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O04996 (SODC_SOLCS) Reviewed, UniProtKB/Swiss-Prot

Last modified March 6, 2013. Version 77. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein attributes

Sequence length153 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript 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.

Subcellular location

Cytoplasm.

Sequence similarities

Belongs to the Cu-Zn superoxide dismutase family.

Ontologies

Keywords
   Cellular componentCytoplasm
   LigandCopper
Metal-binding
Zinc
   Molecular functionAntioxidant
Oxidoreductase
   PTMDisulfide bond
Gene Ontology (GO)
   Biological_processsuperoxide metabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionmetal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

superoxide dismutase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 153152Superoxide dismutase [Cu-Zn]
PRO_0000164155

Sites

Metal binding461Copper; catalytic By similarity
Metal binding481Copper; catalytic By similarity
Metal binding631Copper; catalytic By similarity
Metal binding631Zinc; structural By similarity
Metal binding711Zinc; structural By similarity
Metal binding801Zinc; structural By similarity
Metal binding831Zinc; structural By similarity
Metal binding1201Copper; catalytic By similarity

Amino acid modifications

Disulfide bond57 ↔ 146 By similarity

Sequences

Sequence LengthMass (Da)Tools
O04996 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 1746763A92F42F88

FASTA15315,436
        10         20         30         40         50         60 
MVKAVAVLSS SEGVSGTIFF SQEAEGAPTT VTGDLSGLKP GPHGFHVHAL GDTTNGCMST 

        70         80         90        100        110        120 
GPHYNPHGKD HGAPDDEHRH AGDLGNVTVG EDGTAKFTIV DKQIPLIGAQ SIIGRAVVVH 

       130        140        150 
ADPDDLGKGG HELSKTTGNA GGRVACGIIG LQG 

« Hide

References

[1]"Different transcriptional regulation of cytosolic and plastidic Cu/Zn-superoxide dismutase genes in Solidago altissima (Asteraceae)."
Murai R., Murai K.
Plant Sci. 120:71-79(1996)
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: cv. Nonoichi-Machi.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D49485 mRNA. Translation: BAA19674.1.

3D structure databases

ProteinModelPortalO04996.
SMRO04996. Positions 1-153.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D2.60.40.200. 1 hit.
InterProIPR024134. SOD_Cu/Zn_/chaperones.
IPR018152. SOD_Cu/Zn_BS.
IPR001424. SOD_Cu_Zn_dom.
[Graphical view]
PANTHERPTHR10003. PTHR10003. 1 hit.
PfamPF00080. Sod_Cu. 1 hit.
[Graphical view]
PRINTSPR00068. CUZNDISMTASE.
SUPFAMSSF49329. SOD_Cu_Zn. 1 hit.
PROSITEPS00087. SOD_CU_ZN_1. 1 hit.
PS00332. SOD_CU_ZN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSODC_SOLCS
AccessionPrimary (citable) accession number: O04996
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: January 23, 2007
Last modified: March 6, 2013
This is version 77 of the entry and version 3 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