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Superoxide dismutase [Cu-Zn] 2, chloroplastic (EC 1.15.1.1) (Copper/zinc superoxide dismutase 2)

 SODC2_ARATH             Reviewed;         216 AA.
O78310; Q0WUQ0; Q541D5; Q9SUJ7; Q9SUJ8;
11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
20-JUN-2002, sequence version 2.
20-DEC-2017, entry version 147.
RecName: Full=Superoxide dismutase [Cu-Zn] 2, chloroplastic;
EC=1.15.1.1;
AltName: Full=Copper/zinc superoxide dismutase 2;
Flags: Precursor;
Name=CSD2; Synonyms=KD-SOD, SODCP; OrderedLocusNames=At2g28190;
ORFNames=F24D13.2;
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, SUBCELLULAR LOCATION,
INDUCTION BY LIGHT; UV-B AND OZONE, AND GENE FAMILY.
STRAIN=cv. Columbia;
PubMed=9765550; DOI=10.1104/pp.118.2.637;
Kliebenstein D.J., Monde R.A., Last R.L.;
"Superoxide dismutase in Arabidopsis: an eclectic enzyme family with
disparate regulation and protein localization.";
Plant Physiol. 118:637-650(1998).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND VARIANTS TYR-23;
SER-39; ALA-101 AND LYS-164.
STRAIN=cv. Cvi-1, and cv. Landsberg erecta;
PubMed=11457901; DOI=10.1093/jexbot/52.360.1417;
Abarca D., Roldan M., Martin M., Sabater B.;
"Arabidopsis thaliana ecotype Cvi shows an increased tolerance to
photo-oxidative stress and contains a new chloroplastic copper/zinc
superoxide dismutase isoenzyme.";
J. Exp. Bot. 52:1417-1425(2001).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=10617197; DOI=10.1038/45471;
Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L.,
Moffat K.S., Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L.,
Tallon L.J., Gill J.E., Adams M.D., Carrera A.J., Creasy T.H.,
Goodman H.M., Somerville C.R., Copenhaver G.P., Preuss D.,
Nierman W.C., White O., Eisen J.A., Salzberg S.L., Fraser C.M.,
Venter J.C.;
"Sequence and analysis of chromosome 2 of the plant Arabidopsis
thaliana.";
Nature 402:761-768(1999).
[4]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
The Arabidopsis Information Portal (Araport);
Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
PubMed=14593172; DOI=10.1126/science.1088305;
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
"Empirical analysis of transcriptional activity in the Arabidopsis
genome.";
Science 302:842-846(2003).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J.,
Hayashizaki Y., Shinozaki K.;
"Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
Feldmann K.A.;
"Full-length cDNA from Arabidopsis thaliana.";
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
[8]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=12885779; DOI=10.1074/jbc.M304987200;
Rizhsky L., Liang H., Mittler R.;
"The water-water cycle is essential for chloroplast protection in the
absence of stress.";
J. Biol. Chem. 278:38921-38925(2003).
[9]
FUNCTION, INDUCTION BY OXIDATIVE STRESS, AND TISSUE SPECIFICITY.
PubMed=16861386; DOI=10.1105/tpc.106.041673;
Sunkar R., Kapoor A., Zhu J.-K.;
"Posttranscriptional induction of two Cu/Zn superoxide dismutase genes
in Arabidopsis is mediated by downregulation of miR398 and important
for oxidative stress tolerance.";
Plant Cell 18:2051-2065(2006).
[10]
REGULATION BY ACONITASE.
PubMed=17013749; DOI=10.1007/s11103-006-9087-x;
Moeder W., Del Pozo O., Navarre D.A., Martin G.B., Klessig D.F.;
"Aconitase plays a role in regulating resistance to oxidative stress
and cell death in Arabidopsis and Nicotiana benthamiana.";
Plant Mol. Biol. 63:273-287(2007).
[11]
INDUCTION BY SALT.
STRAIN=cv. Columbia;
PubMed=18275461; DOI=10.1111/j.1399-3054.2007.01009.x;
Attia H., Arnaud N., Karray N., Lachaal M.;
"Long-term effects of mild salt stress on growth, ion accumulation and
superoxide dismutase expression of Arabidopsis rosette leaves.";
Physiol. Plantarum 132:293-305(2008).
[12]
INDUCTION BY SUCROSE.
STRAIN=cv. Columbia;
PubMed=18392778; DOI=10.1007/s11103-008-9329-1;
Dugas D.V., Bartel B.;
"Sucrose induction of Arabidopsis miR398 represses two Cu/Zn
superoxide dismutases.";
Plant Mol. Biol. 67:403-417(2008).
[13]
IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE
SCALE ANALYSIS].
PubMed=18431481; DOI=10.1371/journal.pone.0001994;
Zybailov B., Rutschow H., Friso G., Rudella A., Emanuelsson O.,
Sun Q., van Wijk K.J.;
"Sorting signals, N-terminal modifications and abundance of the
chloroplast proteome.";
PLoS ONE 3:E1994-E1994(2008).
-!- FUNCTION: Destroys radicals which are normally produced within the
cells and which are toxic to biological systems. Mediates
tolerance to stress, including photo-oxidative stress.
{ECO:0000269|PubMed:11457901, ECO:0000269|PubMed:12885779,
ECO:0000269|PubMed:16861386}.
-!- CATALYTIC ACTIVITY: 2 superoxide + 2 H(+) = O(2) + H(2)O(2).
-!- COFACTOR:
Name=Cu cation; Xref=ChEBI:CHEBI:23378; Evidence={ECO:0000250};
Note=Binds 1 copper ion per subunit. {ECO:0000250};
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
Note=Binds 1 zinc ion per subunit. {ECO:0000250};
-!- SUBUNIT: Homotetramer. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Plastid, chloroplast
{ECO:0000269|PubMed:18431481, ECO:0000269|PubMed:9765550}.
-!- TISSUE SPECIFICITY: Expressed in leaves (at protein level). The
spatial localization is regulated by miR398-mediated silencing.
Mostly present in flowers, old rosette leaves and inflorescence,
and, to a lower extent, in cauline leaves, stems and roots.
{ECO:0000269|PubMed:16861386, ECO:0000269|PubMed:9765550}.
-!- INDUCTION: Upon photosynthetically active radiation (PAR) (e.g.
light fluence) increase and UV-B treatment. Accumulates in
response to ozone fumigation, during recovery. Induced in response
to oxidative stress, via a reduction of miR398-mediated silencing.
Repressed by sucrose in a miR398-mediated silencing-dependent
manner. Repressed by salt stress. Down-regulated by aconitase.
{ECO:0000269|PubMed:16861386, ECO:0000269|PubMed:18275461,
ECO:0000269|PubMed:18392778, ECO:0000269|PubMed:9765550}.
-!- DISRUPTION PHENOTYPE: Growth retardation (e.g. delayed flowering)
and abnormal chloroplasts (e.g. less organized with fewer stacks).
This phenotype is reversed under very low light conditions.
Enhanced tolerance to oxidative stress.
{ECO:0000269|PubMed:12885779}.
-!- SIMILARITY: Belongs to the Cu-Zn superoxide dismutase family.
{ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AF061519; AAD10208.1; -; mRNA.
EMBL; AJ238521; CAB51839.1; -; Genomic_DNA.
EMBL; AJ238522; CAB51840.1; -; Genomic_DNA.
EMBL; AC005851; AAM15088.1; -; Genomic_DNA.
EMBL; CP002685; AEC08089.1; -; Genomic_DNA.
EMBL; AY064050; AAL36406.1; -; mRNA.
EMBL; AY133756; AAM91690.1; -; mRNA.
EMBL; AK227096; BAE99148.1; -; mRNA.
EMBL; AY087944; AAM65492.1; -; mRNA.
PIR; T51730; T51730.
RefSeq; NP_565666.1; NM_128379.4.
UniGene; At.20409; -.
ProteinModelPortal; O78310; -.
SMR; O78310; -.
BioGrid; 2715; 2.
IntAct; O78310; 1.
STRING; 3702.AT2G28190.1; -.
iPTMnet; O78310; -.
PaxDb; O78310; -.
PRIDE; O78310; -.
EnsemblPlants; AT2G28190.1; AT2G28190.1; AT2G28190.
GeneID; 817365; -.
Gramene; AT2G28190.1; AT2G28190.1; AT2G28190.
KEGG; ath:AT2G28190; -.
Araport; AT2G28190; -.
TAIR; locus:2046168; AT2G28190.
eggNOG; KOG0441; Eukaryota.
eggNOG; COG2032; LUCA.
HOGENOM; HOG000263447; -.
InParanoid; O78310; -.
KO; K04565; -.
OMA; IHTFGDN; -.
OrthoDB; EOG09360OJH; -.
PhylomeDB; O78310; -.
Reactome; R-ATH-114608; Platelet degranulation.
Reactome; R-ATH-3299685; Detoxification of Reactive Oxygen Species.
PRO; PR:O78310; -.
Proteomes; UP000006548; Chromosome 2.
ExpressionAtlas; O78310; baseline and differential.
Genevisible; O78310; AT.
GO; GO:0048046; C:apoplast; IDA:TAIR.
GO; GO:0009507; C:chloroplast; IDA:UniProtKB.
GO; GO:0009570; C:chloroplast stroma; IDA:TAIR.
GO; GO:0005615; C:extracellular space; IBA:GO_Central.
GO; GO:0009579; C:thylakoid; IDA:TAIR.
GO; GO:0005507; F:copper ion binding; IBA:GO_Central.
GO; GO:0004784; F:superoxide dismutase activity; IEA:UniProtKB-EC.
GO; GO:0008270; F:zinc ion binding; IBA:GO_Central.
GO; GO:0071484; P:cellular response to light intensity; IEP:UniProtKB.
GO; GO:0034599; P:cellular response to oxidative stress; IEP:UniProtKB.
GO; GO:0071457; P:cellular response to ozone; IEP:UniProtKB.
GO; GO:0071472; P:cellular response to salt stress; IEP:UniProtKB.
GO; GO:0071329; P:cellular response to sucrose stimulus; IEP:UniProtKB.
GO; GO:0071493; P:cellular response to UV-B; IEP:UniProtKB.
GO; GO:0035195; P:gene silencing by miRNA; IEP:UniProtKB.
GO; GO:0046688; P:response to copper ion; IEP:TAIR.
GO; GO:0010039; P:response to iron ion; IEP:TAIR.
GO; GO:0006979; P:response to oxidative stress; IDA:TAIR.
CDD; cd00305; Cu-Zn_Superoxide_Dismutase; 1.
Gene3D; 2.60.40.200; -; 1.
InterPro; IPR036423; SOD-like_Cu/Zn_dom_sf.
InterPro; IPR024134; SOD_Cu/Zn_/chaperone.
InterPro; IPR018152; SOD_Cu/Zn_BS.
InterPro; IPR001424; SOD_Cu_Zn_dom.
PANTHER; PTHR10003; PTHR10003; 1.
Pfam; PF00080; Sod_Cu; 1.
PRINTS; PR00068; CUZNDISMTASE.
SUPFAM; SSF49329; SSF49329; 1.
PROSITE; PS00087; SOD_CU_ZN_1; 1.
PROSITE; PS00332; SOD_CU_ZN_2; 1.
1: Evidence at protein level;
Antioxidant; Chloroplast; Complete proteome; Copper; Disulfide bond;
Metal-binding; Oxidoreductase; Plastid; Reference proteome;
Transit peptide; Zinc.
TRANSIT 1 62 Chloroplast.
CHAIN 63 216 Superoxide dismutase [Cu-Zn] 2,
chloroplastic.
/FTId=PRO_0000032844.
METAL 108 108 Copper; catalytic. {ECO:0000250}.
METAL 110 110 Copper; catalytic. {ECO:0000250}.
METAL 125 125 Copper; catalytic. {ECO:0000250}.
METAL 125 125 Zinc; structural. {ECO:0000250}.
METAL 133 133 Zinc; structural. {ECO:0000250}.
METAL 142 142 Zinc; structural. {ECO:0000250}.
METAL 145 145 Zinc; structural. {ECO:0000250}.
METAL 182 182 Copper; catalytic. {ECO:0000250}.
DISULFID 119 208 {ECO:0000250}.
VARIANT 23 23 N -> Y (in strain: cv. Cvi-1; enhanced
stability and better tolerance to photo-
oxidative stress conditions; when
associated with S-39, A-101 and K-164).
{ECO:0000269|PubMed:11457901}.
VARIANT 39 39 N -> S (in strain: cv. Cvi-1; enhanced
stability and better tolerance to photo-
oxidative stress conditions; when
associated with Y-23, A-101 and K-164).
{ECO:0000269|PubMed:11457901}.
VARIANT 101 101 T -> A (in strain: cv. Cvi-1; enhanced
stability and better tolerance to photo-
oxidative stress conditions; when
associated with Y-23, S-39 and K-164).
{ECO:0000269|PubMed:11457901}.
VARIANT 164 164 N -> K (in strain: cv. Cvi-1; enhanced
stability and better tolerance to photo-
oxidative stress conditions; when
associated with Y-23, S-39 and A-101).
{ECO:0000269|PubMed:11457901}.
CONFLICT 32 32 R -> S (in Ref. 1; AAD10208 and 7;
AAM65492). {ECO:0000305}.
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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