OTU1_BOVIN
ID OTU1_BOVIN Reviewed; 348 AA.
AC Q05B57;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 14-NOV-2006, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Ubiquitin thioesterase OTU1;
DE EC=3.4.19.12 {ECO:0000250|UniProtKB:Q5VVQ6};
GN Name=YOD1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-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. May play a role in
CC macroautophagy, regulating for instance the clearance of damaged
CC lysosomes. May recruit PLAA, UBXN6 and VCP to damaged lysosome
CC membranes decorated with K48-linked ubiquitin chains and remove these
CC chains allowing autophagosome formation.
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 -!- SUBUNIT: Interacts with VCP; the interaction is direct. Interacts with
CC FAF2/UBXD8. Interacts with DERL1; however interaction is dependent on
CC the UBAX-like region, suggesting that it may be indirect. Interacts
CC with PLAA, UBXN6 and VCP; may form a complex involved in
CC macroautophagy. {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 -!- DOMAIN: The UBAX-like region mediates the interaction with VCP.
CC {ECO:0000250|UniProtKB:Q5VVQ6}.
CC -!- DOMAIN: The C2H2-type zinc finger mediates specificity for 'Lys-27'-,
CC 'Lys-29'- and 'Lys-33'-linked polyubiquitin chains but not for 'Lys-
CC 11'-linked ubiquitin chains. Selectivity for 'Lys-11'-linked ubiquitin
CC chains is provided by recognition of the sequence surrounding 'Lys-11'
CC in ubiquitin. The S2 site region provides specificity for longer 'Lys-
CC 11'-linked ubiquitin chains. {ECO:0000250|UniProtKB:Q5VVQ6}.
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DR EMBL; BC122788; AAI22789.1; -; mRNA.
DR RefSeq; NP_001073778.1; NM_001080309.2.
DR AlphaFoldDB; Q05B57; -.
DR SMR; Q05B57; -.
DR STRING; 9913.ENSBTAP00000027017; -.
DR MEROPS; C85.007; -.
DR PaxDb; Q05B57; -.
DR Ensembl; ENSBTAT00000027017; ENSBTAP00000027017; ENSBTAG00000020273.
DR GeneID; 539931; -.
DR KEGG; bta:539931; -.
DR CTD; 55432; -.
DR VEuPathDB; HostDB:ENSBTAG00000020273; -.
DR VGNC; VGNC:37033; YOD1.
DR eggNOG; KOG3288; Eukaryota.
DR GeneTree; ENSGT00390000009989; -.
DR HOGENOM; CLU_049327_1_0_1; -.
DR InParanoid; Q05B57; -.
DR OMA; NEEYCDW; -.
DR OrthoDB; 1327072at2759; -.
DR TreeFam; TF323700; -.
DR Proteomes; UP000009136; Chromosome 16.
DR Bgee; ENSBTAG00000020273; Expressed in semen and 87 other tissues.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; ISS:UniProtKB.
DR GO; GO:1990380; F:Lys48-specific deubiquitinase activity; IEA:Ensembl.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IEA:Ensembl.
DR GO; GO:0030968; P:endoplasmic reticulum unfolded protein response; ISS:UniProtKB.
DR GO; GO:0016236; P:macroautophagy; ISS:UniProtKB.
DR GO; GO:1904153; P:negative regulation of retrograde protein transport, ER to cytosol; IEA:Ensembl.
DR GO; GO:0016579; P:protein deubiquitination; IBA:GO_Central.
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..348
FT /note="Ubiquitin thioesterase OTU1"
FT /id="PRO_0000282355"
FT DOMAIN 149..274
FT /note="OTU"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00139"
FT ZN_FING 318..342
FT /note="C2H2-type"
FT REGION 50..128
FT /note="UBX-like"
FT REGION 154..160
FT /note="Cys-loop"
FT /evidence="ECO:0000250|UniProtKB:Q5VVQ6"
FT REGION 213..223
FT /note="Variable-loop"
FT /evidence="ECO:0000250|UniProtKB:Q5VVQ6"
FT REGION 263..267
FT /note="His-loop"
FT /evidence="ECO:0000250|UniProtKB:Q5VVQ6"
FT REGION 291..296
FT /note="S2 site"
FT /evidence="ECO:0000250|UniProtKB:Q5VVQ6"
FT ACT_SITE 157
FT /evidence="ECO:0000250|UniProtKB:Q96FW1"
FT ACT_SITE 160
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q5VVQ6"
FT ACT_SITE 267
FT /evidence="ECO:0000250|UniProtKB:Q5VVQ6"
FT ACT_SITE 342
FT /evidence="ECO:0000250|UniProtKB:Q96FW1"
FT BINDING 266
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q5VVQ6"
SQ SEQUENCE 348 AA; 38021 MW; 9CA87726C44F725F CRC64;
MFGPAKGGHF GVHPAAGCPG GVSQPAAGTK AGPAGVCPVG GRTNAMWRLR CKAKEGTHVL
QGLSSRTRVR ELQGQIAAIT GISPGCQRIL VGYPPECLDL SNGDTILEDL PIQSGDMLIV
EEDQNRPKTS PAFTKYGAPS YVRETLPVLA RMAVPADNSC LFTSVYYVVE GGVLNPACAP
EMRRFIAQIV ASDPDFYSEA ILGKTNEEYC DWIKRDDTWG GAIEISILSK FYQCEICVVD
TQTVRIDRFG EDAGYTKRVL LIYDGIHYDP LHLVFPDPDT PPLTIFSSYD DIVLVQALEL
ADEARKKRQF TDVNRFTLRC MVCQKGLTGQ AEARDHAKET GHTNFGEV
