OTU10_ARATH
ID OTU10_ARATH Reviewed; 356 AA.
AC Q9LZF7; Q0WP26;
DT 18-SEP-2019, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=OVARIAN TUMOR DOMAIN-containing deubiquitinating enzyme 10 {ECO:0000303|PubMed:24659992};
DE Short=OTU domain-containing protein 10 {ECO:0000303|PubMed:24659992};
DE EC=3.4.19.12 {ECO:0000269|PubMed:24659992};
DE AltName: Full=Deubiquitinating enzyme OTU10 {ECO:0000303|PubMed:24659992};
GN Name=OTU10 {ECO:0000303|PubMed:24659992};
GN OrderedLocusNames=At5g03330 {ECO:0000312|Araport:AT5G03330};
GN ORFNames=F12E4.60 {ECO:0000312|EMBL:CAB83289.1};
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] (ISOFORM 1), FUNCTION, BIOPHYSICOCHEMICAL
RP PROPERTIES, 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=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(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 2).
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RA Bautista V.R., Kim C.J., Chen H., Wu S.Y., De Los Reyes C., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (JAN-2007) 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 Cysteine protease with a preference for 'Lys-63' over 'Lys-48' over
CC 'Met-1' -linked ubiquitin (UB) tetramers as substrates
CC (PubMed:24659992). Cleaves also RUB-GST fusion (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:0000269|PubMed:24659992};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 7. {ECO:0000269|PubMed:24659992};
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9LZF7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9LZF7-2; Sequence=VSP_060265, VSP_060266;
CC -!- SIMILARITY: Belongs to the peptidase C85 family. {ECO:0000305}.
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DR EMBL; JQ013456; AFS88958.1; -; mRNA.
DR EMBL; AL162751; CAB83289.1; -; Genomic_DNA.
DR EMBL; CP002688; AED90585.1; -; Genomic_DNA.
DR EMBL; CP002688; AED90586.1; -; Genomic_DNA.
DR EMBL; AK229259; BAF01123.1; -; mRNA.
DR EMBL; BT030018; ABN04756.1; -; mRNA.
DR PIR; T48354; T48354.
DR RefSeq; NP_195953.1; NM_120411.5. [Q9LZF7-1]
DR RefSeq; NP_974725.1; NM_202996.2. [Q9LZF7-1]
DR AlphaFoldDB; Q9LZF7; -.
DR SMR; Q9LZF7; -.
DR STRING; 3702.AT5G03330.1; -.
DR MEROPS; C85.A04; -.
DR iPTMnet; Q9LZF7; -.
DR PaxDb; Q9LZF7; -.
DR PRIDE; Q9LZF7; -.
DR ProteomicsDB; 174760; -. [Q9LZF7-1]
DR DNASU; 831875; -.
DR EnsemblPlants; AT5G03330.1; AT5G03330.1; AT5G03330. [Q9LZF7-1]
DR EnsemblPlants; AT5G03330.2; AT5G03330.2; AT5G03330. [Q9LZF7-1]
DR GeneID; 831875; -.
DR Gramene; AT5G03330.1; AT5G03330.1; AT5G03330. [Q9LZF7-1]
DR Gramene; AT5G03330.2; AT5G03330.2; AT5G03330. [Q9LZF7-1]
DR KEGG; ath:AT5G03330; -.
DR Araport; AT5G03330; -.
DR TAIR; locus:2142659; AT5G03330.
DR eggNOG; KOG2605; Eukaryota.
DR HOGENOM; CLU_044001_0_0_1; -.
DR InParanoid; Q9LZF7; -.
DR OMA; PAYDWHN; -.
DR OrthoDB; 1448656at2759; -.
DR PhylomeDB; Q9LZF7; -.
DR PRO; PR:Q9LZF7; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9LZF7; 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 1: Evidence at protein level;
KW Alternative splicing; Hydrolase; Reference proteome;
KW Ubl conjugation pathway.
FT CHAIN 1..356
FT /note="OVARIAN TUMOR DOMAIN-containing deubiquitinating
FT enzyme 10"
FT /id="PRO_0000447760"
FT DOMAIN 213..337
FT /note="OTU"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00139"
FT REGION 86..117
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 221
FT /evidence="ECO:0000255"
FT ACT_SITE 224
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q96G74"
FT ACT_SITE 330
FT /evidence="ECO:0000250|UniProtKB:Q96G74"
FT VAR_SEQ 208..223
FT /note="LEMFDFTEVKVPGDGN -> YLFLLILCFLSYINHS (in isoform 2)"
FT /id="VSP_060265"
FT VAR_SEQ 224..356
FT /note="Missing (in isoform 2)"
FT /id="VSP_060266"
SQ SEQUENCE 356 AA; 41689 MW; F949426A9CD3F45C CRC64;
MVSHEENTSI VEWFLGPHPY TYPPYGIEMI HEDDEVAVAH HHHHHQSGEY YREYEDHRSS
DVDNDEIIAR TLQDDFLQLE IAESNDYSHQ NQQQQHQQEG YTNNYSNNNN GYAWNDQSPA
VDYSSEWIGN DNDQDGRSDD SVNVFSCSSP SDTDEYVYSW ESDQCDADGE FGRRLNQMVP
IPYIPKINGE IPPEEEAVSD HERLRNRLEM FDFTEVKVPG DGNCQFRALA DQLYKTADRH
KHVRRQIVKQ LKSRPDSYQG YVPMDFSDYL RKMSRSGEWG DHVTLQAAAD AYRVKIVVLT
SFKDTCYIEI LPTSQESKGV IFLSFWAEVH YNAIYLNRDT SETELQRKRK WWRFGN
