SODC3_ARATH
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 03-AUG-2022, entry version 141.
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.AT5G18100.1; -.
DR PaxDb; Q9FK60; -.
DR PRIDE; Q9FK60; -.
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; locus:2172324; AT5G18100.
DR eggNOG; KOG0441; Eukaryota.
DR HOGENOM; CLU_056632_4_1_1; -.
DR InParanoid; Q9FK60; -.
DR OMA; AQRGFHI; -.
DR OrthoDB; 1574423at2759; -.
DR PhylomeDB; Q9FK60; -.
DR PRO; PR:Q9FK60; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FK60; baseline and differential.
DR Genevisible; Q9FK60; AT.
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; IBA:GO_Central.
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:0019430; P:removal of superoxide radicals; IBA:GO_Central.
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; -; 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; PS00332; SOD_CU_ZN_2; 1.
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
