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Extracellular superoxide dismutase [Cu-Zn] (EC-SOD) (EC 1.15.1.1)

 SODE_MOUSE              Reviewed;         251 AA.
O09164;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
01-JUL-1997, sequence version 1.
18-JUL-2018, entry version 160.
RecName: Full=Extracellular superoxide dismutase [Cu-Zn];
Short=EC-SOD;
EC=1.15.1.1;
Flags: Precursor;
Name=Sod3;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 25-36.
STRAIN=C57BL/6 X CBA; TISSUE=Lung;
PubMed=9376114; DOI=10.1165/ajrcmb.17.4.2826;
Folz R.J., Guan J., Seldin M.F., Oury T.D., Enghild J.J., Crapo J.D.;
"Mouse extracellular superoxide dismutase: primary structure, tissue-
specific gene expression, chromosomal localization, and lung in situ
hybridization.";
Am. J. Respir. Cell Mol. Biol. 17:393-403(1997).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=C57BL/6J; TISSUE=Kidney;
PubMed=9163733;
Suh J.-G., Takai S., Yamanishi T., Kikuchi T., Folz R.J., Tanaka K.,
Oh Y.-S., Wada K.;
"Sequence analysis, tissue expression and chromosomal localization of
a mouse secreted superoxide dismutase gene.";
Mol. Cells 7:204-207(1997).
[3]
NUCLEOTIDE SEQUENCE.
STRAIN=C57BL/6J; TISSUE=Liver;
Siegfried M.R., Schultz D., Harrison D.G., Fukai T.;
"Murine extracellular superoxide dismutase genomic sequence.";
Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases.
[4]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brown adipose tissue, Heart, Kidney, Lung, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- FUNCTION: Protect the extracellular space from toxic effect of
reactive oxygen intermediates by converting superoxide radicals
into hydrogen peroxide and oxygen. {ECO:0000250}.
-!- CATALYTIC ACTIVITY: 2 superoxide + 2 H(+) = O(2) + H(2)O(2).
-!- COFACTOR:
Name=Cu cation; Xref=ChEBI:CHEBI:23378; Evidence={ECO:0000250};
Note=Binds 1 copper ion per subunit. {ECO:0000250};
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
Note=Binds 1 zinc ion per subunit. {ECO:0000250};
-!- SUBCELLULAR LOCATION: Secreted, extracellular space.
-!- SIMILARITY: Belongs to the Cu-Zn superoxide dismutase family.
{ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; U38261; AAB51106.1; -; mRNA.
EMBL; D50856; BAA23493.1; -; mRNA.
EMBL; AF223251; AAF27932.1; -; Genomic_DNA.
CCDS; CCDS19283.1; -.
RefSeq; NP_035565.1; NM_011435.3.
UniGene; Mm.2407; -.
PDB; 2DZ2; Model; -; A=120-228.
PDB; 2DZ3; Model; -; A=84-228.
PDBsum; 2DZ2; -.
PDBsum; 2DZ3; -.
ProteinModelPortal; O09164; -.
SMR; O09164; -.
BioGrid; 203389; 1.
IntAct; O09164; 1.
MINT; O09164; -.
STRING; 10090.ENSMUSP00000098768; -.
iPTMnet; O09164; -.
PhosphoSitePlus; O09164; -.
SwissPalm; O09164; -.
UniCarbKB; O09164; -.
EPD; O09164; -.
PaxDb; O09164; -.
PeptideAtlas; O09164; -.
PRIDE; O09164; -.
Ensembl; ENSMUST00000101208; ENSMUSP00000098768; ENSMUSG00000072941.
GeneID; 20657; -.
KEGG; mmu:20657; -.
UCSC; uc008xkl.1; mouse.
CTD; 6649; -.
MGI; MGI:103181; Sod3.
eggNOG; KOG0441; Eukaryota.
eggNOG; COG2032; LUCA.
GeneTree; ENSGT00530000063226; -.
HOGENOM; HOG000263447; -.
HOVERGEN; HBG000062; -.
InParanoid; O09164; -.
KO; K16627; -.
OMA; EQEDDMG; -.
OrthoDB; EOG091G13ID; -.
PhylomeDB; O09164; -.
TreeFam; TF105133; -.
Reactome; R-MMU-3299685; Detoxification of Reactive Oxygen Species.
PRO; PR:O09164; -.
Proteomes; UP000000589; Chromosome 5.
Bgee; ENSMUSG00000072941; -.
CleanEx; MM_SOD3; -.
ExpressionAtlas; O09164; baseline and differential.
Genevisible; O09164; MM.
GO; GO:0005737; C:cytoplasm; ISO:MGI.
GO; GO:0031012; C:extracellular matrix; ISO:MGI.
GO; GO:0005615; C:extracellular space; IDA:MGI.
GO; GO:0005796; C:Golgi lumen; TAS:Reactome.
GO; GO:0005634; C:nucleus; ISO:MGI.
GO; GO:0005507; F:copper ion binding; IBA:GO_Central.
GO; GO:0004784; F:superoxide dismutase activity; IDA:MGI.
GO; GO:0008270; F:zinc ion binding; IBA:GO_Central.
GO; GO:0046688; P:response to copper ion; ISO:MGI.
GO; GO:0001666; P:response to hypoxia; IMP:MGI.
CDD; cd00305; Cu-Zn_Superoxide_Dismutase; 1.
Gene3D; 2.60.40.200; -; 1.
InterPro; IPR036423; SOD-like_Cu/Zn_dom_sf.
InterPro; IPR024134; SOD_Cu/Zn_/chaperone.
InterPro; IPR018152; SOD_Cu/Zn_BS.
InterPro; IPR001424; SOD_Cu_Zn_dom.
PANTHER; PTHR10003; PTHR10003; 1.
Pfam; PF00080; Sod_Cu; 1.
PRINTS; PR00068; CUZNDISMTASE.
SUPFAM; SSF49329; SSF49329; 1.
PROSITE; PS00087; SOD_CU_ZN_1; 1.
PROSITE; PS00332; SOD_CU_ZN_2; 1.
1: Evidence at protein level;
3D-structure; Antioxidant; Complete proteome; Copper;
Direct protein sequencing; Disulfide bond; Glycoprotein;
Metal-binding; Oxidoreductase; Reference proteome; Secreted; Signal;
Zinc.
SIGNAL 1 15 {ECO:0000250}.
PROPEP 16 24 {ECO:0000269|PubMed:9376114}.
/FTId=PRO_0000032856.
CHAIN 25 251 Extracellular superoxide dismutase [Cu-
Zn].
/FTId=PRO_0000032857.
METAL 128 128 Copper; catalytic. {ECO:0000250}.
METAL 130 130 Copper; catalytic. {ECO:0000250}.
METAL 145 145 Copper; catalytic. {ECO:0000250}.
METAL 145 145 Zinc; structural. {ECO:0000250}.
METAL 153 153 Zinc; structural. {ECO:0000250}.
METAL 156 156 Zinc; structural. {ECO:0000250}.
METAL 159 159 Zinc; structural. {ECO:0000250}.
METAL 195 195 Copper; catalytic. {ECO:0000250}.
CARBOHYD 121 121 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 77 222 {ECO:0000250}.
DISULFID 139 221 {ECO:0000250}.
SEQUENCE 251 AA; 27392 MW; 9EAF850E458966C4 CRC64;
MLAFLFYGLL LAACGSVTMS NPGESSFDLA DRLDPVEKID RLDLVEKIGD THAKVLEIWM
ELGRRREVDA AEMHAICRVQ PSATLPPDQP QITGLVLFRQ LGPGSRLEAY FSLEGFPAEQ
NASNRAIHVH EFGDLSQGCD STGPHYNPME VPHPQHPGDF GNFVVRNGQL WRHRVGLTAS
LAGPHAILGR SVVVHAGEDD LGKGGNQASL QNGNAGRRLA CCVVGTSSSA AWESQTKERK
KRRRESECKT T


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