ID SODC2_MAIZE Reviewed; 151 AA. AC P11428; DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 27-MAR-2024, entry version 157. DE RecName: Full=Superoxide dismutase [Cu-Zn] 2; DE EC=1.15.1.1; GN Name=SODCC.1; Synonyms=SOD2; 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; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=3467349; DOI=10.1073/pnas.84.1.179; RA Cannon R.E., White J.A., Scandalios J.G.; RT "Cloning of cDNA for maize superoxide dismutase 2 (SOD2)."; RL Proc. Natl. Acad. Sci. U.S.A. 84:179-183(1987). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=3597043; RA Cannon R.E., Scandalios J.G.; RT "The superoxide dismutase-2 gene of maize."; RL Isozymes Curr. Top. Biol. Med. Res. 14:73-81(1987). 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; M15175; AAA33511.1; -; mRNA. DR EMBL; M54936; AAA33510.1; -; mRNA. DR PIR; A29077; A29077. DR RefSeq; NP_001105335.1; NM_001111865.1. DR RefSeq; XP_008651856.1; XM_008653634.1. DR AlphaFoldDB; P11428; -. DR SMR; P11428; -. DR STRING; 4577.P11428; -. DR PaxDb; 4577-GRMZM2G025992_P01; -. DR EnsemblPlants; Zm00001eb330020_T001; Zm00001eb330020_P001; Zm00001eb330020. DR EnsemblPlants; Zm00001eb330020_T004; Zm00001eb330020_P004; Zm00001eb330020. DR EnsemblPlants; Zm00001eb330020_T006; Zm00001eb330020_P006; Zm00001eb330020. DR GeneID; 542260; -. DR Gramene; Zm00001eb330020_T001; Zm00001eb330020_P001; Zm00001eb330020. DR Gramene; Zm00001eb330020_T004; Zm00001eb330020_P004; Zm00001eb330020. DR Gramene; Zm00001eb330020_T006; Zm00001eb330020_P006; Zm00001eb330020. DR KEGG; zma:542260; -. DR MaizeGDB; 47586; -. DR eggNOG; KOG0441; Eukaryota. DR HOGENOM; CLU_056632_4_1_1; -. DR InParanoid; P11428; -. DR OMA; DNYSDNP; -. DR OrthoDB; 3470597at2759; -. DR Proteomes; UP000007305; Chromosome 7. DR ExpressionAtlas; P11428; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. 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:0019430; P:removal of superoxide radicals; IBA:GO_Central. DR CDD; cd00305; Cu-Zn_Superoxide_Dismutase; 1. DR Gene3D; 2.60.40.200; Superoxide dismutase, copper/zinc binding domain; 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:SF83; SUPEROXIDE DISMUTASE [CU-ZN] 2; 1. DR PANTHER; PTHR10003; SUPEROXIDE DISMUTASE CU-ZN -RELATED; 1. DR Pfam; PF00080; Sod_Cu; 1. DR PRINTS; PR00068; CUZNDISMTASE. DR SUPFAM; SSF49329; Cu,Zn superoxide dismutase-like; 1. DR PROSITE; PS00087; SOD_CU_ZN_1; 1. DR PROSITE; PS00332; SOD_CU_ZN_2; 1. DR Genevisible; P11428; ZM. PE 2: Evidence at transcript level; KW Antioxidant; Copper; Cytoplasm; Disulfide bond; Metal-binding; KW Oxidoreductase; Reference proteome; Zinc. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000250" FT CHAIN 2..151 FT /note="Superoxide dismutase [Cu-Zn] 2" FT /id="PRO_0000164141" FT BINDING 44 FT /ligand="Cu cation" FT /ligand_id="ChEBI:CHEBI:23378" FT /ligand_note="catalytic" FT /evidence="ECO:0000250" FT BINDING 46 FT /ligand="Cu cation" FT /ligand_id="ChEBI:CHEBI:23378" FT /ligand_note="catalytic" FT /evidence="ECO:0000250" FT BINDING 61 FT /ligand="Cu cation" FT /ligand_id="ChEBI:CHEBI:23378" FT /ligand_note="catalytic" FT /evidence="ECO:0000250" FT BINDING 61 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="structural" FT /evidence="ECO:0000250" FT BINDING 69 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="structural" FT /evidence="ECO:0000250" FT BINDING 78 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="structural" FT /evidence="ECO:0000250" FT BINDING 81 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="structural" FT /evidence="ECO:0000250" FT BINDING 118 FT /ligand="Cu cation" FT /ligand_id="ChEBI:CHEBI:23378" FT /ligand_note="catalytic" FT /evidence="ECO:0000250" FT DISULFID 55..144 FT /evidence="ECO:0000250" SQ SEQUENCE 151 AA; 15104 MW; 6B1E8C703B17D216 CRC64; MVKAVAVLAG TDVKGTIFFS QEGDGPTTVT GSISGLKPGL HGFHVHALGD TTNGCMSTGP HFNPVGKEHG APEDEDRHAG DLGNVTAGED GVVNVNITDS QIPLAGPHSI IGRAVVVHAD PDDLGKGGHE LSKSTGNAGG RVACGIIGLQ G //