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Protein

Superoxide dismutase [Cu-Zn]

Gene

Sod1

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

Functioni

Destroys radicals which are normally produced within the cells and which are toxic to biological systems.

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)DescriptionActionsGraphical viewLength
Metal bindingi47Copper; catalyticBy similarity1
Metal bindingi49Copper; catalyticBy similarity1
Metal bindingi64Copper; catalyticBy similarity1
Metal bindingi64Zinc; via pros nitrogen1 Publication1
Metal bindingi72Zinc; via pros nitrogen1 Publication1
Metal bindingi81Zinc; via pros nitrogen1 Publication1
Metal bindingi84Zinc; structural1 Publication1
Metal bindingi121Copper; catalyticBy similarity1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionAntioxidant, Oxidoreductase
LigandCopper, Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiR-MMU-114608 Platelet degranulation
R-MMU-3299685 Detoxification of Reactive Oxygen Species

Names & Taxonomyi

Protein namesi
Recommended name:
Superoxide dismutase [Cu-Zn] (EC:1.15.1.1)
Gene namesi
Name:Sod1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 16

Organism-specific databases

MGIiMGI:98351 Sod1

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Disruption phenotypei

40% reduction in hepatic GPX1 activity.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources
ChainiPRO_00001640622 – 154Superoxide dismutase [Cu-Zn]Add BLAST153

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineCombined sources1
Modified residuei4N6-succinyllysineCombined sources1
Lipidationi7S-palmitoyl cysteineBy similarity1
Modified residuei10N6-succinyllysineCombined sources1
Disulfide bondi58 ↔ 147By similarity
Modified residuei92N6-succinyllysineCombined sources1
Modified residuei99PhosphoserineBy similarity1
Modified residuei106PhosphoserineBy similarity1
Modified residuei108PhosphoserineCombined sources1
Modified residuei123N6-acetyllysine; alternateCombined sources1
Modified residuei123N6-succinyllysine; alternateCombined sources1
Modified residuei137N6-acetyllysine; alternateCombined sources1
Modified residuei137N6-succinyllysine; alternateCombined sources1

Post-translational modificationi

Palmitoylation helps nuclear targeting and decreases catalytic activity.By similarity
Succinylation, adjacent to copper catalytic site, probably inhibits activity. Desuccinylation by SIRT5 enhances activity.By similarity

Keywords - PTMi

Acetylation, Disulfide bond, Lipoprotein, Palmitate, Phosphoprotein

Proteomic databases

EPDiP08228
MaxQBiP08228
PaxDbiP08228
PeptideAtlasiP08228
PRIDEiP08228

2D gel databases

DOSAC-COBS-2DPAGEiP08228
REPRODUCTION-2DPAGEiIPI00130589
P08228
SWISS-2DPAGEiP08228
UCD-2DPAGEiP08228

PTM databases

iPTMnetiP08228
PhosphoSitePlusiP08228
SwissPalmiP08228

Expressioni

Gene expression databases

BgeeiENSMUSG00000022982 Expressed in 306 organ(s), highest expression level in cumulus cell
CleanExiMM_SOD1
GenevisibleiP08228 MM

Interactioni

Subunit structurei

Homodimer.1 Publication

Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

BioGridi203387, 29 interactors
ComplexPortaliCPX-2898 [Cu-Zn] Superoxide dismutase complex
DIPiDIP-48691N
IntActiP08228, 53 interactors
MINTiP08228
STRINGi10090.ENSMUSP00000023707

Structurei

Secondary structure

1154
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

ProteinModelPortaliP08228
SMRiP08228
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP08228

Family & Domainsi

Sequence similaritiesi

Belongs to the Cu-Zn superoxide dismutase family.Curated

Phylogenomic databases

eggNOGiKOG0441 Eukaryota
COG2032 LUCA
GeneTreeiENSGT00530000063226
HOGENOMiHOG000263447
HOVERGENiHBG000062
InParanoidiP08228
KOiK04565
OMAiMAMKAVC
OrthoDBiEOG091G0OG2
PhylomeDBiP08228
TreeFamiTF105131

Family and domain databases

CDDicd00305 Cu-Zn_Superoxide_Dismutase, 1 hit
Gene3Di2.60.40.200, 1 hit
InterProiView protein in InterPro
IPR036423 SOD-like_Cu/Zn_dom_sf
IPR024134 SOD_Cu/Zn_/chaperone
IPR018152 SOD_Cu/Zn_BS
IPR001424 SOD_Cu_Zn_dom
PANTHERiPTHR10003 PTHR10003, 1 hit
PfamiView protein in Pfam
PF00080 Sod_Cu, 1 hit
PRINTSiPR00068 CUZNDISMTASE
SUPFAMiSSF49329 SSF49329, 1 hit
PROSITEiView protein in PROSITE
PS00087 SOD_CU_ZN_1, 1 hit
PS00332 SOD_CU_ZN_2, 1 hit

Sequencei

Sequence statusi: Complete.

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

P08228-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MAMKAVCVLK GDGPVQGTIH FEQKASGEPV VLSGQITGLT EGQHGFHVHQ
60 70 80 90 100
YGDNTQGCTS AGPHFNPHSK KHGGPADEER HVGDLGNVTA GKDGVANVSI
110 120 130 140 150
EDRVISLSGE HSIIGRTMVV HEKQDDLGKG GNEESTKTGN AGSRLACGVI

GIAQ
Length:154
Mass (Da):15,943
Last modified:January 23, 2007 - v2
Checksum:iCAE548C66043BAC4
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti102D → H in AAA40121 (PubMed:2022332).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X06683 mRNA Translation: CAA29880.1
M60798
, M60794, M60795, M60796, M60797 Genomic DNA Translation: AAA40121.1
M35725 mRNA Translation: AAA37518.1
AK020624 mRNA Translation: BAB32154.1
AK077284 mRNA Translation: BAC36730.1
BC002066 mRNA Translation: AAH02066.1
BC048874 mRNA Translation: AAH48874.1
BC086886 mRNA Translation: AAH86886.1
CCDSiCCDS37395.1
PIRiJQ0915
RefSeqiNP_035564.1, NM_011434.1
UniGeneiMm.276325
Mm.466779

Genome annotation databases

EnsembliENSMUST00000023707; ENSMUSP00000023707; ENSMUSG00000022982
GeneIDi20655
KEGGimmu:20655
UCSCiuc007zvz.1 mouse

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X06683 mRNA Translation: CAA29880.1
M60798
, M60794, M60795, M60796, M60797 Genomic DNA Translation: AAA40121.1
M35725 mRNA Translation: AAA37518.1
AK020624 mRNA Translation: BAB32154.1
AK077284 mRNA Translation: BAC36730.1
BC002066 mRNA Translation: AAH02066.1
BC048874 mRNA Translation: AAH48874.1
BC086886 mRNA Translation: AAH86886.1
CCDSiCCDS37395.1
PIRiJQ0915
RefSeqiNP_035564.1, NM_011434.1
UniGeneiMm.276325
Mm.466779

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3GTTX-ray2.40A/B/C/D/E/F2-154[»]
3GTVX-ray2.20A/B/C/D/E/F/G/H/I/J/K/L82-154[»]
3LTVX-ray2.45A/B/C/D/E/F2-81[»]
ProteinModelPortaliP08228
SMRiP08228
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi203387, 29 interactors
ComplexPortaliCPX-2898 [Cu-Zn] Superoxide dismutase complex
DIPiDIP-48691N
IntActiP08228, 53 interactors
MINTiP08228
STRINGi10090.ENSMUSP00000023707

PTM databases

iPTMnetiP08228
PhosphoSitePlusiP08228
SwissPalmiP08228

2D gel databases

DOSAC-COBS-2DPAGEiP08228
REPRODUCTION-2DPAGEiIPI00130589
P08228
SWISS-2DPAGEiP08228
UCD-2DPAGEiP08228

Proteomic databases

EPDiP08228
MaxQBiP08228
PaxDbiP08228
PeptideAtlasiP08228
PRIDEiP08228

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000023707; ENSMUSP00000023707; ENSMUSG00000022982
GeneIDi20655
KEGGimmu:20655
UCSCiuc007zvz.1 mouse

Organism-specific databases

CTDi6647
MGIiMGI:98351 Sod1

Phylogenomic databases

eggNOGiKOG0441 Eukaryota
COG2032 LUCA
GeneTreeiENSGT00530000063226
HOGENOMiHOG000263447
HOVERGENiHBG000062
InParanoidiP08228
KOiK04565
OMAiMAMKAVC
OrthoDBiEOG091G0OG2
PhylomeDBiP08228
TreeFamiTF105131

Enzyme and pathway databases

ReactomeiR-MMU-114608 Platelet degranulation
R-MMU-3299685 Detoxification of Reactive Oxygen Species

Miscellaneous databases

ChiTaRSiSod1 mouse
EvolutionaryTraceiP08228
PROiPR:P08228
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000022982 Expressed in 306 organ(s), highest expression level in cumulus cell
CleanExiMM_SOD1
GenevisibleiP08228 MM

Family and domain databases

CDDicd00305 Cu-Zn_Superoxide_Dismutase, 1 hit
Gene3Di2.60.40.200, 1 hit
InterProiView protein in InterPro
IPR036423 SOD-like_Cu/Zn_dom_sf
IPR024134 SOD_Cu/Zn_/chaperone
IPR018152 SOD_Cu/Zn_BS
IPR001424 SOD_Cu_Zn_dom
PANTHERiPTHR10003 PTHR10003, 1 hit
PfamiView protein in Pfam
PF00080 Sod_Cu, 1 hit
PRINTSiPR00068 CUZNDISMTASE
SUPFAMiSSF49329 SSF49329, 1 hit
PROSITEiView protein in PROSITE
PS00087 SOD_CU_ZN_1, 1 hit
PS00332 SOD_CU_ZN_2, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiSODC_MOUSE
AccessioniPrimary (citable) accession number: P08228
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: January 23, 2007
Last modified: November 7, 2018
This is version 203 of the entry and version 2 of the sequence. See 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. SIMILARITY comments
    Index of protein domains and families
  2. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

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