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 03-AUG-2022, entry version 167.
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; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; 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; SER-39;
RP 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 photo-
RT oxidative stress and contains a new chloroplastic copper/zinc superoxide
RT 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., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis 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 reference
RT 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., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA 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., Hayashizaki Y.,
RA 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 in
RT Arabidopsis is mediated by downregulation of miR398 and important for
RT 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 and
RT 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 superoxide
RT dismutases.";
RL Plant Mol. Biol. 67:403-417(2008).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
RX PubMed=18431481; DOI=10.1371/journal.pone.0001994;
RA Zybailov B., Rutschow H., Friso G., Rudella A., Emanuelsson O., Sun Q.,
RA van Wijk K.J.;
RT "Sorting signals, N-terminal modifications and abundance of the chloroplast
RT 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 tolerance to
CC stress, including photo-oxidative stress. {ECO:0000269|PubMed:11457901,
CC ECO:0000269|PubMed:12885779, 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 spatial
CC localization is regulated by miR398-mediated silencing. Mostly present
CC in flowers, old rosette leaves and inflorescence, and, to a lower
CC 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. light
CC fluence) increase and UV-B treatment. Accumulates in response to ozone
CC fumigation, during recovery. Induced in response to oxidative stress,
CC via a reduction of miR398-mediated silencing. Repressed by sucrose in a
CC miR398-mediated silencing-dependent manner. Repressed by salt stress.
CC Down-regulated by aconitase. {ECO:0000269|PubMed:16861386,
CC ECO:0000269|PubMed:18275461, ECO:0000269|PubMed:18392778,
CC ECO:0000269|PubMed:9765550}.
CC -!- DISRUPTION PHENOTYPE: Growth retardation (e.g. delayed flowering) and
CC abnormal chloroplasts (e.g. less organized with fewer stacks). This
CC phenotype is reversed under very low light conditions. Enhanced
CC tolerance to oxidative stress. {ECO:0000269|PubMed:12885779}.
CC -!- SIMILARITY: Belongs to the Cu-Zn superoxide dismutase family.
CC {ECO:0000305}.
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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 AlphaFoldDB; 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 ProteomicsDB; 232601; -.
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 HOGENOM; CLU_056632_1_0_1; -.
DR InParanoid; O78310; -.
DR OMA; DITYTDP; -.
DR OrthoDB; 1574423at2759; -.
DR PhylomeDB; O78310; -.
DR BRENDA; 1.15.1.1; 399.
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; HDA:TAIR.
DR GO; GO:0009507; C:chloroplast; IDA:UniProtKB.
DR GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
DR GO; GO:0009579; C:thylakoid; HDA: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: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:miRNA-mediated gene silencing; 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 GO; GO:0009651; P:response to salt stress; IEP: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; Copper; Disulfide bond; Metal-binding;
KW Oxidoreductase; Plastid; Reference proteome; Transit peptide; Zinc.
FT TRANSIT 1..62
FT /note="Chloroplast"
FT CHAIN 63..216
FT /note="Superoxide dismutase [Cu-Zn] 2, chloroplastic"
FT /id="PRO_0000032844"
FT BINDING 108
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 110
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 125
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 125
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000250"
FT BINDING 133
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000250"
FT BINDING 142
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000250"
FT BINDING 145
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000250"
FT BINDING 182
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT DISULFID 119..208
FT /evidence="ECO:0000250"
FT VARIANT 23
FT /note="N -> Y (in strain: cv. Cvi-1; enhanced stability and
FT better tolerance to photo-oxidative stress conditions; when
FT associated with S-39, A-101 and K-164)"
FT /evidence="ECO:0000269|PubMed:11457901"
FT VARIANT 39
FT /note="N -> S (in strain: cv. Cvi-1; enhanced stability and
FT better tolerance to photo-oxidative stress conditions; when
FT associated with Y-23, A-101 and K-164)"
FT /evidence="ECO:0000269|PubMed:11457901"
FT VARIANT 101
FT /note="T -> A (in strain: cv. Cvi-1; enhanced stability and
FT better tolerance to photo-oxidative stress conditions; when
FT associated with Y-23, S-39 and K-164)"
FT /evidence="ECO:0000269|PubMed:11457901"
FT VARIANT 164
FT /note="N -> K (in strain: cv. Cvi-1; enhanced stability and
FT better tolerance to photo-oxidative stress conditions; when
FT associated with Y-23, S-39 and A-101)"
FT /evidence="ECO:0000269|PubMed:11457901"
FT CONFLICT 32
FT /note="R -> S (in Ref. 1; AAD10208 and 7; AAM65492)"
FT /evidence="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
