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Protein

Extracellular superoxide dismutase [Cu-Zn]

Gene

Sod3

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

2 superoxide + 2 H+ = O2 + H2O2.

Cofactori

Protein has several cofactor binding sites:
  • Cu cationBy similarityNote: Binds 1 copper ion per subunit.By similarity
  • Zn2+By similarityNote: Binds 1 zinc ion per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi128 – 1281Copper; catalyticBy similarity
Metal bindingi130 – 1301Copper; catalyticBy similarity
Metal bindingi145 – 1451Copper; catalyticBy similarity
Metal bindingi145 – 1451Zinc; structuralBy similarity
Metal bindingi153 – 1531Zinc; structuralBy similarity
Metal bindingi156 – 1561Zinc; structuralBy similarity
Metal bindingi159 – 1591Zinc; structuralBy similarity
Metal bindingi195 – 1951Copper; catalyticBy similarity

GO - Molecular functioni

  1. copper ion binding Source: GO_Central
  2. superoxide dismutase activity Source: MGI
  3. zinc ion binding Source: GO_Central

GO - Biological processi

  1. removal of superoxide radicals Source: GO_Central
  2. response to copper ion Source: Ensembl
  3. response to hypoxia Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Antioxidant, Oxidoreductase

Keywords - Ligandi

Copper, Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_308972. Detoxification of Reactive Oxygen Species.

Names & Taxonomyi

Protein namesi
Recommended name:
Extracellular superoxide dismutase [Cu-Zn] (EC:1.15.1.1)
Short name:
EC-SOD
Gene namesi
Name:Sod3
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 5

Organism-specific databases

MGIiMGI:103181. Sod3.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: GO_Central
  2. extracellular matrix Source: Ensembl
  3. extracellular space Source: MGI
  4. extracellular vesicular exosome Source: MGI
  5. Golgi lumen Source: Reactome
  6. nucleus Source: Ensembl
  7. trans-Golgi network Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1515By similarityAdd
BLAST
Propeptidei16 – 2491 PublicationPRO_0000032856
Chaini25 – 251227Extracellular superoxide dismutase [Cu-Zn]PRO_0000032857Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi77 ↔ 222By similarity
Glycosylationi121 – 1211N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi139 ↔ 221By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiO09164.
PaxDbiO09164.
PRIDEiO09164.

PTM databases

PhosphoSiteiO09164.

Expressioni

Gene expression databases

BgeeiO09164.
CleanExiMM_SOD3.
ExpressionAtlasiO09164. baseline and differential.
GenevestigatoriO09164.

Interactioni

Protein-protein interaction databases

BioGridi203389. 1 interaction.
IntActiO09164. 1 interaction.
MINTiMINT-4135206.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2DZ2model-A120-228[»]
2DZ3model-A84-228[»]
ProteinModelPortaliO09164.
SMRiO09164. Positions 73-235.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the Cu-Zn superoxide dismutase family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG2032.
HOGENOMiHOG000263447.
HOVERGENiHBG000062.
InParanoidiO09164.
KOiK16627.
OMAiHPRHPGD.
OrthoDBiEOG77HDHG.
PhylomeDBiO09164.
TreeFamiTF105133.

Family and domain databases

Gene3Di2.60.40.200. 1 hit.
InterProiIPR018152. SOD_Cu/Zn_BS.
IPR024141. SOD_Cu/Zn_extracel.
IPR001424. SOD_Cu_Zn_dom.
[Graphical view]
PANTHERiPTHR10003:SF36. PTHR10003:SF36. 1 hit.
PfamiPF00080. Sod_Cu. 1 hit.
[Graphical view]
PRINTSiPR00068. CUZNDISMTASE.
SUPFAMiSSF49329. SSF49329. 1 hit.
PROSITEiPS00087. SOD_CU_ZN_1. 1 hit.
PS00332. SOD_CU_ZN_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

O09164-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLAFLFYGLL LAACGSVTMS NPGESSFDLA DRLDPVEKID RLDLVEKIGD
60 70 80 90 100
THAKVLEIWM ELGRRREVDA AEMHAICRVQ PSATLPPDQP QITGLVLFRQ
110 120 130 140 150
LGPGSRLEAY FSLEGFPAEQ NASNRAIHVH EFGDLSQGCD STGPHYNPME
160 170 180 190 200
VPHPQHPGDF GNFVVRNGQL WRHRVGLTAS LAGPHAILGR SVVVHAGEDD
210 220 230 240 250
LGKGGNQASL QNGNAGRRLA CCVVGTSSSA AWESQTKERK KRRRESECKT

T
Length:251
Mass (Da):27,392
Last modified:July 1, 1997 - v1
Checksum:i9EAF850E458966C4
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U38261 mRNA. Translation: AAB51106.1.
D50856 mRNA. Translation: BAA23493.1.
AF223251 Genomic DNA. Translation: AAF27932.1.
CCDSiCCDS19283.1.
RefSeqiNP_035565.1. NM_011435.3.
UniGeneiMm.2407.

Genome annotation databases

EnsembliENSMUST00000101208; ENSMUSP00000098768; ENSMUSG00000072941.
GeneIDi20657.
KEGGimmu:20657.
UCSCiuc008xkl.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U38261 mRNA. Translation: AAB51106.1.
D50856 mRNA. Translation: BAA23493.1.
AF223251 Genomic DNA. Translation: AAF27932.1.
CCDSiCCDS19283.1.
RefSeqiNP_035565.1. NM_011435.3.
UniGeneiMm.2407.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2DZ2model-A120-228[»]
2DZ3model-A84-228[»]
ProteinModelPortaliO09164.
SMRiO09164. Positions 73-235.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi203389. 1 interaction.
IntActiO09164. 1 interaction.
MINTiMINT-4135206.

PTM databases

PhosphoSiteiO09164.

Proteomic databases

MaxQBiO09164.
PaxDbiO09164.
PRIDEiO09164.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000101208; ENSMUSP00000098768; ENSMUSG00000072941.
GeneIDi20657.
KEGGimmu:20657.
UCSCiuc008xkl.1. mouse.

Organism-specific databases

CTDi6649.
MGIiMGI:103181. Sod3.

Phylogenomic databases

eggNOGiCOG2032.
HOGENOMiHOG000263447.
HOVERGENiHBG000062.
InParanoidiO09164.
KOiK16627.
OMAiHPRHPGD.
OrthoDBiEOG77HDHG.
PhylomeDBiO09164.
TreeFamiTF105133.

Enzyme and pathway databases

ReactomeiREACT_308972. Detoxification of Reactive Oxygen Species.

Miscellaneous databases

NextBioi299089.
PROiO09164.
SOURCEiSearch...

Gene expression databases

BgeeiO09164.
CleanExiMM_SOD3.
ExpressionAtlasiO09164. baseline and differential.
GenevestigatoriO09164.

Family and domain databases

Gene3Di2.60.40.200. 1 hit.
InterProiIPR018152. SOD_Cu/Zn_BS.
IPR024141. SOD_Cu/Zn_extracel.
IPR001424. SOD_Cu_Zn_dom.
[Graphical view]
PANTHERiPTHR10003:SF36. PTHR10003:SF36. 1 hit.
PfamiPF00080. Sod_Cu. 1 hit.
[Graphical view]
PRINTSiPR00068. CUZNDISMTASE.
SUPFAMiSSF49329. SSF49329. 1 hit.
PROSITEiPS00087. SOD_CU_ZN_1. 1 hit.
PS00332. SOD_CU_ZN_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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(1996) [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(1996) [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 (DEC-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: C57BL/6.
    Tissue: Liver.

Entry informationi

Entry nameiSODE_MOUSE
AccessioniPrimary (citable) accession number: O09164
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: July 1, 1997
Last modified: April 1, 2015
This is version 131 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.