ID D7LVX1_ARALL Unreviewed; 313 AA.
AC D7LVX1;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE RecName: Full=Ubiquitin thioesterase OTU {ECO:0000256|RuleBase:RU367104};
DE EC=3.4.19.12 {ECO:0000256|RuleBase:RU367104};
GN ORFNames=ARALYDRAFT_486235 {ECO:0000313|EMBL:EFH52698.1};
OS Arabidopsis lyrata subsp. lyrata (Lyre-leaved rock-cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=81972 {ECO:0000313|Proteomes:UP000008694};
RN [1] {ECO:0000313|Proteomes:UP000008694}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. MN47 {ECO:0000313|Proteomes:UP000008694};
RX PubMed=21478890; DOI=10.1038/ng.807;
RA Hu T.T., Pattyn P., Bakker E.G., Cao J., Cheng J.-F., Clark R.M.,
RA Fahlgren N., Fawcett J.A., Grimwood J., Gundlach H., Haberer G.,
RA Hollister J.D., Ossowski S., Ottilar R.P., Salamov A.A., Schneeberger K.,
RA Spannagl M., Wang X., Yang L., Nasrallah M.E., Bergelson J.,
RA Carrington J.C., Gaut B.S., Schmutz J., Mayer K.F.X., Van de Peer Y.,
RA Grigoriev I.V., Nordborg M., Weigel D., Guo Y.-L.;
RT "The Arabidopsis lyrata genome sequence and the basis of rapid genome size
RT change.";
RL Nat. Genet. 43:476-481(2011).
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; GL348717; EFH52698.1; -; Genomic_DNA.
DR RefSeq; XP_002876439.1; XM_002876393.1.
DR AlphaFoldDB; D7LVX1; -.
DR STRING; 81972.D7LVX1; -.
DR EnsemblPlants; fgenesh2_kg.5__2227__AT3G57810.2; fgenesh2_kg.5__2227__AT3G57810.2; fgenesh2_kg.5__2227__AT3G57810.2.
DR Gramene; fgenesh2_kg.5__2227__AT3G57810.2; fgenesh2_kg.5__2227__AT3G57810.2; fgenesh2_kg.5__2227__AT3G57810.2.
DR eggNOG; KOG2606; Eukaryota.
DR HOGENOM; CLU_046927_0_0_1; -.
DR OrthoDB; 1125427at2759; -.
DR Proteomes; UP000008694; Unassembled WGS sequence.
DR GO; GO:0009507; C:chloroplast; IEA:EnsemblPlants.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-UniRule.
DR CDD; cd22760; OTU_plant_OTU4-like; 1.
DR Gene3D; 3.90.70.80; -; 1.
DR InterPro; IPR047947; OTU4_OTU.
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:SF5; UBIQUITIN THIOESTERASE OTU; 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:0000256|RuleBase:RU367104};
KW Reference proteome {ECO:0000313|Proteomes:UP000008694};
KW Thiol protease {ECO:0000256|RuleBase:RU367104};
KW Ubl conjugation pathway {ECO:0000256|RuleBase:RU367104}.
FT DOMAIN 164..302
FT /note="OTU"
FT /evidence="ECO:0000259|PROSITE:PS50802"
SQ SEQUENCE 313 AA; 35482 MW; 4FF7AB2762A9194E CRC64;
MMICYSPITT CSRNAINIKG HLGTHLYGVV AQGSYKFSCH SLLLGLSRRH YTGFRVSVSN
RPSSWHDKRL LINRSTVGPK EKLEVSFLSP DAKMKCSKIE SNMRNLYWYS RFAYTGVIVS
LLVCYSSTSQ SAYADASRDK DANNVHNHSS HGKFHNGKRV YTDYSIIGIP GDGRCLFRSV
AHGFCLRSGK LAPGEKMQRE LADELRTKVA DEFIKRRQET EWFVEGDFDS YVRQIREPHV
WGGEPELFIA SHVLQMPITV YMKDEKAGGL ISIAEYGQEY GKDDPIRVLY HGFGHYDALL
IHESKASIPK SKL
//
