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Q9FK60 (SODC3_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 97. 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·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Superoxide dismutase [Cu-Zn] 3

EC=1.15.1.1
Alternative name(s):
Copper/zinc superoxide dismutase 3
Gene names
Name:CSD3
Ordered Locus Names:At5g18100
ORF Names:MRG7.6
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length164 AA.
Sequence statusComplete.
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 By similarity.

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 By similarity.

Subcellular location

Peroxisome Ref.5 Ref.6.

Tissue specificity

Expressed in leaves (at protein level). Ref.5

Induction

Upon photosynthetically active radiation (PAR) (e.g. light fluence) increase or after high-light pulse, and UV-B treatment. Accumulates in response to ozone fumigation, during recovery. Repressed by salt stress. Ref.5 Ref.7

Sequence similarities

Belongs to the Cu-Zn superoxide dismutase family.

Ontologies

Keywords
   Cellular componentPeroxisome
   Coding sequence diversityAlternative splicing
   LigandCopper
Metal-binding
Zinc
   Molecular functionAntioxidant
Oxidoreductase
   PTMDisulfide bond
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processcellular response to UV-B

Inferred from expression pattern Ref.5. Source: UniProtKB

cellular response to high light intensity

Inferred from expression pattern Ref.5. Source: UniProtKB

cellular response to light intensity

Inferred from expression pattern Ref.5. Source: UniProtKB

cellular response to ozone

Inferred from expression pattern Ref.5. Source: UniProtKB

cellular response to salt stress

Inferred from expression pattern Ref.7. Source: UniProtKB

oxidation-reduction process

Inferred from Biological aspect of Ancestor. Source: RefGenome

removal of superoxide radicals

Inferred from Biological aspect of Ancestor. Source: RefGenome

response to oxidative stress

Traceable author statement Ref.5. Source: TAIR

   Cellular_componentextracellular region

Inferred from Biological aspect of Ancestor. Source: RefGenome

peroxisome

Inferred from direct assay Ref.6. Source: TAIR

vacuole

Inferred from direct assay PubMed 15539469. Source: TAIR

   Molecular_functioncopper ion binding

Inferred from Biological aspect of Ancestor. Source: RefGenome

superoxide dismutase activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

zinc ion binding

Inferred from Biological aspect of Ancestor. Source: RefGenome

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9FK60-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q9FK60-2)

The sequence of this isoform differs from the canonical sequence as follows:
     135-137: GHK → TKH
     138-164: Missing.
Note: Derived from EST data. No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 164164Superoxide dismutase [Cu-Zn] 3
PRO_0000419143

Regions

Motif162 – 1643Peroxisome localization signal By similarity

Sites

Metal binding511Copper; catalytic By similarity
Metal binding531Copper; catalytic By similarity
Metal binding681Copper; catalytic By similarity
Metal binding681Zinc; structural By similarity
Metal binding761Zinc; structural By similarity
Metal binding851Zinc; structural By similarity
Metal binding881Zinc; structural By similarity
Metal binding1251Copper; catalytic By similarity

Amino acid modifications

Disulfide bond62 ↔ 151 By similarity

Natural variations

Alternative sequence135 – 1373GHK → TKH in isoform 2.
VSP_044111
Alternative sequence138 – 16427Missing in isoform 2.
VSP_044112

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: A80B9F4A79D0F365

FASTA16416,941
        10         20         30         40         50         60 
MEAPRGNLRA VALIAGDNNV RGCLQFVQDI SGTTHVTGKI SGLSPGFHGF HIHSFGDTTN 

        70         80         90        100        110        120 
GCISTGPHFN PLNRVHGPPN EEERHAGDLG NILAGSNGVA EILIKDKHIP LSGQYSILGR 

       130        140        150        160 
AVVVHADPDD LGKGGHKLSK STGNAGSRVG CGIIGLQSSA DAKL 

« Hide

Isoform 2 [UniParc].

Checksum: BBD55B91BCC424BD
Show »

FASTA13714,412

References

« Hide 'large scale' references
[1]"Structural analysis of Arabidopsis thaliana chromosome 5. VI. Sequence features of the regions of 1,367,185 bp covered by 19 physically assigned P1 and TAC clones."
Kotani H., Nakamura Y., Sato S., Asamizu E., Kaneko T., Miyajima N., Tabata S.
DNA Res. 5:203-216(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[2]The Arabidopsis Information Resource (TAIR)
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: cv. Columbia.
[3]"Functional annotation of a full-length Arabidopsis cDNA collection."
Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T., Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y., Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K., Shinagawa A., Shinozaki K.
Science 296:141-145(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Strain: cv. Columbia.
[4]"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] (ISOFORM 1).
Strain: cv. Columbia.
[5]"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: NUCLEOTIDE SEQUENCE [MRNA] OF 3-164 (ISOFORM 1), TISSUE SPECIFICITY, SUBCELLULAR LOCATION, INDUCTION BY LIGHT; UV-B AND OZONE, GENE FAMILY.
Strain: cv. Columbia.
[6]"Proteome analysis of Arabidopsis leaf peroxisomes reveals novel targeting peptides, metabolic pathways, and defense mechanisms."
Reumann S., Babujee L., Ma C., Wienkoop S., Siemsen T., Antonicelli G.E., Rasche N., Lueder F., Weckwerth W., Jahn O.
Plant Cell 19:3170-3193(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 85-105 AND 108-120, SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[7]"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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF061520 mRNA. Translation: AAC24833.1.
AB012246 Genomic DNA. Translation: BAB09468.1.
CP002688 Genomic DNA. Translation: AED92506.1.
CP002688 Genomic DNA. Translation: AED92507.1.
AK117742 mRNA. Translation: BAC42391.1.
BT003689 mRNA. Translation: AAO39917.1.
PIRT51731.
RefSeqNP_001119245.1. NM_001125773.1. [Q9FK60-2]
NP_197311.1. NM_121815.3. [Q9FK60-1]
UniGeneAt.49035.
At.7547.

3D structure databases

ProteinModelPortalQ9FK60.
SMRQ9FK60. Positions 9-157.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ9FK60. 1 interaction.
STRING3702.AT5G18100.1-P.

Proteomic databases

PRIDEQ9FK60.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT5G18100.1; AT5G18100.1; AT5G18100. [Q9FK60-1]
GeneID831928.
KEGGath:AT5G18100.

Organism-specific databases

TAIRAT5G18100.

Phylogenomic databases

eggNOGCOG2032.
HOGENOMHOG000263447.
InParanoidQ9FK60.
KOK04565.
OMAEEERHAG.
PhylomeDBQ9FK60.

Gene expression databases

GenevestigatorQ9FK60.

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.
PROSITEPS00332. SOD_CU_ZN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSODC3_ARATH
AccessionPrimary (citable) accession number: Q9FK60
Secondary accession number(s): B3H6P9, O81236
Entry history
Integrated into UniProtKB/Swiss-Prot: October 3, 2012
Last sequence update: March 1, 2001
Last modified: June 11, 2014
This is version 97 of the entry and version 1 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