLGK SNEEYCSWIR REDTWGGAIE VSILSKFYQC EICVVDTQTV RIDRFGEDSG YTKRVLLIYD GIHYDPLQRQ FPDPDMPPMT VFSTTDDEAL VQAMELADDA RKKRQFTDVN QFALRCMACQ KGLTGQSAAR DHAKETGHTN FGEV //