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Database: UniProt
Entry: A0A0D3C8L3_BRAOL
LinkDB: A0A0D3C8L3_BRAOL
Original site: A0A0D3C8L3_BRAOL 
ID   A0A0D3C8L3_BRAOL        Unreviewed;       152 AA.
AC   A0A0D3C8L3;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   10-APR-2019, entry version 17.
DE   RecName: Full=Superoxide dismutase [Cu-Zn] {ECO:0000256|RuleBase:RU000393};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000393};
GN   Name=106344020 {ECO:0000313|EnsemblPlants:Bo5g009310.1};
OS   Brassica oleracea var. oleracea.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
OC   Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Brassiceae;
OC   Brassica.
OX   NCBI_TaxID=109376 {ECO:0000313|EnsemblPlants:Bo5g009310.1, ECO:0000313|Proteomes:UP000032141};
RN   [1] {ECO:0000313|EnsemblPlants:Bo5g009310.1, ECO:0000313|Proteomes:UP000032141}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=cv. TO1000 {ECO:0000313|Proteomes:UP000032141};
RX   PubMed=24916971; DOI=10.1186/gb-2014-15-6-r77;
RA   Parkin I.A., Koh C., Tang H., Robinson S.J., Kagale S., Clarke W.E.,
RA   Town C.D., Nixon J., Krishnakumar V., Bidwell S.L., Denoeud F.,
RA   Belcram H., Links M.G., Just J., Clarke C., Bender T., Huebert T.,
RA   Mason A.S., Pires J.C., Barker G., Moore J., Walley P.G., Manoli S.,
RA   Batley J., Edwards D., Nelson M.N., Wang X., Paterson A.H., King G.,
RA   Bancroft I., Chalhoub B., Sharpe A.G.;
RT   "Transcriptome and methylome profiling reveals relics of genome
RT   dominance in the mesopolyploid Brassica oleracea.";
RL   Genome Biol. 15:R77-R77(2014).
RN   [2] {ECO:0000313|EnsemblPlants:Bo5g009310.1}
RP   IDENTIFICATION.
RG   EnsemblPlants;
RL   Submitted (MAR-2015) to UniProtKB.
CC   -!- FUNCTION: Destroys radicals which are normally produced within the
CC       cells and which are toxic to biological systems.
CC       {ECO:0000256|RuleBase:RU000393}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 H(+) + 2 superoxide = H2O2 + O2; Xref=Rhea:RHEA:20696,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC         ChEBI:CHEBI:18421; EC=1.15.1.1;
CC         Evidence={ECO:0000256|RuleBase:RU000393};
CC   -!- COFACTOR:
CC       Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC         Evidence={ECO:0000256|RuleBase:RU000393};
CC       Note=Binds 1 copper ion per subunit.
CC       {ECO:0000256|RuleBase:RU000393};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|RuleBase:RU000393};
CC       Note=Binds 1 zinc ion per subunit.
CC       {ECO:0000256|RuleBase:RU000393};
CC   -!- SIMILARITY: Belongs to the Cu-Zn superoxide dismutase family.
CC       {ECO:0000256|RuleBase:RU000393}.
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DR   RefSeq; XP_013638847.1; XM_013783393.1.
DR   STRING; 3712.Bo5g009310.1; -.
DR   EnsemblPlants; Bo5g009310.1; Bo5g009310.1; Bo5g009310.
DR   GeneID; 106344020; -.
DR   Gramene; Bo5g009310.1; Bo5g009310.1; Bo5g009310.
DR   KEGG; boe:106344020; -.
DR   KO; K04565; -.
DR   OMA; FHAVANC; -.
DR   Proteomes; UP000032141; Chromosome C5.
DR   GO; GO:0005829; C:cytosol; IEA:EnsemblPlants.
DR   GO; GO:0005634; C:nucleus; IEA:EnsemblPlants.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004784; F:superoxide dismutase activity; IEA:UniProtKB-EC.
DR   GO; GO:0071280; P:cellular response to copper ion; IEA:EnsemblPlants.
DR   GO; GO:0071484; P:cellular response to light intensity; IEA:EnsemblPlants.
DR   GO; GO:0071457; P:cellular response to ozone; IEA:EnsemblPlants.
DR   GO; GO:0071472; P:cellular response to salt stress; IEA:EnsemblPlants.
DR   GO; GO:0071329; P:cellular response to sucrose stimulus; IEA:EnsemblPlants.
DR   GO; GO:0071493; P:cellular response to UV-B; IEA:EnsemblPlants.
DR   GO; GO:0042742; P:defense response to bacterium; IEA:EnsemblPlants.
DR   GO; GO:0035195; P:gene silencing by miRNA; IEA:EnsemblPlants.
DR   GO; GO:0010039; P:response to iron ion; IEA:EnsemblPlants.
DR   CDD; cd00305; Cu-Zn_Superoxide_Dismutase; 1.
DR   Gene3D; 2.60.40.200; -; 1.
DR   InterPro; IPR036423; SOD-like_Cu/Zn_dom_sf.
DR   InterPro; IPR024134; SOD_Cu/Zn_/chaperone.
DR   InterPro; IPR018152; SOD_Cu/Zn_BS.
DR   InterPro; IPR001424; SOD_Cu_Zn_dom.
DR   PANTHER; PTHR10003; PTHR10003; 1.
DR   Pfam; PF00080; Sod_Cu; 1.
DR   PRINTS; PR00068; CUZNDISMTASE.
DR   SUPFAM; SSF49329; SSF49329; 1.
DR   PROSITE; PS00087; SOD_CU_ZN_1; 1.
DR   PROSITE; PS00332; SOD_CU_ZN_2; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000032141};
KW   Copper {ECO:0000256|RuleBase:RU000393};
KW   Metal-binding {ECO:0000256|RuleBase:RU000393};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000393};
KW   Reference proteome {ECO:0000313|Proteomes:UP000032141};
KW   Zinc {ECO:0000256|RuleBase:RU000393}.
FT   DOMAIN       12    148       Sod_Cu. {ECO:0000259|Pfam:PF00080}.
SQ   SEQUENCE   152 AA;  15136 MW;  7FB807C36DCF101F CRC64;
     MGKGVAVLNS SEGVKGTIFF TQEGDGVTSV TGTVSGLKPG LHGFHVHALG DTTNGCMSTG
     PHFNPDGKQH GAPEDANRHA GDLGNIIVGD DGTATFTITD CQIPLSGPNS IVGRAVVVHA
     DPDDLGKGGH ELSLATGNAG GRVACGIIGL QG
//
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