OTUD3_MOUSE
ID OTUD3_MOUSE Reviewed; 396 AA.
AC B1AZ99;
DT 16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=OTU domain-containing protein 3;
DE EC=3.4.19.12;
GN Name=Otud3;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Deubiquitinating enzyme that hydrolyzes 'Lys-6'- and 'Lys-
CC 11'-linked polyubiquitin. Also hydrolyzes heterotypic (mixed and
CC branched) and homotypic chains (By similarity). {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 -!- INTERACTION:
CC B1AZ99; O08586: Pten; NbExp=2; IntAct=EBI-16170692, EBI-1186266;
CC -!- DOMAIN: The UBA-like domain has no influence on ubiquitin hydrolysis.
CC {ECO:0000250}.
CC -!- DOMAIN: Specificity is given by the S1' ubiquitin-binding site within
CC the OTU domain composed of the Cys-, His- and Variable-loops.
CC {ECO:0000250}.
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; AL929473; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466615; EDL13286.1; -; Genomic_DNA.
DR CCDS; CCDS51337.1; -.
DR RefSeq; NP_082729.1; NM_028453.1.
DR AlphaFoldDB; B1AZ99; -.
DR SMR; B1AZ99; -.
DR DIP; DIP-61703N; -.
DR IntAct; B1AZ99; 1.
DR STRING; 10090.ENSMUSP00000095441; -.
DR iPTMnet; B1AZ99; -.
DR PhosphoSitePlus; B1AZ99; -.
DR EPD; B1AZ99; -.
DR MaxQB; B1AZ99; -.
DR PaxDb; B1AZ99; -.
DR PeptideAtlas; B1AZ99; -.
DR PRIDE; B1AZ99; -.
DR ProteomicsDB; 294133; -.
DR Antibodypedia; 29739; 84 antibodies from 18 providers.
DR Ensembl; ENSMUST00000097830; ENSMUSP00000095441; ENSMUSG00000041161.
DR GeneID; 73162; -.
DR KEGG; mmu:73162; -.
DR UCSC; uc008vln.2; mouse.
DR CTD; 23252; -.
DR MGI; MGI:1920412; Otud3.
DR VEuPathDB; HostDB:ENSMUSG00000041161; -.
DR eggNOG; ENOG502QUTD; Eukaryota.
DR GeneTree; ENSGT00390000016392; -.
DR HOGENOM; CLU_056188_0_0_1; -.
DR InParanoid; B1AZ99; -.
DR OMA; DVPFTQH; -.
DR OrthoDB; 1448656at2759; -.
DR PhylomeDB; B1AZ99; -.
DR TreeFam; TF329594; -.
DR Reactome; R-MMU-5689896; Ovarian tumor domain proteases.
DR Reactome; R-MMU-8948751; Regulation of PTEN stability and activity.
DR BioGRID-ORCS; 73162; 1 hit in 73 CRISPR screens.
DR ChiTaRS; Otud3; mouse.
DR PRO; PR:B1AZ99; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; B1AZ99; protein.
DR Bgee; ENSMUSG00000041161; Expressed in seminiferous tubule of testis and 141 other tissues.
DR Genevisible; B1AZ99; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; ISS:UniProtKB.
DR GO; GO:0051898; P:negative regulation of protein kinase B signaling; ISO:MGI.
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; ISO:MGI.
DR GO; GO:0071108; P:protein K48-linked deubiquitination; ISO:MGI.
DR GO; GO:0044313; P:protein K6-linked deubiquitination; ISS:UniProtKB.
DR GO; GO:0050821; P:protein stabilization; ISO:MGI.
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 1: Evidence at protein level;
KW Hydrolase; Protease; Reference proteome; Thiol protease;
KW Ubl conjugation pathway.
FT CHAIN 1..396
FT /note="OTU domain-containing protein 3"
FT /id="PRO_0000424025"
FT DOMAIN 64..188
FT /note="OTU"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00139"
FT DOMAIN 229..269
FT /note="UBA-like"
FT REGION 1..49
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 69..75
FT /note="Cys-loop"
FT /evidence="ECO:0000250"
FT REGION 126..136
FT /note="Variable-loop"
FT /evidence="ECO:0000250"
FT REGION 176..181
FT /note="His-loop"
FT /evidence="ECO:0000250"
FT REGION 275..381
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 14..45
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 280..299
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 315..375
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 72
FT /evidence="ECO:0000250"
FT ACT_SITE 75
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 181
FT /evidence="ECO:0000250"
SQ SEQUENCE 396 AA; 44576 MW; 605943E424F79A47 CRC64;
MSRKQAAKSR PGSGGRRAEA ERKRDERAAR RALAKERRNR PDPGGSGCEE EFVSFANQLQ
ALGLKLREVP GDGNCLFRAL GDQLEGHSRN HLKHRQETVD YMIRQREDFE PFVEDDIPFE
KHVASLSKPG TFAGNDAIVA FARNHQLNVV IHQLNAPLWQ IRGTDKGSTR ELHIAYRYGE
HYDSVRRIND NSEAPAHLLT DFQMLHQDGA NKKEKMKTKG VDVKDGLRDD VEDAVHKVGS
ATGCTDFNLI VQNLEAENYN IKSAITALLQ VNQGTGNDAE ENHEPGDRVK QRGPSREEAG
SGRRLSGNQG RNEGRMETSE ARASPAEESK AHKSQLPKVT NKQRREQQRL EKKKRQEERH
RLKALENRNG SRDTGRSEAD MNTQVTLVKT FAALNI
