Superoxide dismutase [Cu-Zn] 2 - Oryza sativa subsp. japonica (Rice)

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P28757 (SODC2_ORYSJ) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 95. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended 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

Organism

Oryza sativa subsp. japonica (Rice) [Reference proteome]

Taxonomic identifier

39947 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › Liliopsida › Poales › Poaceae › BEP clade › Ehrhartoideae › Oryzeae › Oryza ›

Protein attributes

Sequence length	152 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 component	Cytoplasm
Ligand	Copper Metal-binding Zinc
Molecular function	Antioxidant Oxidoreductase
PTM	Disulfide bond
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	defense response to bacterium Inferred from electronic annotation. Source: EnsemblPlants/Gramene removal of superoxide radicals Inferred from Biological aspect of Ancestor. Source: RefGenome response to copper ion Inferred from electronic annotation. Source: EnsemblPlants/Gramene response to iron ion Inferred from electronic annotation. Source: EnsemblPlants/Gramene response to ozone Inferred from electronic annotation. Source: EnsemblPlants/Gramene response to salt stress Inferred from electronic annotation. Source: EnsemblPlants/Gramene
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	copper 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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed Ref.4

Chain

2 – 152

151

Superoxide dismutase [Cu-Zn] 2

PRO_0000164149

Sites

Metal binding

Copper; catalytic By similarity

Metal binding

Copper; catalytic By similarity

Metal binding

Copper; catalytic By similarity

Metal binding

Zinc; structural By similarity

Metal binding

Zinc; structural By similarity

Metal binding

Zinc; structural By similarity

Metal binding

Zinc; structural By similarity

Metal binding

119

Copper; catalytic By similarity

Amino acid modifications

Disulfide bond

56 ↔ 145

By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

P28757 [UniParc].

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

152

15,081

        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' referencesShow '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.
PIR	S21136.
RefSeq	NP_001060564.1. NM_001067099.2.
UniGene	Os.4169.
3D structure databases
ProteinModelPortal	P28757.
SMR	P28757. Positions 1-152.
ModBase	Search...
Proteomic databases
PaxDb	P28757.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	LOC_Os07g46990.1; LOC_Os07g46990.1; LOC_Os07g46990. LOC_Os07g46990.2; LOC_Os07g46990.2; LOC_Os07g46990.
GeneID	4344210.
KEGG	osa:4344210.
Organism-specific databases
Gramene	P28757.
Phylogenomic databases
eggNOG	COG2032.
HOGENOM	HOG000263447.
KO	K04565.
OMA	APRFESS.
ProtClustDB	PLN02386.
Gene expression databases
ArrayExpress	P28757.
Family and domain databases
Gene3D	2.60.40.200. 1 hit.
InterPro	IPR024134. SOD_Cu/Zn_/chaperones. IPR018152. SOD_Cu/Zn_BS. IPR001424. SOD_Cu_Zn_dom. [Graphical view]
PANTHER	PTHR10003. PTHR10003. 1 hit.
Pfam	PF00080. Sod_Cu. 1 hit. [Graphical view]
PRINTS	PR00068. CUZNDISMTASE.
SUPFAM	SSF49329. SOD_Cu_Zn. 1 hit.
PROSITE	PS00087. SOD_CU_ZN_1. 1 hit. PS00332. SOD_CU_ZN_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

SODC2_ORYSJ

Accession

Primary (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:	April 3, 2013
This is version 95 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program

Relevant documents

Oryza sativa (rice)

Index of Oryza sativa entries and their corresponding gene designations

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Sites

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Entry information

Relevant documents