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P07895 (SODM_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 129. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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 [Mn], mitochondrial

EC=1.15.1.1
Gene names
Name:Sod2
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length222 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems. Ref.5

Catalytic activity

2 superoxide + 2 H+ = O2 + H2O2.

Cofactor

Binds 1 manganese ion per subunit By similarity.

Subunit structure

Homotetramer.

Subcellular location

Mitochondrion matrix.

Post-translational modification

Nitrated under oxidative stress. Nitration coupled with oxidation inhibits the catalytic activity.

Acetylation at Lys-122 decreases enzymatic activity. Deacetylated by SIRT3 upon exposure to ionizing radiations or after long fasting By similarity.

Sequence similarities

Belongs to the iron/manganese superoxide dismutase family.

Ontologies

Keywords
   Cellular componentMitochondrion
   DomainTransit peptide
   LigandManganese
Metal-binding
   Molecular functionOxidoreductase
   PTMAcetylation
Nitration
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processage-dependent response to reactive oxygen species

Inferred from sequence or structural similarity. Source: UniProtKB

aging

Inferred from expression pattern PubMed 16304208. Source: RGD

cellular response to ethanol

Inferred from expression pattern PubMed 19703426. Source: RGD

detection of oxygen

Inferred from electronic annotation. Source: Ensembl

erythrophore differentiation

Inferred from electronic annotation. Source: Ensembl

glutathione metabolic process

Inferred from electronic annotation. Source: Ensembl

heart development

Inferred from electronic annotation. Source: Ensembl

hemopoiesis

Inferred from electronic annotation. Source: Ensembl

hydrogen peroxide biosynthetic process

Inferred from direct assay PubMed 15642720. Source: RGD

hydrogen peroxide metabolic process

Inferred from mutant phenotype PubMed 16716903. Source: RGD

intrinsic apoptotic signaling pathway in response to DNA damage

Inferred from electronic annotation. Source: Ensembl

intrinsic apoptotic signaling pathway in response to oxidative stress

Inferred from electronic annotation. Source: Ensembl

iron ion homeostasis

Inferred from electronic annotation. Source: Ensembl

liver development

Inferred from electronic annotation. Source: Ensembl

locomotory behavior

Inferred from electronic annotation. Source: Ensembl

negative regulation of apoptotic process

Inferred from mutant phenotype PubMed 11961082. Source: RGD

negative regulation of fat cell differentiation

Inferred from electronic annotation. Source: Ensembl

negative regulation of fibroblast proliferation

Inferred from electronic annotation. Source: Ensembl

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

Inferred from electronic annotation. Source: Ensembl

negative regulation of neuron apoptotic process

Inferred from electronic annotation. Source: Ensembl

neuron development

Inferred from electronic annotation. Source: Ensembl

oxygen homeostasis

Inferred from electronic annotation. Source: Ensembl

positive regulation of nitric oxide biosynthetic process

Inferred from electronic annotation. Source: Ensembl

post-embryonic development

Inferred from electronic annotation. Source: Ensembl

protein homooligomerization

Inferred from direct assay PubMed 19384983. Source: RGD

protein homotetramerization

Inferred from electronic annotation. Source: Ensembl

regulation of catalytic activity

Inferred from electronic annotation. Source: Ensembl

regulation of mitochondrial membrane potential

Inferred from electronic annotation. Source: Ensembl

regulation of transcription from RNA polymerase II promoter

Inferred from sequence or structural similarity. Source: UniProtKB

release of cytochrome c from mitochondria

Inferred from electronic annotation. Source: Ensembl

removal of superoxide radicals

Inferred from direct assay PubMed 12107766PubMed 15642720PubMed 19439219. Source: RGD

respiratory electron transport chain

Inferred from electronic annotation. Source: Ensembl

response to L-ascorbic acid

Inferred from expression pattern PubMed 20122981. Source: RGD

response to activity

Inferred from expression pattern PubMed 19297546. Source: RGD

response to axon injury

Inferred from electronic annotation. Source: Ensembl

response to cadmium ion

Inferred from expression pattern PubMed 20107868. Source: RGD

response to cold

Inferred from expression pattern PubMed 20020182. Source: RGD

response to drug

Inferred from direct assay PubMed 15959853. Source: RGD

response to electrical stimulus

Inferred from expression pattern PubMed 17962976. Source: RGD

response to gamma radiation

Inferred from electronic annotation. Source: Ensembl

response to hydrogen peroxide

Inferred from expression pattern PubMed 19917063. Source: RGD

response to hyperoxia

Inferred from electronic annotation. Source: Ensembl

response to hypoxia

Inferred from expression pattern PubMed 16911942. Source: RGD

response to immobilization stress

Inferred from expression pattern PubMed 20020182. Source: RGD

response to isolation stress

Inferred from expression pattern PubMed 20020182. Source: RGD

response to lipopolysaccharide

Inferred from expression pattern PubMed 17804075. Source: RGD

response to magnetism

Inferred from expression pattern PubMed 20037191. Source: RGD

response to manganese ion

Inferred from expression pattern PubMed 17920449. Source: RGD

response to nutrient levels

Inferred from direct assay PubMed 12067840. Source: RGD

response to oxidative stress

Inferred from expression pattern PubMed 15485085. Source: RGD

response to radiation

Inferred from expression pattern PubMed 22780102. Source: RGD

response to selenium ion

Inferred from expression pattern PubMed 17804075. Source: RGD

response to silicon dioxide

Inferred from expression pattern PubMed 17575405. Source: RGD

response to zinc ion

Inferred from expression pattern PubMed 20128680. Source: RGD

superoxide anion generation

Inferred from electronic annotation. Source: Ensembl

superoxide metabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

vasodilation by acetylcholine involved in regulation of systemic arterial blood pressure

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentcytoplasm

Inferred from direct assay PubMed 16372329. Source: RGD

mitochondrial inner membrane

Inferred from electronic annotation. Source: Ensembl

mitochondrial nucleoid

Inferred from direct assay PubMed 19228881. Source: RGD

mitochondrion

Inferred from direct assay PubMed 12107766PubMed 15642720PubMed 15642785. Source: RGD

   Molecular_functionDNA binding

Inferred from direct assay PubMed 19228881. Source: RGD

identical protein binding

Inferred from direct assay PubMed 19384983. Source: RGD

manganese ion binding

Inferred from sequence or structural similarity. Source: UniProtKB

oxygen binding

Inferred from direct assay PubMed 12107766PubMed 15642720. Source: RGD

protein binding

Inferred from physical interaction PubMed 24505357. Source: RGD

superoxide dismutase activity

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 2424Mitochondrion
Chain25 – 222198Superoxide dismutase [Mn], mitochondrial
PRO_0000032874

Sites

Metal binding501Manganese By similarity
Metal binding981Manganese By similarity
Metal binding1831Manganese By similarity
Metal binding1871Manganese By similarity

Amino acid modifications

Modified residue581Nitrated tyrosine Ref.6
Modified residue681N6-acetyllysine; alternate By similarity
Modified residue681N6-succinyllysine; alternate By similarity
Modified residue751N6-acetyllysine; alternate By similarity
Modified residue751N6-succinyllysine; alternate By similarity
Modified residue1141N6-acetyllysine By similarity
Modified residue1221N6-acetyllysine; alternate By similarity
Modified residue1221N6-succinyllysine; alternate By similarity
Modified residue1301N6-acetyllysine; alternate By similarity
Modified residue1301N6-succinyllysine; alternate By similarity
Modified residue2021N6-acetyllysine By similarity

Experimental info

Sequence conflict1671Q → H in CAA68549. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P07895 [UniParc].

Last modified May 1, 1992. Version 2.
Checksum: 8CCC1E0E857B3138

FASTA22224,674
        10         20         30         40         50         60 
MLCRAACSAG RRLGPAASTA GSRHKHSLPD LPYDYGALEP HINAQIMQLH HSKHHATYVN 

        70         80         90        100        110        120 
NLNVTEEKYH EALAKGDVTT QVALQPALKF NGGGHINHSI FWTNLSPKGG GEPKGELLEA 

       130        140        150        160        170        180 
IKRDFGSFEK FKEKLTAVSV GVQGSGWGWL GFNKEQGRLQ IAACSNQDPL QGTTGLIPLL 

       190        200        210        220 
GIDVWEHAYY LQYKNVRPDY LKAIWNVINW ENVSQRYIVC KK 

« Hide

References

« Hide 'large scale' references
[1]"Nucleotide sequences of cDNAs coding for rat manganese-containing superoxide dismutase."
Ho Y.-S., Crapo J.D.
Nucleic Acids Res. 15:10070-10070(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Sprague-Dawley.
Tissue: Liver.
[2]"Molecular structure of a functional rat gene for manganese-containing superoxide dismutase."
Ho Y.-S., Howard A.J., Crapo J.D.
Am. J. Respir. Cell Mol. Biol. 4:278-286(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: Sprague-Dawley.
Tissue: Liver.
[3]"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].
Tissue: Heart.
[4]Lubec G., Afjehi-Sadat L., Diao W., Kang S.U.
Submitted (JUL-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 54-68; 76-108; 135-154 AND 203-216, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: Sprague-Dawley.
Tissue: Brain, Hippocampus and Spinal cord.
[5]"Quantitative assessment of tyrosine nitration of manganese superoxide dismutase in angiotensin II-infused rat kidney."
Guo W., Adachi T., Matsui R., Xu S., Jiang B., Zou M.H., Kirber M., Lieberthal W., Cohen R.A.
Am. J. Physiol. 285:H1396-H1403(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NITRATION, FUNCTION DURING OXIDATIVE STRESS.
[6]"Detection of sequence-specific tyrosine nitration of manganese SOD and SERCA in cardiovascular disease and aging."
Xu S., Ying J., Jiang B., Guo W., Adachi T., Sharov V., Lazar H., Menzoian J., Knyushko T.V., Bigelow D., Schoeneich C., Cohen R.A.
Am. J. Physiol. 290:H2220-H2227(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NITRATION AT TYR-58.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Y00497 mRNA. Translation: CAA68549.1.
X56600 Genomic DNA. Translation: CAA39937.1.
BC070913 mRNA. Translation: AAH70913.1.
PIRDSRTN. S21661.
RefSeqNP_058747.1. NM_017051.2.
UniGeneRn.10488.

3D structure databases

ProteinModelPortalP07895.
SMRP07895. Positions 25-222.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP07895. 1 interaction.

PTM databases

PhosphoSiteP07895.

2D gel databases

World-2DPAGE0004:P07895.

Proteomic databases

PaxDbP07895.
PRIDEP07895.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000025794; ENSRNOP00000025794; ENSRNOG00000019048.
GeneID24787.
KEGGrno:24787.

Organism-specific databases

CTD6648.
RGD3732. Sod2.

Phylogenomic databases

eggNOGCOG0605.
GeneTreeENSGT00390000011877.
HOGENOMHOG000013583.
HOVERGENHBG004451.
InParanoidP07895.
KOK04564.
OMAMAIRCVA.
OrthoDBEOG7FV3R5.
PhylomeDBP07895.
TreeFamTF105132.

Gene expression databases

GenevestigatorP07895.

Family and domain databases

InterProIPR001189. Mn/Fe_SOD.
IPR019833. Mn/Fe_SOD_BS.
IPR019832. Mn/Fe_SOD_C.
IPR019831. Mn/Fe_SOD_N.
[Graphical view]
PANTHERPTHR11404. PTHR11404. 1 hit.
PfamPF02777. Sod_Fe_C. 1 hit.
PF00081. Sod_Fe_N. 1 hit.
[Graphical view]
PIRSFPIRSF000349. SODismutase. 1 hit.
PRINTSPR01703. MNSODISMTASE.
SUPFAMSSF46609. SSF46609. 1 hit.
SSF54719. SSF54719. 1 hit.
PROSITEPS00088. SOD_MN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio604412.
PROP07895.

Entry information

Entry nameSODM_RAT
AccessionPrimary (citable) accession number: P07895
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: May 1, 1992
Last modified: June 11, 2014
This is version 129 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