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O22373 (SODC_CAPAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 72. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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]

EC=1.15.1.1
Gene names
Name:SODCC
OrganismCapsicum annuum (Bell pepper)
Taxonomic identifier4072 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonscore eudicotyledonsasteridslamiidsSolanalesSolanaceaeSolanoideaeCapsiceaeCapsicum

Protein attributes

Sequence length152 AA.
Sequence statusComplete.
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 By similarity.

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

Chain1 – 152152Superoxide dismutase [Cu-Zn]
PRO_0000164135

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
O22373 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: 515546B8ED274168

FASTA15215,279
        10         20         30         40         50         60 
MVKAVAVLSS SECVSGTILF SQDGDAPTTV TGNVSGLKPG LHGFHVHALG DTTNGCMSTG 

        70         80         90        100        110        120 
PHYNPAGKEH GAPEDENRHA GDLGNITVGE DGTASFTITD EQIPLTGPQS IIGRGVVVHA 

       130        140        150 
DPDDLGKGGH ELTKTTGNAG GRVACGIIGL QG 

« Hide

References

[1]"Isolation and characterization of cytosolic copper/zinc superoxide dismutase from Capsicum annuum L."
Kim Y.K., Kwon S.I., An C.S.
Mol. Cells 7:668-673(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF009734 mRNA. Translation: AAB66812.1.
PIRT07925.

3D structure databases

ProteinModelPortalO22373.
SMRO22373. Positions 1-152.
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_CAPAN
AccessionPrimary (citable) accession number: O22373
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: January 1, 1998
Last modified: April 3, 2013
This is version 72 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