OTU6B_XENTR
ID OTU6B_XENTR Reviewed; 294 AA.
AC Q5M8L0;
DT 24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=Deubiquitinase OTUD6B {ECO:0000305};
DE EC=3.4.19.12 {ECO:0000250|UniProtKB:Q8N6M0};
GN Name=otud6b;
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].
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Deubiquitinating enzyme that may play a role in the
CC ubiquitin-dependent regulation of different cellular processes.
CC {ECO:0000250|UniProtKB:Q8N6M0}.
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:Q8N6M0};
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DR EMBL; BC087978; AAH87978.1; -; mRNA.
DR RefSeq; NP_001011269.1; NM_001011269.1.
DR AlphaFoldDB; Q5M8L0; -.
DR SMR; Q5M8L0; -.
DR STRING; 8364.ENSXETP00000031929; -.
DR MEROPS; C85.008; -.
DR PaxDb; Q5M8L0; -.
DR DNASU; 496720; -.
DR Ensembl; ENSXETT00000031929; ENSXETP00000031929; ENSXETG00000014596.
DR GeneID; 496720; -.
DR KEGG; xtr:496720; -.
DR CTD; 51633; -.
DR Xenbase; XB-GENE-985119; otud6b.
DR eggNOG; KOG2606; Eukaryota.
DR HOGENOM; CLU_034963_0_0_1; -.
DR InParanoid; Q5M8L0; -.
DR OrthoDB; 1541668at2759; -.
DR PhylomeDB; Q5M8L0; -.
DR Proteomes; UP000008143; Chromosome 6.
DR Proteomes; UP000790000; Unplaced.
DR Bgee; ENSXETG00000014596; Expressed in ovary and 12 other tissues.
DR ExpressionAtlas; Q5M8L0; baseline.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; ISS:UniProtKB.
DR GO; GO:0016579; P:protein deubiquitination; ISS:UniProtKB.
DR InterPro; IPR003323; OTU_dom.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
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..294
FT /note="Deubiquitinase OTUD6B"
FT /id="PRO_0000076284"
FT DOMAIN 150..287
FT /note="OTU"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00139"
FT REGION 1..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 67..120
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 155..161
FT /note="Cys-loop"
FT /evidence="ECO:0000250"
FT REGION 222..232
FT /note="Variable-loop"
FT /evidence="ECO:0000250"
FT REGION 270..280
FT /note="His-loop"
FT /evidence="ECO:0000250"
FT COMPBIAS 8..27
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 72..101
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 158
FT /evidence="ECO:0000250"
FT ACT_SITE 161
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q8N6M0"
FT ACT_SITE 280
FT /evidence="ECO:0000250"
SQ SEQUENCE 294 AA; 33367 MW; 646F5246455D08D6 CRC64;
MDEAEGNSEE SGLIKQHRKE KRDLQAKIQS MKNSVPKNDK KRRKQLTEDI AKLEADLDVR
HKEELEAFAQ KQPEPTQVSG ITNGVTSLDL GNEAPVQQPR QSKAQKRREK KAAQEKERDE
RIAEAEIANL SGARHLESQK LARILAEREL QIRQIPSDGH CMYRAIEHQL RERGNDLTVA
NLRSQTADYM QNHAEDFLPF LTNSSTGDMY TQEEFLKYCT DIVNTPAWGG QLELRALSHI
LKTAIEVIQA ESSPIVIGEE YSSKAITLVY MRHAYGLGEH YNSVELLDTS TENS