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 24-JAN-2024, entry version 133. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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.Q8LG98; -. DR MEROPS; C65.001; -. DR PaxDb; 3702-AT1G28120-1; -. 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; AT1G28120; OTU1. DR eggNOG; KOG3991; Eukaryota. DR HOGENOM; CLU_014832_3_0_1; -. DR InParanoid; Q8LG98; -. DR OMA; KQNDGNR; -. DR OrthoDB; 148019at2759; -. DR PhylomeDB; Q8LG98; -. DR PRO; PR:Q8LG98; -. DR Proteomes; UP000006548; Chromosome 1. DR ExpressionAtlas; Q8LG98; baseline and differential. DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IDA:TAIR. DR GO; GO:1990380; F:K48-linked deubiquitinase activity; IDA:TAIR. DR GO; GO:0061815; F:Met1-linked polyubiquitin deubiquitinase activity; IDA:TAIR. DR GO; GO:0071108; P:protein K48-linked deubiquitination; IDA:TAIR. DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW. DR CDD; cd22765; AtOTU1-like; 1. DR Gene3D; 3.30.200.60; Peptidase C65 Otubain, subdomain 1; 1. DR Gene3D; 1.20.1300.20; Peptidase C65 Otubain, subdomain 2; 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:SF15; UBIQUITIN THIOESTERASE OTUBAIN-LIKE; 1. DR PANTHER; PTHR12931; UBIQUITIN THIOLESTERASE PROTEIN OTUB; 1. DR Pfam; PF10275; Peptidase_C65; 1. DR PIRSF; PIRSF013503; Ubiquitin_thioesterase_Otubain; 1. DR SUPFAM; SSF54001; Cysteine proteinases; 1. DR PROSITE; PS50802; OTU; 1. DR Genevisible; Q8LG98; AT. 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 FT 'Lys-48'- and 'Lys-63'-linked ubiquitin (UB) tetramers and FT of linear UB polymer." FT /evidence="ECO:0000269|PubMed:24659992" FT MUTAGEN 92 FT /note="C->S: Abolished cleavage activities for FT 'Lys-48'- and 'Lys-63'-linked ubiquitin (UB) tetramers and FT of linear UB polymer." FT /evidence="ECO:0000269|PubMed:24659992" FT MUTAGEN 288 FT /note="H->R: Abolished cleavage activities for FT 'Lys-48'- and 'Lys-63'-linked ubiquitin (UB) tetramers and FT of 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 //