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Database: UniProt/SWISS-PROT
Entry: SODC4_MAIZE SODC5_MAIZE
LinkDB: SODC4_MAIZE SODC5_MAIZE
Original site: SODC4_MAIZE SODC5_MAIZE 
ID   SODC4_MAIZE             Reviewed;         152 AA.
AC   P23345;
DT   01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   13-FEB-2019, entry version 129.
DE   RecName: Full=Superoxide dismutase [Cu-Zn] 4A;
DE            EC=1.15.1.1;
GN   Name=SODCC.3; Synonyms=SOD4A;
OS   Zea mays (Maize).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae;
OC   PACMAD clade; Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae;
OC   Zea.
OX   NCBI_TaxID=4577;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=2482436; DOI=10.1007/BF00261150;
RA   Cannon R.E., Scandalios J.G.;
RT   "Two cDNAs encode two nearly identical Cu/Zn superoxide dismutase
RT   proteins in maize.";
RL   Mol. Gen. Genet. 219:1-8(1989).
CC   -!- FUNCTION: Destroys radicals which are normally produced within the
CC       cells and which are toxic to biological systems.
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   -!- COFACTOR:
CC       Name=Cu cation; Xref=ChEBI:CHEBI:23378; Evidence={ECO:0000250};
CC       Note=Binds 1 copper ion per subunit. {ECO:0000250};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC   -!- SUBUNIT: Homodimer.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the Cu-Zn superoxide dismutase family.
CC       {ECO:0000305}.
DR   EMBL; X17564; -; NOT_ANNOTATED_CDS; mRNA.
DR   PIR; S07007; S07007.
DR   RefSeq; NP_001105704.1; NM_001112234.1.
DR   UniGene; Zm.17820; -.
DR   UniGene; Zm.84947; -.
DR   UniGene; Zm.91536; -.
DR   ProteinModelPortal; P23345; -.
DR   SMR; P23345; -.
DR   PRIDE; P23345; -.
DR   GeneID; 542722; -.
DR   KEGG; zma:542722; -.
DR   MaizeGDB; 47586; -.
DR   eggNOG; KOG0441; Eukaryota.
DR   eggNOG; COG2032; LUCA.
DR   HOGENOM; HOG000263447; -.
DR   KO; K04565; -.
DR   OrthoDB; 1574423at2759; -.
DR   Proteomes; UP000007305; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0005507; F:copper ion binding; IBA:GO_Central.
DR   GO; GO:0004784; F:superoxide dismutase activity; IBA:GO_Central.
DR   GO; GO:0016532; F:superoxide dismutase copper chaperone activity; IBA:GO_Central.
DR   GO; GO:0008270; F:zinc ion binding; IBA:GO_Central.
DR   GO; GO:0019430; P:removal of superoxide radicals; IBA:GO_Central.
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   2: Evidence at transcript level;
KW   Antioxidant; Complete proteome; Copper; Cytoplasm; Disulfide bond;
KW   Metal-binding; Oxidoreductase; Reference proteome; Zinc.
FT   INIT_MET      1      1       Removed. {ECO:0000250}.
FT   CHAIN         2    152       Superoxide dismutase [Cu-Zn] 4A.
FT                                /FTId=PRO_0000164142.
FT   METAL        45     45       Copper; catalytic. {ECO:0000250}.
FT   METAL        47     47       Copper; catalytic. {ECO:0000250}.
FT   METAL        62     62       Copper; catalytic. {ECO:0000250}.
FT   METAL        62     62       Zinc; structural. {ECO:0000250}.
FT   METAL        70     70       Zinc; structural. {ECO:0000250}.
FT   METAL        79     79       Zinc; structural. {ECO:0000250}.
FT   METAL        82     82       Zinc; structural. {ECO:0000250}.
FT   METAL       119    119       Copper; catalytic. {ECO:0000250}.
FT   DISULFID     56    145       {ECO:0000250}.
SQ   SEQUENCE   152 AA;  15115 MW;  C1BF02656CD84AF2 CRC64;
     MVKAVAVLGS SEGVKGTIFF TQEGDGPTTV TGSVSGLKPG LHGFHVHALG DTTNGCMSTG
     PHYNPASKEH GAPEDENRHA GDLGNVTAGA DGVANINVTD SQIPLTGPNS IIGRAVVVHA
     DPDDLGKGGH ELSKSTGNAG GRVACGIIGL QG
//
ID   SODC5_MAIZE             Reviewed;         152 AA.
AC   P23346;
DT   01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   16-JAN-2019, entry version 134.
DE   RecName: Full=Superoxide dismutase [Cu-Zn] 4AP;
DE            EC=1.15.1.1;
GN   Name=SODCC.2; Synonyms=SOD4AP;
OS   Zea mays (Maize).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae;
OC   PACMAD clade; Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae;
OC   Zea.
OX   NCBI_TaxID=4577;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=2482436; DOI=10.1007/BF00261150;
RA   Cannon R.E., Scandalios J.G.;
RT   "Two cDNAs encode two nearly identical Cu/Zn superoxide dismutase
RT   proteins in maize.";
RL   Mol. Gen. Genet. 219:1-8(1989).
CC   -!- FUNCTION: Destroys radicals which are normally produced within the
CC       cells and which are toxic to biological systems.
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   -!- COFACTOR:
CC       Name=Cu cation; Xref=ChEBI:CHEBI:23378; Evidence={ECO:0000250};
CC       Note=Binds 1 copper ion per subunit. {ECO:0000250};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC   -!- SUBUNIT: Homodimer.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the Cu-Zn superoxide dismutase family.
CC       {ECO:0000305}.
DR   EMBL; X17565; CAB57992.1; ALT_SEQ; mRNA.
DR   RefSeq; NP_001105704.1; NM_001112234.1.
DR   RefSeq; NP_001307761.1; NM_001320832.1.
DR   RefSeq; XP_008660153.1; XM_008661931.1.
DR   UniGene; Zm.17820; -.
DR   UniGene; Zm.84947; -.
DR   UniGene; Zm.91536; -.
DR   ProteinModelPortal; P23346; -.
DR   SMR; P23346; -.
DR   STRING; 4577.GRMZM2G058522_P01; -.
DR   PaxDb; P23346; -.
DR   PRIDE; P23346; -.
DR   EnsemblPlants; Zm00001d047479_T003; Zm00001d047479_P003; Zm00001d047479.
DR   EnsemblPlants; Zm00001d047479_T013; Zm00001d047479_P013; Zm00001d047479.
DR   EnsemblPlants; Zm00001d047479_T014; Zm00001d047479_P014; Zm00001d047479.
DR   EnsemblPlants; Zm00001d047479_T015; Zm00001d047479_P015; Zm00001d047479.
DR   EnsemblPlants; Zm00001d047479_T017; Zm00001d047479_P017; Zm00001d047479.
DR   GeneID; 103639134; -.
DR   GeneID; 542722; -.
DR   Gramene; Zm00001d047479_T003; Zm00001d047479_P003; Zm00001d047479.
DR   Gramene; Zm00001d047479_T013; Zm00001d047479_P013; Zm00001d047479.
DR   Gramene; Zm00001d047479_T014; Zm00001d047479_P014; Zm00001d047479.
DR   Gramene; Zm00001d047479_T015; Zm00001d047479_P015; Zm00001d047479.
DR   Gramene; Zm00001d047479_T017; Zm00001d047479_P017; Zm00001d047479.
DR   KEGG; zma:103639134; -.
DR   KEGG; zma:542722; -.
DR   MaizeGDB; 47586; -.
DR   eggNOG; KOG0441; Eukaryota.
DR   eggNOG; COG2032; LUCA.
DR   KO; K04565; -.
DR   OMA; HKGDIGN; -.
DR   OrthoDB; 1574423at2759; -.
DR   Proteomes; UP000007305; Chromosome 9.
DR   ExpressionAtlas; P23346; baseline and differential.
DR   Genevisible; P23346; ZM.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0005507; F:copper ion binding; IBA:GO_Central.
DR   GO; GO:0004784; F:superoxide dismutase activity; IBA:GO_Central.
DR   GO; GO:0016532; F:superoxide dismutase copper chaperone activity; IBA:GO_Central.
DR   GO; GO:0008270; F:zinc ion binding; IBA:GO_Central.
DR   GO; GO:0019430; P:removal of superoxide radicals; IBA:GO_Central.
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   2: Evidence at transcript level;
KW   Antioxidant; Complete proteome; Copper; Cytoplasm; Disulfide bond;
KW   Metal-binding; Oxidoreductase; Reference proteome; Zinc.
FT   INIT_MET      1      1       Removed. {ECO:0000250}.
FT   CHAIN         2    152       Superoxide dismutase [Cu-Zn] 4AP.
FT                                /FTId=PRO_0000164143.
FT   METAL        45     45       Copper; catalytic. {ECO:0000250}.
FT   METAL        47     47       Copper; catalytic. {ECO:0000250}.
FT   METAL        62     62       Copper; catalytic. {ECO:0000250}.
FT   METAL        62     62       Zinc; structural. {ECO:0000250}.
FT   METAL        70     70       Zinc; structural. {ECO:0000250}.
FT   METAL        79     79       Zinc; structural. {ECO:0000250}.
FT   METAL        82     82       Zinc; structural. {ECO:0000250}.
FT   METAL       119    119       Copper; catalytic. {ECO:0000250}.
FT   DISULFID     56    145       {ECO:0000250}.
SQ   SEQUENCE   152 AA;  15071 MW;  C1A373B76C533BB7 CRC64;
     MVKAVAVLGS SDGVKGTIFF TQEGDGPTAV TGSVSGLKPG LHGFHVHALG DTTNGCMSTG
     PHYNPASKEH GAPEDENRHA GDLGNVTAGA DGVANINVTD SQIPLTGPNS IIGRAVVVHA
     DPDDLGKGGH ELSKSTGNAG GRVACGIIGL QG
//
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