Extracellular superoxide dismutase [Cu-Zn] precursor

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O09164 (SODE_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 112. History...

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

Documents (3) |

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:
Extracellular superoxide dismutase [Cu-Zn]
Short name=EC-SOD
EC=1.15.1.1

Gene names

Name:

Sod3

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	251 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	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	Secreted › extracellular space.
Sequence similarities	Belongs to the Cu-Zn superoxide dismutase family.

Ontologies

Keywords
Cellular component	Secreted
Domain	Signal
Ligand	Copper Metal-binding Zinc
Molecular function	Antioxidant Oxidoreductase
PTM	Disulfide bond Glycoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	removal of superoxide radicals Inferred from Biological aspect of Ancestor. Source: RefGenome response to copper ion Inferred from electronic annotation. Source: Compara response to hypoxia Inferred from mutant phenotype PubMed 15016652. Source: MGI
Cellular_component	cytosol Inferred from Biological aspect of Ancestor. Source: RefGenome extracellular matrix Inferred from electronic annotation. Source: Compara extracellular space Inferred from direct assay PubMed 15016652. Source: MGI mitochondrion Inferred from Biological aspect of Ancestor. Source: RefGenome nucleus Inferred from Biological aspect of Ancestor. Source: RefGenome trans-Golgi network Inferred from direct assay PubMed 16371425. Source: MGI
Molecular_function	copper ion binding Inferred from Biological aspect of Ancestor. Source: RefGenome superoxide dismutase activity Inferred from direct assay PubMed 16371425. Source: MGI 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

Signal peptide

1 – 15

By similarity

Propeptide

16 – 24

PRO_0000032856

Chain

25 – 251

227

Extracellular superoxide dismutase [Cu-Zn]

PRO_0000032857

Sites

Metal binding

128

Copper; catalytic By similarity

Metal binding

130

Copper; catalytic By similarity

Metal binding

145

Copper; catalytic By similarity

Metal binding

145

Zinc; structural By similarity

Metal binding

153

Zinc; structural By similarity

Metal binding

156

Zinc; structural By similarity

Metal binding

159

Zinc; structural By similarity

Metal binding

195

Copper; catalytic By similarity

Amino acid modifications

Glycosylation

121

N-linked (GlcNAc...) Potential

Disulfide bond

77 ↔ 222

By similarity

Disulfide bond

139 ↔ 221

By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

O09164 [UniParc].

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

251

27,392

        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.

IPI

IPI00114319.

RefSeq

NP_035565.1. NM_011435.3.

UniGene

Mm.2407.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2DZ2	model	-	A	120-228	[»]
2DZ3	model	-	A	84-228	[»]

ProteinModelPortal

O09164.

SMR

O09164. Positions 73-235.

ModBase

Search...

PTM databases

PhosphoSite

O09164.

Proteomic databases

PaxDb

O09164.

PRIDE

O09164.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSMUST00000101208; ENSMUSP00000098768; ENSMUSG00000072941.

GeneID

20657.

KEGG

mmu:20657.

Organism-specific databases

CTD

6649.

MGI

MGI:103181. Sod3.

Phylogenomic databases

eggNOG

COG2032.

HOGENOM

HOG000263447.

HOVERGEN

HBG000062.

InParanoid

O09164.

K16627.

OMA

CCVIGIC.

OrthoDB

EOG4MCX1S.

Gene expression databases

ArrayExpress

O09164.

Bgee

O09164.

CleanEx

MM_SOD3.

Genevestigator

O09164.

GermOnline

ENSMUSG00000072941. Mus musculus.

Family and domain databases

Gene3D

2.60.40.200. 1 hit.

InterPro

IPR024134. SOD_Cu/Zn_/chaperones.
IPR018152. SOD_Cu/Zn_BS.
IPR024141. SOD_Cu/Zn_extracel.
IPR001424. SOD_Cu_Zn_dom.
[Graphical view]

PANTHER

PTHR10003. PTHR10003. 1 hit.
PTHR10003:SF10. PTHR10003:SF10. 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...

Other

NextBio

299089.

SOURCE

Search...

Entry information

Entry name

SODE_MOUSE

Accession

Primary (citable) accession number: O09164

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	July 1, 1997
Last modified:	April 3, 2013
This is version 112 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

MGD cross-references

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

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

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents