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Protein

Superoxide dismutase [Cu-Zn] 1

Gene

CSD1

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Destroys radicals which are normally produced within the cells and which are toxic to biological systems.

Catalytic activityi

2 superoxide + 2 H+ = O2 + H2O2.

Cofactori

Protein has several cofactor binding sites:
  • Cu cationBy similarityNote: Binds 1 copper ion per subunit.By similarity
  • Zn2+By similarityNote: Binds 1 zinc ion per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi45 – 451Copper; catalyticBy similarity
Metal bindingi47 – 471Copper; catalyticBy similarity
Metal bindingi62 – 621Copper; catalyticBy similarity
Metal bindingi62 – 621Zinc; structuralBy similarity
Metal bindingi70 – 701Zinc; structuralBy similarity
Metal bindingi79 – 791Zinc; structuralBy similarity
Metal bindingi82 – 821Zinc; structuralBy similarity
Metal bindingi119 – 1191Copper; catalyticBy similarity

GO - Molecular functioni

  • copper ion binding Source: GO_Central
  • superoxide dismutase activity Source: TAIR
  • zinc ion binding Source: GO_Central

GO - Biological processi

  • cellular response to copper ion Source: TAIR
  • cellular response to light intensity Source: UniProtKB
  • cellular response to oxidative stress Source: UniProtKB
  • cellular response to ozone Source: UniProtKB
  • cellular response to salt stress Source: UniProtKB
  • cellular response to sucrose stimulus Source: UniProtKB
  • cellular response to UV-B Source: UniProtKB
  • defense response to bacterium Source: TAIR
  • gene silencing by miRNA Source: UniProtKB
  • removal of superoxide radicals Source: GOC
  • response to copper ion Source: TAIR
  • response to iron ion Source: TAIR
  • response to oxidative stress Source: TAIR
  • response to ozone Source: TAIR
  • response to salt stress Source: TAIR
Complete GO annotation...

Keywords - Molecular functioni

Antioxidant, Oxidoreductase

Keywords - Ligandi

Copper, Metal-binding, Zinc

Enzyme and pathway databases

BioCyciARA:AT1G08830-MONOMER.
ARA:GQT-656-MONOMER.
MetaCyc:AT1G08830-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Superoxide dismutase [Cu-Zn] 1 (EC:1.15.1.1)
Alternative name(s):
Copper/zinc superoxide dismutase 1
Gene namesi
Name:CSD1
Synonyms:SODCC
Ordered Locus Names:At1g08830
ORF Names:F22O13.32
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548 Componenti: Chromosome 1

Organism-specific databases

TAIRiAT1G08830.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: GO_Central
  • cytosol Source: UniProtKB
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 152151Superoxide dismutase [Cu-Zn] 1PRO_0000164131Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi56 ↔ 145By similarity

Keywords - PTMi

Disulfide bond

Proteomic databases

PaxDbiP24704.
PRIDEiP24704.

Expressioni

Tissue specificityi

Expressed in leaves and pollen (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.3 Publications

Inductioni

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.4 Publications

Interactioni

Subunit structurei

Homodimer. Interacts with DJ1A and CCS.2 Publications

Protein-protein interaction databases

BioGridi22646. 4 interactions.
IntActiP24704. 1 interaction.
STRINGi3702.AT1G08830.1.

Structurei

3D structure databases

ProteinModelPortaliP24704.
SMRiP24704. Positions 1-152.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the Cu-Zn superoxide dismutase family.Curated

Phylogenomic databases

eggNOGiCOG2032.
HOGENOMiHOG000263447.
InParanoidiP24704.
KOiK04565.
OMAiKVWGSIT.
PhylomeDBiP24704.

Family and domain databases

Gene3Di2.60.40.200. 1 hit.
InterProiIPR018152. SOD_Cu/Zn_BS.
IPR001424. SOD_Cu_Zn_dom.
[Graphical view]
PfamiPF00080. Sod_Cu. 1 hit.
[Graphical view]
PRINTSiPR00068. CUZNDISMTASE.
SUPFAMiSSF49329. SSF49329. 1 hit.
PROSITEiPS00087. SOD_CU_ZN_1. 1 hit.
PS00332. SOD_CU_ZN_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P24704-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAKGVAVLNS SEGVTGTIFF TQEGDGVTTV SGTVSGLKPG LHGFHVHALG
60 70 80 90 100
DTTNGCMSTG PHFNPDGKTH GAPEDANRHA GDLGNITVGD DGTATFTITD
110 120 130 140 150
CQIPLTGPNS IVGRAVVVHA DPDDLGKGGH ELSLATGNAG GRVACGIIGL

QG
Length:152
Mass (Da):15,098
Last modified:January 23, 2007 - v2
Checksum:i59E01FF9794F34BD
GO

Sequence cautioni

The sequence AAF99769.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti148 – 1481I → F in ABN50366 (Ref. 2) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X60935 mRNA. Translation: CAA43270.1.
EF408820 mRNA. Translation: ABN50366.1.
AC003981 Genomic DNA. Translation: AAF99769.1. Sequence problems.
CP002684 Genomic DNA. Translation: AEE28354.1.
CP002684 Genomic DNA. Translation: AEE28355.1.
AY091168 mRNA. Translation: AAM14107.1.
AY050932 mRNA. Translation: AAK93609.1.
AY087273 mRNA. Translation: AAM64826.1.
PIRiS19117. DSMUZ.
RefSeqiNP_001077494.1. NM_001084025.1.
NP_172360.1. NM_100757.3.
UniGeneiAt.25177.

Genome annotation databases

EnsemblPlantsiAT1G08830.1; AT1G08830.1; AT1G08830.
AT1G08830.2; AT1G08830.2; AT1G08830.
GeneIDi837405.
KEGGiath:AT1G08830.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X60935 mRNA. Translation: CAA43270.1.
EF408820 mRNA. Translation: ABN50366.1.
AC003981 Genomic DNA. Translation: AAF99769.1. Sequence problems.
CP002684 Genomic DNA. Translation: AEE28354.1.
CP002684 Genomic DNA. Translation: AEE28355.1.
AY091168 mRNA. Translation: AAM14107.1.
AY050932 mRNA. Translation: AAK93609.1.
AY087273 mRNA. Translation: AAM64826.1.
PIRiS19117. DSMUZ.
RefSeqiNP_001077494.1. NM_001084025.1.
NP_172360.1. NM_100757.3.
UniGeneiAt.25177.

3D structure databases

ProteinModelPortaliP24704.
SMRiP24704. Positions 1-152.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi22646. 4 interactions.
IntActiP24704. 1 interaction.
STRINGi3702.AT1G08830.1.

Proteomic databases

PaxDbiP24704.
PRIDEiP24704.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT1G08830.1; AT1G08830.1; AT1G08830.
AT1G08830.2; AT1G08830.2; AT1G08830.
GeneIDi837405.
KEGGiath:AT1G08830.

Organism-specific databases

TAIRiAT1G08830.

Phylogenomic databases

eggNOGiCOG2032.
HOGENOMiHOG000263447.
InParanoidiP24704.
KOiK04565.
OMAiKVWGSIT.
PhylomeDBiP24704.

Enzyme and pathway databases

BioCyciARA:AT1G08830-MONOMER.
ARA:GQT-656-MONOMER.
MetaCyc:AT1G08830-MONOMER.

Miscellaneous databases

PROiP24704.

Family and domain databases

Gene3Di2.60.40.200. 1 hit.
InterProiIPR018152. SOD_Cu/Zn_BS.
IPR001424. SOD_Cu_Zn_dom.
[Graphical view]
PfamiPF00080. Sod_Cu. 1 hit.
[Graphical view]
PRINTSiPR00068. CUZNDISMTASE.
SUPFAMiSSF49329. SSF49329. 1 hit.
PROSITEiPS00087. SOD_CU_ZN_1. 1 hit.
PS00332. SOD_CU_ZN_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "cDNA and derived amino acid sequence of a cytosolic Cu,Zn superoxide dismutase from Arabidopsis thaliana (L.) Heyhn."
    Hindges R., Slusarenko A.J.
    Plant Mol. Biol. 18:123-125(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: cv. Columbia.
    Tissue: Leaf and Stem.
  2. "Copper, zinc superoxide dismutase [Arabidopsis thaliana]."
    Rani A., Kumar S.
    Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: cv. Columbia.
  3. "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana."
    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.
    Nature 408:816-820(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  4. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  5. "Empirical analysis of transcriptional activity in the Arabidopsis genome."
    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.
    Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  6. "Full-length cDNA from Arabidopsis thaliana."
    Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A.
    Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  7. "Superoxide dismutase in Arabidopsis: an eclectic enzyme family with disparate regulation and protein localization."
    Kliebenstein D.J., Monde R.A., Last R.L.
    Plant Physiol. 118:637-650(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY, INDUCTION BY LIGHT; UV-B AND OZONE, GENE FAMILY.
  8. "A copper chaperone for superoxide dismutase that confers three types of copper/zinc superoxide dismutase activity in Arabidopsis."
    Chu C.C., Lee W.C., Guo W.Y., Pan S.M., Chen L.J., Li H.M., Jinn T.L.
    Plant Physiol. 139:425-436(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CCS.
  9. "Proteome mapping of mature pollen of Arabidopsis thaliana."
    Holmes-Davis R., Tanaka C.K., Vensel W.H., Hurkman W.J., McCormick S.
    Proteomics 5:4864-4884(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY [LARGE SCALE ANALYSIS].
  10. "Posttranscriptional induction of two Cu/Zn superoxide dismutase genes in Arabidopsis is mediated by downregulation of miR398 and important for oxidative stress tolerance."
    Sunkar R., Kapoor A., Zhu J.-K.
    Plant Cell 18:2051-2065(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY, INDUCTION BY OXIDATIVE STRESS.
  11. "Long-term effects of mild salt stress on growth, ion accumulation and superoxide dismutase expression of Arabidopsis rosette leaves."
    Attia H., Arnaud N., Karray N., Lachaal M.
    Physiol. Plantarum 132:293-305(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION BY SALT.
    Strain: cv. Columbia.
  12. "Sucrose induction of Arabidopsis miR398 represses two Cu/Zn superoxide dismutases."
    Dugas D.V., Bartel B.
    Plant Mol. Biol. 67:403-417(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION BY SUCROSE.
    Strain: cv. Columbia.
  13. "The Arabidopsis DJ-1a protein confers stress protection through cytosolic SOD activation."
    Xu X.M., Lin H., Maple J., Bjoerkblom B., Alves G., Larsen J.P., Moeller S.G.
    J. Cell Sci. 123:1644-1651(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, INTERACTION WITH DJ1A.

Entry informationi

Entry nameiSODC1_ARATH
AccessioniPrimary (citable) accession number: P24704
Secondary accession number(s): A3FMJ0, Q9FRQ6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 1, 1992
Last sequence update: January 23, 2007
Last modified: July 22, 2015
This is version 140 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.