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Protein

Superoxide dismutase [Mn] 2, mitochondrial

Gene

sod-3

Organism
Caenorhabditis elegans
Status
Reviewed-Annotation score: Annotation score: 4 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 bindingi179 – 1791ManganeseBy similarity
Metal bindingi183 – 1831ManganeseBy 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

ReactomeiREACT_324379. Detoxification of Reactive Oxygen Species.

Names & Taxonomyi

Protein namesi
Recommended name:
Superoxide dismutase [Mn] 2, mitochondrial (EC:1.15.1.1)
Gene namesi
Name:sod-3
ORF Names:C08A9.1
OrganismiCaenorhabditis elegans
Taxonomic identifieri6239 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaNematodaChromadoreaRhabditidaRhabditoideaRhabditidaePeloderinaeCaenorhabditis
ProteomesiUP000001940 Componenti: Chromosome X

Organism-specific databases

WormBaseiC08A9.1; CE08002; WBGene00004932; sod-3.

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 – 218194Superoxide dismutase [Mn] 2, mitochondrialPRO_0000032877Add
BLAST

Proteomic databases

PaxDbiP41977.
PRIDEiP41977.

Interactioni

Subunit structurei

Homotetramer.By similarity

Protein-protein interaction databases

STRINGi6239.C08A9.1.1.

Structurei

Secondary structure

1
218
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni35 – 417Combined sources
Helixi44 – 529Combined sources
Helixi54 – 7522Combined sources
Helixi78 – 836Combined sources
Helixi85 – 10319Combined sources
Helixi114 – 12411Combined sources
Helixi127 – 13913Combined sources
Beta strandi143 – 15210Combined sources
Turni153 – 1564Combined sources
Beta strandi157 – 1648Combined sources
Beta strandi171 – 1799Combined sources
Helixi182 – 1843Combined sources
Helixi186 – 1894Combined sources
Helixi193 – 2008Combined sources
Helixi201 – 2033Combined sources
Helixi206 – 21712Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3DC5X-ray1.70A/C25-218[»]
ProteinModelPortaliP41977.
SMRiP41977. Positions 25-218.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP41977.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0605.
GeneTreeiENSGT00390000011877.
HOGENOMiHOG000013583.
InParanoidiP41977.
KOiK04564.
OMAiATHKLEV.
OrthoDBiEOG7FV3R5.
PhylomeDBiP41977.

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.

P41977-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLQSTARTAS KLVQPVAGVL AVRSKHTLPD LPFDYADLEP VISHEIMQLH
60 70 80 90 100
HQKHHATYVN NLNQIEEKLH EAVSKGNLKE AIALQPALKF NGGGHINHSI
110 120 130 140 150
FWTNLAKDGG EPSKELMDTI KRDFGSLDNL QKRLSDITIA VQGSGWGWLG
160 170 180 190 200
YCKKDKILKI ATCANQDPLE GMVPLFGIDV WEHAYYLQYK NVRPDYVHAI
210
WKIANWKNIS ERFANARQ
Length:218
Mass (Da):24,661
Last modified:February 1, 1996 - v2
Checksum:iF35375C9E63BCDC7
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X77021 Genomic DNA. Translation: CAA54319.1.
X85790 mRNA. Translation: CAA59790.1.
FO080426 Genomic DNA. Translation: CCD63614.1.
PIRiS52721.
RefSeqiNP_510764.1. NM_078363.6.
UniGeneiCel.17915.

Genome annotation databases

EnsemblMetazoaiC08A9.1; C08A9.1; WBGene00004932.
GeneIDi181748.
KEGGicel:CELE_C08A9.1.
UCSCiC08A9.1.1. c. elegans.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X77021 Genomic DNA. Translation: CAA54319.1.
X85790 mRNA. Translation: CAA59790.1.
FO080426 Genomic DNA. Translation: CCD63614.1.
PIRiS52721.
RefSeqiNP_510764.1. NM_078363.6.
UniGeneiCel.17915.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3DC5X-ray1.70A/C25-218[»]
ProteinModelPortaliP41977.
SMRiP41977. Positions 25-218.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi6239.C08A9.1.1.

Proteomic databases

PaxDbiP41977.
PRIDEiP41977.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiC08A9.1; C08A9.1; WBGene00004932.
GeneIDi181748.
KEGGicel:CELE_C08A9.1.
UCSCiC08A9.1.1. c. elegans.

Organism-specific databases

CTDi181748.
WormBaseiC08A9.1; CE08002; WBGene00004932; sod-3.

Phylogenomic databases

eggNOGiCOG0605.
GeneTreeiENSGT00390000011877.
HOGENOMiHOG000013583.
InParanoidiP41977.
KOiK04564.
OMAiATHKLEV.
OrthoDBiEOG7FV3R5.
PhylomeDBiP41977.

Enzyme and pathway databases

ReactomeiREACT_324379. Detoxification of Reactive Oxygen Species.

Miscellaneous databases

EvolutionaryTraceiP41977.
NextBioi915182.
PROiP41977.

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. "The manganese superoxide dismutase gene of Caenorhabditis elegans."
    Giglio M.P., Hunter T., Bannister J.V., Bannister W.H., Hunter G.J.
    Biochem. Mol. Biol. Int. 33:37-40(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
    Strain: Bristol N2.
  2. "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 nameiSODM2_CAEEL
AccessioniPrimary (citable) accession number: P41977
Secondary accession number(s): Q27469
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: February 1, 1996
Last modified: April 29, 2015
This is version 116 of the entry and version 2 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

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.