Skip Header

Contribute Send feedback
Read comments (?) or add your own

P08228 (SODC_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 139. 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:
Superoxide dismutase [Cu-Zn]

EC=1.15.1.1
Gene names
Name:Sod1
OrganismMus musculus (Mouse)
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.

Sequence similarities

Belongs to the Cu-Zn superoxide dismutase family.

Ontologies

Keywords
   Cellular componentCytoplasm
   LigandCopper
Metal-binding
Zinc
   Molecular functionAntioxidant
Oxidoreductase
   PTMAcetylation
Disulfide bond
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological processDNA fragmentation involved in apoptotic nuclear change

Inferred from direct assay. Source: MGI

activation of MAPK activity

Inferred from direct assay. Source: MGI

anterograde axon cargo transport

Inferred from mutant phenotype. Source: BHF-UCL

auditory receptor cell stereocilium organization

Inferred from mutant phenotype. Source: MGI

cellular iron ion homeostasis

Inferred from mutant phenotype. Source: MGI

double-strand break repair

Inferred from mutant phenotype. Source: MGI

embryo implantation

Inferred from mutant phenotype. Source: MGI

glutathione metabolic process

Inferred from mutant phenotype. Source: MGI

heart contraction

Inferred from mutant phenotype. Source: MGI

hydrogen peroxide biosynthetic process

Inferred from mutant phenotype. Source: MGI

locomotory behavior

Inferred from mutant phenotype. Source: MGI

muscle cell homeostasis

Inferred from mutant phenotype. Source: MGI

myeloid cell homeostasis

Inferred from mutant phenotype. Source: MGI

negative regulation of cholesterol biosynthetic process

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of neuron apoptosis

Inferred from mutant phenotype. Source: MGI

neurofilament cytoskeleton organization

Inferred from mutant phenotype. Source: MGI

ovarian follicle development

Inferred from mutant phenotype. Source: MGI

peripheral nervous system myelin maintenance

Inferred from mutant phenotype. Source: MGI

positive regulation of cytokine production

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of blood pressure

Inferred from mutant phenotype. Source: MGI

regulation of mitochondrial membrane potential

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of multicellular organism growth

Inferred from mutant phenotype. Source: MGI

relaxation of vascular smooth muscle

Inferred from mutant phenotype. Source: MGI

removal of superoxide radicals

Inferred from mutant phenotype. Source: MGI

response to axon injury

Inferred from mutant phenotype. Source: MGI

response to drug

Inferred from mutant phenotype. Source: MGI

response to ethanol

Inferred from mutant phenotype. Source: MGI

response to heat

Inferred from mutant phenotype. Source: MGI

response to hydrogen peroxide

Inferred from mutant phenotype. Source: MGI

retina homeostasis

Inferred from mutant phenotype. Source: MGI

retrograde axon cargo transport

Inferred from mutant phenotype. Source: BHF-UCL

sensory perception of sound

Inferred from mutant phenotype. Source: MGI

spermatogenesis

Inferred from mutant phenotype. Source: MGI

superoxide anion generation

Inferred from direct assay. Source: MGI

   Cellular componentcytoplasmic 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

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 phosphatase 2B binding

Inferred from sequence or structural similarity. Source: UniProtKB

superoxide dismutase activity

Inferred from direct assay. Source: MGI

zinc ion binding

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed
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 residue711N6-acetyllysine Ref.7
Modified residue991Phosphoserine By similarity
Modified residue1231N6-acetyllysine 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: 3362683] [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: 2022332] [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: 16141072] [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: 15489334] [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: 2391363] [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, MASS SPECTROMETRY.
Strain: OF1.
Tissue: Hippocampus.
[7]"Substrate and functional diversity of lysine acetylation revealed by a proteomics survey."
Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T., Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y.
Mol. Cell 23:607-618(2006) [PubMed: 16916647] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-71, MASS SPECTROMETRY.
Tissue: Liver.
[8]"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: 20727846] [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.
IPIIPI00130589.
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[»]
ProteinModelPortalP08228.
SMRP08228. Positions 2-154.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-48691N.
IntActP08228. 3 interactions.
STRINGP08228.

PTM databases

PhosphoSiteP08228.

2D gel databases

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

Proteomic databases

PRIDEP08228.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000023707; ENSMUSP00000023707; ENSMUSG00000022982.
GeneID20655.
KEGGmmu:20655.
NMPDRfig|10090.3.peg.1866.
UCSCuc007zvz.1. mouse.

Organism-specific databases

CTD6647.
MGIMGI:98351. Sod1.

Phylogenomic databases

eggNOGroNOG15892.
GeneTreeENSGT00530000063226.
HOGENOMHBG609879.
HOVERGENHBG000062.
InParanoidP08228.
OMAIHFEQKA.
OrthoDBEOG45HRZM.
PhylomeDBP08228.

Gene expression databases

ArrayExpressP08228.
BgeeP08228.
CleanExMM_SOD1.
GenevestigatorP08228.
GermOnlineENSMUSG00000047905. Mus musculus.

Family and domain databases

InterProIPR024134. SOD_Cu/Zn_/chaperones.
IPR018152. SOD_Cu/Zn_BS.
IPR001424. SOD_Cu_Zn_dom.
[Graphical view]
Gene3DG3DSA:2.60.40.200. SOD_Cu_Zn. 1 hit.
KOK04565.
PANTHERPTHR10003. SOD_Cu_Zn. 1 hit.
PfamPF00080. Sod_Cu. 1 hit.
[Graphical view]
PRINTSPR00068. CUZNDISMTASE.
SUPFAMSSF49329. SOD_Cu_Zn. 1 hit.
PROSITEPS00087. SOD_CU_ZN_1. 1 hit.
PS00332. SOD_CU_ZN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio299081.
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: January 25, 2012
This is version 139 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata 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