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P24704 (SODC1_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 128. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Superoxide dismutase [Cu-Zn] 1

EC=1.15.1.1
Alternative name(s):
Copper/zinc superoxide dismutase 1
Gene names
Name:CSD1
Synonyms:SODCC
Ordered Locus Names:At1g08830
ORF Names:F22O13.32
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length152 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Catalytic activity

2 superoxide + 2 H+ = O2 + H2O2.

Cofactor

Binds 1 copper ion per subunit By similarity.

Binds 1 zinc ion per subunit By similarity.

Subunit structure

Homodimer. Interacts with DJ1A and CCS. Ref.8 Ref.13

Subcellular location

Cytoplasmcytosol. Nucleus Ref.13.

Tissue specificity

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. Ref.7 Ref.10

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. Ref.7 Ref.10 Ref.11 Ref.12

Sequence similarities

Belongs to the Cu-Zn superoxide dismutase family.

Sequence caution

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

Ontologies

Keywords
   Cellular componentCytoplasm
Nucleus
   LigandCopper
Metal-binding
Zinc
   Molecular functionAntioxidant
Oxidoreductase
   PTMDisulfide bond
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcellular response to UV-B

Inferred from expression pattern Ref.7. Source: UniProtKB

cellular response to copper ion

Inferred from expression pattern PubMed 21897129. Source: TAIR

cellular response to light intensity

Inferred from expression pattern Ref.7. Source: UniProtKB

cellular response to oxidative stress

Inferred from expression pattern Ref.10. Source: UniProtKB

cellular response to ozone

Inferred from expression pattern Ref.7. Source: UniProtKB

cellular response to salt stress

Inferred from expression pattern Ref.11. Source: UniProtKB

cellular response to sucrose stimulus

Inferred from expression pattern Ref.12. Source: UniProtKB

defense response to bacterium

Inferred from expression pattern PubMed 19148671. Source: TAIR

gene silencing by miRNA

Inferred from expression pattern Ref.10. Source: UniProtKB

removal of superoxide radicals

Inferred from Biological aspect of Ancestor. Source: RefGenome

response to copper ion

Inferred from expression pattern PubMed 15772282. Source: TAIR

response to iron ion

Inferred from expression pattern Ref.10. Source: TAIR

response to oxidative stress

Traceable author statement PubMed 12028573. Source: TAIR

response to ozone

Inferred from expression pattern PubMed 19148671. Source: TAIR

response to salt stress

Inferred from expression pattern PubMed 19148671. Source: TAIR

   Cellular_componentcytosol

Inferred from direct assay Ref.13. Source: UniProtKB

extracellular region

Inferred from Biological aspect of Ancestor. Source: RefGenome

nucleus

Inferred from direct assay Ref.13. Source: UniProtKB

   Molecular_functioncopper ion binding

Inferred from Biological aspect of Ancestor. Source: RefGenome

protein binding

Inferred from physical interaction Ref.13. Source: UniProtKB

superoxide dismutase activity

Traceable author statement Ref.7. Source: TAIR

zinc ion binding

Inferred from Biological aspect of Ancestor. Source: RefGenome

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 152151Superoxide dismutase [Cu-Zn] 1
PRO_0000164131

Sites

Metal binding451Copper; catalytic By similarity
Metal binding471Copper; catalytic By similarity
Metal binding621Copper; catalytic By similarity
Metal binding621Zinc; structural By similarity
Metal binding701Zinc; structural By similarity
Metal binding791Zinc; structural By similarity
Metal binding821Zinc; structural By similarity
Metal binding1191Copper; catalytic By similarity

Amino acid modifications

Disulfide bond56 ↔ 145 By similarity

Experimental info

Sequence conflict1481I → F in ABN50366. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P24704 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 59E01FF9794F34BD

FASTA15215,098
        10         20         30         40         50         60 
MAKGVAVLNS SEGVTGTIFF TQEGDGVTTV SGTVSGLKPG LHGFHVHALG DTTNGCMSTG 

        70         80         90        100        110        120 
PHFNPDGKTH GAPEDANRHA GDLGNITVGD DGTATFTITD CQIPLTGPNS IVGRAVVVHA 

       130        140        150 
DPDDLGKGGH ELSLATGNAG GRVACGIIGL QG 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRDSMUZ. S19117.
RefSeqNP_001077494.1. NM_001084025.1.
NP_172360.1. NM_100757.3.
UniGeneAt.25177.

3D structure databases

ProteinModelPortalP24704.
SMRP24704. Positions 1-152.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid22646. 4 interactions.
IntActP24704. 1 interaction.

Proteomic databases

PaxDbP24704.
PRIDEP24704.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT1G08830.1; AT1G08830.1; AT1G08830.
AT1G08830.2; AT1G08830.2; AT1G08830.
GeneID837405.
KEGGath:AT1G08830.

Organism-specific databases

TAIRAT1G08830.

Phylogenomic databases

eggNOGCOG2032.
HOGENOMHOG000263447.
InParanoidP24704.
KOK04565.
OMAEIEVKLH.
PhylomeDBP24704.

Enzyme and pathway databases

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

Gene expression databases

ArrayExpressP24704.
GenevestigatorP24704.

Family and domain databases

Gene3D2.60.40.200. 1 hit.
InterProIPR018152. SOD_Cu/Zn_BS.
IPR001424. SOD_Cu_Zn_dom.
[Graphical view]
PfamPF00080. Sod_Cu. 1 hit.
[Graphical view]
PRINTSPR00068. CUZNDISMTASE.
SUPFAMSSF49329. SSF49329. 1 hit.
PROSITEPS00087. SOD_CU_ZN_1. 1 hit.
PS00332. SOD_CU_ZN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSODC1_ARATH
AccessionPrimary (citable) accession number: P24704
Secondary accession number(s): A3FMJ0, Q9FRQ6
Entry history
Integrated into UniProtKB/Swiss-Prot: March 1, 1992
Last sequence update: January 23, 2007
Last modified: June 11, 2014
This is version 128 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names