ID   SODC2_ORYSJ             Reviewed;         152 AA.
AC   P28757; A0A0N7KP08; Q0D3U5; Q8LIB7;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   27-MAR-2024, entry version 160.
DE   RecName: Full=Superoxide dismutase [Cu-Zn] 2;
DE            EC=1.15.1.1;
GN   Name=SODCC2; Synonyms=SODCC.2;
GN   OrderedLocusNames=Os07g0665200, LOC_Os07g46990;
GN   ORFNames=OJ1343_D04.132, P0450A04.103;
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=Seed;
RX   PubMed=1623183; DOI=10.1007/bf00027355;
RA   Sakamoto A., Ohsuga H., Tanaka K.;
RT   "Nucleotide sequences of two cDNA clones encoding different Cu/Zn-
RT   superoxide dismutases expressed in developing rice seed (Oryza sativa
RT   L.).";
RL   Plant Mol. Biol. 19:323-327(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=1568478; DOI=10.1016/0014-5793(92)81244-g;
RA   Sakamoto A., Okumura T., Ohsuga H., Tanaka K.;
RT   "Genomic structure of the gene for copper/zinc-superoxide dismutase in
RT   rice.";
RL   FEBS Lett. 301:185-189(1992).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Wuyujing 3;
RA   Lu L.M., Qin M.L., Lan H.H., Wang P., Niu X.Q., Wu Z.J., Xie L.H.;
RT   "Construction and characterization of a yeast two-hybrid cDNA library from
RT   rice seedling leaves.";
RL   Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases.
RN   [4]
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   [5]
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   [6]
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   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Nipponbare;
RG   The rice full-length cDNA consortium;
RT   "Oryza sativa full length cDNA.";
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN   [8]
RP   PROTEIN SEQUENCE OF 2-11.
RC   STRAIN=cv. Nipponbare; TISSUE=Panicle, and Root;
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: Homodimer.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the Cu-Zn superoxide dismutase family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC10110.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=BAD30565.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=BAT03098.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; D01000; BAA00800.1; -; mRNA.
DR   EMBL; L19434; AAC14465.1; -; Genomic_DNA.
DR   EMBL; EU325984; ABY52933.1; -; mRNA.
DR   EMBL; AP003825; BAC10110.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AP004274; BAD30565.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AP008213; BAF22478.1; -; Genomic_DNA.
DR   EMBL; AP014963; BAT03098.1; ALT_INIT; Genomic_DNA.
DR   EMBL; AK243377; BAH01571.1; -; mRNA.
DR   PIR; S21136; S21136.
DR   RefSeq; XP_015647771.1; XM_015792285.1.
DR   AlphaFoldDB; P28757; -.
DR   SMR; P28757; -.
DR   STRING; 39947.P28757; -.
DR   PaxDb; 39947-P28757; -.
DR   EnsemblPlants; Os07t0665200-01; Os07t0665200-01; Os07g0665200.
DR   GeneID; 4344210; -.
DR   Gramene; Os07t0665200-01; Os07t0665200-01; Os07g0665200.
DR   KEGG; osa:4344210; -.
DR   eggNOG; KOG0441; Eukaryota.
DR   HOGENOM; CLU_056632_4_1_1; -.
DR   InParanoid; P28757; -.
DR   OMA; DNYSDNP; -.
DR   OrthoDB; 3470597at2759; -.
DR   PlantReactome; R-OSA-1119403; Removal of superoxide radicals.
DR   PlantReactome; R-OSA-9611432; Recognition of fungal and bacterial pathogens and immunity response.
DR   Proteomes; UP000000763; Chromosome 7.
DR   Proteomes; UP000059680; Chromosome 7.
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; P28757; OS.
PE   1: Evidence at protein level;
KW   Antioxidant; Copper; Cytoplasm; Direct protein sequencing; Disulfide bond;
KW   Metal-binding; Oxidoreductase; Reference proteome; Zinc.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:14681440"
FT   CHAIN           2..152
FT                   /note="Superoxide dismutase [Cu-Zn] 2"
FT                   /id="PRO_0000164149"
FT   BINDING         45
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         47
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         62
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         62
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="structural"
FT                   /evidence="ECO:0000250"
FT   BINDING         70
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="structural"
FT                   /evidence="ECO:0000250"
FT   BINDING         79
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="structural"
FT                   /evidence="ECO:0000250"
FT   BINDING         82
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="structural"
FT                   /evidence="ECO:0000250"
FT   BINDING         119
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   DISULFID        56..145
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   152 AA;  15081 MW;  8D237FCABFE6EDBE CRC64;
     MVKAVAVLAS SEGVKGTIFF SQEGDGPTSV TGSVSGLKPG LHGFHVHALG DTTNGCMSTG
     PHFNPTGKEH GAPQDENRHA GDLGNITAGA DGVANVNVSD SQIPLTGAHS IIGRAVVVHA
     DPDDLGKGGH ELSKTTGNAG GRVACGIIGL QG
//