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O09164 (SODE_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 121. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:
Extracellular superoxide dismutase [Cu-Zn]

Short name=EC-SOD
EC=1.15.1.1
Gene names
Name:Sod3
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length251 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Protect the extracellular space from toxic effect of reactive oxygen intermediates by converting superoxide radicals into hydrogen peroxide and oxygen By similarity.

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.

Subcellular location

Secretedextracellular space.

Sequence similarities

Belongs to the Cu-Zn superoxide dismutase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1515 By similarity
Propeptide16 – 249
PRO_0000032856
Chain25 – 251227Extracellular superoxide dismutase [Cu-Zn]
PRO_0000032857

Sites

Metal binding1281Copper; catalytic By similarity
Metal binding1301Copper; catalytic By similarity
Metal binding1451Copper; catalytic By similarity
Metal binding1451Zinc; structural By similarity
Metal binding1531Zinc; structural By similarity
Metal binding1561Zinc; structural By similarity
Metal binding1591Zinc; structural By similarity
Metal binding1951Copper; catalytic By similarity

Amino acid modifications

Glycosylation1211N-linked (GlcNAc...) Potential
Disulfide bond77 ↔ 222 By similarity
Disulfide bond139 ↔ 221 By similarity

Sequences

Sequence LengthMass (Da)Tools
O09164 [UniParc].

Last modified July 1, 1997. Version 1.
Checksum: 9EAF850E458966C4

FASTA25127,392
        10         20         30         40         50         60 
MLAFLFYGLL LAACGSVTMS NPGESSFDLA DRLDPVEKID RLDLVEKIGD THAKVLEIWM 

        70         80         90        100        110        120 
ELGRRREVDA AEMHAICRVQ PSATLPPDQP QITGLVLFRQ LGPGSRLEAY FSLEGFPAEQ 

       130        140        150        160        170        180 
NASNRAIHVH EFGDLSQGCD STGPHYNPME VPHPQHPGDF GNFVVRNGQL WRHRVGLTAS 

       190        200        210        220        230        240 
LAGPHAILGR SVVVHAGEDD LGKGGNQASL QNGNAGRRLA CCVVGTSSSA AWESQTKERK 

       250 
KRRRESECKT T 

« Hide

References

[1]"Mouse extracellular superoxide dismutase: primary structure, tissue-specific gene expression, chromosomal localization, and lung in situ hybridization."
Folz R.J., Guan J., Seldin M.F., Oury T.D., Enghild J.J., Crapo J.D.
Am. J. Respir. Cell Mol. Biol. 17:393-403(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 25-36.
Strain: C57BL/6 X CBA.
Tissue: Lung.
[2]"Sequence analysis, tissue expression and chromosomal localization of a mouse secreted superoxide dismutase gene."
Suh J.-G., Takai S., Yamanishi T., Kikuchi T., Folz R.J., Tanaka K., Oh Y.-S., Wada K.
Mol. Cells 7:204-207(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: C57BL/6J.
Tissue: Kidney.
[3]"Murine extracellular superoxide dismutase genomic sequence."
Siegfried M.R., Schultz D., Harrison D.G., Fukai T.
Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE.
Strain: C57BL/6.
Tissue: Liver.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U38261 mRNA. Translation: AAB51106.1.
D50856 mRNA. Translation: BAA23493.1.
AF223251 Genomic DNA. Translation: AAF27932.1.
RefSeqNP_035565.1. NM_011435.3.
UniGeneMm.2407.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2DZ2model-A120-228[»]
2DZ3model-A84-228[»]
ProteinModelPortalO09164.
SMRO09164. Positions 73-235.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid203389. 1 interaction.
IntActO09164. 1 interaction.
MINTMINT-4135206.

PTM databases

PhosphoSiteO09164.

Proteomic databases

PaxDbO09164.
PRIDEO09164.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000101208; ENSMUSP00000098768; ENSMUSG00000072941.
GeneID20657.
KEGGmmu:20657.
UCSCuc008xkl.1. mouse.

Organism-specific databases

CTD6649.
MGIMGI:103181. Sod3.

Phylogenomic databases

eggNOGCOG2032.
HOGENOMHOG000263447.
HOVERGENHBG000062.
InParanoidO09164.
KOK16627.
OMAHPRHPGD.
OrthoDBEOG77HDHG.
PhylomeDBO09164.
TreeFamTF105133.

Enzyme and pathway databases

ReactomeREACT_188957. Cellular responses to stress.

Gene expression databases

ArrayExpressO09164.
BgeeO09164.
CleanExMM_SOD3.
GenevestigatorO09164.

Family and domain databases

Gene3D2.60.40.200. 1 hit.
InterProIPR024134. SOD_Cu/Zn_/chaperone.
IPR018152. SOD_Cu/Zn_BS.
IPR024141. SOD_Cu/Zn_extracel.
IPR001424. SOD_Cu_Zn_dom.
[Graphical view]
PANTHERPTHR10003. PTHR10003. 1 hit.
PTHR10003:SF10. PTHR10003:SF10. 1 hit.
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...

Other

NextBio299089.
PROO09164.
SOURCESearch...

Entry information

Entry nameSODE_MOUSE
AccessionPrimary (citable) accession number: O09164
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: July 1, 1997
Last modified: April 16, 2014
This is version 121 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot