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   30-AUG-2017, entry version 45.
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   GO; GO:0005743; C:mitochondrial inner membrane; IEA:Ensembl.
DR   GO; GO:0043209; C:myelin sheath; IEA:Ensembl.
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:0003069; P:acetylcholine-mediated vasodilation involved in regulation of systemic arterial blood pressure; IEA:Ensembl.
DR   GO; GO:0001306; P:age-dependent response to oxidative stress; IEA:Ensembl.
DR   GO; GO:0003032; P:detection of oxygen; IEA:Ensembl.
DR   GO; GO:0048773; P:erythrophore differentiation; IEA:Ensembl.
DR   GO; GO:0006749; P:glutathione metabolic process; IEA:Ensembl.
DR   GO; GO:0007507; P:heart development; IEA:Ensembl.
DR   GO; GO:0030097; P:hemopoiesis; IEA:Ensembl.
DR   GO; GO:0008630; P:intrinsic apoptotic signaling pathway in response to DNA damage; IEA:Ensembl.
DR   GO; GO:0008631; P:intrinsic apoptotic signaling pathway in response to oxidative stress; IEA:Ensembl.
DR   GO; GO:0055072; P:iron ion homeostasis; IEA:Ensembl.
DR   GO; GO:0001889; P:liver development; IEA:Ensembl.
DR   GO; GO:0007626; P:locomotory behavior; IEA:Ensembl.
DR   GO; GO:0045599; P:negative regulation of fat cell differentiation; IEA:Ensembl.
DR   GO; GO:0048147; P:negative regulation of fibroblast proliferation; IEA:Ensembl.
DR   GO; GO:0048666; P:neuron development; IEA:Ensembl.
DR   GO; GO:0045429; P:positive regulation of nitric oxide biosynthetic process; IEA:Ensembl.
DR   GO; GO:0009791; P:post-embryonic development; IEA:Ensembl.
DR   GO; GO:0050790; P:regulation of catalytic activity; IEA:Ensembl.
DR   GO; GO:0051881; P:regulation of mitochondrial membrane potential; IEA:Ensembl.
DR   GO; GO:0006357; P:regulation of transcription from RNA polymerase II promoter; IEA:Ensembl.
DR   GO; GO:0001836; P:release of cytochrome c from mitochondria; IEA:Ensembl.
DR   GO; GO:0022904; P:respiratory electron transport chain; IEA:Ensembl.
DR   GO; GO:0014823; P:response to activity; IEA:Ensembl.
DR   GO; GO:0048678; P:response to axon injury; IEA:Ensembl.
DR   GO; GO:0010332; P:response to gamma radiation; IEA:Ensembl.
DR   GO; GO:0042542; P:response to hydrogen peroxide; IEA:Ensembl.
DR   GO; GO:0055093; P:response to hyperoxia; IEA:Ensembl.
DR   GO; GO:0042554; P:superoxide anion generation; IEA:Ensembl.
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   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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