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Reviewed, UniProtKB/Swiss-Prot P08228 (SODC_MOUSE)

Last modified November 3, 2009. Version 115. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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 lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMus

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 termDirect protein sequencing
Gene Ontology (GO)
   Biological processDNA fragmentation involved in apoptosis

Inferred from direct assay. Source: MGI

activation of MAPK activity

Inferred from direct assay. Source: MGI

auditory receptor cell stereocilium organization

Inferred from mutant phenotype. Source: MGI

cell aging

Inferred from sequence or structural similarity. Source: UniProtKB

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 homeostasis

Inferred from mutant phenotype. Source: MGI

myelin maintenance in the peripheral nervous system

Inferred from mutant phenotype. Source: MGI

myeloid cell homeostasis

Inferred from genetic interaction. 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 genetic interaction. Source: MGI

ovarian follicle development

Inferred from mutant phenotype. Source: MGI

oxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

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

response to superoxide

Inferred from mutant phenotype. Source: MGI

retina homeostasis

Inferred from mutant phenotype. Source: MGI

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 componentcell soma

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

nucleus

Inferred from sequence or structural similarity. Source: UniProtKB

protein complex

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular functionantioxidant activity

Inferred from electronic annotation. Source: UniProtKB-KW

chaperone 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; structural By similarity
Metal binding721Zinc; structural By similarity
Metal binding811Zinc; structural By similarity
Metal binding841Zinc; structural By similarity
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

Sequences

Sequence LengthMass (Da)Tools
P08228-1 [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.
+Additional computationally mapped references.

Cross-references

Sequence databases

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.
UniGeneMm.276325
Mm.466779

3D structure databases

HSSPHSSP built from PDB template 1HL5 based on UniProtKB P00441.
SMRP08228. Positions 2-154.
ModBaseSearch...

Protein-protein interaction databases

STRINGP08228.

PTM databases

PhosphoSiteP08228.

2-D gel databases

SWISS-2DPAGEP08228.
DOSAC-COBS-2DPAGEP08228.
REPRODUCTION-2DPAGEP08228.

Proteomic databases

PRIDEP08228.

Genome annotation databases

EnsemblENSMUST00000023707; ENSMUSP00000023707; ENSMUSG00000022982; Mus musculus. [Genome view]
GeneID20655.
KEGGmmu:20655.
NMPDRfig|10090.3.peg.1866.
UCSCuc007zvz.1. mouse.

Organism-specific databases

CTD20655.
MGIMGI:98351. Sod1.

Phylogenomic databases

HOGENOMP08228.
HOVERGENP08228.
OMAGPHFNPN.

Enzyme and pathway databases

BRENDA1.15.1.1. 244.

Gene expression databases

BgeeP08228.
CleanExMM_SOD1.
GenevestigatorP08228.
GermOnlineENSMUSG00000047905. Mus musculus.

Family and domain databases

InterProIPR018152. SOD_Cu/Zn_BS.
IPR001424. SOD_Cu_Zn.
[Graphical view]
Gene3DG3DSA:2.60.40.200. SOD_Cu_Zn. 1 hit.
PANTHERPTHR10003. SOD_Cu_Zn. 1 hit.
PfamPF00080. Sod_Cu. 1 hit.
[Graphical view]
PRINTSPR00068. CUZNDISMTASE.
ProDomPD000469. SOD_CU_ZN. 1 hit.
[Graphical view] [Entries sharing at least one domain]
PROSITEPS00087. SOD_CU_ZN_1. 1 hit.
PS00332. SOD_CU_ZN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

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: November 3, 2009
This is version 115 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

MGD cross-references

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

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents