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Protein

Superoxide dismutase [Mn] 1, mitochondrial

Gene

sod-2

Organism
Caenorhabditis elegans
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.

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 bindingi182 – 1821ManganeseBy similarity
Metal bindingi186 – 1861ManganeseBy similarity

GO - Molecular functioni

  • metal ion binding Source: UniProtKB-KW
  • protein homodimerization activity Source: WormBase
  • superoxide dismutase activity Source: WormBase

GO - Biological processi

  • removal of superoxide radicals Source: WormBase
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

Manganese, Metal-binding

Enzyme and pathway databases

ReactomeiR-CEL-3299685. Detoxification of Reactive Oxygen Species.

Names & Taxonomyi

Protein namesi
Recommended name:
Superoxide dismutase [Mn] 1, mitochondrial (EC:1.15.1.1)
Gene namesi
Name:sod-2
Synonyms:sdm-1
ORF Names:F10D11.1
OrganismiCaenorhabditis elegans
Taxonomic identifieri6239 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaNematodaChromadoreaRhabditidaRhabditoideaRhabditidaePeloderinaeCaenorhabditis
Proteomesi
  • UP000001940 Componenti: Chromosome I

Organism-specific databases

WormBaseiF10D11.1; CE09323; WBGene00004931; sod-2.

Subcellular locationi

GO - Cellular componenti

  • mitochondrial matrix Source: UniProtKB-SubCell
  • mitochondrial respiratory chain supercomplex Source: WormBase
  • mitochondrion Source: WormBase
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 2424MitochondrionBy similarityAdd
BLAST
Chaini25 – 221197Superoxide dismutase [Mn] 1, mitochondrialPRO_0000032876Add
BLAST

Proteomic databases

EPDiP31161.
PaxDbiP31161.

PTM databases

iPTMnetiP31161.

Interactioni

Subunit structurei

Homotetramer.

GO - Molecular functioni

  • protein homodimerization activity Source: WormBase

Protein-protein interaction databases

STRINGi6239.F10D11.1.2.

Structurei

Secondary structure

1
221
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni35 – 417Combined sources
Helixi44 – 529Combined sources
Helixi54 – 7421Combined sources
Helixi78 – 836Combined sources
Helixi85 – 10319Combined sources
Helixi114 – 12411Combined sources
Helixi127 – 13913Combined sources
Beta strandi143 – 15210Combined sources
Turni153 – 1564Combined sources
Beta strandi157 – 1648Combined sources
Helixi169 – 1735Combined sources
Beta strandi176 – 1827Combined sources
Helixi185 – 1873Combined sources
Helixi189 – 1924Combined sources
Helixi196 – 2027Combined sources
Helixi203 – 2064Combined sources
Helixi209 – 21911Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3DC6X-ray1.80A/C25-221[»]
ProteinModelPortaliP31161.
SMRiP31161. Positions 25-221.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP31161.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG0876. Eukaryota.
COG0605. LUCA.
GeneTreeiENSGT00390000011877.
HOGENOMiHOG000013583.
InParanoidiP31161.
KOiK04564.
OMAiEQVYDHQ.
PhylomeDBiP31161.

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.

P31161-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLQNTVRCVS KLVQPITGVA AVRSKHSLPD LPYDYADLEP VISHEIMQLH
60 70 80 90 100
HQKHHATYVN NLNQIEEKLH EAVSKGNVKE AIALQPALKF NGGGHINHSI
110 120 130 140 150
FWTNLAKDGG EPSAELLTAI KSDFGSLDNL QKQLSASTVA VQGSGWGWLG
160 170 180 190 200
YCPKGKILKV ATCANQDPLE ATTGLVPLFG IDVWEHAYYL QYKNVRPDYV
210 220
NAIWKIANWK NVSERFAKAQ Q
Length:221
Mass (Da):24,537
Last modified:July 1, 1993 - v1
Checksum:iEEA518B2800379F7
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D12984 mRNA. Translation: BAA02363.1.
D85499 Genomic DNA. Translation: BAA12821.1.
Z81057 Genomic DNA. Translation: CAB02913.1.
PIRiJC5122.
RefSeqiNP_492290.1. NM_059889.4.
UniGeneiCel.112.

Genome annotation databases

EnsemblMetazoaiF10D11.1.1; F10D11.1.1; WBGene00004931.
F10D11.1.2; F10D11.1.2; WBGene00004931.
GeneIDi172632.
KEGGicel:CELE_F10D11.1.
UCSCiF10D11.1.1. c. elegans.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D12984 mRNA. Translation: BAA02363.1.
D85499 Genomic DNA. Translation: BAA12821.1.
Z81057 Genomic DNA. Translation: CAB02913.1.
PIRiJC5122.
RefSeqiNP_492290.1. NM_059889.4.
UniGeneiCel.112.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3DC6X-ray1.80A/C25-221[»]
ProteinModelPortaliP31161.
SMRiP31161. Positions 25-221.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi6239.F10D11.1.2.

PTM databases

iPTMnetiP31161.

Proteomic databases

EPDiP31161.
PaxDbiP31161.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiF10D11.1.1; F10D11.1.1; WBGene00004931.
F10D11.1.2; F10D11.1.2; WBGene00004931.
GeneIDi172632.
KEGGicel:CELE_F10D11.1.
UCSCiF10D11.1.1. c. elegans.

Organism-specific databases

CTDi172632.
WormBaseiF10D11.1; CE09323; WBGene00004931; sod-2.

Phylogenomic databases

eggNOGiKOG0876. Eukaryota.
COG0605. LUCA.
GeneTreeiENSGT00390000011877.
HOGENOMiHOG000013583.
InParanoidiP31161.
KOiK04564.
OMAiEQVYDHQ.
PhylomeDBiP31161.

Enzyme and pathway databases

ReactomeiR-CEL-3299685. Detoxification of Reactive Oxygen Species.

Miscellaneous databases

EvolutionaryTraceiP31161.
NextBioi876347.
PROiP31161.

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. "Cloning and characterization of manganese superoxide dismutase gene in C.elegans."
    Suzuki N., Ishii N., Suzuki K.
    Submitted (SEP-1992) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Cloning, sequencing and mapping of a manganese superoxide dismutase gene of the nematode Caenorhabditis elegans."
    Suzuki N., Inokuma K., Yasuda K., Ishii N.
    DNA Res. 3:171-174(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Genome sequence of the nematode C. elegans: a platform for investigating biology."
    The C. elegans sequencing consortium
    Science 282:2012-2018(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Bristol N2.

Entry informationi

Entry nameiSODM1_CAEEL
AccessioniPrimary (citable) accession number: P31161
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: July 1, 1993
Last modified: March 16, 2016
This is version 119 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programCaenorhabditis annotation project

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Caenorhabditis elegans
    Caenorhabditis elegans: entries, gene names and cross-references to WormBase
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.