P21276 · SODF1_ARATH
- ProteinSuperoxide dismutase [Fe] 1, chloroplastic
- GeneFSD1
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids212 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems.
Catalytic activity
- 2 H+ + 2 superoxide = H2O2 + O2
Cofactor
Note: Binds 1 Fe cation per subunit.
Activity regulation
Activated by cpn20/cpn21.
Features
Showing features for binding site.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | chloroplast | |
Cellular Component | chloroplast envelope | |
Cellular Component | chloroplast membrane | |
Cellular Component | chloroplast stroma | |
Cellular Component | cytoplasm | |
Cellular Component | cytosol | |
Cellular Component | mitochondrion | |
Cellular Component | plasma membrane | |
Cellular Component | thylakoid | |
Molecular Function | copper ion binding | |
Molecular Function | protein domain specific binding | |
Molecular Function | superoxide dismutase activity | |
Biological Process | circadian rhythm | |
Biological Process | response to cadmium ion | |
Biological Process | response to copper ion | |
Biological Process | response to light intensity | |
Biological Process | response to ozone |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameSuperoxide dismutase [Fe] 1, chloroplastic
- EC number
- Alternative names
Gene names
Organism names
- Strains
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > malvids > Brassicales > Brassicaceae > Camelineae > Arabidopsis
Accessions
- Primary accessionP21276
- Secondary accessions
Proteomes
Organism-specific databases
Genome annotation databases
Subcellular Location
UniProt Annotation
GO Annotation
Keywords
- Cellular component
PTM/Processing
Features
Showing features for chain, initiator methionine, transit peptide, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000032889 | ?-212 | Superoxide dismutase [Fe] 1, chloroplastic | |||
Sequence: MAASSAVTANYVLKPPPFALDALEPHMSKQTLEFHWGKHHRAYVDNLKKQVLGTELEGKPLEHIIHSTYNNGDLLPAFNNAAQAWNHEFFWESMKPGGGGKPSGELLALLERDFTSYEKFYEEFNAAAATQFGAGWAWLAYSNEKLKVVKTPNAVNPLVLGSFPLLTIDVWEHAYYLDFQNRRPDYIKTFMTNLVSWEAVSARLEAAKAASA | ||||||
Initiator methionine | 1 | Removed | ||||
Sequence: M | ||||||
Transit peptide | 2-? | Chloroplast | ||||
Sequence: M | ||||||
Modified residue | 2 | N-acetylalanine | ||||
Sequence: A |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Induction
Circadian-regulation. Down-regulated upon photosynthetically active radiation (PAR) (e.g. light fluence) increase and in response to ozone fumigation.
Gene expression databases
Structure
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
This entry describes 1 isoforms produced by Alternative splicing. A number of isoforms are produced. According to EST sequences.
P21276-1
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.
- Name1
- Length212
- Mass (Da)23,791
- Last updated2003-12-15 v4
- ChecksumBCFDA057F040F9DD
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
F4JRV2 | F4JRV2_ARATH | FSD1 | 186 |
Sequence caution
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
M55910 EMBL· GenBank· DDBJ | AAA32791.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AL035523 EMBL· GenBank· DDBJ | CAB36752.1 EMBL· GenBank· DDBJ | Genomic DNA | Sequence problems. | |
AL161562 EMBL· GenBank· DDBJ | CAB79419.1 EMBL· GenBank· DDBJ | Genomic DNA | Sequence problems. | |
CP002687 EMBL· GenBank· DDBJ | AEE85007.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CP002687 EMBL· GenBank· DDBJ | AEE85008.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CP002687 EMBL· GenBank· DDBJ | AEE85009.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CP002687 EMBL· GenBank· DDBJ | AEE85011.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF326862 EMBL· GenBank· DDBJ | AAG41444.1 EMBL· GenBank· DDBJ | mRNA | ||
AF324711 EMBL· GenBank· DDBJ | AAG40062.1 EMBL· GenBank· DDBJ | mRNA | ||
AF339685 EMBL· GenBank· DDBJ | AAK00367.1 EMBL· GenBank· DDBJ | mRNA | ||
AY039560 EMBL· GenBank· DDBJ | AAK62615.1 EMBL· GenBank· DDBJ | mRNA | ||
AY129470 EMBL· GenBank· DDBJ | AAM91056.1 EMBL· GenBank· DDBJ | mRNA | ||
AY087220 EMBL· GenBank· DDBJ | AAM64776.1 EMBL· GenBank· DDBJ | mRNA |