SODE_MOUSE
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 03-AUG-2022, entry version 181.
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 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; O09164; -.
DR PeptideAtlas; O09164; -.
DR PRIDE; O09164; -.
DR ProteomicsDB; 258708; -.
DR Antibodypedia; 3278; 578 antibodies from 36 providers.
DR DNASU; 20657; -.
DR Ensembl; ENSMUST00000101208; ENSMUSP00000098768; ENSMUSG00000072941.
DR GeneID; 20657; -.
DR KEGG; mmu:20657; -.
DR UCSC; uc008xkl.1; mouse.
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; MHAKITE; -.
DR OrthoDB; 1574423at2759; -.
DR PhylomeDB; O09164; -.
DR TreeFam; TF105133; -.
DR Reactome; R-MMU-3299685; Detoxification of Reactive Oxygen Species.
DR BioGRID-ORCS; 20657; 0 hits in 71 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 148 other tissues.
DR ExpressionAtlas; O09164; baseline and differential.
DR Genevisible; O09164; MM.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005615; C:extracellular space; IDA:MGI.
DR GO; GO:0005796; C:Golgi lumen; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0005507; F:copper ion binding; IBA:GO_Central.
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; -; 1.
DR InterPro; IPR024141; EC-SOD.
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 PANTHER; PTHR10003:SF77; PTHR10003:SF77; 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 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
