OTUD5_XENTR
ID OTUD5_XENTR Reviewed; 518 AA.
AC Q6GL44;
DT 20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 67.
DE RecName: Full=OTU domain-containing protein 5;
DE EC=3.4.19.12;
DE AltName: Full=Deubiquitinating enzyme A;
DE Short=DUBA;
GN Name=otud5;
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Deubiquitinating enzyme that may function as negative
CC regulator of the innate immune system. Has peptidase activity towards
CC 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains. Can also cleave
CC 'Lys-11'-linked ubiquitin chains (in vitro) (By similarity).
CC {ECO:0000250}.
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;
CC -!- SIMILARITY: Belongs to the peptidase C85 family. {ECO:0000305}.
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DR EMBL; BC074667; AAH74667.1; -; mRNA.
DR RefSeq; NP_001004849.1; NM_001004849.1.
DR AlphaFoldDB; Q6GL44; -.
DR SMR; Q6GL44; -.
DR MEROPS; C85.001; -.
DR PaxDb; Q6GL44; -.
DR GeneID; 448134; -.
DR KEGG; xtr:448134; -.
DR CTD; 55593; -.
DR Xenbase; XB-GENE-6455884; otud5.
DR eggNOG; KOG2605; Eukaryota.
DR InParanoid; Q6GL44; -.
DR OrthoDB; 1448656at2759; -.
DR Proteomes; UP000008143; Chromosome 8.
DR Proteomes; UP000790000; Unplaced.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; ISS:UniProtKB.
DR GO; GO:0061578; F:Lys63-specific deubiquitinase activity; IBA:GO_Central.
DR GO; GO:0016579; P:protein deubiquitination; IBA:GO_Central.
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:0032496; P:response to lipopolysaccharide; ISS:UniProtKB.
DR InterPro; IPR031084; OTU5.
DR InterPro; IPR003323; OTU_dom.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR PANTHER; PTHR12419:SF4; PTHR12419:SF4; 1.
DR Pfam; PF02338; OTU; 1.
DR SUPFAM; SSF54001; SSF54001; 1.
DR PROSITE; PS50802; OTU; 1.
PE 2: Evidence at transcript level;
KW Hydrolase; Protease; Reference proteome; Thiol protease;
KW Ubl conjugation pathway.
FT CHAIN 1..518
FT /note="OTU domain-containing protein 5"
FT /id="PRO_0000278229"
FT DOMAIN 171..294
FT /note="OTU"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00139"
FT REGION 1..79
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 105..144
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 176..182
FT /note="Cys-loop"
FT /evidence="ECO:0000250"
FT REGION 231..241
FT /note="Variable-loop"
FT /evidence="ECO:0000250"
FT REGION 282..287
FT /note="His-loop"
FT /evidence="ECO:0000250"
FT REGION 371..450
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 41..69
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 374..406
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 179
FT /evidence="ECO:0000255"
FT ACT_SITE 182
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 287
FT /evidence="ECO:0000250"
SQ SEQUENCE 518 AA; 56332 MW; 69368C93932208F4 CRC64;
MTILPKKKPP PPSDPEGNGE RSGSGGADSH SRSGARPRSS PPPRWAYPGN PAPPERHPAG
TPRPQQASPP PCSGGSGGAG SGPLGEGALG PCCCCTGAGG CCSGPGHSKR RRQGVSAGPG
APGSSPDRED GAGNNSEDEY ETAARTQAID PDTAEQQEHW FEKALQEKKG FIIKQMKEDG
ACLFRAVADQ VYGDQDMHEV VRKHCMDYLM KNADYFSNYV TEDFTTYINR KRKNNCHGNH
IEMQAMAEMY NRPVEVYQYG TEPINTFHGI QQNEDEPIRV SYHRNIHYNS VVNPNKATIG
VGLGLPSFKP GFAEQSLMKS AIRTSEESWI EQQMLEDKKR ATDWEATNEA IEEQVARESY
LQWLRDQEKQ ARQPRKASAT CSSATAAASS GLEEWSGRSP RQRSTAGSPE HPDLHAELCM
KPPSPAATLM LGKPPSPCAP GPSNQTCAGA DRATSPLVSL YPALECRAIM QHMSPTAFGL
KDWDDDEILA SVLAVSQQEY LDTIKKSTLR RDSSPDHS