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OTU domain-containing protein 7B (EC 3.4.19.12) (Cellular zinc finger anti-NF-kappa-B protein) (Zinc finger A20 domain-containing protein 1) (Zinc finger protein Cezanne)

 OTU7B_MOUSE             Reviewed;         840 AA.
B2RUR8; Q8CFS0;
06-MAR-2013, integrated into UniProtKB/Swiss-Prot.
01-JUL-2008, sequence version 1.
27-SEP-2017, entry version 88.
RecName: Full=OTU domain-containing protein 7B;
EC=3.4.19.12 {ECO:0000269|PubMed:23334419};
AltName: Full=Cellular zinc finger anti-NF-kappa-B protein;
AltName: Full=Zinc finger A20 domain-containing protein 1;
AltName: Full=Zinc finger protein Cezanne {ECO:0000305};
Name=Otud7b;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain, and Eye;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=17242355; DOI=10.1073/pnas.0609836104;
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
"Large-scale phosphorylation analysis of mouse liver.";
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
[5]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-100; SER-464; SER-467;
SER-471 AND THR-730, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Lung, Pancreas,
Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[6]
FUNCTION, CATALYTIC ACTIVITY, DISRUPTION PHENOTYPE, INTERACTION WITH
TRAF3, MUTAGENESIS OF CYS-194 AND HIS-358, AND ACTIVE SITE.
PubMed=23334419; DOI=10.1038/nature11831;
Hu H., Brittain G.C., Chang J.H., Puebla-Osorio N., Jin J., Zal A.,
Xiao Y., Cheng X., Chang M., Fu Y.X., Zal T., Zhu C., Sun S.C.;
"OTUD7B controls non-canonical NF-kappaB activation through
deubiquitination of TRAF3.";
Nature 494:371-374(2013).
[7]
DISRUPTION PHENOTYPE, FUNCTION, AND INTERACTION WITH ZAP70.
PubMed=26903241; DOI=10.1084/jem.20151426;
Hu H., Wang H., Xiao Y., Jin J., Chang J.H., Zou Q., Xie X., Cheng X.,
Sun S.C.;
"Otud7b facilitates T cell activation and inflammatory responses by
regulating Zap70 ubiquitination.";
J. Exp. Med. 213:399-414(2016).
-!- FUNCTION: Negative regulator of the non-canonical NF-kappa-B
pathway that acts by mediating deubiquitination of TRAF3, an
inhibitor of the NF-kappa-B pathway, thereby acting as a negative
regulator of B-cell responses. In response to non-canonical NF-
kappa-B stimuli, deubiquitinates 'Lys-48'-linked polyubiquitin
chains of TRAF3, preventing TRAF3 proteolysis and over-activation
of non-canonical NF-kappa-B (PubMed:23334419). Negatively
regulates mucosal immunity against infections (PubMed:23334419).
Deubiquitinates ZAP70, and thereby regulates T cell receptor (TCR)
signaling that leads to the activation of NF-kappa-B
(PubMed:26903241). Plays a role in T cell homeostasis and is
required for normal T cell responses, including production of IFNG
and IL2 (PubMed:26903241). Mediates deubiquitination of EGFR (By
similarity). Has deubiquitinating activity toward 'Lys-11', 'Lys-
48' and 'Lys-63'-linked polyubiquitin chains. Has a much higher
catalytic rate with 'Lys-11'-linked polyubiquitin chains (in
vitro); however the physiological significance of these data are
unsure. Hydrolyzes both linear and branched forms of polyubiquitin
(By similarity). {ECO:0000250|UniProtKB:Q6GQQ9,
ECO:0000269|PubMed:23334419, ECO:0000269|PubMed:26903241}.
-!- CATALYTIC ACTIVITY: Thiol-dependent hydrolysis of ester,
thioester, amide, peptide and isopeptide bonds formed by the C-
terminal Gly of ubiquitin (a 76-residue protein attached to
proteins as an intracellular targeting signal).
{ECO:0000269|PubMed:23334419}.
-!- ENZYME REGULATION: Deubiquitinase activity is inhibited following
interaction with PARK7. {ECO:0000250|UniProtKB:Q6GQQ9}.
-!- SUBUNIT: Interacts with TRAF6. Interacts with PARK7, leading to
inhibit deubiquitinase activity. Interacts with EGFR, ITCH and
NEDD4 (By similarity). Interacts with TRAF3 (PubMed:23334419).
Interacts with ZAP70 in activated T cells, but not in resting T
cells (PubMed:26903241). {ECO:0000250|UniProtKB:Q6GQQ9,
ECO:0000269|PubMed:23334419, ECO:0000269|PubMed:26903241}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q6GQQ9}.
Nucleus {ECO:0000250|UniProtKB:Q6GQQ9}. Note=Shuttles be cytoplasm
and the nucleus in a XPO1/CRM1-dependent manner.
{ECO:0000250|UniProtKB:Q6GQQ9}.
-!- DOMAIN: The protein undergoes a significant conformation change
upon binding to ubiquitinated substrates. The loop that precedes
the active site is in an autoinhibitory conformation in the
apoprotein. Ubiquitin binding leads to a conformation change; the
loop is stabilized in a catalytically competent conformation with
the result that the active site Cys can form the reaction state
intermediate. {ECO:0000250|UniProtKB:Q6GQQ9}.
-!- PTM: Phosphorylated by EGFR. {ECO:0000250|UniProtKB:Q6GQQ9}.
-!- DISRUPTION PHENOTYPE: No visible phenotype in neonates
(PubMed:26903241). Mice do not show obvious defects in survival,
except a moderately reduced body weight (PubMed:23334419). They
however display hyperactivation of non-canonical NF-kappa-B
without affecting canonical NF-kappa-B activation. Mice show B-
cell hyper-responsiveness to antigens, lymphoid follicular
hyperplasia in the intestinal mucosa and elevated host-defense
ability against an intestinal bacterial pathogen, Citrobacter
rodentium (PubMed:23334419). At 12 months after birth, mutant mice
display impaired T cell homeostasis with increased numbers of
naive T cells and reduced numbers of Th1 memory-like T cells
(PubMed:26903241). Young adults that have no overt change in T
cell homeostasis still show impaired production of effector T
cells in response to repeated stimulation with an antigen and an
impaired defense against infection by L.monocytogenes
(PubMed:26903241). Conversely, mutant mice are less susceptible to
experimentally induced autoimmune encephalitis (PubMed:26903241).
{ECO:0000269|PubMed:23334419, ECO:0000269|PubMed:26903241}.
-!- SIMILARITY: Belongs to the peptidase C64 family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAH37040.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; AC092094; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH466620; EDL38862.1; -; Genomic_DNA.
EMBL; BC141397; AAI41398.1; -; mRNA.
EMBL; BC037040; AAH37040.1; ALT_SEQ; mRNA.
EMBL; BC141398; AAI41399.1; -; mRNA.
CCDS; CCDS17629.1; -.
RefSeq; NP_001020784.1; NM_001025613.1.
RefSeq; NP_001020785.1; NM_001025614.1.
RefSeq; XP_006501448.1; XM_006501385.3.
RefSeq; XP_006501449.1; XM_006501386.3.
RefSeq; XP_006501452.1; XM_006501389.3.
RefSeq; XP_017175035.1; XM_017319546.1.
RefSeq; XP_017175036.1; XM_017319547.1.
UniGene; Mm.272336; -.
UniGene; Mm.487453; -.
ProteinModelPortal; B2RUR8; -.
SMR; B2RUR8; -.
BioGrid; 230871; 6.
DIP; DIP-60128N; -.
IntAct; B2RUR8; 1.
STRING; 10090.ENSMUSP00000046413; -.
MEROPS; C64.001; -.
iPTMnet; B2RUR8; -.
PhosphoSitePlus; B2RUR8; -.
EPD; B2RUR8; -.
MaxQB; B2RUR8; -.
PaxDb; B2RUR8; -.
PeptideAtlas; B2RUR8; -.
PRIDE; B2RUR8; -.
Ensembl; ENSMUST00000035519; ENSMUSP00000046413; ENSMUSG00000038495.
Ensembl; ENSMUST00000090785; ENSMUSP00000088291; ENSMUSG00000038495.
Ensembl; ENSMUST00000098849; ENSMUSP00000096449; ENSMUSG00000038495.
GeneID; 229603; -.
KEGG; mmu:229603; -.
UCSC; uc008qma.1; mouse.
CTD; 56957; -.
MGI; MGI:2654703; Otud7b.
eggNOG; KOG4345; Eukaryota.
eggNOG; ENOG410XT8E; LUCA.
GeneTree; ENSGT00530000062989; -.
HOGENOM; HOG000048103; -.
HOVERGEN; HBG050904; -.
InParanoid; B2RUR8; -.
KO; K11860; -.
OMA; YATFPRQ; -.
OrthoDB; EOG091G03R0; -.
PhylomeDB; B2RUR8; -.
TreeFam; TF323312; -.
Reactome; R-MMU-5689896; Ovarian tumor domain proteases.
ChiTaRS; Otud7b; mouse.
PRO; PR:B2RUR8; -.
Proteomes; UP000000589; Chromosome 3.
Bgee; ENSMUSG00000038495; -.
ExpressionAtlas; B2RUR8; baseline and differential.
Genevisible; B2RUR8; MM.
GO; GO:0005737; C:cytoplasm; IDA:MGI.
GO; GO:0005634; C:nucleus; ISO:MGI.
GO; GO:0008234; F:cysteine-type peptidase activity; IMP:UniProtKB.
GO; GO:0003677; F:DNA binding; IEA:InterPro.
GO; GO:0070530; F:K63-linked polyubiquitin modification-dependent protein binding; IDA:BHF-UCL.
GO; GO:1990380; F:Lys48-specific deubiquitinase activity; ISO:MGI.
GO; GO:0004843; F:thiol-dependent ubiquitin-specific protease activity; IDA:MGI.
GO; GO:0036459; F:thiol-dependent ubiquitinyl hydrolase activity; IMP:UniProtKB.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
GO; GO:0002385; P:mucosal immune response; IMP:UniProtKB.
GO; GO:0043124; P:negative regulation of I-kappaB kinase/NF-kappaB signaling; IMP:UniProtKB.
GO; GO:0032717; P:negative regulation of interleukin-8 production; ISO:MGI.
GO; GO:1900181; P:negative regulation of protein localization to nucleus; ISO:MGI.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IDA:ParkinsonsUK-UCL.
GO; GO:0016579; P:protein deubiquitination; IDA:MGI.
GO; GO:0071947; P:protein deubiquitination involved in ubiquitin-dependent protein catabolic process; IBA:GO_Central.
GO; GO:0035871; P:protein K11-linked deubiquitination; ISS:UniProtKB.
GO; GO:0071108; P:protein K48-linked deubiquitination; IMP:UniProtKB.
GO; GO:0070536; P:protein K63-linked deubiquitination; ISS:UniProtKB.
InterPro; IPR003323; OTU_dom.
InterPro; IPR002653; Znf_A20.
Pfam; PF02338; OTU; 1.
Pfam; PF01754; zf-A20; 1.
SMART; SM00259; ZnF_A20; 1.
PROSITE; PS50802; OTU; 1.
PROSITE; PS51036; ZF_A20; 1.
1: Evidence at protein level;
Adaptive immunity; Complete proteome; Cytoplasm; Hydrolase; Immunity;
Metal-binding; Nucleus; Phosphoprotein; Protease; Reference proteome;
Thiol protease; Ubl conjugation pathway; Zinc; Zinc-finger.
CHAIN 1 840 OTU domain-containing protein 7B.
/FTId=PRO_0000421819.
DOMAIN 183 365 OTU. {ECO:0000255|PROSITE-
ProRule:PRU00139}.
ZN_FING 793 828 A20-type. {ECO:0000255|PROSITE-
ProRule:PRU00451}.
REGION 152 401 TRAF-binding. {ECO:0000250}.
REGION 167 440 Catalytic. {ECO:0000250}.
REGION 187 193 Regulatory loop.
{ECO:0000250|UniProtKB:Q6GQQ9}.
MOTIF 483 498 Nuclear localization signal.
{ECO:0000255}.
ACT_SITE 191 191 {ECO:0000250}.
ACT_SITE 194 194 Nucleophile.
{ECO:0000269|PubMed:23334419}.
ACT_SITE 358 358 Proton acceptor.
{ECO:0000269|PubMed:23334419}.
SITE 197 197 Stabilizes the conformation of the
regulatory loop.
{ECO:0000250|UniProtKB:Q6GQQ9}.
MOD_RES 100 100 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 464 464 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 467 467 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 471 471 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 730 730 Phosphothreonine.
{ECO:0000244|PubMed:21183079}.
MUTAGEN 194 194 C->S: Loss of deubiquitinating activity;
when associated with R-358.
{ECO:0000269|PubMed:23334419}.
MUTAGEN 358 358 H->R: Loss of deubiquitinating activity;
when associated with S-194.
{ECO:0000269|PubMed:23334419}.
SEQUENCE 840 AA; 91983 MW; B63C06B656CC02EE CRC64;
MTLDMDAVLS DFVRSTGAEP GLARDLLEGK NWDVSAALSD FEQLRQVHAG NLSPPFSGGS
TCPKTPEKGG SDREPTRPSR PILQRQDDVI QEKRLSRGIS HASSSIVSLA RSHVSSNGGG
GGSSEHPLEM PICAFQLPDL TVYKEDFRSF IERDLIEQSM LVALEQAGRL NWWVSMDSTC
QRLLPLATTG DGNCLLHAAS LGMWGFHDRD LVLRKALYAL MEKGVEKEAL RRRWRWQQTQ
QNKESGLVYT EDEWQKEWNE LIKLASSEPR MHLGSNGASG GGVESSEEPV YESLEEFHVF
VLAHVLKRPI VVVADTMLRD SGGEAFAPIP FGGIYLPLEV PASQCHRSPL VLAYDQAHFS
ALVSMEQKES AKEQAVIPLT DSEHKLLPLH FAVDPGKGWE WGKDDNDNVR LASIILSLEV
KLHLLHSYMN VKWIPLSSDS QAPLAQPESP TASAGDEPRS TPESGESDKE SVGSSSLGNE
GSRRKEKSKR DREKDKKRAD SVANKLGSFG KTLGSKLKKN MGGLMHSKGP KPGGLGSGSG
ISSGTETLEK KKKNNTLKSW KGGKEEAAGD GPVSEKPPSE SVGNGGSKYS QEVMQSLSTM
RIAMQGEGKY IFVGTLKMGH RHQYQEEMIQ RYLADAEERF LAEQKQKEVE RKIMNGGLVS
GPPPAKKPEP DGGEDQPSDS PAEPKAMAFS TAYPGGFTIP RPSGGGVHCQ EPRRQLAGGP
CVGGLPSYAT FPRQYPGRPY PHQDNIPALE PGKDGVHRGA LLPPQFRVAD SYSNGYREPP
EPDGWAGAPR GLPPTQTKCK QPNCSFYGHP ETNNLCSCCY REELRRRERE PGGELLAHRF


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