OTU1_CHICK
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 03-AUG-2022, entry version 92.
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}.
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DR EMBL; AJ851744; CAH65378.1; -; mRNA.
DR RefSeq; NP_001026670.1; NM_001031499.1.
DR AlphaFoldDB; Q5F3A6; -.
DR SMR; Q5F3A6; -.
DR STRING; 9031.ENSGALP00000039556; -.
DR MEROPS; C85.007; -.
DR PaxDb; Q5F3A6; -.
DR GeneID; 428266; -.
DR KEGG; gga:428266; -.
DR CTD; 55432; -.
DR VEuPathDB; HostDB:geneid_428266; -.
DR eggNOG; KOG3288; Eukaryota.
DR InParanoid; Q5F3A6; -.
DR OrthoDB; 1327072at2759; -.
DR PhylomeDB; Q5F3A6; -.
DR PRO; PR:Q5F3A6; -.
DR Proteomes; UP000000539; Unplaced.
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: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..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
