ID A0A067F243_CITSI Unreviewed; 370 AA.
AC A0A067F243;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Ubiquitin thioesterase OTU {ECO:0000256|RuleBase:RU367104};
DE EC=3.4.19.12 {ECO:0000256|RuleBase:RU367104};
GN ORFNames=CISIN_1g017519mg {ECO:0000313|EMBL:KDO57256.1};
OS Citrus sinensis (Sweet orange) (Citrus aurantium var. sinensis).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Sapindales; Rutaceae; Aurantioideae; Citrus.
OX NCBI_TaxID=2711 {ECO:0000313|EMBL:KDO57256.1, ECO:0000313|Proteomes:UP000027120};
RN [1] {ECO:0000313|EMBL:KDO57256.1, ECO:0000313|Proteomes:UP000027120}
RP NUCLEOTIDE SEQUENCE.
RG International Citrus Genome Consortium;
RA Gmitter F., Chen C., Farmerie W., Harkins T., Desany B., Mohiuddin M.,
RA Kodira C., Borodovsky M., Lomsadze A., Burns P., Jenkins J., Prochnik S.,
RA Shu S., Chapman J., Pitluck S., Schmutz J., Rokhsar D.;
RL Submitted (APR-2014) 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; KK784964; KDO57256.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A067F243; -.
DR STRING; 2711.A0A067F243; -.
DR Proteomes; UP000027120; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IBA:GO_Central.
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:UP000027120};
KW Signal {ECO:0000256|SAM:SignalP};
KW Thiol protease {ECO:0000256|RuleBase:RU367104};
KW Ubl conjugation pathway {ECO:0000256|RuleBase:RU367104}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..370
FT /note="Ubiquitin thioesterase OTU"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001636804"
FT DOMAIN 223..361
FT /note="OTU"
FT /evidence="ECO:0000259|PROSITE:PS50802"
SQ SEQUENCE 370 AA; 40539 MW; 8A3C1DB9E5D23D56 CRC64;
MFNRFLVIFS VFYLLLLAVV AGDIDGYANM IVSTSICACA KNVVNLGGRF QGQMGGNICG
VTYRGPSSSC CFYLCSGQSK KNYAGISRTI SSSSLNVLQP FQATCFSPGL TKPRCNLRPL
TIRSFIGSRG SQKRHIEISL ACRSMKMRLL VPSQGVLPKL KLNAGPIDWP KGCASAGLIC
GLLVCYSSSK AHAEAADEKE DGEEDYDLSN VKYSHGKKVY TDYSVIGIPG DGRCLFRAVA
HGACLRAGKP APSVSIQREL ADDLRAKVAD EFIKRREETE WFIEGDFDLY VSQIRKPHVW
GGEPELLMAS HVLRMPITVY MHDKDAGGLI SIAEYGQEYG KEKPIRVLYH GFGHYDALQN
LGHEGGISKL
//
