OTU1_ARATH
ID OTU1_ARATH Reviewed; 306 AA.
AC Q8LG98; K9M9G0; Q9C7E1;
DT 01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2004, sequence version 2.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=OVARIAN TUMOR DOMAIN-containing deubiquitinating enzyme 1 {ECO:0000303|PubMed:24659992};
DE Short=OTU domain-containing protein 1 {ECO:0000303|PubMed:24659992};
DE EC=3.4.19.12 {ECO:0000269|PubMed:24659992};
DE AltName: Full=Deubiquitinating enzyme OTU1 {ECO:0000303|PubMed:24659992};
GN Name=OTU1 {ECO:0000303|PubMed:24659992}; OrderedLocusNames=At1g28120;
GN ORFNames=F13K9.21;
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 ASP-89; CYS-92 AND
RP HIS-288, ACTIVITY REGULATION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, GENE FAMILY, AND 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=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]
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 (PubMed:24659992).
CC Cysteine protease with a preference for Met-1 and 'Lys-48' over 'Lys-
CC 63'-linked ubiquitin (UB) tetramers (e.g. Ub2, Ub3 and Ub4) as
CC substrates (PubMed:24659992). {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 -!- ACTIVITY REGULATION: Cleavage activities for 'Lys-48'- and 'Lys-63'-
CC linked ubiquitin (UB) tetramers is inhibited by UB aldehyde and N-
CC ethylmaleimide but not by the metalloprotease inhibitors 1,10-
CC phenanthroline and EDTA, and the serine protease inhibitor
CC phenylmethylsulfonyl fluoride. {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 C65 family. {ECO:0000305}.
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DR EMBL; JQ013442; AFS88945.1; -; mRNA.
DR EMBL; AC069471; AAG51478.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE30920.1; -; Genomic_DNA.
DR EMBL; AY136373; AAM97039.1; -; mRNA.
DR EMBL; BT000164; AAN15483.1; -; mRNA.
DR EMBL; AY084389; AAM60966.1; -; mRNA.
DR PIR; A86407; A86407.
DR RefSeq; NP_564299.1; NM_102577.4.
DR AlphaFoldDB; Q8LG98; -.
DR SMR; Q8LG98; -.
DR BioGRID; 24940; 4.
DR IntAct; Q8LG98; 2.
DR STRING; 3702.AT1G28120.1; -.
DR MEROPS; C65.001; -.
DR PaxDb; Q8LG98; -.
DR PRIDE; Q8LG98; -.
DR ProteomicsDB; 226044; -.
DR EnsemblPlants; AT1G28120.1; AT1G28120.1; AT1G28120.
DR GeneID; 839705; -.
DR Gramene; AT1G28120.1; AT1G28120.1; AT1G28120.
DR KEGG; ath:AT1G28120; -.
DR Araport; AT1G28120; -.
DR TAIR; locus:2010469; AT1G28120.
DR eggNOG; KOG3991; Eukaryota.
DR HOGENOM; CLU_014832_3_0_1; -.
DR InParanoid; Q8LG98; -.
DR OMA; VRVRYMD; -.
DR OrthoDB; 1257066at2759; -.
DR PhylomeDB; Q8LG98; -.
DR PRO; PR:Q8LG98; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q8LG98; baseline and differential.
DR Genevisible; Q8LG98; AT.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IDA:TAIR.
DR GO; GO:1990380; F:Lys48-specific deubiquitinase activity; IDA:TAIR.
DR GO; GO:0061815; F:Met1-linked polyubiquitin deubiquitinase activity; IDA:TAIR.
DR GO; GO:0043130; F:ubiquitin binding; IBA:GO_Central.
DR GO; GO:0071108; P:protein K48-linked deubiquitination; IDA:TAIR.
DR Gene3D; 1.20.1300.20; -; 1.
DR Gene3D; 3.30.200.60; -; 1.
DR InterPro; IPR003323; OTU_dom.
DR InterPro; IPR016615; Otubain.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR019400; Peptidase_C65_otubain.
DR InterPro; IPR042468; Peptidase_C65_otubain_sub1.
DR InterPro; IPR042467; Peptidase_C65_otubain_sub2.
DR PANTHER; PTHR12931; PTHR12931; 1.
DR Pfam; PF10275; Peptidase_C65; 1.
DR PIRSF; PIRSF013503; Ubiquitin_thioesterase_Otubain; 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..306
FT /note="OVARIAN TUMOR DOMAIN-containing deubiquitinating
FT enzyme 1"
FT /id="PRO_0000221014"
FT DOMAIN 81..295
FT /note="OTU"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00139"
FT ACT_SITE 89
FT /evidence="ECO:0000250|UniProtKB:Q96DC9"
FT ACT_SITE 92
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q96DC9"
FT ACT_SITE 259
FT /evidence="ECO:0000250|UniProtKB:Q96FW1"
FT ACT_SITE 288
FT /evidence="ECO:0000250|UniProtKB:Q96DC9"
FT MUTAGEN 89
FT /note="D->E: Abolished cleavage activities for 'Lys-
FT 48'- and 'Lys-63'-linked ubiquitin (UB) tetramers and of
FT linear UB polymer."
FT /evidence="ECO:0000269|PubMed:24659992"
FT MUTAGEN 92
FT /note="C->S: Abolished cleavage activities for 'Lys-
FT 48'- and 'Lys-63'-linked ubiquitin (UB) tetramers and of
FT linear UB polymer."
FT /evidence="ECO:0000269|PubMed:24659992"
FT MUTAGEN 288
FT /note="H->R: Abolished cleavage activities for 'Lys-
FT 48'- and 'Lys-63'-linked ubiquitin (UB) tetramers and of
FT linear UB polymer."
FT /evidence="ECO:0000269|PubMed:24659992"
FT CONFLICT 5
FT /note="I -> N (in Ref. 5; AAM60966)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 306 AA; 34434 MW; 7D8822E69806AC87 CRC64;
MQNQIDMVKD EAEVAASISA IKGEEWGNCS SVEDQPSFQE EEAAKVPYVG DKEPLSSLAA
EYQSGSPILL EKIKILDSQY IGIRRTRGDG NCFFRSFMFS YLEHILESQD RAEVDRIKVN
VEKCRKTLQN LGYTDFTFED FFALFLEQLD DILQGTEESI SYDELVNRSR DQSVSDYIVM
FFRFVTAGDI RTRADFFEPF ITGLSNATVD QFCKSSVEPM GEESDHIHIT ALSDALGVAI
RVVYLDRSSC DSGGVTVNHH DFVPVGITNE KDEEASAPFI TLLYRPGHYD ILYPKPSCKV
SDNVGK
