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Database: UniProt
Entry: C0HEK6_MAIZE
LinkDB: C0HEK6_MAIZE
Original site: C0HEK6_MAIZE 
ID   C0HEK6_MAIZE            Unreviewed;       280 AA.
AC   C0HEK6;
DT   05-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   05-MAY-2009, sequence version 1.
DT   24-JAN-2024, entry version 44.
DE   RecName: Full=Ubiquitin thioesterase OTU {ECO:0000256|RuleBase:RU367104};
DE            EC=3.4.19.12 {ECO:0000256|RuleBase:RU367104};
GN   Name=100284472 {ECO:0000313|EnsemblPlants:Zm00001eb034890_P005};
OS   Zea mays (Maize).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC   Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX   NCBI_TaxID=4577 {ECO:0000313|EMBL:ACN25459.1};
RN   [1] {ECO:0000313|EMBL:ACN25459.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=B73 {ECO:0000313|EMBL:ACN25459.1};
RX   PubMed=19936069; DOI=10.1371/journal.pgen.1000740;
RA   Soderlund C., Descour A., Kudrna D., Bomhoff M., Boyd L., Currie J.,
RA   Angelova A., Collura K., Wissotski M., Ashley E., Morrow D., Fernandes J.,
RA   Walbot V., Yu Y.;
RT   "Sequencing, mapping, and analysis of 27,455 maize full-length cDNAs.";
RL   PLoS Genet. 5:E1000740-E1000740(2009).
RN   [2] {ECO:0000313|EnsemblPlants:Zm00001eb034890_P005, ECO:0000313|Proteomes:UP000007305}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. B73 {ECO:0000313|EnsemblPlants:Zm00001eb034890_P005,
RC   ECO:0000313|Proteomes:UP000007305};
RG   Maize Genome Sequencing Project;
RA   Ware D.;
RT   "Update maize B73 reference genome by single molecule sequencing
RT   technologies.";
RL   Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EnsemblPlants:Zm00001eb034890_P005}
RP   IDENTIFICATION.
RC   STRAIN=cv. B73 {ECO:0000313|EnsemblPlants:Zm00001eb034890_P005};
RG   EnsemblPlants;
RL   Submitted (MAY-2021) to UniProtKB.
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; BT060762; ACN25459.1; -; mRNA.
DR   AlphaFoldDB; C0HEK6; -.
DR   EnsemblPlants; Zm00001eb034890_T005; Zm00001eb034890_P005; Zm00001eb034890.
DR   Gramene; Zm00001eb034890_T005; Zm00001eb034890_P005; Zm00001eb034890.
DR   Proteomes; UP000007305; Chromosome 1.
DR   ExpressionAtlas; C0HEK6; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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:SF4; OTU DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF02338; OTU; 1.
DR   SUPFAM; SSF54001; Cysteine proteinases; 1.
DR   PROSITE; PS50802; OTU; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm {ECO:0000256|RuleBase:RU367104};
KW   Hydrolase {ECO:0000256|RuleBase:RU367104};
KW   Protease {ECO:0000256|RuleBase:RU367104};
KW   Proteomics identification {ECO:0007829|PeptideAtlas:C0HEK6};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007305};
KW   Thiol protease {ECO:0000256|RuleBase:RU367104};
KW   Ubl conjugation pathway {ECO:0000256|RuleBase:RU367104}.
FT   DOMAIN          133..271
FT                   /note="OTU"
FT                   /evidence="ECO:0000259|PROSITE:PS50802"
SQ   SEQUENCE   280 AA;  30972 MW;  E197C00CF16CFB6C CRC64;
     MASWKCSHSP SSPYLAKSGL VDSSLNRNVK SSQPQSIKYF VSLMGQQFRC GLSTREGSLS
     VKLDIPSHEK SRIGWNWKNM HQKIGGVAGG LCFGFSVTGV ASAEVPIIRV KDNAETSSSS
     TSSTHGKEVY TDYSVTGIPG DGRCLFRSVV HGACIRSGRP IPNEDLQRKL ADELRATVAD
     EFVKRRKETE WFVEGDFDTY VSHIREPHVW GGEPELFMAS HVLQMPITVY MRDEDAGGLI
     AIAEYGQQYG KEDPIQVLYH GFGHYDALQI PAKVGSKRKL
//
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