SODM_DROME
ID SODM_DROME Reviewed; 217 AA.
AC Q00637; Q9V7T8;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 3.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Superoxide dismutase [Mn], mitochondrial;
DE EC=1.15.1.1;
DE Flags: Precursor;
GN Name=Sod2; ORFNames=CG8905;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Canton-S;
RX PubMed=8206377; DOI=10.1016/0378-1119(94)90100-7;
RA Duttaroy A., Meidinger R., Kirby K., Carmichael S., Hilliker A.,
RA Phillips J.;
RT "A manganese superoxide dismutase-encoding cDNA from Drosophila
RT melanogaster.";
RL Gene 143:223-225(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Canton-S;
RA Phillips J.P., Kirby K.;
RT "Sequence analysis of a genomic clone encoding for manganese superoxide
RT dismutase (mnSOD) in D. melanogaster.";
RL Submitted (JUL-1994) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Head;
RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., Champe M.,
RA Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.A.,
RA Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., Miranda A.,
RA Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., Patel S.,
RA Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., Celniker S.E.;
RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 34-176.
RC STRAIN=Oregon-R;
RX PubMed=1556751; DOI=10.1007/bf00182394;
RA Smith M.W., Doolittle R.F.;
RT "A comparison of evolutionary rates of the two major kinds of superoxide
RT dismutase.";
RL J. Mol. Evol. 34:175-184(1992).
CC -!- FUNCTION: Destroys superoxide anion radicals which are normally
CC produced within the cells and which are toxic to biological systems.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 H(+) + 2 superoxide = H2O2 + O2; Xref=Rhea:RHEA:20696,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:18421; EC=1.15.1.1;
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC Note=Binds 1 Mn(2+) ion per subunit. {ECO:0000250};
CC -!- SUBUNIT: Homotetramer.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix.
CC -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase family.
CC {ECO:0000305}.
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DR EMBL; L18947; AAA20533.1; -; mRNA.
DR EMBL; L34276; AAA28694.1; -; Genomic_DNA.
DR EMBL; AE013599; AAF57955.1; -; Genomic_DNA.
DR EMBL; BT004505; AAO42669.1; -; mRNA.
DR EMBL; X64062; CAA45418.1; -; mRNA.
DR PIR; S23657; S23657.
DR RefSeq; NP_001286503.1; NM_001299574.1.
DR RefSeq; NP_476925.1; NM_057577.4.
DR AlphaFoldDB; Q00637; -.
DR SMR; Q00637; -.
DR BioGRID; 62587; 19.
DR STRING; 7227.FBpp0086226; -.
DR Allergome; 868; Dro m MnSOD.
DR PaxDb; Q00637; -.
DR PRIDE; Q00637; -.
DR DNASU; 36878; -.
DR GeneID; 36878; -.
DR KEGG; dme:Dmel_CG8905; -.
DR CTD; 6648; -.
DR FlyBase; FBgn0010213; Sod2.
DR VEuPathDB; VectorBase:FBgn0010213; -.
DR eggNOG; KOG0876; Eukaryota.
DR HOGENOM; CLU_031625_2_1_1; -.
DR InParanoid; Q00637; -.
DR PhylomeDB; Q00637; -.
DR Reactome; R-DME-3299685; Detoxification of Reactive Oxygen Species.
DR BioGRID-ORCS; 36878; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 36878; -.
DR PRO; PR:Q00637; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR ExpressionAtlas; Q00637; baseline and differential.
DR Genevisible; Q00637; DM.
DR GO; GO:0005759; C:mitochondrial matrix; ISS:FlyBase.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0016209; F:antioxidant activity; NAS:FlyBase.
DR GO; GO:0030145; F:manganese ion binding; IBA:GO_Central.
DR GO; GO:0004784; F:superoxide dismutase activity; ISS:FlyBase.
DR GO; GO:0008340; P:determination of adult lifespan; IMP:FlyBase.
DR GO; GO:0003007; P:heart morphogenesis; IMP:FlyBase.
DR GO; GO:0038001; P:paracrine signaling; IMP:FlyBase.
DR GO; GO:0072593; P:reactive oxygen species metabolic process; IMP:FlyBase.
DR GO; GO:1903146; P:regulation of autophagy of mitochondrion; IGI:FlyBase.
DR GO; GO:0035206; P:regulation of hemocyte proliferation; IMP:FlyBase.
DR GO; GO:0019222; P:regulation of metabolic process; IMP:FlyBase.
DR GO; GO:0048167; P:regulation of synaptic plasticity; IMP:UniProtKB.
DR GO; GO:0019430; P:removal of superoxide radicals; ISS:FlyBase.
DR Gene3D; 1.10.287.990; -; 1.
DR Gene3D; 3.55.40.20; -; 1.
DR InterPro; IPR001189; Mn/Fe_SOD.
DR InterPro; IPR019833; Mn/Fe_SOD_BS.
DR InterPro; IPR019832; Mn/Fe_SOD_C.
DR InterPro; IPR019831; Mn/Fe_SOD_N.
DR InterPro; IPR036324; Mn/Fe_SOD_N_sf.
DR InterPro; IPR036314; SOD_C_sf.
DR Pfam; PF02777; Sod_Fe_C; 1.
DR Pfam; PF00081; Sod_Fe_N; 1.
DR PIRSF; PIRSF000349; SODismutase; 1.
DR PRINTS; PR01703; MNSODISMTASE.
DR SUPFAM; SSF46609; SSF46609; 1.
DR SUPFAM; SSF54719; SSF54719; 1.
DR PROSITE; PS00088; SOD_MN; 1.
PE 2: Evidence at transcript level;
KW Manganese; Metal-binding; Mitochondrion; Oxidoreductase;
KW Reference proteome; Transit peptide.
FT TRANSIT 1..17
FT /note="Mitochondrion"
FT /evidence="ECO:0000250"
FT CHAIN 18..217
FT /note="Superoxide dismutase [Mn], mitochondrial"
FT /id="PRO_0000032879"
FT BINDING 43
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 91
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 175
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 179
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT CONFLICT 9..14
FT /note="PNCKPG -> QTASLA (in Ref. 2 and 3)"
FT /evidence="ECO:0000305"
FT CONFLICT 127
FT /note="L -> V (in Ref. 6; CAA45418)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 217 AA; 24684 MW; 05900339EA92432B CRC64;
MFVARKISPN CKPGVRGKHT LPKLPYDYAA LEPIICREIM ELHHQKHHQT YVNNLNAAEE
QLEEAKSKSD TTKLIQLAPA LRFNGGGHIN HTIFWQNLSP NKTQPSDDLK KAIESQWKSL
EEFKKELTTL TVAVQGSGWG WLGFNKKSGK LQLAALPNQD PLEASTGLIP LFGIDVWEHA
YYLQYKNVRP SYVEAIWDIA NWDDISCRFQ EAKKLGC
