OTU7A_MOUSE
ID OTU7A_MOUSE Reviewed; 926 AA.
AC Q8R554;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=OTU domain-containing protein 7A;
DE EC=3.4.19.12;
DE AltName: Full=Zinc finger protein Cezanne 2;
GN Name=Otud7a; Synonyms=Cezanne2, Otud7;
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 [MRNA].
RC STRAIN=C57BL/6J;
RA Evans P.C., Coadwell W.J., Kilshaw P.J.;
RT "Isolation of a novel murine gene, Cezanne 2.";
RL Submitted (FEB-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-121, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [3]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-880, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
CC -!- FUNCTION: Has deubiquitinating activity towards 'Lys-11'-linked
CC polyubiquitin chains. {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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase C64 family. {ECO:0000305}.
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DR EMBL; AJ430384; CAD23048.1; -; mRNA.
DR CCDS; CCDS21330.1; -.
DR RefSeq; NP_570950.1; NM_130880.1.
DR AlphaFoldDB; Q8R554; -.
DR BMRB; Q8R554; -.
DR SMR; Q8R554; -.
DR BioGRID; 228387; 1.
DR STRING; 10090.ENSMUSP00000057282; -.
DR MEROPS; C64.002; -.
DR iPTMnet; Q8R554; -.
DR PhosphoSitePlus; Q8R554; -.
DR MaxQB; Q8R554; -.
DR PaxDb; Q8R554; -.
DR PeptideAtlas; Q8R554; -.
DR PRIDE; Q8R554; -.
DR ProteomicsDB; 287746; -.
DR Antibodypedia; 22563; 96 antibodies from 19 providers.
DR DNASU; 170711; -.
DR Ensembl; ENSMUST00000058476; ENSMUSP00000057282; ENSMUSG00000033510.
DR GeneID; 170711; -.
DR KEGG; mmu:170711; -.
DR UCSC; uc009hfl.1; mouse.
DR CTD; 161725; -.
DR MGI; MGI:2158505; Otud7a.
DR VEuPathDB; HostDB:ENSMUSG00000033510; -.
DR eggNOG; KOG4345; Eukaryota.
DR GeneTree; ENSGT00940000158999; -.
DR InParanoid; Q8R554; -.
DR OMA; HVANDCS; -.
DR PhylomeDB; Q8R554; -.
DR TreeFam; TF323312; -.
DR Reactome; R-MMU-5689896; Ovarian tumor domain proteases.
DR BioGRID-ORCS; 170711; 3 hits in 72 CRISPR screens.
DR ChiTaRS; Otud7a; mouse.
DR PRO; PR:Q8R554; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q8R554; protein.
DR Bgee; ENSMUSG00000033510; Expressed in substantia nigra and 86 other tissues.
DR ExpressionAtlas; Q8R554; baseline and differential.
DR Genevisible; Q8R554; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; ISS:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0070530; F:K63-linked polyubiquitin modification-dependent protein binding; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0043124; P:negative regulation of I-kappaB kinase/NF-kappaB signaling; IBA:GO_Central.
DR GO; GO:0071947; P:protein deubiquitination involved in ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR GO; GO:0035871; P:protein K11-linked deubiquitination; ISS:UniProtKB.
DR GO; GO:0071108; P:protein K48-linked deubiquitination; IBA:GO_Central.
DR GO; GO:0070536; P:protein K63-linked deubiquitination; IBA:GO_Central.
DR InterPro; IPR033477; Cezanne-2.
DR InterPro; IPR003323; OTU_dom.
DR InterPro; IPR002653; Znf_A20.
DR PANTHER; PTHR13367:SF9; PTHR13367:SF9; 1.
DR Pfam; PF02338; OTU; 1.
DR Pfam; PF01754; zf-A20; 1.
DR PROSITE; PS50802; OTU; 1.
DR PROSITE; PS51036; ZF_A20; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Hydrolase; Metal-binding; Methylation; Nucleus; Phosphoprotein;
KW Protease; Reference proteome; Thiol protease; Ubl conjugation pathway;
KW Zinc; Zinc-finger.
FT CHAIN 1..926
FT /note="OTU domain-containing protein 7A"
FT /id="PRO_0000188790"
FT DOMAIN 201..377
FT /note="OTU"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00139"
FT ZN_FING 884..919
FT /note="A20-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00451"
FT REGION 170..413
FT /note="TRAF-binding"
FT /evidence="ECO:0000250"
FT REGION 185..452
FT /note="Catalytic"
FT /evidence="ECO:0000250"
FT REGION 455..517
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 540..615
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 671..779
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 497..512
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 456..493
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 494..515
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 558..576
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 577..598
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 209
FT /evidence="ECO:0000250"
FT ACT_SITE 212
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 370
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 890
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00451"
FT BINDING 895
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00451"
FT BINDING 907
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00451"
FT BINDING 910
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00451"
FT MOD_RES 121
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 880
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
SQ SEQUENCE 926 AA; 100797 MW; 4D6BD05A0410BED9 CRC64;
MVSSLLPNPP SAECWAALLH DPMTLDMDAV LSDFVRSTGA EPGLARDLLE GKNWDLTAAL
SDYEQLRQVH TANLPHVFNE GRCAKQAERE LPQPGHKVER PCLQRQDDIA QAEKRLSRGI
SHASSAIVSL ARSHVANECN NEQFPLEMPI YTFQLPDLSV YSEDFRSFIE RDLIEQATMV
ALEQAGRLNW WSTVCTSCKR LLPLATTGDG NCLLHAASLG MWGFHDRDLV LRKALYTMMR
TGAEREALKR RWRWQQTQQN KEEEWEREWT ELLKLASSEP RTHFSKNGSG TGGGVDNSED
PVYESLEEFH VFVLAHILRR PIVVVADTML RDSGGEAFAP IPFGGIYLPL EVPPNRCHCS
PLVLAYDQAH FSALVSMEQR DQQREQAVIP LTDSEHKLLP LHFAVDPGKD WEWGKDDNDN
ARLANLILSL EAKLNLLHSY MNVTWIRIPS ETRAPLAQPE SPTASAGEDV QSLAESLDSD
RDSVCSNSNS NNGKNGKDKE KEKQRKDKDK TRADSVANKL GSFSKTLGIK LKKNMGGLGG
LVHGKMGRAN SANGKNGDSA ERNKEKKSKS RKGSKEESGA SASTSPSEKT TPSPTDKASG
ASPADKGSGS RGDAWKYSTD VKLSLNILRA AMQGERKFIF AGLLLTSHRH QFHEEMIGYY
LTSAQERFSA EQEQRRRDAA AAAAAATATA TVKRPARRPE AEGAPGPERA SPGPTAAQPT
QLVLKLKERP SPGTGASARA ARAAGGAASP GPGGGARRAA PGTGGPTPGR SPPAPARQSV
IHVQAAARDE ACAPTVGALR PCATYPQQNR SLWSQSYSPA RSALRTVNTV ESLAPGGADA
PGPAEHKSQT YSNGFGAARD GLEFADADAP AARSNAECGR GGPGPAQRRC QRENCAFYGR
AETEHFCSYC YREELRRRRE ARAARP
