ID   SODE_MOUSE              Reviewed;         251 AA.
AC   O09164;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   24-JAN-2024, entry version 189.
DE   RecName: Full=Extracellular superoxide dismutase [Cu-Zn];
DE            Short=EC-SOD;
DE            EC=1.15.1.1 {ECO:0000305|PubMed:16371425};
DE   Flags: Precursor;
GN   Name=Sod3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 25-36.
RC   STRAIN=C57BL/6 X CBA; TISSUE=Lung;
RX   PubMed=9376114; DOI=10.1165/ajrcmb.17.4.2826;
RA   Folz R.J., Guan J., Seldin M.F., Oury T.D., Enghild J.J., Crapo J.D.;
RT   "Mouse extracellular superoxide dismutase: primary structure, tissue-
RT   specific gene expression, chromosomal localization, and lung in situ
RT   hybridization.";
RL   Am. J. Respir. Cell Mol. Biol. 17:393-403(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Kidney;
RX   PubMed=9163733;
RA   Suh J.-G., Takai S., Yamanishi T., Kikuchi T., Folz R.J., Tanaka K.,
RA   Oh Y.-S., Wada K.;
RT   "Sequence analysis, tissue expression and chromosomal localization of a
RT   mouse secreted superoxide dismutase gene.";
RL   Mol. Cells 7:204-207(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Liver;
RA   Siegfried M.R., Schultz D., Harrison D.G., Fukai T.;
RT   "Murine extracellular superoxide dismutase genomic sequence.";
RL   Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   SUBCELLULAR LOCATION, INTERACTION WITH ATP7A, AND CATALYTIC ACTIVITY.
RX   PubMed=16371425; DOI=10.1096/fj.05-4564fje;
RA   Qin Z., Itoh S., Jeney V., Ushio-Fukai M., Fukai T.;
RT   "Essential role for the Menkes ATPase in activation of extracellular
RT   superoxide dismutase: implication for vascular oxidative stress.";
RL   FASEB J. 20:334-336(2006).
RN   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brown adipose tissue, Heart, Kidney, Lung, 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 expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: Protect the extracellular space from toxic effect of reactive
CC       oxygen intermediates by converting superoxide radicals into hydrogen
CC       peroxide and oxygen. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 H(+) + 2 superoxide = H2O2 + O2; Xref=Rhea:RHEA:20696,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC         ChEBI:CHEBI:18421; EC=1.15.1.1;
CC         Evidence={ECO:0000305|PubMed:16371425};
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: Homotetramer (By similarity). Directly interacts with
CC       ATP7A/MNK; this interaction is copper-dependent and is required for
CC       SOD3 activity (By similarity). {ECO:0000250|UniProtKB:P08294}.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space. Golgi apparatus,
CC       trans-Golgi network {ECO:0000269|PubMed:16371425}.
CC   -!- SIMILARITY: Belongs to the Cu-Zn superoxide dismutase family.
CC       {ECO:0000305}.
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DR   EMBL; U38261; AAB51106.1; -; mRNA.
DR   EMBL; D50856; BAA23493.1; -; mRNA.
DR   EMBL; AF223251; AAF27932.1; -; Genomic_DNA.
DR   CCDS; CCDS19283.1; -.
DR   RefSeq; NP_035565.1; NM_011435.3.
DR   AlphaFoldDB; O09164; -.
DR   SMR; O09164; -.
DR   BioGRID; 203389; 2.
DR   IntAct; O09164; 1.
DR   MINT; O09164; -.
DR   STRING; 10090.ENSMUSP00000098768; -.
DR   GlyCosmos; O09164; 1 site, 15 glycans.
DR   GlyGen; O09164; 1 site, 15 N-linked glycans (1 site).
DR   iPTMnet; O09164; -.
DR   PhosphoSitePlus; O09164; -.
DR   SwissPalm; O09164; -.
DR   CPTAC; non-CPTAC-3378; -.
DR   EPD; O09164; -.
DR   jPOST; O09164; -.
DR   PaxDb; 10090-ENSMUSP00000098768; -.
DR   PeptideAtlas; O09164; -.
DR   ProteomicsDB; 258708; -.
DR   Antibodypedia; 3278; 621 antibodies from 36 providers.
DR   DNASU; 20657; -.
DR   Ensembl; ENSMUST00000101208.6; ENSMUSP00000098768.5; ENSMUSG00000072941.6.
DR   GeneID; 20657; -.
DR   KEGG; mmu:20657; -.
DR   UCSC; uc008xkl.1; mouse.
DR   AGR; MGI:103181; -.
DR   CTD; 6649; -.
DR   MGI; MGI:103181; Sod3.
DR   VEuPathDB; HostDB:ENSMUSG00000072941; -.
DR   eggNOG; KOG0441; Eukaryota.
DR   GeneTree; ENSGT00940000162224; -.
DR   HOGENOM; CLU_056632_3_1_1; -.
DR   InParanoid; O09164; -.
DR   OMA; DGSLWKY; -.
DR   OrthoDB; 3470597at2759; -.
DR   PhylomeDB; O09164; -.
DR   TreeFam; TF105133; -.
DR   Reactome; R-MMU-3299685; Detoxification of Reactive Oxygen Species.
DR   BioGRID-ORCS; 20657; 1 hit in 76 CRISPR screens.
DR   ChiTaRS; Sod3; mouse.
DR   PRO; PR:O09164; -.
DR   Proteomes; UP000000589; Chromosome 5.
DR   RNAct; O09164; Protein.
DR   Bgee; ENSMUSG00000072941; Expressed in choroid plexus of fourth ventricle and 149 other cell types or tissues.
DR   ExpressionAtlas; O09164; baseline and differential.
DR   GO; GO:0062023; C:collagen-containing extracellular matrix; ISO:MGI.
DR   GO; GO:0005615; C:extracellular space; IDA:MGI.
DR   GO; GO:0005796; C:Golgi lumen; TAS:Reactome.
DR   GO; GO:0005507; F:copper ion binding; IBA:GO_Central.
DR   GO; GO:0060090; F:molecular adaptor activity; ISO:MGI.
DR   GO; GO:0004784; F:superoxide dismutase activity; IDA:MGI.
DR   GO; GO:0097746; P:blood vessel diameter maintenance; ISO:MGI.
DR   GO; GO:0019430; P:removal of superoxide radicals; IBA:GO_Central.
DR   GO; GO:0046688; P:response to copper ion; ISO:MGI.
DR   GO; GO:0001666; P:response to hypoxia; IMP:MGI.
DR   CDD; cd00305; Cu-Zn_Superoxide_Dismutase; 1.
DR   Gene3D; 2.60.40.200; Superoxide dismutase, copper/zinc binding domain; 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:SF77; EXTRACELLULAR SUPEROXIDE DISMUTASE [CU-ZN]; 1.
DR   PANTHER; PTHR10003; SUPEROXIDE DISMUTASE CU-ZN -RELATED; 1.
DR   Pfam; PF00080; Sod_Cu; 1.
DR   PRINTS; PR00068; CUZNDISMTASE.
DR   SUPFAM; SSF49329; Cu,Zn superoxide dismutase-like; 1.
DR   PROSITE; PS00087; SOD_CU_ZN_1; 1.
DR   PROSITE; PS00332; SOD_CU_ZN_2; 1.
DR   Genevisible; O09164; MM.
PE   1: Evidence at protein level;
KW   Antioxidant; Copper; Direct protein sequencing; Disulfide bond;
KW   Glycoprotein; Golgi apparatus; Metal-binding; Oxidoreductase;
KW   Reference proteome; Secreted; Signal; Zinc.
FT   SIGNAL          1..15
FT                   /evidence="ECO:0000250"
FT   PROPEP          16..24
FT                   /evidence="ECO:0000269|PubMed:9376114"
FT                   /id="PRO_0000032856"
FT   CHAIN           25..251
FT                   /note="Extracellular superoxide dismutase [Cu-Zn]"
FT                   /id="PRO_0000032857"
FT   REGION          230..251
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        234..251
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         128
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         130
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         145
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         145
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="structural"
FT                   /evidence="ECO:0000250"
FT   BINDING         153
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="structural"
FT                   /evidence="ECO:0000250"
FT   BINDING         156
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="structural"
FT                   /evidence="ECO:0000250"
FT   BINDING         159
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="structural"
FT                   /evidence="ECO:0000250"
FT   BINDING         195
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        121
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        77..222
FT                   /evidence="ECO:0000250"
FT   DISULFID        139..221
FT                   /evidence="ECO:0000250"
SQ   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
//