OTU12_ARATH
ID OTU12_ARATH Reviewed; 219 AA.
AC Q9SGA5; A0A178VFU2; Q0WTB0;
DT 18-SEP-2019, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=OVARIAN TUMOR DOMAIN-containing deubiquitinating enzyme 12 {ECO:0000303|PubMed:24659992};
DE Short=OTU domain-containing protein 12 {ECO:0000303|PubMed:24659992};
DE EC=3.4.19.12 {ECO:0000250|UniProtKB:Q96G74};
DE AltName: Full=Deubiquitinating enzyme OTU12 {ECO:0000303|PubMed:24659992};
GN Name=OTU12 {ECO:0000303|PubMed:24659992};
GN OrderedLocusNames=At3g02070 {ECO:0000312|Araport:AT3G02070};
GN ORFNames=F1C9.14 {ECO:0000312|EMBL:AAF14829.1};
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, GENE FAMILY, AND
RP 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).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(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 Cheuk R.F., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=cv. Columbia; TISSUE=Rosette leaf;
RX PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA Shinozaki K.;
RT "Analysis of multiple occurrences of alternative splicing events in
RT Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL DNA Res. 16:155-164(2009).
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;
CC IsoId=Q9SGA5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9SGA5-2; Sequence=VSP_060268, VSP_060269;
CC -!- SIMILARITY: Belongs to the peptidase C85 family. {ECO:0000305}.
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DR EMBL; JQ013459; AFS88961.1; -; mRNA.
DR EMBL; AC011664; AAF14829.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE73759.1; -; Genomic_DNA.
DR EMBL; CP002686; ANM65420.1; -; Genomic_DNA.
DR EMBL; BT012213; AAS76700.1; -; mRNA.
DR EMBL; BT012408; AAS92324.1; -; mRNA.
DR EMBL; AK227651; BAE99638.1; -; mRNA.
DR EMBL; AK317486; BAH20151.1; -; mRNA.
DR RefSeq; NP_001319447.1; NM_001337380.1. [Q9SGA5-1]
DR RefSeq; NP_186856.1; NM_111073.4. [Q9SGA5-1]
DR AlphaFoldDB; Q9SGA5; -.
DR SMR; Q9SGA5; -.
DR STRING; 3702.AT3G02070.1; -.
DR MEROPS; C85.A02; -.
DR PaxDb; Q9SGA5; -.
DR PRIDE; Q9SGA5; -.
DR ProteomicsDB; 177414; -. [Q9SGA5-1]
DR DNASU; 821202; -.
DR EnsemblPlants; AT3G02070.1; AT3G02070.1; AT3G02070. [Q9SGA5-1]
DR EnsemblPlants; AT3G02070.2; AT3G02070.2; AT3G02070. [Q9SGA5-1]
DR GeneID; 821202; -.
DR Gramene; AT3G02070.1; AT3G02070.1; AT3G02070. [Q9SGA5-1]
DR Gramene; AT3G02070.2; AT3G02070.2; AT3G02070. [Q9SGA5-1]
DR KEGG; ath:AT3G02070; -.
DR Araport; AT3G02070; -.
DR TAIR; locus:2078648; AT3G02070.
DR eggNOG; KOG2605; Eukaryota.
DR HOGENOM; CLU_044001_2_1_1; -.
DR InParanoid; Q9SGA5; -.
DR OMA; EIMPQYQ; -.
DR OrthoDB; 1448656at2759; -.
DR PhylomeDB; Q9SGA5; -.
DR PRO; PR:Q9SGA5; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9SGA5; 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..219
FT /note="OVARIAN TUMOR DOMAIN-containing deubiquitinating
FT enzyme 12"
FT /id="PRO_0000447762"
FT DOMAIN 79..203
FT /note="OTU"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00139"
FT ACT_SITE 87
FT /evidence="ECO:0000255"
FT ACT_SITE 90
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q96G74"
FT ACT_SITE 196
FT /evidence="ECO:0000250|UniProtKB:Q96G74"
FT VAR_SEQ 92..97
FT /note="FRALSD -> VNGGYI (in isoform 2)"
FT /id="VSP_060268"
FT VAR_SEQ 98..219
FT /note="Missing (in isoform 2)"
FT /id="VSP_060269"
SQ SEQUENCE 219 AA; 25571 MW; A0E0E3275E894776 CRC64;
MGDSSSSTSW SSKKDTEDDR MIAFMLSEEY SKLDGAVGRR LSNLAPVPHV PRINCYIPNL
NDATLDHQRL LQRLNVYGLC ELKVSGDGNC QFRALSDQLY RSPEYHKQVR REVVKQLKEC
RSMYESYVPM KYKRYYKKMG KFGEWGDHIT LQAAADRFAA KICLLTSFRD TCFIEIIPQY
QAPKGVLWLS FWSEVHYNSL YDIQAAPVQH KPKRKHWLF
