OTU2_ARATH
ID OTU2_ARATH Reviewed; 208 AA.
AC Q9LPT6; A0A178W4L6;
DT 18-SEP-2019, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=OVARIAN TUMOR DOMAIN-containing deubiquitinating enzyme 2 {ECO:0000303|PubMed:24659992};
DE Short=OTU domain-containing protein 2 {ECO:0000303|PubMed:24659992};
DE EC=3.4.19.12 {ECO:0000269|PubMed:24659992};
DE AltName: Full=Deubiquitinating enzyme OTU2 {ECO:0000303|PubMed:24659992};
GN Name=OTU2 {ECO:0000303|PubMed:24659992};
GN OrderedLocusNames=At1g50670 {ECO:0000312|Araport:AT1G50670};
GN ORFNames=F17J6.19 {ECO:0000312|EMBL:AAG51183.1};
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, MUTAGENESIS OF CYS-63; CYS-99;
RP CYS-179 AND HIS-195, 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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(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;
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).
RN [5] {ECO:0007744|PubMed:22223895}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
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' and 'Lys-48' -linked
CC ubiquitin (UB) tetramers as substrates (PubMed:24659992).
CC {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 -!- INTERACTION:
CC Q9LPT6; O04492: DRB1; NbExp=3; IntAct=EBI-20796120, EBI-632620;
CC -!- SIMILARITY: Belongs to the peptidase C85 family. {ECO:0000305}.
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DR EMBL; JQ013443; AFS88946.1; -; mRNA.
DR EMBL; AC012561; AAF87868.1; -; Genomic_DNA.
DR EMBL; AC079279; AAG51183.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE32577.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM58781.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM58782.1; -; Genomic_DNA.
DR EMBL; BT002977; AAO22786.1; -; mRNA.
DR EMBL; BT004408; AAO42402.1; -; mRNA.
DR PIR; D96543; D96543.
DR RefSeq; NP_001321194.1; NM_001333447.1.
DR RefSeq; NP_001321195.1; NM_001333448.1.
DR RefSeq; NP_175482.1; NM_103949.4.
DR AlphaFoldDB; Q9LPT6; -.
DR SMR; Q9LPT6; -.
DR IntAct; Q9LPT6; 2.
DR STRING; 3702.AT1G50670.1; -.
DR iPTMnet; Q9LPT6; -.
DR PaxDb; Q9LPT6; -.
DR PRIDE; Q9LPT6; -.
DR ProteomicsDB; 185854; -.
DR DNASU; 841489; -.
DR EnsemblPlants; AT1G50670.1; AT1G50670.1; AT1G50670.
DR EnsemblPlants; AT1G50670.2; AT1G50670.2; AT1G50670.
DR EnsemblPlants; AT1G50670.3; AT1G50670.3; AT1G50670.
DR GeneID; 841489; -.
DR Gramene; AT1G50670.1; AT1G50670.1; AT1G50670.
DR Gramene; AT1G50670.2; AT1G50670.2; AT1G50670.
DR Gramene; AT1G50670.3; AT1G50670.3; AT1G50670.
DR KEGG; ath:AT1G50670; -.
DR Araport; AT1G50670; -.
DR TAIR; locus:2007991; AT1G50670.
DR eggNOG; KOG3288; Eukaryota.
DR HOGENOM; CLU_108141_1_0_1; -.
DR InParanoid; Q9LPT6; -.
DR OMA; NEEYCDW; -.
DR OrthoDB; 1327072at2759; -.
DR PhylomeDB; Q9LPT6; -.
DR PRO; PR:Q9LPT6; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9LPT6; baseline and differential.
DR GO; GO:0005634; C:nucleus; HDA:TAIR.
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; Protease; Reference proteome; Thiol protease;
KW Ubl conjugation pathway.
FT CHAIN 1..208
FT /note="OVARIAN TUMOR DOMAIN-containing deubiquitinating
FT enzyme 2"
FT /id="PRO_0000447753"
FT DOMAIN 5..127
FT /note="OTU"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00139"
FT ACT_SITE 13
FT /evidence="ECO:0000250|UniProtKB:Q96DC9"
FT ACT_SITE 16
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q96DC9"
FT ACT_SITE 120
FT /evidence="ECO:0000250|UniProtKB:Q96FW1"
FT ACT_SITE 201
FT /evidence="ECO:0000250|UniProtKB:Q96DC9"
FT MUTAGEN 63
FT /note="C->S: Reduced'Lys-48'- and 'Lys-63'-linked ubiquitin
FT (UB) chains. Abolished Lys-48- and Lys-63-linked UB chains;
FT when associated with S-99."
FT /evidence="ECO:0000269|PubMed:24659992"
FT MUTAGEN 99
FT /note="C->S: Reduced'Lys-48'- and 'Lys-63'-linked ubiquitin
FT (UB) chains. Abolished Lys-48- and Lys-63-linked UB chains;
FT when associated with S-63."
FT /evidence="ECO:0000269|PubMed:24659992"
FT MUTAGEN 179
FT /note="C->S: Normal ubiquitin (UB) binding. Abolished'Lys-
FT 48'- and 'Lys-63'-linked UB chains; when associated with R-
FT 195."
FT /evidence="ECO:0000269|PubMed:24659992"
FT MUTAGEN 195
FT /note="H->R: Normal ubiquitin (UB) binding. Abolished'Lys-
FT 48'- and 'Lys-63'-linked UB chains; when associated with S-
FT 179."
FT /evidence="ECO:0000269|PubMed:24659992"
SQ SEQUENCE 208 AA; 23425 MW; FE1640C393650EA3 CRC64;
MEGIIVRRVI PSDNSCLFNA IGYVMDKDKN KAPELRQVIA AAVASNKEKY NEAFLGKLNE
EYCAWILNPD KWGGAIELSI LADYYGREIA AYDIQTSRCD LYGQTRNYDE RVMLIYDGLH
YDALALSPFE GAEEDFDMTI YPVGKDRSIG SIEGLALNLV KDQQRKRSYT DTANFTLRCG
VCQIGVIGQK EAVEHAQATG HVNFQEYK
