ID   SODC3_ARATH             Reviewed;         164 AA.
AC   Q9FK60; B3H6P9; O81236;
DT   03-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   24-JAN-2024, entry version 147.
DE   RecName: Full=Superoxide dismutase [Cu-Zn] 3;
DE            EC=1.15.1.1;
DE   AltName: Full=Copper/zinc superoxide dismutase 3;
GN   Name=CSD3; OrderedLocusNames=At5g18100; ORFNames=MRG7.6;
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 [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=9734815; DOI=10.1093/dnares/5.3.203;
RA   Kotani H., Nakamura Y., Sato S., Asamizu E., Kaneko T., Miyajima N.,
RA   Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 5. VI. Sequence
RT   features of the regions of 1,367,185 bp covered by 19 physically assigned
RT   P1 and TAC clones.";
RL   DNA Res. 5:203-216(1998).
RN   [2]
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=cv. Columbia;
RX   PubMed=11910074; DOI=10.1126/science.1071006;
RA   Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA   Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA   Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA   Shinagawa A., Shinozaki K.;
RT   "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL   Science 296:141-145(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 3-164 (ISOFORM 1), TISSUE SPECIFICITY,
RP   SUBCELLULAR LOCATION, 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   [6]
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=17951448; DOI=10.1105/tpc.107.050989;
RA   Reumann S., Babujee L., Ma C., Wienkoop S., Siemsen T., Antonicelli G.E.,
RA   Rasche N., Lueder F., Weckwerth W., Jahn O.;
RT   "Proteome analysis of Arabidopsis leaf peroxisomes reveals novel targeting
RT   peptides, metabolic pathways, and defense mechanisms.";
RL   Plant Cell 19:3170-3193(2007).
RN   [7]
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).
CC   -!- FUNCTION: Destroys radicals which are normally produced within the
CC       cells and which are toxic to biological systems. {ECO:0000250}.
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. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000269|PubMed:9765550}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9FK60-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9FK60-2; Sequence=VSP_044111, VSP_044112;
CC   -!- TISSUE SPECIFICITY: Expressed in leaves (at protein level).
CC       {ECO:0000269|PubMed:9765550}.
CC   -!- INDUCTION: Upon photosynthetically active radiation (PAR) (e.g. light
CC       fluence) increase or after high-light pulse, and UV-B treatment.
CC       Accumulates in response to ozone fumigation, during recovery. Repressed
CC       by salt stress. {ECO:0000269|PubMed:18275461,
CC       ECO:0000269|PubMed:9765550}.
CC   -!- SIMILARITY: Belongs to the Cu-Zn superoxide dismutase family.
CC       {ECO:0000305}.
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DR   EMBL; AF061520; AAC24833.1; -; mRNA.
DR   EMBL; AB012246; BAB09468.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED92506.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED92507.1; -; Genomic_DNA.
DR   EMBL; AK117742; BAC42391.1; -; mRNA.
DR   EMBL; BT003689; AAO39917.1; -; mRNA.
DR   PIR; T51731; T51731.
DR   RefSeq; NP_001119245.1; NM_001125773.1. [Q9FK60-2]
DR   RefSeq; NP_197311.1; NM_121815.3. [Q9FK60-1]
DR   AlphaFoldDB; Q9FK60; -.
DR   SMR; Q9FK60; -.
DR   BioGRID; 17204; 2.
DR   IntAct; Q9FK60; 1.
DR   STRING; 3702.Q9FK60; -.
DR   PaxDb; 3702-AT5G18100-1; -.
DR   ProteomicsDB; 232513; -. [Q9FK60-1]
DR   EnsemblPlants; AT5G18100.1; AT5G18100.1; AT5G18100. [Q9FK60-1]
DR   EnsemblPlants; AT5G18100.2; AT5G18100.2; AT5G18100. [Q9FK60-2]
DR   GeneID; 831928; -.
DR   Gramene; AT5G18100.1; AT5G18100.1; AT5G18100. [Q9FK60-1]
DR   Gramene; AT5G18100.2; AT5G18100.2; AT5G18100. [Q9FK60-2]
DR   KEGG; ath:AT5G18100; -.
DR   Araport; AT5G18100; -.
DR   TAIR; AT5G18100; CSD3.
DR   eggNOG; KOG0441; Eukaryota.
DR   HOGENOM; CLU_056632_4_1_1; -.
DR   InParanoid; Q9FK60; -.
DR   OMA; AQRGFHI; -.
DR   OrthoDB; 3470597at2759; -.
DR   PhylomeDB; Q9FK60; -.
DR   PRO; PR:Q9FK60; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q9FK60; baseline and differential.
DR   GO; GO:0005777; C:peroxisome; HDA:TAIR.
DR   GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR   GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR   GO; GO:0004784; F:superoxide dismutase activity; ISS:TAIR.
DR   GO; GO:0071486; P:cellular response to high light intensity; IEP:UniProtKB.
DR   GO; GO:0071484; P:cellular response to light intensity; 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:0071493; P:cellular response to UV-B; IEP:UniProtKB.
DR   GO; GO:0006979; P:response to oxidative stress; TAS:TAIR.
DR   CDD; cd00305; Cu-Zn_Superoxide_Dismutase; 1.
DR   Gene3D; 2.60.40.200; Superoxide dismutase, copper/zinc binding domain; 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:SF31; SUPEROXIDE DISMUTASE [CU-ZN] 3; 1.
DR   PANTHER; PTHR10003; SUPEROXIDE DISMUTASE CU-ZN -RELATED; 1.
DR   Pfam; PF00080; Sod_Cu; 1.
DR   PRINTS; PR00068; CUZNDISMTASE.
DR   SUPFAM; SSF49329; Cu,Zn superoxide dismutase-like; 1.
DR   PROSITE; PS00332; SOD_CU_ZN_2; 1.
DR   Genevisible; Q9FK60; AT.
PE   1: Evidence at protein level;
KW   Alternative splicing; Antioxidant; Copper; Disulfide bond; Metal-binding;
KW   Oxidoreductase; Peroxisome; Reference proteome; Zinc.
FT   CHAIN           1..164
FT                   /note="Superoxide dismutase [Cu-Zn] 3"
FT                   /id="PRO_0000419143"
FT   MOTIF           162..164
FT                   /note="Peroxisome localization signal"
FT                   /evidence="ECO:0000250"
FT   BINDING         51
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         53
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         68
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         68
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="structural"
FT                   /evidence="ECO:0000250"
FT   BINDING         76
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="structural"
FT                   /evidence="ECO:0000250"
FT   BINDING         85
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="structural"
FT                   /evidence="ECO:0000250"
FT   BINDING         88
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="structural"
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   DISULFID        62..151
FT                   /evidence="ECO:0000250"
FT   VAR_SEQ         135..137
FT                   /note="GHK -> TKH (in isoform 2)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_044111"
FT   VAR_SEQ         138..164
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_044112"
SQ   SEQUENCE   164 AA;  16941 MW;  A80B9F4A79D0F365 CRC64;
     MEAPRGNLRA VALIAGDNNV RGCLQFVQDI SGTTHVTGKI SGLSPGFHGF HIHSFGDTTN
     GCISTGPHFN PLNRVHGPPN EEERHAGDLG NILAGSNGVA EILIKDKHIP LSGQYSILGR
     AVVVHADPDD LGKGGHKLSK STGNAGSRVG CGIIGLQSSA DAKL
//