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Database: UniProt/SWISS-PROT
Entry: SODC_MOUSE
LinkDB: SODC_MOUSE
Original site: SODC_MOUSE 
ID   SODC_MOUSE              Reviewed;         154 AA.
AC   P08228;
DT   01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   25-OCT-2017, entry version 196.
DE   RecName: Full=Superoxide dismutase [Cu-Zn];
DE            EC=1.15.1.1;
GN   Name=Sod1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=SWR/J; TISSUE=Liver;
RX   PubMed=3362683; DOI=10.1093/nar/16.6.2728;
RA   Bewley G.C.;
RT   "cDNA and deduced amino acid sequence of murine Cu-Zn superoxide
RT   dismutase.";
RL   Nucleic Acids Res. 16:2728-2728(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2022332; DOI=10.1016/0378-1119(91)90126-V;
RA   Benedetto M.T., Anzai Y., Gordon J.W.;
RT   "Isolation and analysis of the mouse genomic sequence encoding Cu(2+)-
RT   Zn2+ superoxide dismutase.";
RL   Gene 99:191-195(1991).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Ovary, Urinary bladder, and Uterus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Liver, Mammary gland, and Retina;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   PROTEIN SEQUENCE OF 4-23.
RX   PubMed=2391363; DOI=10.1083/jcb.111.3.1217;
RA   Pluthero F.G., Shreeve M., Eskinazi D., van der Gaag H., Huang K.S.,
RA   Hulmes J.D., Blum M., Axelrad A.A.;
RT   "Purification of an inhibitor of erythroid progenitor cell cycling and
RT   antagonist to interleukin 3 from mouse marrow cell supernatants and
RT   its identification as cytosolic superoxide dismutase.";
RL   J. Cell Biol. 111:1217-1223(1990).
RN   [6]
RP   PROTEIN SEQUENCE OF 11-24 AND 104-116, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RC   STRAIN=OF1; TISSUE=Hippocampus;
RA   Lubec G., Klug S., Sunyer B., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-108, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
RC   Pancreas, Spleen, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and
RT   expression.";
RL   Cell 143:1174-1189(2010).
RN   [8]
RP   DISRUPTION PHENOTYPE.
RC   TISSUE=Liver;
RX   PubMed=21420488; DOI=10.1016/j.freeradbiomed.2011.03.018;
RA   Wang S.K., Weaver J.D., Zhang S., Lei X.G.;
RT   "Knockout of SOD1 promotes conversion of selenocysteine to
RT   dehydroalanine in murine hepatic GPX1 protein.";
RL   Free Radic. Biol. Med. 51:197-204(2011).
RN   [9]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2 AND LYS-123, SUCCINYLATION
RP   [LARGE SCALE ANALYSIS] AT LYS-4; LYS-10; LYS-92; LYS-123 AND LYS-137,
RP   CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Embryonic fibroblast, and Liver;
RX   PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA   Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z.,
RA   Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT   "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT   pathways.";
RL   Mol. Cell 50:919-930(2013).
RN   [10]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-137, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=23576753; DOI=10.1073/pnas.1302961110;
RA   Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J.,
RA   Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.;
RT   "Label-free quantitative proteomics of the lysine acetylome in
RT   mitochondria identifies substrates of SIRT3 in metabolic pathways.";
RL   Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013).
RN   [11]
RP   X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 2-154 IN COMPLEX WITH ZINC.
RX   PubMed=20727846; DOI=10.1016/j.abb.2010.08.014;
RA   Seetharaman S.V., Taylor A.B., Holloway S., Hart P.J.;
RT   "Structures of mouse SOD1 and human/mouse SOD1 chimeras.";
RL   Arch. Biochem. Biophys. 503:183-190(2010).
CC   -!- FUNCTION: Destroys radicals which are normally produced within the
CC       cells and which are toxic to biological systems.
CC   -!- CATALYTIC ACTIVITY: 2 superoxide + 2 H(+) = O(2) + H(2)O(2).
CC   -!- COFACTOR:
CC       Name=Cu cation; Xref=ChEBI:CHEBI:23378; Evidence={ECO:0000250};
CC       Note=Binds 1 copper ion per subunit. {ECO:0000250};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:20727846}.
CC   -!- INTERACTION:
CC       P63001:Rac1; NbExp=4; IntAct=EBI-1635090, EBI-413646;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus {ECO:0000250}.
CC   -!- PTM: Palmitoylation helps nuclear targeting and decreases
CC       catalytic activity. {ECO:0000250}.
CC   -!- PTM: Succinylation, adjacent to copper catalytic site, probably
CC       inhibits activity. Desuccinylation by SIRT5 enhances activity.
CC       {ECO:0000250|UniProtKB:P00441}.
CC   -!- DISRUPTION PHENOTYPE: 40% reduction in hepatic GPX1 activity.
CC       {ECO:0000269|PubMed:21420488}.
CC   -!- SIMILARITY: Belongs to the Cu-Zn superoxide dismutase family.
CC       {ECO:0000305}.
DR   EMBL; X06683; CAA29880.1; -; mRNA.
DR   EMBL; M60798; AAA40121.1; -; Genomic_DNA.
DR   EMBL; M60794; AAA40121.1; JOINED; Genomic_DNA.
DR   EMBL; M60795; AAA40121.1; JOINED; Genomic_DNA.
DR   EMBL; M60796; AAA40121.1; JOINED; Genomic_DNA.
DR   EMBL; M60797; AAA40121.1; JOINED; Genomic_DNA.
DR   EMBL; M35725; AAA37518.1; -; mRNA.
DR   EMBL; AK020624; BAB32154.1; -; mRNA.
DR   EMBL; AK077284; BAC36730.1; -; mRNA.
DR   EMBL; BC002066; AAH02066.1; -; mRNA.
DR   EMBL; BC048874; AAH48874.1; -; mRNA.
DR   EMBL; BC086886; AAH86886.1; -; mRNA.
DR   CCDS; CCDS37395.1; -.
DR   PIR; JQ0915; JQ0915.
DR   RefSeq; NP_035564.1; NM_011434.1.
DR   UniGene; Mm.276325; -.
DR   UniGene; Mm.466779; -.
DR   PDB; 3GTT; X-ray; 2.40 A; A/B/C/D/E/F=2-154.
DR   PDB; 3GTV; X-ray; 2.20 A; A/B/C/D/E/F/G/H/I/J/K/L=82-154.
DR   PDB; 3LTV; X-ray; 2.45 A; A/B/C/D/E/F=2-81.
DR   PDBsum; 3GTT; -.
DR   PDBsum; 3GTV; -.
DR   PDBsum; 3LTV; -.
DR   ProteinModelPortal; P08228; -.
DR   SMR; P08228; -.
DR   BioGrid; 203387; 30.
DR   DIP; DIP-48691N; -.
DR   IntAct; P08228; 33.
DR   MINT; MINT-1869618; -.
DR   STRING; 10090.ENSMUSP00000023707; -.
DR   iPTMnet; P08228; -.
DR   PhosphoSitePlus; P08228; -.
DR   SwissPalm; P08228; -.
DR   DOSAC-COBS-2DPAGE; P08228; -.
DR   REPRODUCTION-2DPAGE; IPI00130589; -.
DR   REPRODUCTION-2DPAGE; P08228; -.
DR   SWISS-2DPAGE; P08228; -.
DR   UCD-2DPAGE; P08228; -.
DR   EPD; P08228; -.
DR   MaxQB; P08228; -.
DR   PaxDb; P08228; -.
DR   PeptideAtlas; P08228; -.
DR   PRIDE; P08228; -.
DR   Ensembl; ENSMUST00000023707; ENSMUSP00000023707; ENSMUSG00000022982.
DR   GeneID; 20655; -.
DR   KEGG; mmu:20655; -.
DR   UCSC; uc007zvz.1; mouse.
DR   CTD; 6647; -.
DR   MGI; MGI:98351; Sod1.
DR   eggNOG; KOG0441; Eukaryota.
DR   eggNOG; COG2032; LUCA.
DR   GeneTree; ENSGT00530000063226; -.
DR   HOGENOM; HOG000263447; -.
DR   HOVERGEN; HBG000062; -.
DR   InParanoid; P08228; -.
DR   KO; K04565; -.
DR   OMA; IHTFGDN; -.
DR   OrthoDB; EOG091G0OG2; -.
DR   PhylomeDB; P08228; -.
DR   TreeFam; TF105131; -.
DR   Reactome; R-MMU-114608; Platelet degranulation.
DR   Reactome; R-MMU-3299685; Detoxification of Reactive Oxygen Species.
DR   ChiTaRS; Sod1; mouse.
DR   EvolutionaryTrace; P08228; -.
DR   PRO; PR:P08228; -.
DR   Proteomes; UP000000589; Chromosome 16.
DR   Bgee; ENSMUSG00000022982; -.
DR   CleanEx; MM_SOD1; -.
DR   Genevisible; P08228; MM.
DR   GO; GO:1904115; C:axon cytoplasm; IEA:GOC.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0031410; C:cytoplasmic vesicle; ISS:UniProtKB.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0032839; C:dendrite cytoplasm; ISS:UniProtKB.
DR   GO; GO:0031045; C:dense core granule; IEA:Ensembl.
DR   GO; GO:0070062; C:extracellular exosome; ISO:MGI.
DR   GO; GO:0031012; C:extracellular matrix; ISS:UniProtKB.
DR   GO; GO:0005615; C:extracellular space; IDA:BHF-UCL.
DR   GO; GO:0005764; C:lysosome; IEA:Ensembl.
DR   GO; GO:0005758; C:mitochondrial intermembrane space; TAS:Reactome.
DR   GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR   GO; GO:0043209; C:myelin sheath; IDA:UniProtKB.
DR   GO; GO:0043025; C:neuronal cell body; ISS:UniProtKB.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0005777; C:peroxisome; ISO:MGI.
DR   GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR   GO; GO:0043234; C:protein complex; ISS:UniProtKB.
DR   GO; GO:0051087; F:chaperone binding; ISS:UniProtKB.
DR   GO; GO:0005507; F:copper ion binding; ISS:UniProtKB.
DR   GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR   GO; GO:0030346; F:protein phosphatase 2B binding; ISS:UniProtKB.
DR   GO; GO:0048365; F:Rac GTPase binding; ISO:MGI.
DR   GO; GO:0004784; F:superoxide dismutase activity; IDA:MGI.
DR   GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR   GO; GO:0000187; P:activation of MAPK activity; IDA:MGI.
DR   GO; GO:0007568; P:aging; IMP:MGI.
DR   GO; GO:0008089; P:anterograde axonal transport; IMP:BHF-UCL.
DR   GO; GO:0060088; P:auditory receptor cell stereocilium organization; IMP:MGI.
DR   GO; GO:0007569; P:cell aging; ISO:MGI.
DR   GO; GO:0006879; P:cellular iron ion homeostasis; IMP:MGI.
DR   GO; GO:0071318; P:cellular response to ATP; IEA:Ensembl.
DR   GO; GO:0071276; P:cellular response to cadmium ion; IEA:Ensembl.
DR   GO; GO:0034599; P:cellular response to oxidative stress; TAS:Reactome.
DR   GO; GO:0035865; P:cellular response to potassium ion; IEA:Ensembl.
DR   GO; GO:0007566; P:embryo implantation; IMP:MGI.
DR   GO; GO:0006749; P:glutathione metabolic process; IMP:MGI.
DR   GO; GO:0060047; P:heart contraction; IMP:MGI.
DR   GO; GO:0050665; P:hydrogen peroxide biosynthetic process; IMP:MGI.
DR   GO; GO:0007626; P:locomotory behavior; IMP:MGI.
DR   GO; GO:0046716; P:muscle cell cellular homeostasis; IMP:MGI.
DR   GO; GO:0002262; P:myeloid cell homeostasis; IMP:MGI.
DR   GO; GO:0043066; P:negative regulation of apoptotic process; IDA:MGI.
DR   GO; GO:0045541; P:negative regulation of cholesterol biosynthetic process; ISS:UniProtKB.
DR   GO; GO:0043524; P:negative regulation of neuron apoptotic process; IMP:MGI.
DR   GO; GO:0060052; P:neurofilament cytoskeleton organization; IMP:MGI.
DR   GO; GO:0001541; P:ovarian follicle development; IMP:MGI.
DR   GO; GO:0032287; P:peripheral nervous system myelin maintenance; IMP:MGI.
DR   GO; GO:0043085; P:positive regulation of catalytic activity; ISS:UniProtKB.
DR   GO; GO:0001819; P:positive regulation of cytokine production; ISS:UniProtKB.
DR   GO; GO:1902177; P:positive regulation of oxidative stress-induced intrinsic apoptotic signaling pathway; ISO:MGI.
DR   GO; GO:0032930; P:positive regulation of superoxide anion generation; ISO:MGI.
DR   GO; GO:0072593; P:reactive oxygen species metabolic process; ISS:UniProtKB.
DR   GO; GO:0008217; P:regulation of blood pressure; IMP:MGI.
DR   GO; GO:0043087; P:regulation of GTPase activity; ISO:MGI.
DR   GO; GO:0051881; P:regulation of mitochondrial membrane potential; ISS:UniProtKB.
DR   GO; GO:0040014; P:regulation of multicellular organism growth; IMP:MGI.
DR   GO; GO:0045859; P:regulation of protein kinase activity; ISS:UniProtKB.
DR   GO; GO:0060087; P:relaxation of vascular smooth muscle; IMP:MGI.
DR   GO; GO:0019430; P:removal of superoxide radicals; IMP:MGI.
DR   GO; GO:0001975; P:response to amphetamine; IEA:Ensembl.
DR   GO; GO:0046677; P:response to antibiotic; IEA:Ensembl.
DR   GO; GO:0097332; P:response to antipsychotic drug; IEA:Ensembl.
DR   GO; GO:0048678; P:response to axon injury; IMP:MGI.
DR   GO; GO:0034465; P:response to carbon monoxide; IEA:Ensembl.
DR   GO; GO:0046688; P:response to copper ion; IEA:Ensembl.
DR   GO; GO:0042493; P:response to drug; IMP:MGI.
DR   GO; GO:0045471; P:response to ethanol; IMP:MGI.
DR   GO; GO:0009408; P:response to heat; IMP:MGI.
DR   GO; GO:0042542; P:response to hydrogen peroxide; IMP:MGI.
DR   GO; GO:0031667; P:response to nutrient levels; IEA:Ensembl.
DR   GO; GO:0010033; P:response to organic substance; ISS:UniProtKB.
DR   GO; GO:0006979; P:response to oxidative stress; IDA:MGI.
DR   GO; GO:0000302; P:response to reactive oxygen species; IMP:MGI.
DR   GO; GO:0000303; P:response to superoxide; IMP:MGI.
DR   GO; GO:0001895; P:retina homeostasis; IMP:MGI.
DR   GO; GO:0008090; P:retrograde axonal transport; IMP:BHF-UCL.
DR   GO; GO:0007605; P:sensory perception of sound; IMP:MGI.
DR   GO; GO:0007283; P:spermatogenesis; IMP:MGI.
DR   GO; GO:0042554; P:superoxide anion generation; IDA:MGI.
DR   GO; GO:0006801; P:superoxide metabolic process; IMP:MGI.
DR   GO; GO:0019226; P:transmission of nerve impulse; IMP:MGI.
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   3D-structure; Acetylation; Antioxidant; Complete proteome; Copper;
KW   Cytoplasm; Direct protein sequencing; Disulfide bond; Lipoprotein;
KW   Metal-binding; Nucleus; Oxidoreductase; Palmitate; Phosphoprotein;
KW   Reference proteome; Zinc.
FT   INIT_MET      1      1       Removed. {ECO:0000244|PubMed:23806337}.
FT   CHAIN         2    154       Superoxide dismutase [Cu-Zn].
FT                                /FTId=PRO_0000164062.
FT   METAL        47     47       Copper; catalytic. {ECO:0000250}.
FT   METAL        49     49       Copper; catalytic. {ECO:0000250}.
FT   METAL        64     64       Copper; catalytic. {ECO:0000250}.
FT   METAL        64     64       Zinc; via pros nitrogen.
FT                                {ECO:0000269|PubMed:20727846}.
FT   METAL        72     72       Zinc; via pros nitrogen.
FT                                {ECO:0000269|PubMed:20727846}.
FT   METAL        81     81       Zinc; via pros nitrogen.
FT                                {ECO:0000269|PubMed:20727846}.
FT   METAL        84     84       Zinc; structural.
FT                                {ECO:0000269|PubMed:20727846}.
FT   METAL       121    121       Copper; catalytic. {ECO:0000250}.
FT   MOD_RES       2      2       N-acetylalanine.
FT                                {ECO:0000244|PubMed:23806337}.
FT   MOD_RES       4      4       N6-succinyllysine.
FT                                {ECO:0000244|PubMed:23806337}.
FT   MOD_RES      10     10       N6-succinyllysine.
FT                                {ECO:0000244|PubMed:23806337}.
FT   MOD_RES      92     92       N6-succinyllysine.
FT                                {ECO:0000244|PubMed:23806337}.
FT   MOD_RES      99     99       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P00441}.
FT   MOD_RES     106    106       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P07632}.
FT   MOD_RES     108    108       Phosphoserine.
FT                                {ECO:0000244|PubMed:21183079}.
FT   MOD_RES     123    123       N6-acetyllysine; alternate.
FT                                {ECO:0000244|PubMed:23806337}.
FT   MOD_RES     123    123       N6-succinyllysine; alternate.
FT                                {ECO:0000244|PubMed:23806337}.
FT   MOD_RES     137    137       N6-acetyllysine; alternate.
FT                                {ECO:0000244|PubMed:23576753}.
FT   MOD_RES     137    137       N6-succinyllysine; alternate.
FT                                {ECO:0000244|PubMed:23806337}.
FT   LIPID         7      7       S-palmitoyl cysteine. {ECO:0000250}.
FT   DISULFID     58    147       {ECO:0000250}.
FT   CONFLICT    102    102       D -> H (in Ref. 2; AAA40121).
FT                                {ECO:0000305}.
FT   STRAND        3     10       {ECO:0000244|PDB:3GTT}.
FT   STRAND       12     14       {ECO:0000244|PDB:3GTT}.
FT   STRAND       16     25       {ECO:0000244|PDB:3GTT}.
FT   STRAND       30     38       {ECO:0000244|PDB:3GTT}.
FT   STRAND       41     50       {ECO:0000244|PDB:3GTT}.
FT   TURN         55     58       {ECO:0000244|PDB:3GTT}.
FT   HELIX        59     61       {ECO:0000244|PDB:3GTT}.
FT   STRAND       77     79       {ECO:0000244|PDB:3LTV}.
FT   STRAND       84     90       {ECO:0000244|PDB:3GTV}.
FT   STRAND       96    109       {ECO:0000244|PDB:3GTV}.
FT   STRAND      116    123       {ECO:0000244|PDB:3GTV}.
FT   STRAND      130    132       {ECO:0000244|PDB:3GTV}.
FT   HELIX       133    138       {ECO:0000244|PDB:3GTV}.
FT   STRAND      143    149       {ECO:0000244|PDB:3GTV}.
SQ   SEQUENCE   154 AA;  15943 MW;  CAE548C66043BAC4 CRC64;
     MAMKAVCVLK GDGPVQGTIH FEQKASGEPV VLSGQITGLT EGQHGFHVHQ YGDNTQGCTS
     AGPHFNPHSK KHGGPADEER HVGDLGNVTA GKDGVANVSI EDRVISLSGE HSIIGRTMVV
     HEKQDDLGKG GNEESTKTGN AGSRLACGVI GIAQ
//
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