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P28757 (SODC2_ORYSJ) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 105. 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] 2

EC=1.15.1.1
Gene names
Name:SODCC2
Synonyms:SODCC.2
Ordered Locus Names:Os07g0665200, LOC_Os07g46990
ORF Names:OJ1343_D04.132, P0450A04.103
OrganismOryza sativa subsp. japonica (Rice) [Reference proteome]
Taxonomic identifier39947 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaPoalesPoaceaeBEP cladeEhrhartoideaeOryzeaeOryza

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.

Subcellular location

Cytoplasm.

Sequence similarities

Belongs to the Cu-Zn superoxide dismutase family.

Sequence caution

The sequence BAC10110.1 differs from that shown. Reason: Erroneous gene model prediction.

The sequence BAD30565.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
   Cellular componentCytoplasm
   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 electronic annotation. Source: EnsemblPlants/Gramene

cellular response to copper ion

Inferred from electronic annotation. Source: EnsemblPlants/Gramene

cellular response to light intensity

Inferred from electronic annotation. Source: EnsemblPlants/Gramene

cellular response to ozone

Inferred from electronic annotation. Source: EnsemblPlants/Gramene

cellular response to salt stress

Inferred from electronic annotation. Source: EnsemblPlants/Gramene

cellular response to sucrose stimulus

Inferred from electronic annotation. Source: EnsemblPlants/Gramene

defense response to bacterium

Inferred from electronic annotation. Source: EnsemblPlants/Gramene

gene silencing by miRNA

Inferred from electronic annotation. Source: EnsemblPlants/Gramene

removal of superoxide radicals

Inferred from Biological aspect of Ancestor. Source: RefGenome

response to iron ion

Inferred from electronic annotation. Source: EnsemblPlants/Gramene

   Cellular_componentcytoplasm

Inferred from Biological aspect of Ancestor. Source: RefGenome

   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...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.4
Chain2 – 152151Superoxide dismutase [Cu-Zn] 2
PRO_0000164149

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

Sequences

Sequence LengthMass (Da)Tools
P28757 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 8D237FCABFE6EDBE

FASTA15215,081
        10         20         30         40         50         60 
MVKAVAVLAS SEGVKGTIFF SQEGDGPTSV TGSVSGLKPG LHGFHVHALG DTTNGCMSTG 

        70         80         90        100        110        120 
PHFNPTGKEH GAPQDENRHA GDLGNITAGA DGVANVNVSD SQIPLTGAHS IIGRAVVVHA 

       130        140        150 
DPDDLGKGGH ELSKTTGNAG GRVACGIIGL QG 

« Hide

References

« Hide 'large scale' references
[1]"Nucleotide sequences of two cDNA clones encoding different Cu/Zn-superoxide dismutases expressed in developing rice seed (Oryza sativa L.)."
Sakamoto A., Ohsuga H., Tanaka K.
Plant Mol. Biol. 19:323-327(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: cv. Nipponbare.
Tissue: Seed.
[2]"Genomic structure of the gene for copper/zinc-superoxide dismutase in rice."
Sakamoto A., Okumura T., Ohsuga H., Tanaka K.
FEBS Lett. 301:185-189(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: cv. Nipponbare.
[3]"The map-based sequence of the rice genome."
International rice genome sequencing project (IRGSP)
Nature 436:793-800(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Nipponbare.
[4]"Rice proteome database based on two-dimensional polyacrylamide gel electrophoresis: its status in 2003."
Komatsu S., Kojima K., Suzuki K., Ozaki K., Higo K.
Nucleic Acids Res. 32:D388-D392(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-11.
Strain: cv. Nipponbare.
Tissue: Panicle and Root.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D01000 mRNA. Translation: BAA00800.1.
L19434 Genomic DNA. Translation: AAC14465.1.
AP003825 Genomic DNA. Translation: BAC10110.1. Sequence problems.
AP004274 Genomic DNA. Translation: BAD30565.1. Sequence problems.
PIRS21136.
RefSeqNP_001060564.1. NM_001067099.2.
UniGeneOs.4169.

3D structure databases

ProteinModelPortalP28757.
SMRP28757. Positions 1-152.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PaxDbP28757.
PRIDEP28757.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4344210.
KEGGosa:4344210.

Organism-specific databases

GrameneP28757.

Phylogenomic databases

eggNOGCOG2032.
HOGENOMHOG000263447.
KOK04565.
OMAEIEVKLH.

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 nameSODC2_ORYSJ
AccessionPrimary (citable) accession number: P28757
Secondary accession number(s): Q8LIB7
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 105 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

Oryza sativa (rice)

Index of Oryza sativa entries and their corresponding gene designations