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Database: UniProt/SWISS-PROT
Entry: SODCP_ORYSJ
LinkDB: SODCP_ORYSJ
Original site: SODCP_ORYSJ 
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   13-FEB-2019, entry version 136.
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; Magnoliophyta; 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.,
RA   McCombie W.R., Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S.,
RA   Childs K.L., Davidson R.M., Lin H., Quesada-Ocampo L.,
RA   Vaillancourt B., Sakai H., Lee S.S., Kim J., Numa H., Itoh T.,
RA   Buell C.R., Matsumoto T.;
RT   "Improvement of the Oryza sativa Nipponbare reference genome using
RT   next 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};
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   UniGene; Os.5522; -.
DR   ProteinModelPortal; P93407; -.
DR   SMR; P93407; -.
DR   STRING; 39947.LOC_Os08g44770.1; -.
DR   PaxDb; P93407; -.
DR   PRIDE; 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   eggNOG; COG2032; LUCA.
DR   HOGENOM; HOG000263447; -.
DR   InParanoid; P93407; -.
DR   KO; K04565; -.
DR   OMA; MAKAVCT; -.
DR   OrthoDB; 1574423at2759; -.
DR   Reactome; R-OSA-114608; Platelet degranulation.
DR   Reactome; R-OSA-3299685; Detoxification of Reactive Oxygen Species.
DR   Proteomes; UP000059680; Chromosome 8.
DR   Genevisible; P93407; OS.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
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   1: Evidence at protein level;
KW   Antioxidant; Chloroplast; Complete proteome; Copper;
KW   Direct protein sequencing; Disulfide bond; Metal-binding;
KW   Oxidoreductase; Plastid; Reference proteome; Transit peptide; Zinc.
FT   TRANSIT       1     57       Chloroplast.
FT                                {ECO:0000269|PubMed:14681440}.
FT   CHAIN        58    211       Superoxide dismutase [Cu-Zn],
FT                                chloroplastic.
FT                                /FTId=PRO_0000032847.
FT   METAL       103    103       Copper; catalytic. {ECO:0000250}.
FT   METAL       105    105       Copper; catalytic. {ECO:0000250}.
FT   METAL       120    120       Copper; catalytic. {ECO:0000250}.
FT   METAL       120    120       Zinc; structural. {ECO:0000250}.
FT   METAL       128    128       Zinc; structural. {ECO:0000250}.
FT   METAL       137    137       Zinc; structural. {ECO:0000250}.
FT   METAL       140    140       Zinc; structural. {ECO:0000250}.
FT   METAL       177    177       Copper; catalytic. {ECO:0000250}.
FT   DISULFID    114    203       {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
//
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