ID   Q6P980_DANRE            Unreviewed;       224 AA.
AC   Q6P980; A0A8M1PC95;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   27-MAR-2024, entry version 142.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   Name=sod2 {ECO:0000313|EMBL:AAH60895.1,
GN   ECO:0000313|Ensembl:ENSDARP00000062555,
GN   ECO:0000313|RefSeq:NP_956270.1,
GN   ECO:0000313|ZFIN:ZDB-GENE-030131-7742};
GN   Synonyms=cb463 {ECO:0000313|RefSeq:NP_956270.1}, wu:fj33b01
GN   {ECO:0000313|RefSeq:NP_956270.1}, zgc:73051
GN   {ECO:0000313|RefSeq:NP_956270.1};
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955 {ECO:0000313|EMBL:AAH60895.1};
RN   [1] {ECO:0000313|EMBL:AAH60895.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Wild-type {ECO:0000313|EMBL:AAH60895.1};
RC   TISSUE=Eye {ECO:0000313|EMBL:AAH60895.1};
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|RefSeq:NP_956270.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Wild-type {ECO:0000313|RefSeq:NP_956270.1};
RX   PubMed=15533794;
RA   Malek R.L., Sajadi H., Abraham J., Grundy M.A., Gerhard G.S.;
RT   "The effects of temperature reduction on gene expression and oxidative
RT   stress in skeletal muscle from adult zebrafish.";
RL   Comp. Biochem. Physiol. C Toxicol. Pharmacol. 138:363-373(2004).
RN   [3] {ECO:0000313|RefSeq:NP_956270.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Wild-type {ECO:0000313|RefSeq:NP_956270.1};
RX   PubMed=15984772;
RA   Gonzalez P., Dominique Y., Massabuau J.C., Boudou A., Bourdineaud J.P.;
RT   "Comparative effects of dietary methylmercury on gene expression in liver,
RT   skeletal muscle, and brain of the zebrafish (Danio rerio).";
RL   Environ. Sci. Technol. 39:3972-3980(2005).
RN   [4] {ECO:0000313|RefSeq:NP_956270.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Wild-type {ECO:0000313|RefSeq:NP_956270.1};
RX   PubMed=16799861;
RA   Gonzalez P., Baudrimont M., Boudou A., Bourdineaud J.P.;
RT   "Comparative effects of direct cadmium contamination on gene expression in
RT   gills, liver, skeletal muscles and brain of the zebrafish (Danio rerio).";
RL   BioMetals 19:225-235(2006).
RN   [5] {ECO:0000313|RefSeq:NP_956270.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Wild-type {ECO:0000313|RefSeq:NP_956270.1};
RX   PubMed=16324874; DOI=10.1016/j.biocel.2005.10.016;
RA   Ikebuchi M., Takeuchi K., Yamane T., Ogikubo O., Maeda T., Kimura H.,
RA   Ohkubo I.;
RT   "Primary structure and properties of Mn-superoxide dismutase from scallop
RT   adductor muscle.";
RL   Int. J. Biochem. Cell Biol. 38:521-532(2006).
RN   [6] {ECO:0000313|RefSeq:NP_956270.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Wild-type {ECO:0000313|RefSeq:NP_956270.1};
RX   PubMed=16882884;
RA   Lam S.H., Winata C.L., Tong Y., Korzh S., Lim W.S., Korzh V.,
RA   Spitsbergen J., Mathavan S., Miller L.D., Liu E.T., Gong Z.;
RT   "Transcriptome kinetics of arsenic-induced adaptive response in zebrafish
RT   liver.";
RL   Physiol. Genomics 27:351-361(2006).
RN   [7] {ECO:0000313|Ensembl:ENSDARP00000062555}
RP   IDENTIFICATION.
RC   STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000062555};
RG   Ensembl;
RL   Submitted (FEB-2012) to UniProtKB.
RN   [8] {ECO:0000313|Ensembl:ENSDARP00000062555, ECO:0000313|Proteomes:UP000000437}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000062555};
RX   PubMed=23594743; DOI=10.1038/nature12111;
RG   Genome Reference Consortium Zebrafish;
RA   Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA   Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA   Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA   White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA   Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA   Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA   Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA   Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA   Clee C., Oliver K., Clark R., Riddle C., Elliot D., Eliott D.,
RA   Threadgold G., Harden G., Ware D., Begum S., Mortimore B., Mortimer B.,
RA   Kerry G., Heath P., Phillimore B., Tracey A., Corby N., Dunn M.,
RA   Johnson C., Wood J., Clark S., Pelan S., Griffiths G., Smith M.,
RA   Glithero R., Howden P., Barker N., Lloyd C., Stevens C., Harley J.,
RA   Holt K., Panagiotidis G., Lovell J., Beasley H., Henderson C., Gordon D.,
RA   Auger K., Wright D., Collins J., Raisen C., Dyer L., Leung K.,
RA   Robertson L., Ambridge K., Leongamornlert D., McGuire S., Gilderthorp R.,
RA   Griffiths C., Manthravadi D., Nichol S., Barker G., Whitehead S., Kay M.,
RA   Brown J., Murnane C., Gray E., Humphries M., Sycamore N., Barker D.,
RA   Saunders D., Wallis J., Babbage A., Hammond S., Mashreghi-Mohammadi M.,
RA   Barr L., Martin S., Wray P., Ellington A., Matthews N., Ellwood M.,
RA   Woodmansey R., Clark G., Cooper J., Cooper J., Tromans A., Grafham D.,
RA   Skuce C., Pandian R., Andrews R., Harrison E., Kimberley A., Garnett J.,
RA   Fosker N., Hall R., Garner P., Kelly D., Bird C., Palmer S., Gehring I.,
RA   Berger A., Dooley C.M., Ersan-Urun Z., Eser C., Geiger H., Geisler M.,
RA   Karotki L., Kirn A., Konantz J., Konantz M., Oberlander M.,
RA   Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G., Osoegawa K., Zhu B.,
RA   Rapp A., Widaa S., Langford C., Yang F., Schuster S.C., Carter N.P.,
RA   Harrow J., Ning Z., Herrero J., Searle S.M., Enright A., Geisler R.,
RA   Plasterk R.H., Lee C., Westerfield M., de Jong P.J., Zon L.I.,
RA   Postlethwait J.H., Nusslein-Volhard C., Hubbard T.J., Roest Crollius H.,
RA   Rogers J., Stemple D.L.;
RT   "The zebrafish reference genome sequence and its relationship to the human
RT   genome.";
RL   Nature 496:498-503(2013).
RN   [9] {ECO:0000313|RefSeq:NP_956270.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Wild-type {ECO:0000313|RefSeq:NP_956270.1};
RX   PubMed=30618751;
RA   Xia Q., Wei L., Zhang Y., Kong H., Shi Y., Wang X., Chen X., Han L.,
RA   Liu K.;
RT   "Psoralen Induces Developmental Toxicity in Zebrafish Embryos/Larvae
RT   Through Oxidative Stress, Apoptosis, and Energy Metabolism Disorder.";
RL   Front. Pharmacol. 9:1457-1457(2018).
RN   [10] {ECO:0000313|RefSeq:NP_956270.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Wild-type {ECO:0000313|RefSeq:NP_956270.1};
RX   PubMed=30758177;
RA   Wei X., Li L., Liu J., Yu L., Li H., Cheng F., Yi X., He J., Li B.;
RT   "Green Synthesis of Fluorescent Carbon Dots from Gynostemma for Bioimaging
RT   and Antioxidant in Zebrafish.";
RL   ACS Appl. Mater. Interfaces 11:9832-9840(2019).
RN   [11] {ECO:0000313|RefSeq:NP_956270.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Wild-type {ECO:0000313|RefSeq:NP_956270.1};
RX   PubMed=30718751;
RA   Park K.H., Ye Z.W., Zhang J., Hammad S.M., Townsend D.M., Rockey D.C.,
RA   Kim S.H.;
RT   "3-ketodihydrosphingosine reductase mutation induces steatosis and hepatic
RT   injury in zebrafish.";
RL   Sci. Rep. 9:1138-1138(2019).
RN   [12] {ECO:0000313|RefSeq:NP_956270.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Wild-type {ECO:0000313|RefSeq:NP_956270.1};
RX   PubMed=30846767;
RA   Toms M., Burgoyne T., Tracey-White D., Richardson R., Dubis A.M.,
RA   Webster A.R., Futter C., Moosajee M.;
RT   "Phagosomal and mitochondrial alterations in RPE may contribute to KCNJ13
RT   retinopathy.";
RL   Sci. Rep. 9:3793-3793(2019).
RN   [13] {ECO:0000313|RefSeq:NP_956270.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Wild-type {ECO:0000313|RefSeq:NP_956270.1};
RX   PubMed=30658072;
RA   Liu L., Hu Y., Lu J., Wang G.;
RT   "An imidazole coumarin derivative enhances the antiviral response to spring
RT   viremia of carp virus infection in zebrafish.";
RL   Virus Res. 263:112-118(2019).
RN   [14] {ECO:0000313|RefSeq:NP_956270.1}
RP   IDENTIFICATION.
RC   STRAIN=Wild-type {ECO:0000313|RefSeq:NP_956270.1};
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- FUNCTION: Destroys radicals which are normally produced within the
CC       cells and which are toxic to biological systems.
CC       {ECO:0000256|RuleBase:RU000414}.
CC   -!- FUNCTION: Destroys superoxide anion radicals which are normally
CC       produced within the cells and which are toxic to biological systems.
CC       {ECO:0000256|ARBA:ARBA00002170}.
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:0000256|ARBA:ARBA00001605,
CC         ECO:0000256|RuleBase:RU000414};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC       {ECO:0000256|ARBA:ARBA00004305}.
CC   -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase family.
CC       {ECO:0000256|ARBA:ARBA00008714, ECO:0000256|RuleBase:RU000414}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AL929182; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC060895; AAH60895.1; -; mRNA.
DR   RefSeq; NP_956270.1; NM_199976.1.
DR   STRING; 7955.ENSDARP00000062555; -.
DR   PaxDb; 7955-ENSDARP00000062555; -.
DR   Ensembl; ENSDART00000062556.4; ENSDARP00000062555.3; ENSDARG00000042644.6.
DR   GeneID; 335799; -.
DR   KEGG; dre:335799; -.
DR   AGR; ZFIN:ZDB-GENE-030131-7742; -.
DR   CTD; 6648; -.
DR   ZFIN; ZDB-GENE-030131-7742; sod2.
DR   eggNOG; KOG0876; Eukaryota.
DR   HOGENOM; CLU_031625_2_1_1; -.
DR   OMA; DSLINWD; -.
DR   OrthoDB; 4839at2759; -.
DR   TreeFam; TF105132; -.
DR   Reactome; R-DRE-2151201; Transcriptional activation of mitochondrial biogenesis.
DR   Reactome; R-DRE-3299685; Detoxification of Reactive Oxygen Species.
DR   Proteomes; UP000000437; Chromosome 20.
DR   Bgee; ENSDARG00000042644; Expressed in cardiac ventricle and 39 other cell types or tissues.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0030145; F:manganese ion binding; IBA:GO_Central.
DR   GO; GO:0004784; F:superoxide dismutase activity; IDA:ZFIN.
DR   GO; GO:0045087; P:innate immune response; IMP:ZFIN.
DR   GO; GO:0001780; P:neutrophil homeostasis; IMP:ZFIN.
DR   GO; GO:0019430; P:removal of superoxide radicals; IMP:ZFIN.
DR   GO; GO:0046686; P:response to cadmium ion; IEP:ZFIN.
DR   GO; GO:0051597; P:response to methylmercury; IDA:ZFIN.
DR   Gene3D; 1.10.287.990; Fe,Mn superoxide dismutase (SOD) domain; 1.
DR   Gene3D; 3.55.40.20; Iron/manganese superoxide dismutase, C-terminal domain; 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   PANTHER; PTHR11404; SUPEROXIDE DISMUTASE 2; 1.
DR   PANTHER; PTHR11404:SF6; SUPEROXIDE DISMUTASE [MN], MITOCHONDRIAL; 1.
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; SSF54719; Fe,Mn superoxide dismutase (SOD), C-terminal domain; 1.
DR   SUPFAM; SSF46609; Fe,Mn superoxide dismutase (SOD), N-terminal domain; 1.
DR   PROSITE; PS00088; SOD_MN; 1.
PE   1: Evidence at protein level;
KW   Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW   Manganese {ECO:0000256|ARBA:ARBA00023211};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR000349-1};
KW   Nitration {ECO:0000256|ARBA:ARBA00023074};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU000414};
KW   Proteomics identification {ECO:0007829|PeptideAtlas:Q6P980};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000437};
KW   Ubl conjugation {ECO:0000256|ARBA:ARBA00022843}.
FT   DOMAIN          27..108
FT                   /note="Manganese/iron superoxide dismutase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00081"
FT   DOMAIN          115..218
FT                   /note="Manganese/iron superoxide dismutase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02777"
FT   BINDING         52
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000349-1"
FT   BINDING         100
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000349-1"
FT   BINDING         185
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000349-1"
FT   BINDING         189
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000349-1"
SQ   SEQUENCE   224 AA;  25008 MW;  7E184E4361F82066 CRC64;
     MLCRVGYVRR CAATFNPLLG AVTSRQKHAL PDLTYDYGAL EPHICAEIMQ LHHSKHHATY
     VNNLNVTEEK YQEALAKGDV TTQVSLQPAL KFNGGGHINH TIFWTNLSPN GGGEPQGELL
     EAIKRDFGSF QKMKEKISAA TVAVQGSGWG WLGFEKESGR LRIAACANQD PLQGTTGLIP
     LLGIDVWEHA YYLQYKNVRP DYVKAIWNVV NWENVSERFQ AAKK
//