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P08228 (SODC_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 163. 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·Interactions·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:Sod1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length154 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein 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.

Subcellular location

Cytoplasm. Nucleus By similarity.

Post-translational modification

Palmitoylation helps nuclear targeting and decreases catalytic activity By similarity.

Succinylation, adjacent to copper catalytic site probably inhibit activity. Desuccinylated by SIRT5, enhancing activity By similarity.

Disruption phenotype

40% reduction in hepatic GPX1 activity. Ref.7

Sequence similarities

Belongs to the Cu-Zn superoxide dismutase family.

Ontologies

Keywords
   Cellular componentCytoplasm
Nucleus
   LigandCopper
Metal-binding
Zinc
   Molecular functionAntioxidant
Oxidoreductase
   PTMAcetylation
Disulfide bond
Lipoprotein
Palmitate
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processactivation of MAPK activity

Inferred from direct assay PubMed 12223545. Source: MGI

aging

Inferred from mutant phenotype PubMed 16377630. Source: MGI

anterograde axon cargo transport

Inferred from mutant phenotype PubMed 20510358. Source: BHF-UCL

auditory receptor cell stereocilium organization

Inferred from mutant phenotype PubMed 10464373PubMed 10466888. Source: MGI

cell aging

Inferred from electronic annotation. Source: Ensembl

cellular iron ion homeostasis

Inferred from mutant phenotype PubMed 16377630. Source: MGI

embryo implantation

Inferred from mutant phenotype PubMed 9516486. Source: MGI

glutathione metabolic process

Inferred from mutant phenotype PubMed 16377630. Source: MGI

heart contraction

Inferred from mutant phenotype PubMed 10679476. Source: MGI

hydrogen peroxide biosynthetic process

Inferred from mutant phenotype PubMed 14679182. Source: MGI

locomotory behavior

Inferred from mutant phenotype PubMed 10433959. Source: MGI

muscle cell cellular homeostasis

Inferred from mutant phenotype PubMed 16716900. Source: MGI

myeloid cell homeostasis

Inferred from mutant phenotype PubMed 11493445. Source: MGI

negative regulation of apoptotic process

Inferred from direct assay PubMed 12223545. Source: MGI

negative regulation of cholesterol biosynthetic process

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of neuron apoptotic process

Inferred from mutant phenotype PubMed 10464373. Source: MGI

neurofilament cytoskeleton organization

Inferred from mutant phenotype PubMed 11343650. Source: MGI

ovarian follicle development

Inferred from mutant phenotype PubMed 9724058. Source: MGI

peripheral nervous system myelin maintenance

Inferred from mutant phenotype PubMed 10433959. Source: MGI

positive regulation of catalytic activity

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of cytokine production

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of intrinsic apoptotic signaling pathway in response to oxidative stress

Inferred from electronic annotation. Source: Ensembl

positive regulation of superoxide anion generation

Inferred from electronic annotation. Source: Ensembl

reactive oxygen species metabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of Rac GTPase activity

Inferred from electronic annotation. Source: Ensembl

regulation of blood pressure

Inferred from mutant phenotype PubMed 12433839. Source: MGI

regulation of mitochondrial membrane potential

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of multicellular organism growth

Inferred from mutant phenotype PubMed 16377630. Source: MGI

regulation of protein kinase activity

Inferred from sequence or structural similarity. Source: UniProtKB

relaxation of vascular smooth muscle

Inferred from mutant phenotype PubMed 12433839PubMed 14679182. Source: MGI

removal of superoxide radicals

Inferred from mutant phenotype PubMed 10436316PubMed 10471451PubMed 10679476PubMed 11493445PubMed 12433839PubMed 17448893PubMed 8673102PubMed 9516486PubMed 9788901. Source: MGI

response to amphetamine

Inferred from electronic annotation. Source: Ensembl

response to axon injury

Inferred from mutant phenotype PubMed 8673102. Source: MGI

response to copper ion

Inferred from electronic annotation. Source: Ensembl

response to drug

Inferred from mutant phenotype PubMed 16831125. Source: MGI

response to ethanol

Inferred from mutant phenotype PubMed 17448893. Source: MGI

response to heat

Inferred from mutant phenotype PubMed 16942767. Source: MGI

response to hydrogen peroxide

Inferred from mutant phenotype PubMed 15642323. Source: MGI

response to nutrient levels

Inferred from electronic annotation. Source: Ensembl

response to organic substance

Inferred from sequence or structural similarity. Source: UniProtKB

response to oxidative stress

Inferred from direct assay PubMed 12223545. Source: MGI

response to reactive oxygen species

Inferred from mutant phenotype PubMed 17059387. Source: MGI

response to superoxide

Inferred from mutant phenotype PubMed 16357131PubMed 9516486PubMed 9788901. Source: MGI

retina homeostasis

Inferred from mutant phenotype PubMed 16844785. Source: MGI

retrograde axon cargo transport

Inferred from mutant phenotype PubMed 20510358. Source: BHF-UCL

sensory perception of sound

Inferred from mutant phenotype PubMed 10436316PubMed 10464373PubMed 16055286. Source: MGI

spermatogenesis

Inferred from mutant phenotype PubMed 16036348. Source: MGI

superoxide anion generation

Inferred from direct assay PubMed 15317809. Source: MGI

superoxide metabolic process

Inferred from mutant phenotype PubMed 11404260. Source: MGI

transmission of nerve impulse

Inferred from mutant phenotype PubMed 10433959. Source: MGI

   Cellular_componentcytoplasm

Inferred from sequence or structural similarity. Source: UniProtKB

cytoplasmic vesicle

Inferred from sequence or structural similarity. Source: UniProtKB

cytosol

Inferred from sequence or structural similarity. Source: UniProtKB

dendrite cytoplasm

Inferred from sequence or structural similarity. Source: UniProtKB

extracellular matrix

Inferred from sequence or structural similarity. Source: UniProtKB

extracellular space

Inferred from sequence or structural similarity. Source: UniProtKB

mitochondrion

Inferred from sequence or structural similarity. Source: UniProtKB

neuronal cell body

Inferred from sequence or structural similarity. Source: UniProtKB

nucleus

Inferred from sequence or structural similarity. Source: UniProtKB

peroxisome

Inferred from electronic annotation. Source: Ensembl

plasma membrane

Inferred from electronic annotation. Source: Ensembl

protein complex

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionchaperone binding

Inferred from sequence or structural similarity. Source: UniProtKB

copper ion binding

Inferred from sequence or structural similarity. Source: UniProtKB

protein binding

Inferred from physical interaction PubMed 18219391. Source: IntAct

protein phosphatase 2B binding

Inferred from sequence or structural similarity. Source: UniProtKB

superoxide dismutase activity

Inferred from direct assay PubMed 12646716PubMed 12968068PubMed 15317809PubMed 291939PubMed 7444718. Source: MGI

zinc ion binding

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Rac1P630014EBI-1635090,EBI-413646

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 154153Superoxide dismutase [Cu-Zn]
PRO_0000164062

Sites

Metal binding471Copper; catalytic By similarity
Metal binding491Copper; catalytic By similarity
Metal binding641Copper; catalytic By similarity
Metal binding641Zinc; via pros nitrogen
Metal binding721Zinc; via pros nitrogen
Metal binding811Zinc; via pros nitrogen
Metal binding841Zinc; structural
Metal binding1211Copper; catalytic By similarity

Amino acid modifications

Modified residue21N-acetylalanine Ref.8
Modified residue41N6-succinyllysine Ref.8
Modified residue101N6-succinyllysine Ref.8
Modified residue921N6-succinyllysine Ref.8
Modified residue991Phosphoserine By similarity
Modified residue1231N6-acetyllysine; alternate Ref.8
Modified residue1231N6-succinyllysine; alternate Ref.8
Modified residue1371N6-acetyllysine; alternate Ref.9
Modified residue1371N6-succinyllysine; alternate Ref.8
Lipidation71S-palmitoyl cysteine By similarity
Disulfide bond58 ↔ 147 By similarity

Experimental info

Sequence conflict1021D → H in AAA40121. Ref.2

Secondary structure

........................... 154
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P08228 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: CAE548C66043BAC4

FASTA15415,943
        10         20         30         40         50         60 
MAMKAVCVLK GDGPVQGTIH FEQKASGEPV VLSGQITGLT EGQHGFHVHQ YGDNTQGCTS 

        70         80         90        100        110        120 
AGPHFNPHSK KHGGPADEER HVGDLGNVTA GKDGVANVSI EDRVISLSGE HSIIGRTMVV 

       130        140        150 
HEKQDDLGKG GNEESTKTGN AGSRLACGVI GIAQ 

« Hide

References

« Hide 'large scale' references
[1]"cDNA and deduced amino acid sequence of murine Cu-Zn superoxide dismutase."
Bewley G.C.
Nucleic Acids Res. 16:2728-2728(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: SWR/J.
Tissue: Liver.
[2]"Isolation and analysis of the mouse genomic sequence encoding Cu(2+)-Zn2+ superoxide dismutase."
Benedetto M.T., Anzai Y., Gordon J.W.
Gene 99:191-195(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Ovary, Urinary bladder and Uterus.
[4]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Liver, Mammary gland and Retina.
[5]"Purification of an inhibitor of erythroid progenitor cell cycling and antagonist to interleukin 3 from mouse marrow cell supernatants and its identification as cytosolic superoxide dismutase."
Pluthero F.G., Shreeve M., Eskinazi D., van der Gaag H., Huang K.S., Hulmes J.D., Blum M., Axelrad A.A.
J. Cell Biol. 111:1217-1223(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 4-23.
[6]Lubec G., Klug S., Sunyer B., Chen W.-Q.
Submitted (JAN-2009) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 11-24 AND 104-116, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: OF1.
Tissue: Hippocampus.
[7]"Knockout of SOD1 promotes conversion of selenocysteine to dehydroalanine in murine hepatic GPX1 protein."
Wang S.K., Weaver J.D., Zhang S., Lei X.G.
Free Radic. Biol. Med. 51:197-204(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: DISRUPTION PHENOTYPE.
Tissue: Liver.
[8]"SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2 AND LYS-123, SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-4; LYS-10; LYS-92; LYS-123 AND LYS-137, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
Tissue: Embryonic fibroblast and Liver.
[9]"Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways."
Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.
Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-137, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[10]"Structures of mouse SOD1 and human/mouse SOD1 chimeras."
Seetharaman S.V., Taylor A.B., Holloway S., Hart P.J.
Arch. Biochem. Biophys. 503:183-190(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 2-154 IN COMPLEX WITH ZINC.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X06683 mRNA. Translation: CAA29880.1.
M60798 expand/collapse EMBL AC list , 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.
CCDSCCDS37395.1.
PIRJQ0915.
RefSeqNP_035564.1. NM_011434.1.
UniGeneMm.276325.
Mm.466779.

3D structure databases

PDBe
RCSB-PDB
PDBj
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/F2-154[»]
ProteinModelPortalP08228.
SMRP08228. Positions 2-154.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid203387. 9 interactions.
DIPDIP-48691N.
IntActP08228. 11 interactions.
MINTMINT-1869618.
STRING10090.ENSMUSP00000023707.

PTM databases

PhosphoSiteP08228.

2D gel databases

DOSAC-COBS-2DPAGEP08228.
REPRODUCTION-2DPAGEIPI00130589.
P08228.
SWISS-2DPAGEP08228.
UCD-2DPAGEP08228.

Proteomic databases

MaxQBP08228.
PaxDbP08228.
PRIDEP08228.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000023707; ENSMUSP00000023707; ENSMUSG00000022982.
GeneID20655.
KEGGmmu:20655.
UCSCuc007zvz.1. mouse.

Organism-specific databases

CTD6647.
MGIMGI:98351. Sod1.

Phylogenomic databases

eggNOGCOG2032.
GeneTreeENSGT00530000063226.
HOGENOMHOG000263447.
HOVERGENHBG000062.
InParanoidP08228.
KOK04565.
OMANDPNAKR.
OrthoDBEOG776SR4.
PhylomeDBP08228.
TreeFamTF105131.

Enzyme and pathway databases

ReactomeREACT_188957. Cellular responses to stress.

Gene expression databases

BgeeP08228.
CleanExMM_SOD1.
GenevestigatorP08228.

Family and domain databases

Gene3D2.60.40.200. 1 hit.
InterProIPR018152. SOD_Cu/Zn_BS.
IPR001424. SOD_Cu_Zn_dom.
[Graphical view]
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

ChiTaRSSOD1. mouse.
EvolutionaryTraceP08228.
NextBio299081.
PROP08228.
SOURCESearch...

Entry information

Entry nameSODC_MOUSE
AccessionPrimary (citable) accession number: P08228
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 163 of the entry and version 2 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