ID OTU1_CHICK Reviewed; 302 AA. AC Q5F3A6; DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 27-MAR-2024, entry version 98. DE RecName: Full=Ubiquitin thioesterase OTU1; DE EC=3.4.19.12 {ECO:0000250|UniProtKB:Q5VVQ6}; GN Name=YOD1; ORFNames=RCJMB04_24h21; OS Gallus gallus (Chicken). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda; OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae; OC Phasianinae; Gallus. OX NCBI_TaxID=9031; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=CB; TISSUE=Bursa of Fabricius; RX PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6; RA Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P., RA Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P., RA Hayashizaki Y., Buerstedde J.-M.; RT "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene RT function analysis."; RL Genome Biol. 6:R6.1-R6.9(2005). 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; AJ851744; CAH65378.1; -; mRNA. DR RefSeq; NP_001026670.1; NM_001031499.1. DR AlphaFoldDB; Q5F3A6; -. DR SMR; Q5F3A6; -. DR STRING; 9031.ENSGALP00000048440; -. DR MEROPS; C85.007; -. DR PaxDb; 9031-ENSGALP00000039556; -. DR GeneID; 428266; -. DR KEGG; gga:428266; -. DR CTD; 55432; -. DR VEuPathDB; HostDB:geneid_428266; -. DR eggNOG; KOG3288; Eukaryota. DR InParanoid; Q5F3A6; -. DR OMA; TRCILVY; -. DR OrthoDB; 5486835at2759; -. DR PhylomeDB; Q5F3A6; -. DR PRO; PR:Q5F3A6; -. DR Proteomes; UP000000539; Unassembled WGS sequence. 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 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..302 FT /note="Ubiquitin thioesterase OTU1" FT /id="PRO_0000282359" FT DOMAIN 103..228 FT /note="OTU" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00139" FT ZN_FING 272..296 FT /note="C2H2-type" FT REGION 5..83 FT /note="UBX-like" FT REGION 108..114 FT /note="Cys-loop" FT /evidence="ECO:0000250|UniProtKB:Q5VVQ6" FT REGION 167..177 FT /note="Variable-loop" FT /evidence="ECO:0000250|UniProtKB:Q5VVQ6" FT REGION 217..221 FT /note="His-loop" FT /evidence="ECO:0000250|UniProtKB:Q5VVQ6" FT REGION 245..250 FT /note="S2 site" FT /evidence="ECO:0000250|UniProtKB:Q5VVQ6" FT ACT_SITE 111 FT /evidence="ECO:0000250|UniProtKB:Q96FW1" FT ACT_SITE 114 FT /note="Nucleophile" FT /evidence="ECO:0000250|UniProtKB:Q5VVQ6" FT ACT_SITE 221 FT /evidence="ECO:0000250|UniProtKB:Q5VVQ6" FT ACT_SITE 296 FT /evidence="ECO:0000250|UniProtKB:Q96FW1" FT BINDING 220 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:Q5VVQ6" SQ SEQUENCE 302 AA; 33384 MW; 6ABA3C65C985248C CRC64; MLRLRCKARS GTQPLPGLTA HSRLRDMQAA LAALTGVPAP AQRLLLGFPP RSLDLSDGER RLGELGIHSG DTLIVEEDTS KPSAGSPVVA KRTMAVREAV PVLARRVVPA DNSCLFTSVY YVVEGGVYDP GCAPEMRSLI AQIVASDPEA YCEAVLGKTN REYCEWIRRE ETWGGAIEVS ILSKFYQCEI CVVDTQTVRI DRFGEDAGYT KRVLLIYDGI HYDPLERKIP DSDVPPQTIF STTDDVVLAQ ALELADEARR KRQFTDVNRF TLRCMVCQKG LTGQVEAREH AKETGHTNFG EV //