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   03-AUG-2022, entry version 72.
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}.
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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   CTD; 779300; -.
DR   Xenbase; XB-GENE-998963; yod1.L.
DR   OMA; NEEYCDW; -.
DR   OrthoDB; 1327072at2759; -.
DR   Proteomes; UP000186698; Chromosome 2L.
DR   Bgee; 779300; Expressed in blastula and 19 other 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   InterPro; IPR039138; OTU1_2_3.
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; PTHR13312; 1.
DR   Pfam; PF02338; OTU; 1.
DR   SUPFAM; SSF54001; SSF54001; 1.
DR   SUPFAM; SSF54236; SSF54236; 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