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Database: UniProt/SWISS-PROT
Entry: SODC3_ARATH
LinkDB: SODC3_ARATH
Original site: 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   23-MAY-2018, entry version 123.
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; Magnoliophyta; eudicotyledons; Gunneridae;
OC   Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
OC   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.
RT   Sequence features of the regions of 1,367,185 bp covered by 19
RT   physically assigned 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
RT   reference 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.,
RA   Hayashizaki Y., Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T.,
RA   Shibata K., 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.,
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   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 3-164 (ISOFORM 1), TISSUE SPECIFICITY,
RP   SUBCELLULAR LOCATION, INDUCTION BY LIGHT; UV-B AND OZONE, AND GENE
RP   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.,
RA   Antonicelli G.E., Rasche N., Lueder F., Weckwerth W., Jahn O.;
RT   "Proteome analysis of Arabidopsis leaf peroxisomes reveals novel
RT   targeting 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: 2 superoxide + 2 H(+) = O(2) + H(2)O(2).
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         Note=Derived from EST data. No experimental confirmation
CC         available.;
CC   -!- TISSUE SPECIFICITY: Expressed in leaves (at protein level).
CC       {ECO:0000269|PubMed:9765550}.
CC   -!- INDUCTION: Upon photosynthetically active radiation (PAR) (e.g.
CC       light fluence) increase or after high-light pulse, and UV-B
CC       treatment. Accumulates in response to ozone fumigation, during
CC       recovery. Repressed 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}.
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   UniGene; At.49035; -.
DR   UniGene; At.7547; -.
DR   ProteinModelPortal; Q9FK60; -.
DR   SMR; Q9FK60; -.
DR   BioGrid; 17204; 2.
DR   IntAct; Q9FK60; 1.
DR   STRING; 3702.AT5G18100.1; -.
DR   PaxDb; Q9FK60; -.
DR   PRIDE; Q9FK60; -.
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   eggNOG; COG2032; LUCA.
DR   HOGENOM; HOG000263447; -.
DR   InParanoid; Q9FK60; -.
DR   KO; K04565; -.
DR   OMA; GKSVIIH; -.
DR   OrthoDB; EOG09360P4O; -.
DR   PhylomeDB; Q9FK60; -.
DR   Reactome; R-ATH-114608; Platelet degranulation.
DR   Reactome; R-ATH-3299685; Detoxification of Reactive Oxygen Species.
DR   PRO; PR:Q9FK60; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q9FK60; baseline and differential.
DR   Genevisible; Q9FK60; AT.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0005777; C:peroxisome; IDA:TAIR.
DR   GO; GO:0005773; C:vacuole; IDA: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:0008270; F:zinc ion binding; IBA:GO_Central.
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; -; 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; Complete proteome; Copper;
KW   Disulfide bond; Metal-binding; Oxidoreductase; Peroxisome;
KW   Reference proteome; Zinc.
FT   CHAIN         1    164       Superoxide dismutase [Cu-Zn] 3.
FT                                /FTId=PRO_0000419143.
FT   MOTIF       162    164       Peroxisome localization signal.
FT                                {ECO:0000250}.
FT   METAL        51     51       Copper; catalytic. {ECO:0000250}.
FT   METAL        53     53       Copper; catalytic. {ECO:0000250}.
FT   METAL        68     68       Copper; catalytic. {ECO:0000250}.
FT   METAL        68     68       Zinc; structural. {ECO:0000250}.
FT   METAL        76     76       Zinc; structural. {ECO:0000250}.
FT   METAL        85     85       Zinc; structural. {ECO:0000250}.
FT   METAL        88     88       Zinc; structural. {ECO:0000250}.
FT   METAL       125    125       Copper; catalytic. {ECO:0000250}.
FT   DISULFID     62    151       {ECO:0000250}.
FT   VAR_SEQ     135    137       GHK -> TKH (in isoform 2). {ECO:0000305}.
FT                                /FTId=VSP_044111.
FT   VAR_SEQ     138    164       Missing (in isoform 2). {ECO:0000305}.
FT                                /FTId=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
//
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