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Database: UniProt/SWISS-PROT
Entry: SODC1_ARATH
LinkDB: SODC1_ARATH
Original site: SODC1_ARATH 
ID   SODC1_ARATH             Reviewed;         152 AA.
AC   P24704; A3FMJ0; Q9FRQ6;
DT   01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   16-JAN-2019, entry version 163.
DE   RecName: Full=Superoxide dismutase [Cu-Zn] 1;
DE            EC=1.15.1.1;
DE   AltName: Full=Copper/zinc superoxide dismutase 1;
GN   Name=CSD1; Synonyms=SODCC; OrderedLocusNames=At1g08830;
GN   ORFNames=F22O13.32;
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 [MRNA].
RC   STRAIN=cv. Columbia; TISSUE=Leaf, and Stem;
RX   PubMed=1731963; DOI=10.1007/BF00018463;
RA   Hindges R., Slusarenko A.J.;
RT   "cDNA and derived amino acid sequence of a cytosolic Cu,Zn superoxide
RT   dismutase from Arabidopsis thaliana (L.) Heyhn.";
RL   Plant Mol. Biol. 18:123-125(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Columbia;
RA   Rani A., Kumar S.;
RT   "Copper, zinc superoxide dismutase [Arabidopsis thaliana].";
RL   Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11130712; DOI=10.1038/35048500;
RA   Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S.,
RA   White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y.,
RA   Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W.,
RA   Chung M.K., Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K.,
RA   Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y.,
RA   Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L.,
RA   Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E.,
RA   Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B.,
RA   Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P.,
RA   Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A.,
RA   Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I.,
RA   Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D.,
RA   Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M.,
RA   Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA   Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M.,
RA   Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT   "Sequence and analysis of chromosome 1 of the plant Arabidopsis
RT   thaliana.";
RL   Nature 408:816-820(2000).
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
RT   reference 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.,
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   [6]
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   [7]
RP   TISSUE SPECIFICITY, INDUCTION BY LIGHT; UV-B AND OZONE, AND GENE
RP   FAMILY.
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   [8]
RP   INTERACTION WITH CCS.
RX   PubMed=16126858; DOI=10.1104/pp.105.065284;
RA   Chu C.C., Lee W.C., Guo W.Y., Pan S.M., Chen L.J., Li H.M., Jinn T.L.;
RT   "A copper chaperone for superoxide dismutase that confers three types
RT   of copper/zinc superoxide dismutase activity in Arabidopsis.";
RL   Plant Physiol. 139:425-436(2005).
RN   [9]
RP   TISSUE SPECIFICITY, AND INDUCTION BY OXIDATIVE STRESS.
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
RT   in Arabidopsis is mediated by downregulation of miR398 and important
RT   for oxidative stress tolerance.";
RL   Plant Cell 18:2051-2065(2006).
RN   [10]
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   [11]
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
RT   superoxide dismutases.";
RL   Plant Mol. Biol. 67:403-417(2008).
RN   [12]
RP   SUBCELLULAR LOCATION, AND INTERACTION WITH DJ1A.
RX   PubMed=20406884; DOI=10.1242/jcs.063222;
RA   Xu X.M., Lin H., Maple J., Bjoerkblom B., Alves G., Larsen J.P.,
RA   Moeller S.G.;
RT   "The Arabidopsis DJ-1a protein confers stress protection through
RT   cytosolic SOD activation.";
RL   J. Cell Sci. 123:1644-1651(2010).
CC   -!- FUNCTION: Destroys radicals which are normally produced within the
CC       cells and which are toxic to biological systems.
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. Interacts with DJ1A and CCS.
CC       {ECO:0000269|PubMed:16126858, ECO:0000269|PubMed:20406884}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC       {ECO:0000269|PubMed:20406884}. Nucleus
CC       {ECO:0000269|PubMed:20406884}.
CC   -!- TISSUE SPECIFICITY: Expressed in leaves (at protein level). The
CC       spatial localization is regulated by miR398-mediated silencing.
CC       Mostly present in flowers, old rosette leaves and inflorescence,
CC       and, to a lower 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.
CC       light fluence) increase and UV-B treatment. Accumulates in
CC       response to ozone fumigation. Induced in response to oxidative
CC       stress, via a reduction of miR398-mediated silencing. Repressed by
CC       sucrose in a miR398-mediated silencing-dependent manner. Induced
CC       by salt stress. {ECO:0000269|PubMed:16861386,
CC       ECO:0000269|PubMed:18275461, ECO:0000269|PubMed:18392778,
CC       ECO:0000269|PubMed:9765550}.
CC   -!- SIMILARITY: Belongs to the Cu-Zn superoxide dismutase family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAF99769.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
DR   EMBL; X60935; CAA43270.1; -; mRNA.
DR   EMBL; EF408820; ABN50366.1; -; mRNA.
DR   EMBL; AC003981; AAF99769.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002684; AEE28354.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE28355.1; -; Genomic_DNA.
DR   EMBL; AY091168; AAM14107.1; -; mRNA.
DR   EMBL; AY050932; AAK93609.1; -; mRNA.
DR   EMBL; AY087273; AAM64826.1; -; mRNA.
DR   PIR; S19117; DSMUZ.
DR   RefSeq; NP_001077494.1; NM_001084025.1.
DR   RefSeq; NP_172360.1; NM_100757.4.
DR   UniGene; At.25177; -.
DR   ProteinModelPortal; P24704; -.
DR   SMR; P24704; -.
DR   BioGrid; 22646; 5.
DR   IntAct; P24704; 1.
DR   STRING; 3702.AT1G08830.1; -.
DR   PaxDb; P24704; -.
DR   PRIDE; P24704; -.
DR   EnsemblPlants; AT1G08830.1; AT1G08830.1; AT1G08830.
DR   EnsemblPlants; AT1G08830.2; AT1G08830.2; AT1G08830.
DR   GeneID; 837405; -.
DR   Gramene; AT1G08830.1; AT1G08830.1; AT1G08830.
DR   Gramene; AT1G08830.2; AT1G08830.2; AT1G08830.
DR   KEGG; ath:AT1G08830; -.
DR   Araport; AT1G08830; -.
DR   TAIR; locus:2025595; AT1G08830.
DR   eggNOG; KOG0441; Eukaryota.
DR   eggNOG; COG2032; LUCA.
DR   HOGENOM; HOG000263447; -.
DR   InParanoid; P24704; -.
DR   KO; K04565; -.
DR   OMA; HKGDIGN; -.
DR   OrthoDB; 1574423at2759; -.
DR   PhylomeDB; P24704; -.
DR   BioCyc; ARA:AT1G08830-MONOMER; -.
DR   BioCyc; MetaCyc:AT1G08830-MONOMER; -.
DR   Reactome; R-ATH-114608; Platelet degranulation.
DR   Reactome; R-ATH-3299685; Detoxification of Reactive Oxygen Species.
DR   PRO; PR:P24704; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; P24704; baseline and differential.
DR   Genevisible; P24704; AT.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
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:0016532; F:superoxide dismutase copper chaperone activity; IBA:GO_Central.
DR   GO; GO:0008270; F:zinc ion binding; IBA:GO_Central.
DR   GO; GO:0071280; P:cellular response to copper ion; IEP:TAIR.
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:0042742; P:defense response to bacterium; IEP:TAIR.
DR   GO; GO:0035195; P:gene silencing by miRNA; 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; TAS:TAIR.
DR   GO; GO:0010193; P:response to ozone; IEP: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; Complete proteome; Copper; Cytoplasm; Disulfide bond;
KW   Metal-binding; Nucleus; Oxidoreductase; Reference proteome; Zinc.
FT   CHAIN         1    152       Superoxide dismutase [Cu-Zn] 1.
FT                                /FTId=PRO_0000164131.
FT   METAL        45     45       Copper; catalytic. {ECO:0000250}.
FT   METAL        47     47       Copper; catalytic. {ECO:0000250}.
FT   METAL        62     62       Copper; catalytic. {ECO:0000250}.
FT   METAL        62     62       Zinc; structural. {ECO:0000250}.
FT   METAL        70     70       Zinc; structural. {ECO:0000250}.
FT   METAL        79     79       Zinc; structural. {ECO:0000250}.
FT   METAL        82     82       Zinc; structural. {ECO:0000250}.
FT   METAL       119    119       Copper; catalytic. {ECO:0000250}.
FT   DISULFID     56    145       {ECO:0000250}.
FT   CONFLICT    148    148       I -> F (in Ref. 2; ABN50366).
FT                                {ECO:0000305}.
SQ   SEQUENCE   152 AA;  15098 MW;  59E01FF9794F34BD CRC64;
     MAKGVAVLNS SEGVTGTIFF TQEGDGVTTV SGTVSGLKPG LHGFHVHALG DTTNGCMSTG
     PHFNPDGKTH GAPEDANRHA GDLGNITVGD DGTATFTITD CQIPLTGPNS IVGRAVVVHA
     DPDDLGKGGH ELSLATGNAG GRVACGIIGL QG
//
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