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Database: UniProt/SWISS-PROT
Entry: SODC2_ARATH
LinkDB: SODC2_ARATH
Original site: SODC2_ARATH 
ID   SODC2_ARATH             Reviewed;         216 AA.
AC   O78310; Q0WUQ0; Q541D5; Q9SUJ7; Q9SUJ8;
DT   11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   20-JUN-2002, sequence version 2.
DT   16-JAN-2019, entry version 151.
DE   RecName: Full=Superoxide dismutase [Cu-Zn] 2, chloroplastic;
DE            EC=1.15.1.1;
DE   AltName: Full=Copper/zinc superoxide dismutase 2;
DE   Flags: Precursor;
GN   Name=CSD2; Synonyms=KD-SOD, SODCP; OrderedLocusNames=At2g28190;
GN   ORFNames=F24D13.2;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
OC   Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
OC   Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, SUBCELLULAR LOCATION,
RP   INDUCTION BY LIGHT; UV-B AND OZONE, AND GENE FAMILY.
RC   STRAIN=cv. Columbia;
RX   PubMed=9765550; DOI=10.1104/pp.118.2.637;
RA   Kliebenstein D.J., Monde R.A., Last R.L.;
RT   "Superoxide dismutase in Arabidopsis: an eclectic enzyme family with
RT   disparate regulation and protein localization.";
RL   Plant Physiol. 118:637-650(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND VARIANTS TYR-23;
RP   SER-39; ALA-101 AND LYS-164.
RC   STRAIN=cv. Cvi-1, and cv. Landsberg erecta;
RX   PubMed=11457901; DOI=10.1093/jexbot/52.360.1417;
RA   Abarca D., Roldan M., Martin M., Sabater B.;
RT   "Arabidopsis thaliana ecotype Cvi shows an increased tolerance to
RT   photo-oxidative stress and contains a new chloroplastic copper/zinc
RT   superoxide dismutase isoenzyme.";
RL   J. Exp. Bot. 52:1417-1425(2001).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10617197; DOI=10.1038/45471;
RA   Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA   Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA   Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L.,
RA   Moffat K.S., Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L.,
RA   Tallon L.J., Gill J.E., Adams M.D., Carrera A.J., Creasy T.H.,
RA   Goodman H.M., Somerville C.R., Copenhaver G.P., Preuss D.,
RA   Nierman W.C., White O., Eisen J.A., Salzberg S.L., Fraser C.M.,
RA   Venter J.C.;
RT   "Sequence and analysis of chromosome 2 of the plant Arabidopsis
RT   thaliana.";
RL   Nature 402:761-768(1999).
RN   [4]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana
RT   reference genome.";
RL   Plant J. 89:789-804(2017).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
RA   Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
RA   Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
RA   Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
RA   Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
RA   Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
RA   Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
RA   Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
RA   Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
RA   Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
RA   Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
RA   Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RA   Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA   Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA   Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA   Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J.,
RA   Hayashizaki Y., Shinozaki K.;
RT   "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL   Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA   Feldmann K.A.;
RT   "Full-length cDNA from Arabidopsis thaliana.";
RL   Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN   [8]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=12885779; DOI=10.1074/jbc.M304987200;
RA   Rizhsky L., Liang H., Mittler R.;
RT   "The water-water cycle is essential for chloroplast protection in the
RT   absence of stress.";
RL   J. Biol. Chem. 278:38921-38925(2003).
RN   [9]
RP   FUNCTION, INDUCTION BY OXIDATIVE STRESS, AND TISSUE SPECIFICITY.
RX   PubMed=16861386; DOI=10.1105/tpc.106.041673;
RA   Sunkar R., Kapoor A., Zhu J.-K.;
RT   "Posttranscriptional induction of two Cu/Zn superoxide dismutase genes
RT   in Arabidopsis is mediated by downregulation of miR398 and important
RT   for oxidative stress tolerance.";
RL   Plant Cell 18:2051-2065(2006).
RN   [10]
RP   REGULATION BY ACONITASE.
RX   PubMed=17013749; DOI=10.1007/s11103-006-9087-x;
RA   Moeder W., Del Pozo O., Navarre D.A., Martin G.B., Klessig D.F.;
RT   "Aconitase plays a role in regulating resistance to oxidative stress
RT   and cell death in Arabidopsis and Nicotiana benthamiana.";
RL   Plant Mol. Biol. 63:273-287(2007).
RN   [11]
RP   INDUCTION BY SALT.
RC   STRAIN=cv. Columbia;
RX   PubMed=18275461; DOI=10.1111/j.1399-3054.2007.01009.x;
RA   Attia H., Arnaud N., Karray N., Lachaal M.;
RT   "Long-term effects of mild salt stress on growth, ion accumulation and
RT   superoxide dismutase expression of Arabidopsis rosette leaves.";
RL   Physiol. Plantarum 132:293-305(2008).
RN   [12]
RP   INDUCTION BY SUCROSE.
RC   STRAIN=cv. Columbia;
RX   PubMed=18392778; DOI=10.1007/s11103-008-9329-1;
RA   Dugas D.V., Bartel B.;
RT   "Sucrose induction of Arabidopsis miR398 represses two Cu/Zn
RT   superoxide dismutases.";
RL   Plant Mol. Biol. 67:403-417(2008).
RN   [13]
RP   IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE
RP   SCALE ANALYSIS].
RX   PubMed=18431481; DOI=10.1371/journal.pone.0001994;
RA   Zybailov B., Rutschow H., Friso G., Rudella A., Emanuelsson O.,
RA   Sun Q., van Wijk K.J.;
RT   "Sorting signals, N-terminal modifications and abundance of the
RT   chloroplast proteome.";
RL   PLoS ONE 3:E1994-E1994(2008).
CC   -!- FUNCTION: Destroys radicals which are normally produced within the
CC       cells and which are toxic to biological systems. Mediates
CC       tolerance to stress, including photo-oxidative stress.
CC       {ECO:0000269|PubMed:11457901, ECO:0000269|PubMed:12885779,
CC       ECO:0000269|PubMed:16861386}.
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       {ECO:0000269|PubMed:18431481, ECO:0000269|PubMed:9765550}.
CC   -!- TISSUE SPECIFICITY: Expressed in leaves (at protein level). The
CC       spatial localization is regulated by miR398-mediated silencing.
CC       Mostly present in flowers, old rosette leaves and inflorescence,
CC       and, to a lower extent, in cauline leaves, stems and roots.
CC       {ECO:0000269|PubMed:16861386, ECO:0000269|PubMed:9765550}.
CC   -!- INDUCTION: Upon photosynthetically active radiation (PAR) (e.g.
CC       light fluence) increase and UV-B treatment. Accumulates in
CC       response to ozone fumigation, during recovery. Induced in response
CC       to oxidative stress, via a reduction of miR398-mediated silencing.
CC       Repressed by sucrose in a miR398-mediated silencing-dependent
CC       manner. Repressed by salt stress. Down-regulated by aconitase.
CC       {ECO:0000269|PubMed:16861386, ECO:0000269|PubMed:18275461,
CC       ECO:0000269|PubMed:18392778, ECO:0000269|PubMed:9765550}.
CC   -!- DISRUPTION PHENOTYPE: Growth retardation (e.g. delayed flowering)
CC       and abnormal chloroplasts (e.g. less organized with fewer stacks).
CC       This phenotype is reversed under very low light conditions.
CC       Enhanced tolerance to oxidative stress.
CC       {ECO:0000269|PubMed:12885779}.
CC   -!- SIMILARITY: Belongs to the Cu-Zn superoxide dismutase family.
CC       {ECO:0000305}.
DR   EMBL; AF061519; AAD10208.1; -; mRNA.
DR   EMBL; AJ238521; CAB51839.1; -; Genomic_DNA.
DR   EMBL; AJ238522; CAB51840.1; -; Genomic_DNA.
DR   EMBL; AC005851; AAM15088.1; -; Genomic_DNA.
DR   EMBL; CP002685; AEC08089.1; -; Genomic_DNA.
DR   EMBL; AY064050; AAL36406.1; -; mRNA.
DR   EMBL; AY133756; AAM91690.1; -; mRNA.
DR   EMBL; AK227096; BAE99148.1; -; mRNA.
DR   EMBL; AY087944; AAM65492.1; -; mRNA.
DR   PIR; T51730; T51730.
DR   RefSeq; NP_565666.1; NM_128379.4.
DR   UniGene; At.20409; -.
DR   ProteinModelPortal; O78310; -.
DR   SMR; O78310; -.
DR   BioGrid; 2715; 2.
DR   IntAct; O78310; 1.
DR   STRING; 3702.AT2G28190.1; -.
DR   iPTMnet; O78310; -.
DR   PaxDb; O78310; -.
DR   PRIDE; O78310; -.
DR   EnsemblPlants; AT2G28190.1; AT2G28190.1; AT2G28190.
DR   GeneID; 817365; -.
DR   Gramene; AT2G28190.1; AT2G28190.1; AT2G28190.
DR   KEGG; ath:AT2G28190; -.
DR   Araport; AT2G28190; -.
DR   TAIR; locus:2046168; AT2G28190.
DR   eggNOG; KOG0441; Eukaryota.
DR   eggNOG; COG2032; LUCA.
DR   HOGENOM; HOG000263447; -.
DR   InParanoid; O78310; -.
DR   KO; K04565; -.
DR   OMA; MAKAVCT; -.
DR   OrthoDB; 1574423at2759; -.
DR   PhylomeDB; O78310; -.
DR   Reactome; R-ATH-114608; Platelet degranulation.
DR   Reactome; R-ATH-3299685; Detoxification of Reactive Oxygen Species.
DR   PRO; PR:O78310; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; O78310; baseline and differential.
DR   Genevisible; O78310; AT.
DR   GO; GO:0048046; C:apoplast; IDA:TAIR.
DR   GO; GO:0009507; C:chloroplast; IDA:UniProtKB.
DR   GO; GO:0009570; C:chloroplast stroma; IDA:TAIR.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0009579; C:thylakoid; IDA:TAIR.
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:0071484; P:cellular response to light intensity; IEP:UniProtKB.
DR   GO; GO:0034599; P:cellular response to oxidative stress; IEP:UniProtKB.
DR   GO; GO:0071457; P:cellular response to ozone; IEP:UniProtKB.
DR   GO; GO:0071472; P:cellular response to salt stress; IEP:UniProtKB.
DR   GO; GO:0071329; P:cellular response to sucrose stimulus; IEP:UniProtKB.
DR   GO; GO:0071493; P:cellular response to UV-B; IEP:UniProtKB.
DR   GO; GO:0035195; P:gene silencing by miRNA; IEP:UniProtKB.
DR   GO; GO:0019430; P:removal of superoxide radicals; IBA:GO_Central.
DR   GO; GO:0046688; P:response to copper ion; IEP:TAIR.
DR   GO; GO:0010039; P:response to iron ion; IEP:TAIR.
DR   GO; GO:0006979; P:response to oxidative stress; IDA:TAIR.
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; Disulfide bond;
KW   Metal-binding; Oxidoreductase; Plastid; Reference proteome;
KW   Transit peptide; Zinc.
FT   TRANSIT       1     62       Chloroplast.
FT   CHAIN        63    216       Superoxide dismutase [Cu-Zn] 2,
FT                                chloroplastic.
FT                                /FTId=PRO_0000032844.
FT   METAL       108    108       Copper; catalytic. {ECO:0000250}.
FT   METAL       110    110       Copper; catalytic. {ECO:0000250}.
FT   METAL       125    125       Copper; catalytic. {ECO:0000250}.
FT   METAL       125    125       Zinc; structural. {ECO:0000250}.
FT   METAL       133    133       Zinc; structural. {ECO:0000250}.
FT   METAL       142    142       Zinc; structural. {ECO:0000250}.
FT   METAL       145    145       Zinc; structural. {ECO:0000250}.
FT   METAL       182    182       Copper; catalytic. {ECO:0000250}.
FT   DISULFID    119    208       {ECO:0000250}.
FT   VARIANT      23     23       N -> Y (in strain: cv. Cvi-1; enhanced
FT                                stability and better tolerance to photo-
FT                                oxidative stress conditions; when
FT                                associated with S-39, A-101 and K-164).
FT                                {ECO:0000269|PubMed:11457901}.
FT   VARIANT      39     39       N -> S (in strain: cv. Cvi-1; enhanced
FT                                stability and better tolerance to photo-
FT                                oxidative stress conditions; when
FT                                associated with Y-23, A-101 and K-164).
FT                                {ECO:0000269|PubMed:11457901}.
FT   VARIANT     101    101       T -> A (in strain: cv. Cvi-1; enhanced
FT                                stability and better tolerance to photo-
FT                                oxidative stress conditions; when
FT                                associated with Y-23, S-39 and K-164).
FT                                {ECO:0000269|PubMed:11457901}.
FT   VARIANT     164    164       N -> K (in strain: cv. Cvi-1; enhanced
FT                                stability and better tolerance to photo-
FT                                oxidative stress conditions; when
FT                                associated with Y-23, S-39 and A-101).
FT                                {ECO:0000269|PubMed:11457901}.
FT   CONFLICT     32     32       R -> S (in Ref. 1; AAD10208 and 7;
FT                                AAM65492). {ECO:0000305}.
SQ   SEQUENCE   216 AA;  22244 MW;  5F0E4333E1C1581C CRC64;
     MAATNTILAF SSPSRLLIPP SSNPSTLRSS FRGVSLNNNN LHRLQSVSFA VKAPSKALTV
     VSAAKKAVAV LKGTSDVEGV VTLTQDDSGP TTVNVRITGL TPGPHGFHLH EFGDTTNGCI
     STGPHFNPNN MTHGAPEDEC RHAGDLGNIN ANADGVAETT IVDNQIPLTG PNSVVGRAFV
     VHELKDDLGK GGHELSLTTG NAGGRLACGV IGLTPL
//
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