SODE_DROME
ID SODE_DROME Reviewed; 181 AA.
AC Q7JR71; D8FT33; Q0E9C3; Q5U195; Q95T42;
DT 15-MAR-2017, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Extracellular superoxide dismutase [Cu-Zn] {ECO:0000303|PubMed:21635891};
DE EC=1.15.1.1 {ECO:0000255|RuleBase:RU000393, ECO:0000269|PubMed:21635891, ECO:0000269|PubMed:25339624};
DE Flags: Precursor;
GN Name=Sod3 {ECO:0000312|FlyBase:FBgn0033631};
GN ORFNames=CG9027 {ECO:0000312|FlyBase:FBgn0033631};
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 {ECO:0000312|Proteomes:UP000000803};
RN [1] {ECO:0000312|EMBL:AIU57094.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, CATALYTIC
RP ACTIVITY, AND TISSUE SPECIFICITY.
RX PubMed=25339624; DOI=10.1042/bsr20140133;
RA Blackney M.J., Cox R., Shepherd D., Parker J.D.;
RT "Cloning and expression analysis of Drosophila extracellular Cu Zn
RT superoxide dismutase.";
RL Biosci. Rep. 34:E00164-E00164(2014).
RN [2] {ECO:0000312|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
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 [3] {ECO:0000312|Proteomes:UP000000803}
RP GENOME REANNOTATION.
RC STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
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 [4] {ECO:0000312|EMBL:AAL25378.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=Berkeley {ECO:0000312|EMBL:AAL25378.1};
RC TISSUE=Head {ECO:0000312|EMBL:AAL25378.1};
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [5] {ECO:0000312|EMBL:AAO24980.1, ECO:0000312|EMBL:AAV36882.1, ECO:0000312|EMBL:ADJ93828.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=Berkeley {ECO:0000312|EMBL:AAO24980.1, ECO:0000312|EMBL:AAV36882.1,
RC ECO:0000312|EMBL:ADJ93828.1};
RC TISSUE=Embryo {ECO:0000312|EMBL:AAV36882.1},
RC Larva {ECO:0000312|EMBL:AAO24980.1}, and
RC Pupae {ECO:0000312|EMBL:AAO24980.1};
RA Stapleton M., Brokstein P., Hong L., Agbayani A., Booth B., Carlson J.,
RA Champe M., Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E.,
RA George R., Gonzalez M., Guarin H., Kronmiller B., Li P., Liao G.,
RA Miranda A., Mungall C.J., Nunoo J., Pacleb J., Paragas V., Park S.,
RA Patel S., Phouanenavong S., Sandler J., Wan K., Yu C., Lewis S.E.,
RA Rubin G.M., Celniker S.;
RL Submitted (JUL-2010) to the EMBL/GenBank/DDBJ databases.
RN [6] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=21635891; DOI=10.1016/j.febslet.2011.05.033;
RA Jung I., Kim T.Y., Kim-Ha J.;
RT "Identification of Drosophila SOD3 and its protective role against
RT phototoxic damage to cells.";
RL FEBS Lett. 585:1973-1978(2011).
CC -!- FUNCTION: Protects the extracellular space from the toxic effects of
CC reactive oxygen intermediates by converting superoxide radicals into
CC hydrogen peroxide and oxygen. {ECO:0000269|PubMed:21635891,
CC ECO:0000269|PubMed:25339624}.
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 Evidence={ECO:0000255|RuleBase:RU000393, ECO:0000269|PubMed:21635891,
CC ECO:0000269|PubMed:25339624};
CC -!- COFACTOR:
CC Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC Evidence={ECO:0000250|UniProtKB:P00441,
CC ECO:0000255|RuleBase:RU000393};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:P00441,
CC ECO:0000255|RuleBase:RU000393};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:21635891}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1 {ECO:0000303|PubMed:25339624}; Synonyms=A
CC {ECO:0000312|FlyBase:FBgn0033631}, B {ECO:0000312|FlyBase:FBgn0033631},
CC F {ECO:0000312|FlyBase:FBgn0033631};
CC IsoId=Q7JR71-1; Sequence=Displayed;
CC Name=2 {ECO:0000303|PubMed:25339624}; Synonyms=D
CC {ECO:0000312|FlyBase:FBgn0033631};
CC IsoId=Q7JR71-2; Sequence=VSP_058824;
CC -!- TISSUE SPECIFICITY: Expressed at higher levels in females compared to
CC males. {ECO:0000269|PubMed:25339624}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown results in reduced
CC lifespan and increased sensitivity to paraquat-induced oxidative
CC stress. {ECO:0000269|PubMed:21635891}.
CC -!- SIMILARITY: Belongs to the Cu-Zn superoxide dismutase family.
CC {ECO:0000255|RuleBase:RU000393}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL25378.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAV36882.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=ADJ93828.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; KM360086; AIU57094.1; -; mRNA.
DR EMBL; KM360087; AIU57095.1; -; mRNA.
DR EMBL; AE013599; AAF58647.3; -; Genomic_DNA.
DR EMBL; AE013599; AAG22285.1; -; Genomic_DNA.
DR EMBL; AE013599; ABI31086.1; -; Genomic_DNA.
DR EMBL; AE013599; ALI30174.1; -; Genomic_DNA.
DR EMBL; AY060339; AAL25378.1; ALT_INIT; mRNA.
DR EMBL; BT003225; AAO24980.1; -; mRNA.
DR EMBL; BT015997; AAV36882.1; ALT_INIT; mRNA.
DR EMBL; BT125055; ADJ93828.1; ALT_INIT; mRNA.
DR RefSeq; NP_001036536.1; NM_001043071.2. [Q7JR71-2]
DR RefSeq; NP_001303344.1; NM_001316415.1. [Q7JR71-1]
DR RefSeq; NP_610682.2; NM_136838.3. [Q7JR71-1]
DR RefSeq; NP_725046.2; NM_165829.3. [Q7JR71-1]
DR AlphaFoldDB; Q7JR71; -.
DR SMR; Q7JR71; -.
DR IntAct; Q7JR71; 70.
DR STRING; 7227.FBpp0110197; -.
DR GlyGen; Q7JR71; 3 sites.
DR DNASU; 36232; -.
DR EnsemblMetazoa; FBtr0089938; FBpp0088877; FBgn0033631. [Q7JR71-1]
DR EnsemblMetazoa; FBtr0089939; FBpp0088878; FBgn0033631. [Q7JR71-1]
DR EnsemblMetazoa; FBtr0110897; FBpp0110197; FBgn0033631. [Q7JR71-2]
DR EnsemblMetazoa; FBtr0433531; FBpp0390663; FBgn0033631. [Q7JR71-1]
DR GeneID; 36232; -.
DR KEGG; dme:Dmel_CG9027; -.
DR UCSC; CG9027-RA; d. melanogaster. [Q7JR71-1]
DR CTD; 6649; -.
DR FlyBase; FBgn0033631; Sod3.
DR VEuPathDB; VectorBase:FBgn0033631; -.
DR eggNOG; KOG0441; Eukaryota.
DR GeneTree; ENSGT00940000168521; -.
DR HOGENOM; CLU_056632_4_0_1; -.
DR OMA; DITYTDP; -.
DR PhylomeDB; Q7JR71; -.
DR Reactome; R-DME-114608; Platelet degranulation.
DR Reactome; R-DME-3299685; Detoxification of Reactive Oxygen Species.
DR SignaLink; Q7JR71; -.
DR BioGRID-ORCS; 36232; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 36232; -.
DR PRO; PR:Q7JR71; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0033631; Expressed in secondary oocyte and 27 other tissues.
DR ExpressionAtlas; Q7JR71; baseline and differential.
DR Genevisible; Q95T42; DM.
DR GO; GO:0005615; C:extracellular space; IDA:FlyBase.
DR GO; GO:0005886; C:plasma membrane; HDA:FlyBase.
DR GO; GO:0005507; F:copper ion binding; IBA:GO_Central.
DR GO; GO:0004784; F:superoxide dismutase activity; IDA:FlyBase.
DR GO; GO:0019430; P:removal of superoxide radicals; IMP:FlyBase.
DR GO; GO:0006979; P:response to oxidative stress; IMP:FlyBase.
DR GO; GO:0009650; P:UV protection; IDA:FlyBase.
DR CDD; cd00305; Cu-Zn_Superoxide_Dismutase; 1.
DR Gene3D; 2.60.40.200; -; 1.
DR InterPro; IPR036423; SOD-like_Cu/Zn_dom_sf.
DR InterPro; IPR024134; SOD_Cu/Zn_/chaperone.
DR InterPro; IPR018152; SOD_Cu/Zn_BS.
DR InterPro; IPR001424; SOD_Cu_Zn_dom.
DR PANTHER; PTHR10003; PTHR10003; 1.
DR Pfam; PF00080; Sod_Cu; 1.
DR PRINTS; PR00068; CUZNDISMTASE.
DR SUPFAM; SSF49329; SSF49329; 1.
DR PROSITE; PS00087; SOD_CU_ZN_1; 1.
DR PROSITE; PS00332; SOD_CU_ZN_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Antioxidant; Copper; Disulfide bond; Glycoprotein;
KW Metal-binding; Oxidoreductase; Reference proteome; Secreted; Signal; Zinc.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..181
FT /note="Extracellular superoxide dismutase [Cu-Zn]"
FT /id="PRO_5008177262"
FT BINDING 75
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P00441"
FT BINDING 77
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P00441"
FT BINDING 92
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P00441"
FT BINDING 92
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000250|UniProtKB:P00441"
FT BINDING 100
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000250|UniProtKB:P00441"
FT BINDING 109
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000250|UniProtKB:P00441"
FT BINDING 112
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000250|UniProtKB:P00441"
FT BINDING 149
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P00441"
FT CARBOHYD 46
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 119
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 159
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 86..175
FT /evidence="ECO:0000250|UniProtKB:P00441"
FT VAR_SEQ 181
FT /note="K -> NSDVDEWPCRDGGAGALRYSFSILTVIVALIMARSLD (in
FT isoform 2)"
FT /id="VSP_058824"
SQ SEQUENCE 181 AA; 19221 MW; 68EACE43F8D05CA1 CRC64;
MMQYLVVSLA LCATICSAAQ TRNMPIQAIA YLIGPVQSDN TQVKGNVTFT QNDCGQNVHV
RVQLEGLKEG KHGFHIHEKG DLTNGCISMG AHYNPDKVDH GGPDHEVRHV GDLGNLEANS
TGIIDVTYTD QVITLTGKLG IIGRGVVVHE LEDDLGLGNH TDSKKTGNAG GRIACGVIGI
K
