ID A0A096P979_OSTTA Unreviewed; 216 AA.
AC A0A096P979; A0A1Y5I763; A0A454Y3H9;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=Ubiquitin thioesterase OTU {ECO:0000256|RuleBase:RU367104};
DE EC=3.4.19.12 {ECO:0000256|RuleBase:RU367104};
GN ORFNames=BE221DRAFT_206442 {ECO:0000313|EMBL:OUS45399.1},
GN OT_ostta17g01310 {ECO:0000313|EMBL:CEG00573.1};
OS Ostreococcus tauri.
OC Eukaryota; Viridiplantae; Chlorophyta; Mamiellophyceae; Mamiellales;
OC Bathycoccaceae; Ostreococcus.
OX NCBI_TaxID=70448 {ECO:0000313|EMBL:CEG00573.1, ECO:0000313|Proteomes:UP000009170};
RN [1] {ECO:0000313|Proteomes:UP000009170}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OTTH0595 {ECO:0000313|Proteomes:UP000009170};
RX PubMed=16868079; DOI=10.1073/pnas.0604795103;
RA Derelle E., Ferraz C., Rombauts S., Rouze P., Worden A.Z., Robbens S.,
RA Partensky F., Degroeve S., Echeynie S., Cooke R., Saeys Y., Wuyts J.,
RA Jabbari K., Bowler C., Panaud O., Piegu B., Ball S.G., Ral J.-P.,
RA Bouget F.-Y., Piganeau G., De Baets B., Picard A., Delseny M., Demaille J.,
RA Van de Peer Y., Moreau H.;
RT "Genome analysis of the smallest free-living eukaryote Ostreococcus tauri
RT unveils many unique features.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:11647-11652(2006).
RN [2] {ECO:0000313|EMBL:CEG00573.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=RCC4221 {ECO:0000313|EMBL:CEG00573.1};
RA Derelle E., Ferraz C., Rombauts S., Rouze P., Worden A.Z., Robbens S.,
RA Partensky F., Degroeve S., Echeynie S., Cooke R., Saeys Y., Wuyts J.,
RA Jabbari K., Bowler C., Panaud O., Piegu B., Ball S., Ral J.P., Bouget F.Y.,
RA Piganeau G., De Baets B., Picard A., Delseny M., Demaille J.,
RA Van de Peer Y., Moreau H.;
RT "Genome analysis of the smallest free-living eukaryote Ostreococcus tauri
RT unveils many unique features.";
RL Proc. Natl. Acad. Sci. U.S.A. 131:11647-11652(2006).
RN [3] {ECO:0000313|EMBL:CEG00573.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=RCC4221 {ECO:0000313|EMBL:CEG00573.1};
RX PubMed=25494611; DOI=10.1186/1471-2164-15-1103;
RA Blanc-Mathieu R., Verhelst B., Derelle E., Rombauts S., Bouget F.Y.,
RA Carre I., Chateau A., Eyre-Walker A., Grimsley N., Moreau H., Piegu B.,
RA Rivals E., Schackwitz W., Van de Peer Y., Piganeau G.;
RT "An improved genome of the model marine alga Ostreococcus tauri unfolds by
RT assessing Illumina de novo assemblies.";
RL BMC Genomics 15:1103-1103(2014).
RN [4] {ECO:0000313|EMBL:OUS45399.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RCC 1115 {ECO:0000313|EMBL:OUS45399.1};
RG DOE Joint Genome Institute;
RA Blanc-Mathieu R., Krasovec M., Hebrard M., Yau S., Desgranges E.,
RA Martin J., Schackwitz W., Kuo A., Salin G., Donnadieu C., Desdevises Y.,
RA Sanchez-Ferandin S., Moreau H., Rivals E., Grigoriev I.V., Grimsley N.,
RA Eyre-Walker A., Piganeau G.;
RT "Population genomics of picophytoplankton unveils novel chromosome
RT hypervariability.";
RL Submitted (APR-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Hydrolase that can remove conjugated ubiquitin from proteins
CC and may therefore play an important regulatory role at the level of
CC protein turnover by preventing degradation.
CC {ECO:0000256|RuleBase:RU367104}.
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:0000256|RuleBase:RU367104};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU367104}.
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DR EMBL; CAID01000017; CEG00573.1; -; Genomic_DNA.
DR EMBL; KZ155790; OUS45399.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A096P979; -.
DR STRING; 70448.A0A096P979; -.
DR InParanoid; A0A096P979; -.
DR OrthoDB; 1201at2759; -.
DR Proteomes; UP000009170; Chromosome 17.
DR Proteomes; UP000195557; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd22759; OTU_plant_OTU3-like; 1.
DR Gene3D; 3.90.70.80; -; 1.
DR InterPro; IPR003323; OTU_dom.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR PANTHER; PTHR13312; HIV-INDUCED PROTEIN-7-LIKE PROTEASE; 1.
DR PANTHER; PTHR13312:SF3; OVARIAN TUMOR DOMAIN-CONTAINING DEUBIQUITINATING ENZYME 3; 1.
DR Pfam; PF02338; OTU; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR PROSITE; PS50802; OTU; 1.
PE 4: Predicted;
KW Cytoplasm {ECO:0000256|RuleBase:RU367104};
KW Hydrolase {ECO:0000256|RuleBase:RU367104};
KW Protease {ECO:0000313|EMBL:OUS45399.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000009170};
KW Thiol protease {ECO:0000256|RuleBase:RU367104};
KW Ubl conjugation pathway {ECO:0000256|RuleBase:RU367104}.
FT DOMAIN 65..216
FT /note="OTU"
FT /evidence="ECO:0000259|PROSITE:PS50802"
FT REGION 1..60
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..19
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 216 AA; 23857 MW; 9C5054B781B7AAE7 CRC64;
MSDGGRAQSA SSAARAAHSS VATNFPPPPL GRPRELAQVA KASAKSKKRT KSGTNKTPRR
KGEFYDVVRV RGDGRCMFRA LALALANVAG RVMTSGEEER EADELRLAVA ESLCRTPEKR
QDFSEAVMAI SYEQGLETYC RRILEPAFWG GEPELLVLSR LIKRPIMVYI HASQAKNAEG
HGFVAIQTYG EEFSKGGKRK PCRLLYNGEN HYDLLI
//
