OTU3_ARATH
ID OTU3_ARATH Reviewed; 234 AA.
AC Q8GYW0;
DT 18-SEP-2019, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=OVARIAN TUMOR DOMAIN-containing deubiquitinating enzyme 3 {ECO:0000303|PubMed:24659992};
DE Short=OTU domain-containing protein 3 {ECO:0000303|PubMed:24659992};
DE EC=3.4.19.12 {ECO:0000269|PubMed:24659992};
DE AltName: Full=Deubiquitinating enzyme OTU3 {ECO:0000303|PubMed:24659992};
GN Name=OTU3 {ECO:0000303|PubMed:24659992};
GN OrderedLocusNames=At2g38025 {ECO:0000312|Araport:AT2G38025};
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 [MRNA], FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES,
RP CATALYTIC ACTIVITY, GENE FAMILY, AND NOMENCLATURE.
RC STRAIN=cv. Columbia;
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).
RN [2]
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
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 (PubMed:24659992).
CC Cysteine protease with a preference for 'Lys-63' over 'Lys-48' over
CC 'Met-1' -linked ubiquitin (UB) tetramers (e.g. Ub3 and Ub4) as
CC substrates (PubMed:24659992). Cleaves also RUB-GST fusion
CC (PubMed:24659992). {ECO:0000269|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:0000269|PubMed:24659992};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 7. {ECO:0000269|PubMed:24659992};
CC -!- SIMILARITY: Belongs to the peptidase C85 family. {ECO:0000305}.
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DR EMBL; JQ013444; AFS88947.1; -; mRNA.
DR EMBL; LR215053; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002685; AEC09481.1; -; Genomic_DNA.
DR EMBL; AK117356; BAC42026.1; -; mRNA.
DR EMBL; BT005253; AAO63317.1; -; mRNA.
DR RefSeq; NP_850290.1; NM_179959.4.
DR AlphaFoldDB; Q8GYW0; -.
DR SMR; Q8GYW0; -.
DR STRING; 3702.AT2G38025.1; -.
DR PaxDb; Q8GYW0; -.
DR PRIDE; Q8GYW0; -.
DR ProteomicsDB; 183108; -.
DR EnsemblPlants; AT2G38025.1; AT2G38025.1; AT2G38025.
DR GeneID; 818381; -.
DR Gramene; AT2G38025.1; AT2G38025.1; AT2G38025.
DR KEGG; ath:AT2G38025; -.
DR Araport; AT2G38025; -.
DR TAIR; locus:504955906; AT2G38025.
DR eggNOG; ENOG502QS0W; Eukaryota.
DR HOGENOM; CLU_082874_0_0_1; -.
DR InParanoid; Q8GYW0; -.
DR OMA; NRYCQRI; -.
DR OrthoDB; 1448656at2759; -.
DR PhylomeDB; Q8GYW0; -.
DR PRO; PR:Q8GYW0; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q8GYW0; baseline and differential.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IBA:GO_Central.
DR GO; GO:0030968; P:endoplasmic reticulum unfolded protein response; IBA:GO_Central.
DR GO; GO:0016579; P:protein deubiquitination; IBA:GO_Central.
DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IBA:GO_Central.
DR InterPro; IPR039138; OTU1_2_3.
DR InterPro; IPR003323; OTU_dom.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR PANTHER; PTHR13312; PTHR13312; 1.
DR Pfam; PF02338; OTU; 1.
DR SUPFAM; SSF54001; SSF54001; 1.
DR PROSITE; PS50802; OTU; 1.
PE 1: Evidence at protein level;
KW Hydrolase; Reference proteome; Ubl conjugation pathway.
FT CHAIN 1..234
FT /note="OVARIAN TUMOR DOMAIN-containing deubiquitinating
FT enzyme 3"
FT /id="PRO_0000447754"
FT DOMAIN 76..234
FT /note="OTU"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00139"
FT REGION 81..87
FT /note="Cys-loop"
FT /evidence="ECO:0000250|UniProtKB:Q9XIP2"
FT REGION 154..164
FT /note="Variable-loop"
FT /evidence="ECO:0000250|UniProtKB:Q9XIP2"
FT REGION 224..229
FT /note="His-loop"
FT /evidence="ECO:0000250|UniProtKB:Q9XIP2"
FT ACT_SITE 84
FT /evidence="ECO:0000255"
FT ACT_SITE 87
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q96G74"
FT ACT_SITE 229
FT /evidence="ECO:0000250|UniProtKB:Q96G74"
SQ SEQUENCE 234 AA; 26273 MW; 31E06C051886FE0F CRC64;
MELKSSSNNN ILEQLRNGFA RFELVSSPTA SVSDSISSTS LPASFISTTK GNSYVFFARI
NSSMNRSPAA KKVEKYAVDR VKGDGRCLFR ALVKGMAFNK GITLNPQRER DDADELRMAV
KEVICNDPKE REKYKEALVA ITVDESLKRF CQRIGRHDFW GGESELLVLS KLCKQPIIVY
IPEHEHGRGG GYGPGFIPIQ EYGSEFRGGW GKGKTNKNVV RLLYSGRNHY DLLR
