OTU9_ARATH
ID OTU9_ARATH Reviewed; 345 AA.
AC Q8LBW2; Q9FYD6;
DT 18-SEP-2019, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=OVARIAN TUMOR DOMAIN-containing deubiquitinating enzyme 9 {ECO:0000303|PubMed:24659992};
DE Short=OTU domain-containing protein 9 {ECO:0000303|PubMed:24659992};
DE EC=3.4.19.12 {ECO:0000269|PubMed:24659992};
DE AltName: Full=Deubiquitinating enzyme OTU9 {ECO:0000303|PubMed:24659992};
GN Name=OTU9 {ECO:0000303|PubMed:24659992};
GN OrderedLocusNames=At5g04250 {ECO:0000312|Araport:AT5G04250};
GN ORFNames=F21E1.170 {ECO:0000312|EMBL:CAC05507.1},
GN T19N18.9 {ECO:0000312|EMBL:AED90718.1};
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], 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=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].
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 (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Shinn P., Chen H., Kim C.J., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 Cysteine protease with a preference for 'Lys-63' and 'Lys-48' -linked
CC ubiquitin (UB) tetramers as substrates (PubMed:24659992). Cleaves also
CC RUB-GST fusion (PubMed:24659992). {ECO:0000269|PubMed:24659992,
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: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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAC05507.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; JQ013455; AFS88957.1; -; mRNA.
DR EMBL; AL391716; CAC05507.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED90718.1; -; Genomic_DNA.
DR EMBL; CP002688; AED90719.1; -; Genomic_DNA.
DR EMBL; AK221616; BAD95211.1; -; mRNA.
DR EMBL; BT024878; ABD85149.1; -; mRNA.
DR EMBL; AY086961; AAM64524.1; -; mRNA.
DR RefSeq; NP_001119168.1; NM_001125696.1.
DR RefSeq; NP_568136.1; NM_120507.5.
DR AlphaFoldDB; Q8LBW2; -.
DR SMR; Q8LBW2; -.
DR STRING; 3702.AT5G04250.2; -.
DR MEROPS; C85.A03; -.
DR iPTMnet; Q8LBW2; -.
DR PaxDb; Q8LBW2; -.
DR PRIDE; Q8LBW2; -.
DR ProteomicsDB; 191835; -.
DR EnsemblPlants; AT5G04250.1; AT5G04250.1; AT5G04250.
DR EnsemblPlants; AT5G04250.2; AT5G04250.2; AT5G04250.
DR GeneID; 830304; -.
DR Gramene; AT5G04250.1; AT5G04250.1; AT5G04250.
DR Gramene; AT5G04250.2; AT5G04250.2; AT5G04250.
DR KEGG; ath:AT5G04250; -.
DR Araport; AT5G04250; -.
DR TAIR; locus:2146673; AT5G04250.
DR eggNOG; KOG2605; Eukaryota.
DR HOGENOM; CLU_044001_0_0_1; -.
DR InParanoid; Q8LBW2; -.
DR OMA; HNFVREQ; -.
DR OrthoDB; 1448656at2759; -.
DR PhylomeDB; Q8LBW2; -.
DR PRO; PR:Q8LBW2; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q8LBW2; 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 Hydrolase; Reference proteome; Ubl conjugation pathway.
FT CHAIN 1..345
FT /note="OVARIAN TUMOR DOMAIN-containing deubiquitinating
FT enzyme 9"
FT /id="PRO_0000447759"
FT DOMAIN 204..328
FT /note="OTU"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00139"
FT ACT_SITE 212
FT /evidence="ECO:0000255"
FT ACT_SITE 215
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q96G74"
FT ACT_SITE 321
FT /evidence="ECO:0000250|UniProtKB:Q96G74"
SQ SEQUENCE 345 AA; 39231 MW; EBFCCBCDC9ACC03F CRC64;
MGYEPDPDAL RWGLHDLEVC TLTNAGSCSS VTRYESGGGG TQGYVREGYN QPVTGYVDND
AVIAQFYQDE LSRVARAEAS GINSLSPTSV VAQDWPHPHQ GQENQGEAID ITQESDILHN
HNGNMEDKNV ARIRFEGGQS SPSRDDDSVC SVEIEEESWS EVGKRLNQMI PIAHVPKING
ELPSEDEQIS DHERLFQRLQ LYGLVENKIE GDGNCQFRSL SDQLYRSPEH HNFVREQVVN
QLAYNREIYE GYVPMAYNDY LKAMKRNGEW GDHVTLQAAA DLFGVRMFVI TSFKDTCYIE
ILPHFQKSNR LICLSFWAEV HYNSIYPEGE LPIPEGKKKK KYWVF
