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Protein

Superoxide dismutase [Mn], mitochondrial

Gene

Sod2

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems.1 Publication

Catalytic activityi

2 superoxide + 2 H+ = O2 + H2O2.

Cofactori

Mn2+By similarityNote: Binds 1 Mn2+ ion per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi50 – 501ManganeseBy similarity
Metal bindingi98 – 981ManganeseBy similarity
Metal bindingi183 – 1831ManganeseBy similarity
Metal bindingi187 – 1871ManganeseBy similarity

GO - Molecular functioni

  • DNA binding Source: RGD
  • identical protein binding Source: RGD
  • manganese ion binding Source: UniProtKB
  • oxygen binding Source: RGD
  • superoxide dismutase activity Source: UniProtKB

GO - Biological processi

  • age-dependent response to reactive oxygen species Source: UniProtKB
  • aging Source: RGD
  • cellular response to ethanol Source: RGD
  • detection of oxygen Source: Ensembl
  • erythrophore differentiation Source: Ensembl
  • glutathione metabolic process Source: Ensembl
  • heart development Source: Ensembl
  • hemopoiesis Source: Ensembl
  • hydrogen peroxide biosynthetic process Source: RGD
  • hydrogen peroxide metabolic process Source: RGD
  • intrinsic apoptotic signaling pathway in response to DNA damage Source: Ensembl
  • intrinsic apoptotic signaling pathway in response to oxidative stress Source: Ensembl
  • iron ion homeostasis Source: Ensembl
  • liver development Source: Ensembl
  • locomotory behavior Source: Ensembl
  • negative regulation of apoptotic process Source: RGD
  • negative regulation of fat cell differentiation Source: Ensembl
  • negative regulation of fibroblast proliferation Source: Ensembl
  • negative regulation of neuron apoptotic process Source: Ensembl
  • negative regulation of oxidative stress-induced intrinsic apoptotic signaling pathway Source: Ensembl
  • neuron development Source: Ensembl
  • oxygen homeostasis Source: Ensembl
  • positive regulation of nitric oxide biosynthetic process Source: Ensembl
  • post-embryonic development Source: Ensembl
  • protein homooligomerization Source: RGD
  • protein homotetramerization Source: Ensembl
  • regulation of catalytic activity Source: Ensembl
  • regulation of mitochondrial membrane potential Source: Ensembl
  • regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  • release of cytochrome c from mitochondria Source: Ensembl
  • removal of superoxide radicals Source: RGD
  • respiratory electron transport chain Source: Ensembl
  • response to activity Source: RGD
  • response to axon injury Source: Ensembl
  • response to cadmium ion Source: RGD
  • response to cold Source: RGD
  • response to drug Source: RGD
  • response to electrical stimulus Source: RGD
  • response to gamma radiation Source: Ensembl
  • response to hydrogen peroxide Source: RGD
  • response to hyperoxia Source: Ensembl
  • response to hypoxia Source: RGD
  • response to immobilization stress Source: RGD
  • response to isolation stress Source: RGD
  • response to L-ascorbic acid Source: RGD
  • response to lipopolysaccharide Source: RGD
  • response to magnetism Source: RGD
  • response to manganese ion Source: RGD
  • response to nutrient levels Source: RGD
  • response to oxidative stress Source: RGD
  • response to radiation Source: RGD
  • response to selenium ion Source: RGD
  • response to silicon dioxide Source: RGD
  • response to zinc ion Source: RGD
  • superoxide anion generation Source: Ensembl
  • superoxide metabolic process Source: UniProtKB
  • vasodilation by acetylcholine involved in regulation of systemic arterial blood pressure Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

Manganese, Metal-binding

Enzyme and pathway databases

ReactomeiREACT_317923. Detoxification of Reactive Oxygen Species.

Names & Taxonomyi

Protein namesi
Recommended name:
Superoxide dismutase [Mn], mitochondrial (EC:1.15.1.1)
Gene namesi
Name:Sod2
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494 Componenti: Chromosome 1

Organism-specific databases

RGDi3732. Sod2.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: RGD
  • extracellular exosome Source: Ensembl
  • mitochondrial inner membrane Source: Ensembl
  • mitochondrial nucleoid Source: RGD
  • mitochondrion Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 2424MitochondrionAdd
BLAST
Chaini25 – 222198Superoxide dismutase [Mn], mitochondrialPRO_0000032874Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei58 – 581Nitrated tyrosine1 Publication
Modified residuei68 – 681N6-acetyllysine; alternateBy similarity
Modified residuei68 – 681N6-succinyllysine; alternateBy similarity
Modified residuei75 – 751N6-acetyllysine; alternateBy similarity
Modified residuei75 – 751N6-succinyllysine; alternateBy similarity
Modified residuei114 – 1141N6-acetyllysineBy similarity
Modified residuei122 – 1221N6-acetyllysine; alternateBy similarity
Modified residuei122 – 1221N6-succinyllysine; alternateBy similarity
Modified residuei130 – 1301N6-acetyllysine; alternateBy similarity
Modified residuei130 – 1301N6-succinyllysine; alternateBy similarity
Modified residuei202 – 2021N6-acetyllysineBy similarity

Post-translational modificationi

Nitrated under oxidative stress. Nitration coupled with oxidation inhibits the catalytic activity.2 Publications
Acetylation at Lys-122 decreases enzymatic activity. Deacetylated by SIRT3 upon exposure to ionizing radiations or after long fasting (By similarity).By similarity

Keywords - PTMi

Acetylation, Nitration

Proteomic databases

PaxDbiP07895.
PRIDEiP07895.

2D gel databases

World-2DPAGE0004:P07895.

PTM databases

PhosphoSiteiP07895.

Expressioni

Gene expression databases

ExpressionAtlasiP07895. baseline and differential.
GenevisibleiP07895. RN.

Interactioni

Subunit structurei

Homotetramer.

Protein-protein interaction databases

IntActiP07895. 1 interaction.
STRINGi10116.ENSRNOP00000025794.

Structurei

3D structure databases

ProteinModelPortaliP07895.
SMRiP07895. Positions 25-222.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0605.
GeneTreeiENSGT00390000011877.
HOGENOMiHOG000013583.
HOVERGENiHBG004451.
InParanoidiP07895.
KOiK04564.
OMAiGTEWAEW.
OrthoDBiEOG7FV3R5.
PhylomeDBiP07895.
TreeFamiTF105132.

Family and domain databases

InterProiIPR001189. Mn/Fe_SOD.
IPR019833. Mn/Fe_SOD_BS.
IPR019832. Mn/Fe_SOD_C.
IPR019831. Mn/Fe_SOD_N.
[Graphical view]
PANTHERiPTHR11404. PTHR11404. 1 hit.
PfamiPF02777. Sod_Fe_C. 1 hit.
PF00081. Sod_Fe_N. 1 hit.
[Graphical view]
PIRSFiPIRSF000349. SODismutase. 1 hit.
PRINTSiPR01703. MNSODISMTASE.
SUPFAMiSSF46609. SSF46609. 1 hit.
SSF54719. SSF54719. 1 hit.
PROSITEiPS00088. SOD_MN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P07895-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLCRAACSAG RRLGPAASTA GSRHKHSLPD LPYDYGALEP HINAQIMQLH
60 70 80 90 100
HSKHHATYVN NLNVTEEKYH EALAKGDVTT QVALQPALKF NGGGHINHSI
110 120 130 140 150
FWTNLSPKGG GEPKGELLEA IKRDFGSFEK FKEKLTAVSV GVQGSGWGWL
160 170 180 190 200
GFNKEQGRLQ IAACSNQDPL QGTTGLIPLL GIDVWEHAYY LQYKNVRPDY
210 220
LKAIWNVINW ENVSQRYIVC KK
Length:222
Mass (Da):24,674
Last modified:May 1, 1992 - v2
Checksum:i8CCC1E0E857B3138
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti167 – 1671Q → H in CAA68549 (PubMed:3697077).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y00497 mRNA. Translation: CAA68549.1.
X56600 Genomic DNA. Translation: CAA39937.1.
BC070913 mRNA. Translation: AAH70913.1.
PIRiS21661. DSRTN.
RefSeqiNP_058747.1. NM_017051.2.
UniGeneiRn.10488.

Genome annotation databases

EnsembliENSRNOT00000025794; ENSRNOP00000025794; ENSRNOG00000019048.
GeneIDi24787.
KEGGirno:24787.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y00497 mRNA. Translation: CAA68549.1.
X56600 Genomic DNA. Translation: CAA39937.1.
BC070913 mRNA. Translation: AAH70913.1.
PIRiS21661. DSRTN.
RefSeqiNP_058747.1. NM_017051.2.
UniGeneiRn.10488.

3D structure databases

ProteinModelPortaliP07895.
SMRiP07895. Positions 25-222.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP07895. 1 interaction.
STRINGi10116.ENSRNOP00000025794.

PTM databases

PhosphoSiteiP07895.

2D gel databases

World-2DPAGE0004:P07895.

Proteomic databases

PaxDbiP07895.
PRIDEiP07895.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000025794; ENSRNOP00000025794; ENSRNOG00000019048.
GeneIDi24787.
KEGGirno:24787.

Organism-specific databases

CTDi6648.
RGDi3732. Sod2.

Phylogenomic databases

eggNOGiCOG0605.
GeneTreeiENSGT00390000011877.
HOGENOMiHOG000013583.
HOVERGENiHBG004451.
InParanoidiP07895.
KOiK04564.
OMAiGTEWAEW.
OrthoDBiEOG7FV3R5.
PhylomeDBiP07895.
TreeFamiTF105132.

Enzyme and pathway databases

ReactomeiREACT_317923. Detoxification of Reactive Oxygen Species.

Miscellaneous databases

NextBioi604412.
PROiP07895.

Gene expression databases

ExpressionAtlasiP07895. baseline and differential.
GenevisibleiP07895. RN.

Family and domain databases

InterProiIPR001189. Mn/Fe_SOD.
IPR019833. Mn/Fe_SOD_BS.
IPR019832. Mn/Fe_SOD_C.
IPR019831. Mn/Fe_SOD_N.
[Graphical view]
PANTHERiPTHR11404. PTHR11404. 1 hit.
PfamiPF02777. Sod_Fe_C. 1 hit.
PF00081. Sod_Fe_N. 1 hit.
[Graphical view]
PIRSFiPIRSF000349. SODismutase. 1 hit.
PRINTSiPR01703. MNSODISMTASE.
SUPFAMiSSF46609. SSF46609. 1 hit.
SSF54719. SSF54719. 1 hit.
PROSITEiPS00088. SOD_MN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.

Entry informationi

Entry nameiSODM_RAT
AccessioniPrimary (citable) accession number: P07895
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: May 1, 1992
Last modified: June 24, 2015
This is version 138 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.