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Protein

Superoxide dismutase [Mn], mitochondrial

Gene

sod2

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
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+1 PublicationNote: Binds 1 Mn2+ ion per subunit.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi50 – 501ManganeseBy similarity
Metal bindingi96 – 961ManganeseBy similarity
Metal bindingi181 – 1811ManganeseBy similarity
Metal bindingi185 – 1851ManganeseBy similarity

GO - Molecular functioni

  1. manganese ion binding Source: PomBase
  2. superoxide dismutase activity Source: PomBase

GO - Biological processi

  1. age-dependent response to reactive oxygen species involved in chronological cell aging Source: PomBase
  2. removal of superoxide radicals Source: PomBase
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

Manganese, Metal-binding

Enzyme and pathway databases

ReactomeiREACT_219607. Detoxification of Reactive Oxygen Species.

Names & Taxonomyi

Protein namesi
Recommended name:
Superoxide dismutase [Mn], mitochondrial (EC:1.15.1.1)
Gene namesi
Name:sod2
ORF Names:SPAC1486.01
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
ProteomesiUP000002485: Chromosome I

Organism-specific databases

PomBaseiSPAC1486.01.

Subcellular locationi

Mitochondrion matrix 1 Publication

GO - Cellular componenti

  1. mitochondrial matrix Source: PomBase
  2. mitochondrion Source: PomBase
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 2121Mitochondrion1 PublicationAdd
BLAST
Chaini22 – 218197Superoxide dismutase [Mn], mitochondrialPRO_0000032887Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei129 – 1291Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9UQX0.
PaxDbiQ9UQX0.

Expressioni

Inductioni

By high osmolarity and heat.1 Publication

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

BioGridi279331. 33 interactions.
MINTiMINT-4706830.
STRINGi4896.SPAC1486.01-1.

Structurei

3D structure databases

ProteinModelPortaliQ9UQX0.
SMRiQ9UQX0. Positions 25-217.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0605.
HOGENOMiHOG000013583.
KOiK04564.
OMAiVNWDDVE.
PhylomeDBiQ9UQX0.

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.

Q9UQX0-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MLRFLSKNSV AAIRNVSIAR GVHTKATLPP LPYAYNALEP ALSETIMKLH
60 70 80 90 100
HDKHHQTYVN NLNAAQEKLA DPNLDLEGEV ALQAAIKFNG GGHINHSLFW
110 120 130 140 150
KILAPQKEGG GKPVTSGSLH KAITSKWGSL EDFQKEMNAA LASIQGSGWA
160 170 180 190 200
WLIVDKDGSL RITTTANQDT IVKSKPIIGI DAWEHAYYPQ YENRKAEYFK
210
AIWNVINWKE AESRYSNR
Length:218
Mass (Da):24,347
Last modified:May 1, 2000 - v1
Checksum:iF701C8375830DDE7
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF069292 Genomic DNA. Translation: AAF19051.1.
CU329670 Genomic DNA. Translation: CAB62411.1.
PIRiT50070.
RefSeqiNP_594089.1. NM_001019513.2.

Genome annotation databases

EnsemblFungiiSPAC1486.01.1; SPAC1486.01.1:pep; SPAC1486.01.
GeneIDi2542886.
KEGGispo:SPAC1486.01.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF069292 Genomic DNA. Translation: AAF19051.1.
CU329670 Genomic DNA. Translation: CAB62411.1.
PIRiT50070.
RefSeqiNP_594089.1. NM_001019513.2.

3D structure databases

ProteinModelPortaliQ9UQX0.
SMRiQ9UQX0. Positions 25-217.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi279331. 33 interactions.
MINTiMINT-4706830.
STRINGi4896.SPAC1486.01-1.

Proteomic databases

MaxQBiQ9UQX0.
PaxDbiQ9UQX0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPAC1486.01.1; SPAC1486.01.1:pep; SPAC1486.01.
GeneIDi2542886.
KEGGispo:SPAC1486.01.

Organism-specific databases

PomBaseiSPAC1486.01.

Phylogenomic databases

eggNOGiCOG0605.
HOGENOMiHOG000013583.
KOiK04564.
OMAiVNWDDVE.
PhylomeDBiQ9UQX0.

Enzyme and pathway databases

ReactomeiREACT_219607. Detoxification of Reactive Oxygen Species.

Miscellaneous databases

NextBioi20803926.
PROiQ9UQX0.

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. "Isolation and characterization of the sod2+ gene encoding a putative mitochondrial manganese superoxide dismutase in Schizosaccharomyces pombe."
    Jeong J.-H., Kwon E.-S., Roe J.-H.
    J. Microbiol. 39:37-41(2001)
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 972 / ATCC 24843.
  2. "The genome sequence of Schizosaccharomyces pombe."
    Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.
    , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
    Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 972 / ATCC 24843.
  3. "Characterization of the manganese-containing superoxide dismutase and its gene regulation in stress response of Schizosaccharomyces pombe."
    Jeong J.-H., Kwon E.-S., Roe J.-H.
    Biochem. Biophys. Res. Commun. 283:908-914(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 22-34, COFACTOR, SUBUNIT, SUBCELLULAR LOCATION, INDUCTION.
    Strain: JH201.
  4. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-129, IDENTIFICATION BY MASS SPECTROMETRY.

Entry informationi

Entry nameiSODM_SCHPO
AccessioniPrimary (citable) accession number: Q9UQX0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 27, 2002
Last sequence update: May 1, 2000
Last modified: January 7, 2015
This is version 105 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  2. 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.