OTU8_ARATH
ID OTU8_ARATH Reviewed; 189 AA.
AC O80949;
DT 18-SEP-2019, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Putative OVARIAN TUMOR DOMAIN-containing deubiquitinating enzyme 8 {ECO:0000303|PubMed:24659992};
DE Short=OTU domain-containing protein 8 {ECO:0000303|PubMed:24659992};
DE EC=3.4.19.12 {ECO:0000250|UniProtKB:F4K3M6};
DE AltName: Full=Deubiquitinating enzyme OTU8 {ECO:0000303|PubMed:24659992};
GN Name=OTU8 {ECO:0000303|PubMed:24659992};
GN OrderedLocusNames=At2g39320 {ECO:0000312|Araport:AT2G39320};
GN ORFNames=T16B24.4 {ECO:0000312|EMBL:AEC09661.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=24659992; DOI=10.3389/fpls.2014.00084;
RA Radjacommare R., Usharani R., Kuo C.-H., Fu H.;
RT "Distinct phylogenetic relationships and biochemical properties of
RT Arabidopsis ovarian tumor-related deubiquitinases support their functional
RT differentiation.";
RL Front. Plant Sci. 5:84-84(2014).
CC -!- FUNCTION: Hydrolase that can remove conjugated ubiquitin from proteins
CC in vitro and may therefore play an important regulatory role at the
CC level of protein turnover by preventing degradation.
CC {ECO:0000305|PubMed:24659992}.
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:0000250|UniProtKB:F4K3M6};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00768}.
CC -!- SIMILARITY: Belongs to the peptidase C85 family. {ECO:0000305}.
CC -!- CAUTION: Could be the product of a pseudogene.
CC {ECO:0000303|PubMed:24659992}.
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DR EMBL; AC004697; AAC28978.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC09661.1; -; Genomic_DNA.
DR PIR; T02570; T02570.
DR RefSeq; NP_181464.1; NM_129489.2.
DR AlphaFoldDB; O80949; -.
DR SMR; O80949; -.
DR STRING; 3702.AT2G39320.1; -.
DR PaxDb; O80949; -.
DR PRIDE; O80949; -.
DR EnsemblPlants; AT2G39320.1; AT2G39320.1; AT2G39320.
DR GeneID; 818517; -.
DR Gramene; AT2G39320.1; AT2G39320.1; AT2G39320.
DR KEGG; ath:AT2G39320; -.
DR Araport; AT2G39320; -.
DR TAIR; locus:2056133; AT2G39320.
DR eggNOG; KOG2605; Eukaryota.
DR HOGENOM; CLU_1442902_0_0_1; -.
DR InParanoid; O80949; -.
DR OMA; SDCHELV; -.
DR OrthoDB; 1448656at2759; -.
DR PhylomeDB; O80949; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O80949; baseline and differential.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC.
DR InterPro; IPR003323; OTU_dom.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR SUPFAM; SSF54001; SSF54001; 1.
DR PROSITE; PS50802; OTU; 1.
PE 5: Uncertain;
KW Coiled coil; Hydrolase; Nucleus; Reference proteome;
KW Ubl conjugation pathway.
FT CHAIN 1..189
FT /note="Putative OVARIAN TUMOR DOMAIN-containing
FT deubiquitinating enzyme 8"
FT /id="PRO_0000447758"
FT DOMAIN 1..103
FT /note="OTU"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00139"
FT REGION 105..189
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 120..181
FT /evidence="ECO:0000255"
FT MOTIF 125..132
FT /note="Nuclear localization signal 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT MOTIF 163..170
FT /note="Nuclear localization signal 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT COMPBIAS 123..168
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 5
FT /evidence="ECO:0000255"
FT ACT_SITE 8
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q96G74"
FT ACT_SITE 96
FT /evidence="ECO:0000250|UniProtKB:Q96G74"
SQ SEQUENCE 189 AA; 22398 MW; 23D7DF43CF4A29F0 CRC64;
MMKSDGNCQF RALADQLYQN SDCHELVRQE IVKQNMSLST NSQWGDEVTL RVAADVYQVK
IILITSIKLI PFMEFLPKSQ KEPDKVIHMS YLAGIHFNSI YKKNKEKGSR SSSSSSSAVW
MKLQRKKENE AKKKEEEEKE RKDMEKEEKK KDKEDKKKDK EDKKKAKVQK EKKEKKEKKN
RNHHFHYSE
