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Protein

Superoxide dismutase [Mn], mitochondrial

Gene

SOD2

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

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

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

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

Manganese, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Superoxide dismutase [Mn], mitochondrial (EC:1.15.1.1)
Gene namesi
Name:SOD2
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 2424MitochondrionBy similarityAdd
BLAST
Chaini25 – 222198Superoxide dismutase [Mn], mitochondrialPRO_0000032866Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei58 – 581Nitrated tyrosineBy similarity
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 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 (By similarity).By similarity
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

PaxDbiP41976.
PRIDEiP41976.

Interactioni

Subunit structurei

Homotetramer.By similarity

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000008569.

Structurei

3D structure databases

ProteinModelPortaliP41976.
SMRiP41976. Positions 25-222.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG0876. Eukaryota.
COG0605. LUCA.
HOVERGENiHBG004451.
InParanoidiP41976.
KOiK04564.

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.

P41976-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLSRAACSTS RRLVPALSVL GSRQKHSLPD LPYDYGALEP HINAQIMQLH
60 70 80 90 100
HSKHHAAYVN NLNVAEEKYR EALEKGDVTA QIALQPALKF NGGGHINHSI
110 120 130 140 150
FWTNLSPNGG GEPQGELLEA IKRDFGSFAK FKEKLTAVSV GVQGSGWGWL
160 170 180 190 200
GFNKEQGRLQ IAACSNQDPL QGTTGLIPLL GIDVWEHAYY LQYKNVRPDY
210 220
LKAIWNVINW ENVTARYTAC SK
Length:222
Mass (Da):24,638
Last modified:November 1, 1995 - v1
Checksum:i806CC3FCB1A74413
GO

Sequence cautioni

The sequence AAA30655.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti8 – 81S → R in AAD14001 (PubMed:8292376).Curated
Sequence conflicti14 – 141V → A in AAX09005 (PubMed:16305752).Curated
Sequence conflicti90 – 901F → V in AAC60522 (PubMed:8292376).Curated
Sequence conflicti94 – 952GH → AI in BAC56526 (PubMed:12658628).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L22092 mRNA. Translation: AAA30655.1. Different initiation.
L22093 Genomic DNA. Translation: AAA30656.1.
S67818 mRNA. Translation: AAC60522.2.
S67819 Genomic DNA. Translation: AAD14001.1.
BT020988 mRNA. Translation: AAX09005.1.
BC105378 mRNA. Translation: AAI05379.1.
AB099036 mRNA. Translation: BAC56526.1.
PIRiI51918.
RefSeqiNP_963285.2. NM_201527.2.
XP_010807032.1. XM_010808730.1.
UniGeneiBt.4748.

Genome annotation databases

GeneIDi104973000.
281496.
KEGGibta:104973000.
bta:281496.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L22092 mRNA. Translation: AAA30655.1. Different initiation.
L22093 Genomic DNA. Translation: AAA30656.1.
S67818 mRNA. Translation: AAC60522.2.
S67819 Genomic DNA. Translation: AAD14001.1.
BT020988 mRNA. Translation: AAX09005.1.
BC105378 mRNA. Translation: AAI05379.1.
AB099036 mRNA. Translation: BAC56526.1.
PIRiI51918.
RefSeqiNP_963285.2. NM_201527.2.
XP_010807032.1. XM_010808730.1.
UniGeneiBt.4748.

3D structure databases

ProteinModelPortaliP41976.
SMRiP41976. Positions 25-222.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000008569.

Proteomic databases

PaxDbiP41976.
PRIDEiP41976.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi104973000.
281496.
KEGGibta:104973000.
bta:281496.

Organism-specific databases

CTDi6648.

Phylogenomic databases

eggNOGiKOG0876. Eukaryota.
COG0605. LUCA.
HOVERGENiHBG004451.
InParanoidiP41976.
KOiK04564.

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. "Identification and functional characterization of the bovine manganous superoxide dismutase promoter."
    Meyrick B., Magnuson M.A.
    Am. J. Respir. Cell Mol. Biol. 10:113-121(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
    Tissue: Lung.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  3. NIH - Mammalian Gene Collection (MGC) project
    Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Crossbred X Angus.
    Tissue: Ileum.
  4. "Characterization of gene expression profiles in early bovine pregnancy using a custom cDNA microarray."
    Ishiwata H., Katsuma S., Kizaki K., Patel O.V., Nakano H., Takahashi T., Imai K., Hirasawa A., Shiojima S., Ikawa H., Suzuki Y., Tsujimoto G., Izaike Y., Todoroki J., Hashizume K.
    Mol. Reprod. Dev. 65:9-18(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 93-201.

Entry informationi

Entry nameiSODM_BOVIN
AccessioniPrimary (citable) accession number: P41976
Secondary accession number(s): Q2KJE8, Q5E9D2, Q862F8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: June 8, 2016
This is version 112 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

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 one 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.