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Database: UniProt
Entry: SODC1_ORYSJ
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ID   SODC1_ORYSJ             Reviewed;         152 AA.
AC   Q0DRV6; A0A0P0VYC1; P28756; Q10LG6; Q4TUB3;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   10-APR-2019, entry version 90.
DE   RecName: Full=Superoxide dismutase [Cu-Zn] 1;
DE            EC=1.15.1.1;
GN   Name=SODCC1; Synonyms=SODCC.1;
GN   OrderedLocusNames=Os03g0351500, LOC_Os03g22810; ORFNames=OsJ_010399;
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=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=7724677; DOI=10.1104/pp.107.2.651;
RA   Sakamoto A., Okumura T., Kaminaka H., Tanaka K.;
RT   "Molecular cloning of the gene (SodCc1) that encodes a cytosolic
RT   copper/zinc-superoxide dismutase from rice (Oryza sativa L.).";
RL   Plant Physiol. 107:651-652(1995).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Tainung 67; TISSUE=Shoot;
RA   Pan S.M., Huang G.B.;
RT   "Cloning and expression of CuZnSOD from rice.";
RL   Submitted (SEP-1994) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=16109971; DOI=10.1101/gr.3869505;
RG   The rice chromosome 3 sequencing consortium;
RA   Buell C.R., Yuan Q., Ouyang S., Liu J., Zhu W., Wang A., Maiti R.,
RA   Haas B., Wortman J., Pertea M., Jones K.M., Kim M., Overton L.,
RA   Tsitrin T., Fadrosh D., Bera J., Weaver B., Jin S., Johri S.,
RA   Reardon M., Webb K., Hill J., Moffat K., Tallon L., Van Aken S.,
RA   Lewis M., Utterback T., Feldblyum T., Zismann V., Iobst S., Hsiao J.,
RA   de Vazeille A.R., Salzberg S.L., White O., Fraser C.M., Yu Y., Kim H.,
RA   Rambo T., Currie J., Collura K., Kernodle-Thompson S., Wei F.,
RA   Kudrna K., Ammiraju J.S.S., Luo M., Goicoechea J.L., Wing R.A.,
RA   Henry D., Oates R., Palmer M., Pries G., Saski C., Simmons J.,
RA   Soderlund C., Nelson W., de la Bastide M., Spiegel L., Nascimento L.,
RA   Huang E., Preston R., Zutavern T., Palmer L., O'Shaughnessy A.,
RA   Dike S., McCombie W.R., Minx P., Cordum H., Wilson R., Jin W.,
RA   Lee H.R., Jiang J., Jackson S.;
RT   "Sequence, annotation, and analysis of synteny between rice chromosome
RT   3 and diverged grass species.";
RL   Genome Res. 15:1284-1291(2005).
RN   [5]
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   [6]
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   [7]
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   [8]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA   Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA   Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H.,
RA   Cong L., Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J.,
RA   Wang J., Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X.,
RA   Wang J., Wang X., Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y.,
RA   Zhang Z., Bao J., Han Y., Dong L., Ji J., Chen P., Wu S., Liu J.,
RA   Xiao Y., Bu D., Tan J., Yang L., Ye C., Zhang J., Xu J., Zhou Y.,
RA   Yu Y., Zhang B., Zhuang S., Wei H., Liu B., Lei M., Yu H., Li Y.,
RA   Xu H., Wei S., He X., Fang L., Zhang Z., Zhang Y., Huang X., Su Z.,
RA   Tong W., Li J., Tong Z., Li S., Ye J., Wang L., Fang L., Lei T.,
RA   Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F., Xu H.,
RA   Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q., Li W.,
RA   Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J., Gao L.,
RA   Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M., McDermott J.,
RA   Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT   "The genomes of Oryza sativa: a history of duplications.";
RL   PLoS Biol. 3:266-281(2005).
RN   [9]
RP   PROTEIN SEQUENCE OF 2-11.
RC   STRAIN=cv. Nipponbare;
RC   TISSUE=Anther, Callus, Panicle, Root, Sheath, and Stem;
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=ABF95937.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=EAZ26916.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
DR   EMBL; D00999; BAA00799.1; -; mRNA.
DR   EMBL; L19435; AAC14464.1; -; Genomic_DNA.
DR   EMBL; L36320; AAA33917.1; -; mRNA.
DR   EMBL; DP000009; ABF95937.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AP008209; BAF12032.1; -; Genomic_DNA.
DR   EMBL; AP014959; BAS84200.1; -; Genomic_DNA.
DR   EMBL; CM000140; EAZ26916.1; ALT_SEQ; Genomic_DNA.
DR   PIR; S22508; S22508.
DR   PIR; S29149; S29149.
DR   RefSeq; XP_015632608.1; XM_015777122.1.
DR   RefSeq; XP_015632609.1; XM_015777123.1.
DR   UniGene; Os.186; -.
DR   ProteinModelPortal; Q0DRV6; -.
DR   SMR; Q0DRV6; -.
DR   STRING; 4530.OS03T0351500-01; -.
DR   PaxDb; Q0DRV6; -.
DR   EnsemblPlants; Os03t0351500-01; Os03t0351500-01; Os03g0351500.
DR   GeneID; 4332846; -.
DR   Gramene; Os03t0351500-01; Os03t0351500-01; Os03g0351500.
DR   KEGG; osa:4332846; -.
DR   eggNOG; KOG0441; Eukaryota.
DR   eggNOG; COG2032; LUCA.
DR   InParanoid; Q0DRV6; -.
DR   KO; K04565; -.
DR   OMA; HKGDIGN; -.
DR   OrthoDB; 1574423at2759; -.
DR   Reactome; R-OSA-114608; Platelet degranulation.
DR   Reactome; R-OSA-3299685; Detoxification of Reactive Oxygen Species.
DR   Proteomes; UP000059680; Chromosome 3.
DR   Genevisible; Q0DRV6; OS.
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; Complete proteome; Copper; Cytoplasm;
KW   Direct protein sequencing; Disulfide bond; Metal-binding;
KW   Oxidoreductase; Reference proteome; Zinc.
FT   INIT_MET      1      1       Removed. {ECO:0000269|PubMed:14681440}.
FT   CHAIN         2    152       Superoxide dismutase [Cu-Zn] 1.
FT                                /FTId=PRO_0000164148.
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}.
FT   CONFLICT     57     57       M -> I (in Ref. 3; AAA33917).
FT                                {ECO:0000305}.
SQ   SEQUENCE   152 AA;  15251 MW;  9282FDE7CD07AD32 CRC64;
     MVKAVVVLGS SEIVKGTIHF VQEGDGPTTV TGSVSGLKPG LHGFHIHALG DTTNGCMSTG
     PHYNPAGKEH GAPEDETRHA GDLGNVTAGE DGVANIHVVD SQIPLTGPNS IIGRAVVVHA
     DPDDLGKGGH ELSKTTGNAG GRVACGIIGL QG
//
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