ID SODCP_ORYSJ Reviewed; 211 AA.
AC P93407; Q0J3N7; Q6YYW6; Q76MX3;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 27-MAR-2024, entry version 156.
DE RecName: Full=Superoxide dismutase [Cu-Zn], chloroplastic;
DE EC=1.15.1.1;
DE Flags: Precursor;
GN Name=SODCP; OrderedLocusNames=Os08g0561700, LOC_Os08g44770;
GN ORFNames=P0543D10.3, P0604E01.43;
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Nipponbare; TISSUE=Leaf;
RX PubMed=9057336; DOI=10.1093/oxfordjournals.pcp.a029086;
RA Kaminaka H., Morita S., Yokoi H., Masumura T., Tanaka K.;
RT "Molecular cloning and characterization of a cDNA for plastidic
RT copper/zinc-superoxide dismutase in rice (Oryza sativa L.).";
RL Plant Cell Physiol. 38:65-69(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RA Kaminaka H., Morita S., Tokumoto M., Tanaka K.;
RT "Gene cloning of rice plastidic copper/zinc-superoxide dismutase.";
RL Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [5]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12869764; DOI=10.1126/science.1081288;
RG The rice full-length cDNA consortium;
RT "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT japonica rice.";
RL Science 301:376-379(2003).
RN [7]
RP PROTEIN SEQUENCE OF 58-67.
RC STRAIN=cv. Nipponbare; TISSUE=Leaf, Panicle, and Sheath;
RX PubMed=14681440; DOI=10.1093/nar/gkh020;
RA Komatsu S., Kojima K., Suzuki K., Ozaki K., Higo K.;
RT "Rice proteome database based on two-dimensional polyacrylamide gel
RT electrophoresis: its status in 2003.";
RL Nucleic Acids Res. 32:D388-D392(2004).
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: Homotetramer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC -!- SIMILARITY: Belongs to the Cu-Zn superoxide dismutase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD09607.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAD13222.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; D85239; BAA12745.1; -; mRNA.
DR EMBL; AB026724; BAB21760.1; -; Genomic_DNA.
DR EMBL; AP004587; BAD09607.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AP005544; BAD13222.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AP008214; BAF24428.1; -; Genomic_DNA.
DR EMBL; AP014964; BAT06708.1; -; Genomic_DNA.
DR EMBL; AK059841; BAG87162.1; -; mRNA.
DR EMBL; AK068627; BAG90999.1; -; mRNA.
DR EMBL; AK104013; BAG96371.1; -; mRNA.
DR PIR; T03685; T03685.
DR RefSeq; XP_015649518.1; XM_015794032.1.
DR AlphaFoldDB; P93407; -.
DR SMR; P93407; -.
DR STRING; 39947.P93407; -.
DR PaxDb; 39947-P93407; -.
DR EnsemblPlants; Os08t0561700-01; Os08t0561700-01; Os08g0561700.
DR GeneID; 4346329; -.
DR Gramene; Os08t0561700-01; Os08t0561700-01; Os08g0561700.
DR KEGG; osa:4346329; -.
DR eggNOG; KOG0441; Eukaryota.
DR HOGENOM; CLU_056632_1_0_1; -.
DR InParanoid; P93407; -.
DR OMA; AAHTLML; -.
DR OrthoDB; 3470597at2759; -.
DR PlantReactome; R-OSA-1119403; Removal of superoxide radicals.
DR Proteomes; UP000000763; Chromosome 8.
DR Proteomes; UP000059680; Chromosome 8.
DR Genevisible; P93407; OS.
DR GO; GO:0009507; C:chloroplast; 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:SF103; SUPEROXIDE DISMUTASE [CU-ZN]; 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.
PE 1: Evidence at protein level;
KW Antioxidant; Chloroplast; Copper; Direct protein sequencing;
KW Disulfide bond; Metal-binding; Oxidoreductase; Plastid; Reference proteome;
KW Transit peptide; Zinc.
FT TRANSIT 1..57
FT /note="Chloroplast"
FT /evidence="ECO:0000269|PubMed:14681440"
FT CHAIN 58..211
FT /note="Superoxide dismutase [Cu-Zn], chloroplastic"
FT /id="PRO_0000032847"
FT BINDING 103
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 105
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 120
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 120
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000250"
FT BINDING 128
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000250"
FT BINDING 137
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000250"
FT BINDING 140
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000250"
FT BINDING 177
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT DISULFID 114..203
FT /evidence="ECO:0000250"
SQ SEQUENCE 211 AA; 21301 MW; E9F073F8D4AFC9F7 CRC64;
MQAILAAAMA AQTLLFSATA PPASLFQSPS SARPFHSLRL AAGPAGAAAA RALVVADATK
KAVAVLKGTS QVEGVVTLTQ DDQGPTTVNV RVTGLTPGLH GFHLHEFGDT TNGCISTGPH
FNPNNLTHGA PEDEVRHAGD LGNIVANAEG VAEATIVDKQ IPLSGPNSVV GRAFVVHELE
DDLGKGGHEL SLSTGNAGGR LACGVVGLTP L
//
