OTU7A_HUMAN
ID OTU7A_HUMAN Reviewed; 926 AA.
AC Q8TE49; Q8IWK5;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 149.
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=C15orf16, CEZANNE2, OTUD7;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Evans P.C., Coadwell W.J., Kilshaw P.J.;
RT "Isolation of a novel human gene, Cezanne 2.";
RL Submitted (FEB-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-678 (ISOFORM 2).
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP FUNCTION.
RX PubMed=20622874; DOI=10.1038/nsmb.1873;
RA Bremm A., Freund S.M., Komander D.;
RT "Lys11-linked ubiquitin chains adopt compact conformations and are
RT preferentially hydrolyzed by the deubiquitinase Cezanne.";
RL Nat. Struct. Mol. Biol. 17:939-947(2010).
RN [4]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=23827681; DOI=10.1016/j.cell.2013.05.046;
RA Mevissen T.E., Hospenthal M.K., Geurink P.P., Elliott P.R., Akutsu M.,
RA Arnaudo N., Ekkebus R., Kulathu Y., Wauer T., El Oualid F., Freund S.M.,
RA Ovaa H., Komander D.;
RT "OTU deubiquitinases reveal mechanisms of linkage specificity and enable
RT ubiquitin chain restriction analysis.";
RL Cell 154:169-184(2013).
RN [5]
RP STRUCTURE BY NMR OF 11-83.
RG Structural genomics consortium (SGC);
RT "The amino-terminal UBA domain of OTUD7A.";
RL Submitted (FEB-2012) to the PDB data bank.
CC -!- FUNCTION: Has deubiquitinating activity towards 'Lys-11'-linked
CC polyubiquitin chains. {ECO:0000269|PubMed:20622874,
CC ECO:0000269|PubMed:23827681}.
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:0000269|PubMed:23827681};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8TE49-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8TE49-2; Sequence=VSP_011430;
CC -!- SIMILARITY: Belongs to the peptidase C64 family. {ECO:0000305}.
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DR EMBL; AJ430383; CAD23047.1; -; mRNA.
DR EMBL; BC035668; AAH35668.1; -; mRNA.
DR CCDS; CCDS10026.1; -. [Q8TE49-1]
DR RefSeq; NP_570971.1; NM_130901.2. [Q8TE49-1]
DR PDB; 2L2D; NMR; -; A=11-83.
DR PDBsum; 2L2D; -.
DR AlphaFoldDB; Q8TE49; -.
DR BMRB; Q8TE49; -.
DR SMR; Q8TE49; -.
DR BioGRID; 127799; 16.
DR IntAct; Q8TE49; 1.
DR STRING; 9606.ENSP00000305926; -.
DR MEROPS; C64.002; -.
DR iPTMnet; Q8TE49; -.
DR PhosphoSitePlus; Q8TE49; -.
DR BioMuta; OTUD7A; -.
DR DMDM; 51701344; -.
DR EPD; Q8TE49; -.
DR jPOST; Q8TE49; -.
DR MassIVE; Q8TE49; -.
DR MaxQB; Q8TE49; -.
DR PaxDb; Q8TE49; -.
DR PeptideAtlas; Q8TE49; -.
DR PRIDE; Q8TE49; -.
DR ProteomicsDB; 74392; -. [Q8TE49-1]
DR ProteomicsDB; 74393; -. [Q8TE49-2]
DR Antibodypedia; 22563; 96 antibodies from 19 providers.
DR DNASU; 161725; -.
DR Ensembl; ENST00000307050.6; ENSP00000305926.5; ENSG00000169918.10. [Q8TE49-2]
DR Ensembl; ENST00000560598.2; ENSP00000453883.2; ENSG00000169918.10. [Q8TE49-1]
DR Ensembl; ENST00000678495.1; ENSP00000503326.1; ENSG00000169918.10. [Q8TE49-1]
DR GeneID; 161725; -.
DR KEGG; hsa:161725; -.
DR MANE-Select; ENST00000307050.6; ENSP00000305926.5; NM_001382637.1; NP_001369566.1. [Q8TE49-2]
DR UCSC; uc001zfq.4; human. [Q8TE49-1]
DR CTD; 161725; -.
DR DisGeNET; 161725; -.
DR GeneCards; OTUD7A; -.
DR HGNC; HGNC:20718; OTUD7A.
DR HPA; ENSG00000169918; Tissue enriched (brain).
DR MalaCards; OTUD7A; -.
DR MIM; 612024; gene.
DR neXtProt; NX_Q8TE49; -.
DR OpenTargets; ENSG00000169918; -.
DR PharmGKB; PA134877572; -.
DR VEuPathDB; HostDB:ENSG00000169918; -.
DR eggNOG; KOG4345; Eukaryota.
DR GeneTree; ENSGT00940000158999; -.
DR HOGENOM; CLU_013263_0_0_1; -.
DR InParanoid; Q8TE49; -.
DR OMA; HVANDCS; -.
DR OrthoDB; 728724at2759; -.
DR PhylomeDB; Q8TE49; -.
DR TreeFam; TF323312; -.
DR PathwayCommons; Q8TE49; -.
DR Reactome; R-HSA-5689896; Ovarian tumor domain proteases.
DR SignaLink; Q8TE49; -.
DR SIGNOR; Q8TE49; -.
DR BioGRID-ORCS; 161725; 11 hits in 1112 CRISPR screens.
DR ChiTaRS; OTUD7A; human.
DR EvolutionaryTrace; Q8TE49; -.
DR GenomeRNAi; 161725; -.
DR Pharos; Q8TE49; Tbio.
DR PRO; PR:Q8TE49; -.
DR Proteomes; UP000005640; Chromosome 15.
DR RNAct; Q8TE49; protein.
DR Bgee; ENSG00000169918; Expressed in endothelial cell and 123 other tissues.
DR ExpressionAtlas; Q8TE49; baseline and differential.
DR Genevisible; Q8TE49; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IDA: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:0016579; P:protein deubiquitination; TAS:Reactome.
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; IDA: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 SMART; SM00259; ZnF_A20; 1.
DR PROSITE; PS50802; OTU; 1.
DR PROSITE; PS51036; ZF_A20; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cytoplasm; Hydrolase; Metal-binding;
KW Methylation; Nucleus; Phosphoprotein; Protease; Reference proteome;
KW Thiol protease; Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..926
FT /note="OTU domain-containing protein 7A"
FT /id="PRO_0000188789"
FT DOMAIN 199..374
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 75..99
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 168..410
FT /note="TRAF-binding"
FT /evidence="ECO:0000250"
FT REGION 183..449
FT /note="Catalytic"
FT /evidence="ECO:0000250"
FT REGION 452..514
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 537..613
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 668..768
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 494..509
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 82..99
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 453..490
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 491..512
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 555..573
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 574..594
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 207
FT /evidence="ECO:0000250"
FT ACT_SITE 210
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 367
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 119
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8R554"
FT MOD_RES 880
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q8R554"
FT VAR_SEQ 260
FT /note="E -> ESGLVYTE (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_011430"
FT STRAND 13..15
FT /evidence="ECO:0007829|PDB:2L2D"
FT STRAND 22..24
FT /evidence="ECO:0007829|PDB:2L2D"
FT HELIX 27..38
FT /evidence="ECO:0007829|PDB:2L2D"
FT HELIX 42..51
FT /evidence="ECO:0007829|PDB:2L2D"
FT TURN 52..54
FT /evidence="ECO:0007829|PDB:2L2D"
FT HELIX 56..68
FT /evidence="ECO:0007829|PDB:2L2D"
FT STRAND 71..75
FT /evidence="ECO:0007829|PDB:2L2D"
SQ SEQUENCE 926 AA; 100677 MW; 6E4623C2EB2C8058 CRC64;
MVSSVLPNPT SAECWAALLH DPMTLDMDAV LSDFVRSTGA EPGLARDLLE GKNWDLTAAL
SDYEQLRQVH TANLPHVFNE GRGPKQPERE PQPGHKVERP CLQRQDDIAQ EKRLSRGISH
ASSAIVSLAR SHVASECNNE QFPLEMPIYT FQLPDLSVYS EDFRSFIERD LIEQATMVAL
EQAGRLNWWS TVCTSCKRLL PLATTGDGNC LLHAASLGMW GFHDRDLVLR KALYTMMRTG
AEREALKRRW RWQQTQQNKE EEWEREWTEL LKLASSEPRT HFSKNGGTGG GVDNSEDPVY
ESLEEFHVFV LAHILRRPIV VVADTMLRDS GGEAFAPIPF GGIYLPLEVP PNRCHCSPLV
LAYDQAHFSA LVSMEQRDQQ REQAVIPLTD SEHKLLPLHF AVDPGKDWEW GKDDNDNARL
AHLILSLEAK LNLLHSYMNV TWIRIPSETR APLAQPESPT ASAGEDVQSL ADSLDSDRDS
VCSNSNSNNG KNGKDKEKEK QRKEKDKTRA DSVANKLGSF SKTLGIKLKK NMGGLGGLVH
GKMGRANSAN GKNGDSAERG KEKKAKSRKG SKEESGASAS TSPSEKTTPS PTDKAAGASP
AEKGGGPRGD AWKYSTDVKL SLNILRAAMQ GERKFIFAGL LLTSHRHQFH EEMIGYYLTS
AQERFSAEQE QRRRDAATAA AAAAAAAAAT AKRPPRRPET EGVPVPERAS PGPPTQLVLK
LKERPSPGPA AGRAARAAAG GTASPGGGAR RASASGPVPG RSPPAPARQS VIHVQASGAR
DEACAPAVGA LRPCATYPQQ NRSLSSQSYS PARAAALRTV NTVESLARAV PGALPGAAGT
AGAAEHKSQT YTNGFGALRD GLEFADADAP TARSNGECGR GGPGPVQRRC QRENCAFYGR
AETEHYCSYC YREELRRRRE ARGARP
