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 03-AUG-2022, entry version 179.
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; ORFNames=F22O13.32;
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].
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., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., 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., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis 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 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].
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 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 of
RT 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 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 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 superoxide
RT 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 cytosolic
RT 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 {ECO:0000269|PubMed:20406884}.
CC Nucleus {ECO:0000269|PubMed:20406884}.
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. Induced in response to oxidative stress, via a reduction of
CC miR398-mediated silencing. Repressed by sucrose in a miR398-mediated
CC silencing-dependent manner. Induced by salt stress.
CC {ECO:0000269|PubMed:16861386, ECO:0000269|PubMed:18275461,
CC ECO:0000269|PubMed:18392778, 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};
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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 AlphaFoldDB; P24704; -.
DR SMR; P24704; -.
DR BioGRID; 22646; 5.
DR IntAct; P24704; 1.
DR STRING; 3702.AT1G08830.1; -.
DR PaxDb; P24704; -.
DR PRIDE; P24704; -.
DR ProteomicsDB; 234479; -.
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 HOGENOM; CLU_056632_4_1_1; -.
DR InParanoid; P24704; -.
DR OMA; KWVAFHV; -.
DR OrthoDB; 1574423at2759; -.
DR PhylomeDB; P24704; -.
DR BioCyc; ARA:AT1G08830-MON; -.
DR BioCyc; MetaCyc:AT1G08830-MON; -.
DR BRENDA; 1.15.1.1; 399.
DR PRO; PR:P24704; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; P24704; baseline and differential.
DR Genevisible; P24704; AT.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
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: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: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; 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; Copper; Cytoplasm; Disulfide bond; Metal-binding; Nucleus;
KW Oxidoreductase; Reference proteome; Zinc.
FT CHAIN 1..152
FT /note="Superoxide dismutase [Cu-Zn] 1"
FT /id="PRO_0000164131"
FT BINDING 45
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 47
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 62
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 62
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000250"
FT BINDING 70
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000250"
FT BINDING 79
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000250"
FT BINDING 82
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000250"
FT BINDING 119
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT DISULFID 56..145
FT /evidence="ECO:0000250"
FT CONFLICT 148
FT /note="I -> F (in Ref. 2; ABN50366)"
FT /evidence="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
