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Database: UniProt/TrEMBL
Entry: Q6P980_DANRE
LinkDB: Q6P980_DANRE
Original site: Q6P980_DANRE 
ID   Q6P980_DANRE            Unreviewed;       224 AA.
AC   Q6P980;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   23-MAY-2018, entry version 113.
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|ZFIN:ZDB-GENE-030131-7742};
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Cyprinidae; 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|Ensembl:ENSDARP00000062555}
RP   IDENTIFICATION.
RC   STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000062555};
RG   Ensembl;
RL   Submitted (FEB-2012) to UniProtKB.
RN   [3] {ECO:0000313|Ensembl:ENSDARP00000062555, ECO:0000313|Proteomes:UP000000437}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000062555,
RC   ECO:0000313|Proteomes:UP000000437};
RX   PubMed=23594743; DOI=10.1038/nature12111;
RA   Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C.,
RA   Muffato M., Collins J.E., Humphray S., McLaren K., Matthews L.,
RA   McLaren S., Sealy I., Caccamo M., Churcher C., Scott C., Barrett J.C.,
RA   Koch R., Rauch G.J., White S., Chow W., Kilian B., Quintais L.T.,
RA   Guerra-Assuncao J.A., Zhou Y., Gu Y., Yen J., Vogel J.H., Eyre T.,
RA   Redmond S., Banerjee R., Chi J., Fu B., Langley E., Maguire S.F.,
RA   Laird G.K., Lloyd D., Kenyon E., Donaldson S., Sehra H.,
RA   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., Threadgold G.,
RA   Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA   Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J.,
RA   Clark S., Pelan S., Griffiths G., Smith M., Glithero R., Howden P.,
RA   Barker N., Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G.,
RA   Lovell J., Beasley H., Henderson C., Gordon D., Auger K., Wright D.,
RA   Collins J., Raisen C., Dyer L., Leung K., Robertson L., Ambridge K.,
RA   Leongamornlert D., McGuire S., Gilderthorp R., Griffiths C.,
RA   Manthravadi D., Nichol S., Barker G., Whitehead S., Kay M., Brown J.,
RA   Murnane C., Gray E., Humphries M., Sycamore N., Barker D.,
RA   Saunders D., Wallis J., Babbage A., Hammond S.,
RA   Mashreghi-Mohammadi M., Barr L., Martin S., Wray P., Ellington A.,
RA   Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA   Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA   Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D.,
RA   Bird C., Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z.,
RA   Eser C., Geiger H., Geisler M., Karotki L., Kirn A., Konantz J.,
RA   Konantz M., Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C.,
RA   Raddatz G., Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C.,
RA   Yang F., Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J.,
RA   Searle S.M., Enright A., Geisler R., Plasterk R.H., Lee C.,
RA   Westerfield M., de Jong P.J., Zon L.I., Postlethwait J.H.,
RA   Nusslein-Volhard C., Hubbard T.J., Roest Crollius H., Rogers J.,
RA   Stemple D.L.;
RT   "The zebrafish reference genome sequence and its relationship to the
RT   human genome.";
RL   Nature 496:498-503(2013).
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   -!- CATALYTIC ACTIVITY: 2 superoxide + 2 H(+) = O(2) + H(2)O(2).
CC       {ECO:0000256|RuleBase:RU000414}.
CC   -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase
CC       family. {ECO:0000256|RuleBase:RU000414}.
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DR   EMBL; AL929182; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC060895; AAH60895.1; -; mRNA.
DR   RefSeq; NP_956270.1; NM_199976.1.
DR   UniGene; Dr.6314; -.
DR   STRING; 7955.ENSDARP00000062555; -.
DR   Ensembl; ENSDART00000062556; ENSDARP00000062555; ENSDARG00000042644.
DR   GeneID; 335799; -.
DR   KEGG; dre:335799; -.
DR   CTD; 6648; -.
DR   ZFIN; ZDB-GENE-030131-7742; sod2.
DR   eggNOG; KOG0876; Eukaryota.
DR   eggNOG; COG0605; LUCA.
DR   GeneTree; ENSGT00390000011877; -.
DR   HOVERGEN; HBG004451; -.
DR   KO; K04564; -.
DR   OMA; KWGSFDK; -.
DR   OrthoDB; EOG091G0MVL; -.
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; -.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004784; F:superoxide dismutase activity; IEA:UniProtKB-EC.
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; -; 1.
DR   Gene3D; 2.40.500.20; -; 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   1: Evidence at protein level;
KW   Complete proteome {ECO:0000313|Proteomes:UP000000437};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000349-1,
KW   ECO:0000256|RuleBase:RU000414};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000414};
KW   Proteomics identification {ECO:0000213|PeptideAtlas:Q6P980};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000437}.
FT   DOMAIN       27    108       Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT   DOMAIN      115    218       Sod_Fe_C. {ECO:0000259|Pfam:PF02777}.
FT   METAL        52     52       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       100    100       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       185    185       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       189    189       Divalent metal cation.
FT                                {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
//
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