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Superoxide dismutase [Cu-Zn] 1 (EC 1.15.1.1) (Copper/zinc superoxide dismutase 1)

 SODC1_ARATH             Reviewed;         152 AA.
P24704; A3FMJ0; Q9FRQ6;
01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 2.
23-MAY-2018, entry version 159.
RecName: Full=Superoxide dismutase [Cu-Zn] 1;
EC=1.15.1.1;
AltName: Full=Copper/zinc superoxide dismutase 1;
Name=CSD1; Synonyms=SODCC; OrderedLocusNames=At1g08830;
ORFNames=F22O13.32;
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=cv. Columbia; TISSUE=Leaf, and Stem;
PubMed=1731963; DOI=10.1007/BF00018463;
Hindges R., Slusarenko A.J.;
"cDNA and derived amino acid sequence of a cytosolic Cu,Zn superoxide
dismutase from Arabidopsis thaliana (L.) Heyhn.";
Plant Mol. Biol. 18:123-125(1992).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=cv. Columbia;
Rani A., Kumar S.;
"Copper, zinc superoxide dismutase [Arabidopsis thaliana].";
Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=11130712; DOI=10.1038/35048500;
Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S.,
White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y.,
Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W.,
Chung M.K., Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K.,
Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y.,
Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L.,
Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E.,
Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B.,
Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P.,
Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A.,
Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I.,
Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D.,
Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M.,
Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M.,
Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.;
"Sequence and analysis of chromosome 1 of the plant Arabidopsis
thaliana.";
Nature 408:816-820(2000).
[4]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
PubMed=27862469; DOI=10.1111/tpj.13415;
Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
Town C.D.;
"Araport11: a complete reannotation of the Arabidopsis thaliana
reference genome.";
Plant J. 89:789-804(2017).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
PubMed=14593172; DOI=10.1126/science.1088305;
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
"Empirical analysis of transcriptional activity in the Arabidopsis
genome.";
Science 302:842-846(2003).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
Feldmann K.A.;
"Full-length cDNA from Arabidopsis thaliana.";
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
[7]
TISSUE SPECIFICITY, INDUCTION BY LIGHT; UV-B AND OZONE, AND GENE
FAMILY.
PubMed=9765550; DOI=10.1104/pp.118.2.637;
Kliebenstein D.J., Monde R.A., Last R.L.;
"Superoxide dismutase in Arabidopsis: an eclectic enzyme family with
disparate regulation and protein localization.";
Plant Physiol. 118:637-650(1998).
[8]
INTERACTION WITH CCS.
PubMed=16126858; DOI=10.1104/pp.105.065284;
Chu C.C., Lee W.C., Guo W.Y., Pan S.M., Chen L.J., Li H.M., Jinn T.L.;
"A copper chaperone for superoxide dismutase that confers three types
of copper/zinc superoxide dismutase activity in Arabidopsis.";
Plant Physiol. 139:425-436(2005).
[9]
TISSUE SPECIFICITY, AND INDUCTION BY OXIDATIVE STRESS.
PubMed=16861386; DOI=10.1105/tpc.106.041673;
Sunkar R., Kapoor A., Zhu J.-K.;
"Posttranscriptional induction of two Cu/Zn superoxide dismutase genes
in Arabidopsis is mediated by downregulation of miR398 and important
for oxidative stress tolerance.";
Plant Cell 18:2051-2065(2006).
[10]
INDUCTION BY SALT.
STRAIN=cv. Columbia;
PubMed=18275461; DOI=10.1111/j.1399-3054.2007.01009.x;
Attia H., Arnaud N., Karray N., Lachaal M.;
"Long-term effects of mild salt stress on growth, ion accumulation and
superoxide dismutase expression of Arabidopsis rosette leaves.";
Physiol. Plantarum 132:293-305(2008).
[11]
INDUCTION BY SUCROSE.
STRAIN=cv. Columbia;
PubMed=18392778; DOI=10.1007/s11103-008-9329-1;
Dugas D.V., Bartel B.;
"Sucrose induction of Arabidopsis miR398 represses two Cu/Zn
superoxide dismutases.";
Plant Mol. Biol. 67:403-417(2008).
[12]
SUBCELLULAR LOCATION, AND INTERACTION WITH DJ1A.
PubMed=20406884; DOI=10.1242/jcs.063222;
Xu X.M., Lin H., Maple J., Bjoerkblom B., Alves G., Larsen J.P.,
Moeller S.G.;
"The Arabidopsis DJ-1a protein confers stress protection through
cytosolic SOD activation.";
J. Cell Sci. 123:1644-1651(2010).
-!- FUNCTION: Destroys radicals which are normally produced within the
cells and which are toxic to biological systems.
-!- CATALYTIC ACTIVITY: 2 superoxide + 2 H(+) = O(2) + H(2)O(2).
-!- COFACTOR:
Name=Cu cation; Xref=ChEBI:CHEBI:23378; Evidence={ECO:0000250};
Note=Binds 1 copper ion per subunit. {ECO:0000250};
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
Note=Binds 1 zinc ion per subunit. {ECO:0000250};
-!- SUBUNIT: Homodimer. Interacts with DJ1A and CCS.
{ECO:0000269|PubMed:16126858, ECO:0000269|PubMed:20406884}.
-!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
{ECO:0000269|PubMed:20406884}. Nucleus
{ECO:0000269|PubMed:20406884}.
-!- TISSUE SPECIFICITY: Expressed in leaves (at protein level). The
spatial localization is regulated by miR398-mediated silencing.
Mostly present in flowers, old rosette leaves and inflorescence,
and, to a lower extent, in cauline leaves, stems and roots.
{ECO:0000269|PubMed:16861386, ECO:0000269|PubMed:9765550}.
-!- INDUCTION: Upon photosynthetically active radiation (PAR) (e.g.
light fluence) increase and UV-B treatment. Accumulates in
response to ozone fumigation. Induced in response to oxidative
stress, via a reduction of miR398-mediated silencing. Repressed by
sucrose in a miR398-mediated silencing-dependent manner. Induced
by salt stress. {ECO:0000269|PubMed:16861386,
ECO:0000269|PubMed:18275461, ECO:0000269|PubMed:18392778,
ECO:0000269|PubMed:9765550}.
-!- SIMILARITY: Belongs to the Cu-Zn superoxide dismutase family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAF99769.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; X60935; CAA43270.1; -; mRNA.
EMBL; EF408820; ABN50366.1; -; mRNA.
EMBL; AC003981; AAF99769.1; ALT_SEQ; Genomic_DNA.
EMBL; CP002684; AEE28354.1; -; Genomic_DNA.
EMBL; CP002684; AEE28355.1; -; Genomic_DNA.
EMBL; AY091168; AAM14107.1; -; mRNA.
EMBL; AY050932; AAK93609.1; -; mRNA.
EMBL; AY087273; AAM64826.1; -; mRNA.
PIR; S19117; DSMUZ.
RefSeq; NP_001077494.1; NM_001084025.1.
RefSeq; NP_172360.1; NM_100757.4.
UniGene; At.25177; -.
ProteinModelPortal; P24704; -.
SMR; P24704; -.
BioGrid; 22646; 5.
IntAct; P24704; 1.
STRING; 3702.AT1G08830.1; -.
PaxDb; P24704; -.
PRIDE; P24704; -.
EnsemblPlants; AT1G08830.1; AT1G08830.1; AT1G08830.
EnsemblPlants; AT1G08830.2; AT1G08830.2; AT1G08830.
GeneID; 837405; -.
Gramene; AT1G08830.1; AT1G08830.1; AT1G08830.
Gramene; AT1G08830.2; AT1G08830.2; AT1G08830.
KEGG; ath:AT1G08830; -.
Araport; AT1G08830; -.
TAIR; locus:2025595; AT1G08830.
eggNOG; KOG0441; Eukaryota.
eggNOG; COG2032; LUCA.
HOGENOM; HOG000263447; -.
InParanoid; P24704; -.
KO; K04565; -.
OMA; HKGDIGN; -.
OrthoDB; EOG09360P4O; -.
PhylomeDB; P24704; -.
BioCyc; ARA:AT1G08830-MONOMER; -.
BioCyc; MetaCyc:AT1G08830-MONOMER; -.
Reactome; R-ATH-114608; Platelet degranulation.
Reactome; R-ATH-3299685; Detoxification of Reactive Oxygen Species.
PRO; PR:P24704; -.
Proteomes; UP000006548; Chromosome 1.
ExpressionAtlas; P24704; differential.
Genevisible; P24704; AT.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:0005615; C:extracellular space; IBA:GO_Central.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0005507; F:copper ion binding; IBA:GO_Central.
GO; GO:0004784; F:superoxide dismutase activity; TAS:TAIR.
GO; GO:0008270; F:zinc ion binding; IBA:GO_Central.
GO; GO:0071280; P:cellular response to copper ion; IEP:TAIR.
GO; GO:0071484; P:cellular response to light intensity; IEP:UniProtKB.
GO; GO:0034599; P:cellular response to oxidative stress; IEP:UniProtKB.
GO; GO:0071457; P:cellular response to ozone; IEP:UniProtKB.
GO; GO:0071472; P:cellular response to salt stress; IEP:UniProtKB.
GO; GO:0071329; P:cellular response to sucrose stimulus; IEP:UniProtKB.
GO; GO:0071493; P:cellular response to UV-B; IEP:UniProtKB.
GO; GO:0042742; P:defense response to bacterium; IEP:TAIR.
GO; GO:0035195; P:gene silencing by miRNA; IEP:UniProtKB.
GO; GO:0046688; P:response to copper ion; IEP:TAIR.
GO; GO:0010039; P:response to iron ion; IEP:TAIR.
GO; GO:0006979; P:response to oxidative stress; TAS:TAIR.
GO; GO:0010193; P:response to ozone; IEP:TAIR.
GO; GO:0009651; P:response to salt stress; IEP:TAIR.
CDD; cd00305; Cu-Zn_Superoxide_Dismutase; 1.
Gene3D; 2.60.40.200; -; 1.
InterPro; IPR036423; SOD-like_Cu/Zn_dom_sf.
InterPro; IPR024134; SOD_Cu/Zn_/chaperone.
InterPro; IPR018152; SOD_Cu/Zn_BS.
InterPro; IPR001424; SOD_Cu_Zn_dom.
PANTHER; PTHR10003; PTHR10003; 1.
Pfam; PF00080; Sod_Cu; 1.
PRINTS; PR00068; CUZNDISMTASE.
SUPFAM; SSF49329; SSF49329; 1.
PROSITE; PS00087; SOD_CU_ZN_1; 1.
PROSITE; PS00332; SOD_CU_ZN_2; 1.
1: Evidence at protein level;
Antioxidant; Complete proteome; Copper; Cytoplasm; Disulfide bond;
Metal-binding; Nucleus; Oxidoreductase; Reference proteome; Zinc.
CHAIN 1 152 Superoxide dismutase [Cu-Zn] 1.
/FTId=PRO_0000164131.
METAL 45 45 Copper; catalytic. {ECO:0000250}.
METAL 47 47 Copper; catalytic. {ECO:0000250}.
METAL 62 62 Copper; catalytic. {ECO:0000250}.
METAL 62 62 Zinc; structural. {ECO:0000250}.
METAL 70 70 Zinc; structural. {ECO:0000250}.
METAL 79 79 Zinc; structural. {ECO:0000250}.
METAL 82 82 Zinc; structural. {ECO:0000250}.
METAL 119 119 Copper; catalytic. {ECO:0000250}.
DISULFID 56 145 {ECO:0000250}.
CONFLICT 148 148 I -> F (in Ref. 2; ABN50366).
{ECO:0000305}.
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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