GenomeNet

Database: UniProt/TrEMBL
Entry: H9EUV0_MACMU
LinkDB: H9EUV0_MACMU
Original site: H9EUV0_MACMU 
ID   H9EUV0_MACMU            Unreviewed;       222 AA.
AC   H9EUV0;
DT   16-MAY-2012, integrated into UniProtKB/TrEMBL.
DT   16-MAY-2012, sequence version 1.
DT   23-MAY-2018, entry version 50.
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:AFE66159.1,
GN   ECO:0000313|Ensembl:ENSMMUP00000057723};
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544 {ECO:0000313|EMBL:AFE66159.1};
RN   [1] {ECO:0000313|Ensembl:ENSMMUP00000057723, ECO:0000313|Proteomes:UP000006718}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=17573 {ECO:0000313|Ensembl:ENSMMUP00000057723,
RC   ECO:0000313|Proteomes:UP000006718};
RX   PubMed=17431167; DOI=10.1126/science.1139247;
RA   Gibbs R.A., Rogers J., Katze M.G., Bumgarner R., Weinstock G.M.,
RA   Mardis E.R., Remington K.A., Strausberg R.L., Venter J.C.,
RA   Wilson R.K., Batzer M.A., Bustamante C.D., Eichler E.E., Hahn M.W.,
RA   Hardison R.C., Makova K.D., Miller W., Milosavljevic A., Palermo R.E.,
RA   Siepel A., Sikela J.M., Attaway T., Bell S., Bernard K.E., Buhay C.J.,
RA   Chandrabose M.N., Dao M., Davis C., Delehaunty K.D., Ding Y.,
RA   Dinh H.H., Dugan-Rocha S., Fulton L.A., Gabisi R.A., Garner T.T.,
RA   Godfrey J., Hawes A.C., Hernandez J., Hines S., Holder M., Hume J.,
RA   Jhangiani S.N., Joshi V., Khan Z.M., Kirkness E.F., Cree A.,
RA   Fowler R.G., Lee S., Lewis L.R., Li Z., Liu Y.-S., Moore S.M.,
RA   Muzny D., Nazareth L.V., Ngo D.N., Okwuonu G.O., Pai G., Parker D.,
RA   Paul H.A., Pfannkoch C., Pohl C.S., Rogers Y.-H.C., Ruiz S.J.,
RA   Sabo A., Santibanez J., Schneider B.W., Smith S.M., Sodergren E.,
RA   Svatek A.F., Utterback T.R., Vattathil S., Warren W., White C.S.,
RA   Chinwalla A.T., Feng Y., Halpern A.L., Hillier L.W., Huang X.,
RA   Minx P., Nelson J.O., Pepin K.H., Qin X., Sutton G.G., Venter E.,
RA   Walenz B.P., Wallis J.W., Worley K.C., Yang S.-P., Jones S.M.,
RA   Marra M.A., Rocchi M., Schein J.E., Baertsch R., Clarke L., Csuros M.,
RA   Glasscock J., Harris R.A., Havlak P., Jackson A.R., Jiang H., Liu Y.,
RA   Messina D.N., Shen Y., Song H.X.-Z., Wylie T., Zhang L., Birney E.,
RA   Han K., Konkel M.K., Lee J., Smit A.F.A., Ullmer B., Wang H., Xing J.,
RA   Burhans R., Cheng Z., Karro J.E., Ma J., Raney B., She X., Cox M.J.,
RA   Demuth J.P., Dumas L.J., Han S.-G., Hopkins J., Karimpour-Fard A.,
RA   Kim Y.H., Pollack J.R., Vinar T., Addo-Quaye C., Degenhardt J.,
RA   Denby A., Hubisz M.J., Indap A., Kosiol C., Lahn B.T., Lawson H.A.,
RA   Marklein A., Nielsen R., Vallender E.J., Clark A.G., Ferguson B.,
RA   Hernandez R.D., Hirani K., Kehrer-Sawatzki H., Kolb J., Patil S.,
RA   Pu L.-L., Ren Y., Smith D.G., Wheeler D.A., Schenck I., Ball E.V.,
RA   Chen R., Cooper D.N., Giardine B., Hsu F., Kent W.J., Lesk A.,
RA   Nelson D.L., O'brien W.E., Pruefer K., Stenson P.D., Wallace J.C.,
RA   Ke H., Liu X.-M., Wang P., Xiang A.P., Yang F., Barber G.P.,
RA   Haussler D., Karolchik D., Kern A.D., Kuhn R.M., Smith K.E.,
RA   Zwieg A.S.;
RT   "Evolutionary and biomedical insights from the rhesus macaque
RT   genome.";
RL   Science 316:222-234(2007).
RN   [2] {ECO:0000313|EMBL:AFE66159.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Caudate {ECO:0000313|EMBL:AFE66159.1}, Testis
RC   {ECO:0000313|EMBL:AFI34979.1}, and Thymus
RC   {ECO:0000313|EMBL:AFH29278.1};
RX   PubMed=25319552; DOI=10.1186/1745-6150-9-20;
RA   Zimin A.V., Cornish A.S., Maudhoo M.D., Gibbs R.M., Zhang X.,
RA   Pandey S., Meehan D.T., Wipfler K., Bosinger S.E., Johnson Z.P.,
RA   Tharp G.K., Marcais G., Roberts M., Ferguson B., Fox H.S.,
RA   Treangen T., Salzberg S.L., Yorke J.A., Norgren R.B.Jr.;
RT   "A new rhesus macaque assembly and annotation for next-generation
RT   sequencing analyses.";
RL   Biol. Direct 9:20-20(2014).
RN   [3] {ECO:0000313|Ensembl:ENSMMUP00000057723}
RP   IDENTIFICATION.
RC   STRAIN=17573 {ECO:0000313|Ensembl:ENSMMUP00000057723};
RG   Ensembl;
RL   Submitted (OCT-2016) 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   -!- 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; JSUE03032541; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; JU322402; AFE66158.1; -; mRNA.
DR   EMBL; JU322403; AFE66159.1; -; mRNA.
DR   EMBL; JU472474; AFH29278.1; -; mRNA.
DR   EMBL; JU472475; AFH29279.1; -; mRNA.
DR   EMBL; JV044908; AFI34979.1; -; mRNA.
DR   RefSeq; NP_001027977.2; NM_001032805.2.
DR   RefSeq; XP_014992736.1; XM_015137250.1.
DR   UniGene; Mmu.1131; -.
DR   SMR; H9EUV0; -.
DR   Ensembl; ENSMMUT00000054603; ENSMMUP00000057723; ENSMMUG00000038719.
DR   GeneID; 574097; -.
DR   KEGG; mcc:574097; -.
DR   CTD; 6648; -.
DR   eggNOG; KOG0876; Eukaryota.
DR   eggNOG; COG0605; LUCA.
DR   GeneTree; ENSGT00390000011877; -.
DR   KO; K04564; -.
DR   Proteomes; UP000006718; Chromosome 4.
DR   ExpressionAtlas; H9EUV0; baseline.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004784; F:superoxide dismutase activity; IEA:UniProtKB-EC.
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   2: Evidence at transcript level;
KW   Complete proteome {ECO:0000313|Proteomes:UP000006718};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000349-1,
KW   ECO:0000256|RuleBase:RU000414};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000414};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006718}.
FT   DOMAIN       25    106       Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT   DOMAIN      113    216       Sod_Fe_C. {ECO:0000259|Pfam:PF02777}.
FT   METAL        50     50       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL        98     98       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       183    183       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       187    187       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
SQ   SEQUENCE   222 AA;  24697 MW;  C9F1A0FC5902B434 CRC64;
     MLSRAVCGTG RQLAPALGYL GSRQKHSLPD LPYDYGALEP HINAQIMQLH HSKHHAAYVN
     NLNVTEEKYQ EALAKGDVTA QIALQPALKF NGGGHINHSI FWTNLSPNGG GEPKGELLEA
     IKRDFGSFEK FKEKLTAASV GVQGSGWGWL GFNKERGQLQ IAACPNQDPL QGTTGLIPLL
     GIDVWEHAYY LQYKNVRPDY LKAIWNVINW ENVTERYMAC KK
//
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