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Protein

Superoxide dismutase [Mn], mitochondrial

Gene

Sod2

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 5 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 bindingi43 – 431ManganeseBy similarity
Metal bindingi91 – 911ManganeseBy similarity
Metal bindingi175 – 1751ManganeseBy similarity
Metal bindingi179 – 1791ManganeseBy similarity

GO - Molecular functioni

  • antioxidant activity Source: FlyBase
  • metal ion binding Source: UniProtKB-KW
  • superoxide dismutase activity Source: FlyBase

GO - Biological processi

  • determination of adult lifespan Source: FlyBase
  • heart morphogenesis Source: FlyBase
  • paracrine signaling Source: FlyBase
  • reactive oxygen species metabolic process Source: FlyBase
  • regulation of hemocyte proliferation Source: FlyBase
  • regulation of metabolic process Source: FlyBase
  • regulation of mitophagy Source: FlyBase
  • removal of superoxide radicals Source: FlyBase
  • superoxide metabolic process Source: FlyBase
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

Manganese, Metal-binding

Enzyme and pathway databases

ReactomeiR-DME-3299685. 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:CG8905
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 2R

Organism-specific databases

FlyBaseiFBgn0010213. Sod2.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Protein family/group databases

Allergomei868. Dro m MnSOD.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 1717MitochondrionBy similarityAdd
BLAST
Chaini18 – 217200Superoxide dismutase [Mn], mitochondrialPRO_0000032879Add
BLAST

Proteomic databases

PaxDbiQ00637.
PRIDEiQ00637.

Expressioni

Gene expression databases

BgeeiQ00637.
GenevisibleiQ00637. DM.

Interactioni

Subunit structurei

Homotetramer.

Protein-protein interaction databases

BioGridi62587. 6 interactions.
MINTiMINT-860718.
STRINGi7227.FBpp0086226.

Structurei

3D structure databases

ProteinModelPortaliQ00637.
SMRiQ00637. Positions 18-214.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG0876. Eukaryota.
COG0605. LUCA.
InParanoidiQ00637.
KOiK04564.
OrthoDBiEOG7FV3R5.
PhylomeDBiQ00637.

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.

Q00637-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFVARKISPN CKPGVRGKHT LPKLPYDYAA LEPIICREIM ELHHQKHHQT
60 70 80 90 100
YVNNLNAAEE QLEEAKSKSD TTKLIQLAPA LRFNGGGHIN HTIFWQNLSP
110 120 130 140 150
NKTQPSDDLK KAIESQWKSL EEFKKELTTL TVAVQGSGWG WLGFNKKSGK
160 170 180 190 200
LQLAALPNQD PLEASTGLIP LFGIDVWEHA YYLQYKNVRP SYVEAIWDIA
210
NWDDISCRFQ EAKKLGC
Length:217
Mass (Da):24,684
Last modified:November 1, 1995 - v3
Checksum:i05900339EA92432B
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti9 – 146PNCKPG → QTASLA (Ref. 2) Curated
Sequence conflicti9 – 146PNCKPG → QTASLA (PubMed:10731132).Curated
Sequence conflicti127 – 1271L → V in CAA45418 (PubMed:1556751).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L18947 mRNA. Translation: AAA20533.1.
L34276 Genomic DNA. Translation: AAA28694.1.
AE013599 Genomic DNA. Translation: AAF57955.1.
BT004505 mRNA. Translation: AAO42669.1.
X64062 mRNA. Translation: CAA45418.1.
PIRiS23657.
RefSeqiNP_001286503.1. NM_001299574.1.
NP_476925.1. NM_057577.4.
UniGeneiDm.4800.

Genome annotation databases

GeneIDi36878.
KEGGidme:Dmel_CG8905.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L18947 mRNA. Translation: AAA20533.1.
L34276 Genomic DNA. Translation: AAA28694.1.
AE013599 Genomic DNA. Translation: AAF57955.1.
BT004505 mRNA. Translation: AAO42669.1.
X64062 mRNA. Translation: CAA45418.1.
PIRiS23657.
RefSeqiNP_001286503.1. NM_001299574.1.
NP_476925.1. NM_057577.4.
UniGeneiDm.4800.

3D structure databases

ProteinModelPortaliQ00637.
SMRiQ00637. Positions 18-214.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi62587. 6 interactions.
MINTiMINT-860718.
STRINGi7227.FBpp0086226.

Protein family/group databases

Allergomei868. Dro m MnSOD.

Proteomic databases

PaxDbiQ00637.
PRIDEiQ00637.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi36878.
KEGGidme:Dmel_CG8905.

Organism-specific databases

CTDi6648.
FlyBaseiFBgn0010213. Sod2.

Phylogenomic databases

eggNOGiKOG0876. Eukaryota.
COG0605. LUCA.
InParanoidiQ00637.
KOiK04564.
OrthoDBiEOG7FV3R5.
PhylomeDBiQ00637.

Enzyme and pathway databases

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

Miscellaneous databases

GenomeRNAii36878.
PROiQ00637.

Gene expression databases

BgeeiQ00637.
GenevisibleiQ00637. DM.

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. "A manganese superoxide dismutase-encoding cDNA from Drosophila melanogaster."
    Duttaroy A., Meidinger R., Kirby K., Carmichael S., Hilliker A., Phillips J.
    Gene 143:223-225(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Canton-S.
  2. "Sequence analysis of a genomic clone encoding for manganese superoxide dismutase (mnSOD) in D. melanogaster."
    Phillips J.P., Kirby K.
    Submitted (JUL-1994) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: Canton-S.
  3. "The genome sequence of Drosophila melanogaster."
    Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
    , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
    Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Berkeley.
  4. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Berkeley.
    Tissue: Head.
  6. "A comparison of evolutionary rates of the two major kinds of superoxide dismutase."
    Smith M.W., Doolittle R.F.
    J. Mol. Evol. 34:175-184(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 34-176.
    Strain: Oregon-R.

Entry informationi

Entry nameiSODM_DROME
AccessioniPrimary (citable) accession number: Q00637
Secondary accession number(s): Q9V7T8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: November 1, 1995
Last modified: June 8, 2016
This is version 124 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. 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.