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   27-MAR-2024, entry version 136.
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; 47.
DR   STRING; 10090.ENSMUSP00000057282; -.
DR   MEROPS; C64.002; -.
DR   iPTMnet; Q8R554; -.
DR   PhosphoSitePlus; Q8R554; -.
DR   MaxQB; Q8R554; -.
DR   PaxDb; 10090-ENSMUSP00000057282; -.
DR   PeptideAtlas; Q8R554; -.
DR   ProteomicsDB; 287746; -.
DR   Antibodypedia; 22563; 109 antibodies from 19 providers.
DR   DNASU; 170711; -.
DR   Ensembl; ENSMUST00000058476.14; ENSMUSP00000057282.8; ENSMUSG00000033510.15.
DR   GeneID; 170711; -.
DR   KEGG; mmu:170711; -.
DR   UCSC; uc009hfl.1; mouse.
DR   AGR; MGI:2158505; -.
DR   CTD; 161725; -.
DR   MGI; MGI:2158505; Otud7a.
DR   VEuPathDB; HostDB:ENSMUSG00000033510; -.
DR   eggNOG; KOG4345; Eukaryota.
DR   GeneTree; ENSGT00940000158999; -.
DR   InParanoid; Q8R554; -.
DR   OMA; RCAKQPE; -.
DR   PhylomeDB; Q8R554; -.
DR   TreeFam; TF323312; -.
DR   Reactome; R-MMU-5689896; Ovarian tumor domain proteases.
DR   BioGRID-ORCS; 170711; 3 hits in 77 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 88 other cell types or tissues.
DR   ExpressionAtlas; Q8R554; baseline and differential.
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:0035871; P:protein K11-linked deubiquitination; ISS:UniProtKB.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd14347; UBA_Cezanne_like; 1.
DR   Gene3D; 1.20.5.4770; -; 1.
DR   Gene3D; 1.10.8.10; DNA helicase RuvA subunit, C-terminal domain; 1.
DR   InterPro; IPR003323; OTU_dom.
DR   InterPro; IPR002653; Znf_A20.
DR   PANTHER; PTHR13367:SF9; OTU DOMAIN-CONTAINING PROTEIN 7A; 1.
DR   PANTHER; PTHR13367; UBIQUITIN THIOESTERASE; 1.
DR   Pfam; PF02338; OTU; 1.
DR   Pfam; PF01754; zf-A20; 1.
DR   SUPFAM; SSF57716; Glucocorticoid receptor-like (DNA-binding domain); 1.
DR   PROSITE; PS50802; OTU; 1.
DR   PROSITE; PS51036; ZF_A20; 1.
DR   Genevisible; Q8R554; MM.
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
//