OTU11_ARATH
ID OTU11_ARATH Reviewed; 245 AA.
AC Q0V869; A0A178VDZ2; A0A178VG73; F4J076; Q8LF73; Q9LHJ1;
DT 18-SEP-2019, integrated into UniProtKB/Swiss-Prot.
DT 03-MAY-2011, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=OVARIAN TUMOR DOMAIN-containing deubiquitinating enzyme 11 {ECO:0000303|PubMed:24659992};
DE Short=OTU domain-containing protein 11 {ECO:0000303|PubMed:24659992};
DE EC=3.4.19.12 {ECO:0000250|UniProtKB:Q96G74};
DE AltName: Full=Deubiquitinating enzyme OTU11 {ECO:0000303|PubMed:24659992};
GN Name=OTU11 {ECO:0000303|PubMed:24659992};
GN OrderedLocusNames=At3g22260 {ECO:0000312|Araport:AT3G22260};
GN ORFNames=MMP21.4 {ECO:0000312|EMBL:BAB01944.1};
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 [MRNA] (ISOFORMS 1 AND 2), FUNCTION, GENE FAMILY, AND
RP 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=10907853; DOI=10.1093/dnares/7.3.217;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence
RT features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC
RT clones.";
RL DNA Res. 7:217-221(2000).
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] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RA Bautista V.R., Kim C.J., Chen H., Quinitio C., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
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 (Probable).
CC Inactive cysteine protease (PubMed:24659992).
CC {ECO:0000269|PubMed:24659992, 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:Q96G74};
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=OTU11a {ECO:0000303|PubMed:24659992};
CC IsoId=Q0V869-1; Sequence=Displayed;
CC Name=2; Synonyms=OTU11b {ECO:0000303|PubMed:24659992};
CC IsoId=Q0V869-2; Sequence=VSP_060267;
CC -!- SIMILARITY: Belongs to the peptidase C85 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB01944.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; JQ013457; AFS88959.1; -; mRNA.
DR EMBL; JQ013458; AFS88960.1; -; mRNA.
DR EMBL; AP002046; BAB01944.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE76613.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE76614.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE76615.1; -; Genomic_DNA.
DR EMBL; CP002686; ANM64660.1; -; Genomic_DNA.
DR EMBL; CP002686; ANM64661.1; -; Genomic_DNA.
DR EMBL; CP002686; ANM64662.1; -; Genomic_DNA.
DR EMBL; BT026351; ABH04458.1; -; mRNA.
DR EMBL; AY085012; AAM61570.1; -; mRNA.
DR RefSeq; NP_001189948.1; NM_001203019.2. [Q0V869-1]
DR RefSeq; NP_001326673.1; NM_001338577.1. [Q0V869-1]
DR RefSeq; NP_001326674.1; NM_001338575.1. [Q0V869-1]
DR RefSeq; NP_001326675.1; NM_001338576.1. [Q0V869-1]
DR RefSeq; NP_566704.1; NM_113124.3. [Q0V869-2]
DR RefSeq; NP_974352.1; NM_202623.4. [Q0V869-1]
DR AlphaFoldDB; Q0V869; -.
DR SMR; Q0V869; -.
DR IntAct; Q0V869; 4.
DR STRING; 3702.AT3G22260.2; -.
DR MEROPS; C85.A01; -.
DR iPTMnet; Q0V869; -.
DR PaxDb; Q0V869; -.
DR PRIDE; Q0V869; -.
DR ProteomicsDB; 183018; -.
DR ProteomicsDB; 185679; -. [Q0V869-1]
DR EnsemblPlants; AT3G22260.1; AT3G22260.1; AT3G22260. [Q0V869-2]
DR EnsemblPlants; AT3G22260.2; AT3G22260.2; AT3G22260. [Q0V869-1]
DR EnsemblPlants; AT3G22260.3; AT3G22260.3; AT3G22260. [Q0V869-1]
DR EnsemblPlants; AT3G22260.4; AT3G22260.4; AT3G22260. [Q0V869-1]
DR EnsemblPlants; AT3G22260.5; AT3G22260.5; AT3G22260. [Q0V869-1]
DR EnsemblPlants; AT3G22260.6; AT3G22260.6; AT3G22260. [Q0V869-1]
DR GeneID; 821796; -.
DR Gramene; AT3G22260.1; AT3G22260.1; AT3G22260. [Q0V869-2]
DR Gramene; AT3G22260.2; AT3G22260.2; AT3G22260. [Q0V869-1]
DR Gramene; AT3G22260.3; AT3G22260.3; AT3G22260. [Q0V869-1]
DR Gramene; AT3G22260.4; AT3G22260.4; AT3G22260. [Q0V869-1]
DR Gramene; AT3G22260.5; AT3G22260.5; AT3G22260. [Q0V869-1]
DR Gramene; AT3G22260.6; AT3G22260.6; AT3G22260. [Q0V869-1]
DR KEGG; ath:AT3G22260; -.
DR Araport; AT3G22260; -.
DR TAIR; locus:2091633; AT3G22260.
DR eggNOG; KOG2605; Eukaryota.
DR HOGENOM; CLU_044001_2_1_1; -.
DR InParanoid; Q0V869; -.
DR OMA; YYGNSRA; -.
DR OrthoDB; 1448656at2759; -.
DR PhylomeDB; Q0V869; -.
DR PRO; PR:Q0V869; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q0V869; baseline and differential.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IBA:GO_Central.
DR GO; GO:0016579; P:protein deubiquitination; IBA:GO_Central.
DR InterPro; IPR003323; OTU_dom.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR Pfam; PF02338; OTU; 1.
DR SUPFAM; SSF54001; SSF54001; 1.
DR PROSITE; PS50802; OTU; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Hydrolase; Reference proteome;
KW Ubl conjugation pathway.
FT CHAIN 1..245
FT /note="OVARIAN TUMOR DOMAIN-containing deubiquitinating
FT enzyme 11"
FT /id="PRO_0000447761"
FT DOMAIN 101..225
FT /note="OTU"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00139"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 7..37
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 109
FT /evidence="ECO:0000255"
FT ACT_SITE 112
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q96G74"
FT ACT_SITE 218
FT /evidence="ECO:0000250|UniProtKB:Q96G74"
FT VAR_SEQ 227..231
FT /note="Missing (in isoform 2)"
FT /id="VSP_060267"
FT CONFLICT 84
FT /note="D -> N (in Ref. 5; AAM61570)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 245 AA; 28228 MW; 49628606281EC0EE CRC64;
MDENHRNPFA NASTSARASG STSASSNSSF SSSVADTDDD QTIARILAED ESLRREGKLG
KRLSHLDSIP HTPRVNREIP DINDATLDHE LLSGRLATYG LAELQMEGDG NCQFRALADQ
LFRNADYHKH VRKHVVKQLK QQRKLYEEYV PMKYRHYTRK MKKHGEWGDH VTLQAAADRF
EAKICLVTSF RDQSYIEILP HNKNPLREAW LSFWSEVHYN SLYANGVLAL PDVPTRKPRR
KHWLF
