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

 SODE_HUMAN              Reviewed;         240 AA.
P08294; Q5U781; Q6FHA2;
01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
30-MAY-2006, sequence version 2.
18-JUL-2018, entry version 195.
RecName: Full=Extracellular superoxide dismutase [Cu-Zn];
Short=EC-SOD;
EC=1.15.1.1;
Flags: Precursor;
Name=SOD3;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, AND VARIANT
THR-58.
PubMed=3476950; DOI=10.1073/pnas.84.18.6340;
Hjalmarsson K., Marklund S.L., Engstroem A., Edlund T.;
"Isolation and sequence of complementary DNA encoding human
extracellular superoxide dismutase.";
Proc. Natl. Acad. Sci. U.S.A. 84:6340-6344(1987).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT THR-58.
TISSUE=Blood;
PubMed=7959763; DOI=10.1006/geno.1994.1357;
Folz R.J., Crapo J.D.;
"Extracellular superoxide dismutase (SOD3): tissue-specific
expression, genomic characterization, and computer-assisted sequence
analysis of the human EC SOD gene.";
Genomics 22:162-171(1994).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT THR-58.
Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S.,
Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W.,
Korn B., Zuo D., Hu Y., LaBaer J.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS THR-58; THR-91 AND
GLY-231.
NIEHS SNPs program;
Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT THR-58.
TISSUE=Colon;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
GLYCATION AT LYS-229 AND LYS-230.
PubMed=1505778; DOI=10.1016/0891-5849(92)90016-A;
Adachi T., Ohta H., Hayashi K., Hirano K., Marklund S.L.;
"The site of nonenzymic glycation of human extracellular-superoxide
dismutase in vitro.";
Free Radic. Biol. Med. 13:205-210(1992).
[7]
REVIEW.
PubMed=16087389; DOI=10.1016/j.biocel.2005.06.012;
Nozik-Grayck E., Suliman H.B., Piantadosi C.A.;
"Extracellular superoxide dismutase.";
Int. J. Biochem. Cell Biol. 37:2466-2471(2005).
[8]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-107.
TISSUE=Plasma;
PubMed=16335952; DOI=10.1021/pr0502065;
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,
Moore R.J., Smith R.D.;
"Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
hydrazide chemistry, and mass spectrometry.";
J. Proteome Res. 4:2070-2080(2005).
[9]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-107.
TISSUE=Liver;
PubMed=19159218; DOI=10.1021/pr8008012;
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
"Glycoproteomics analysis of human liver tissue by combination of
multiple enzyme digestion and hydrazide chemistry.";
J. Proteome Res. 8:651-661(2009).
[10]
X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 19-240, SUBUNIT,
METAL-BINDING SITES, AND DISULFIDE BONDS.
PubMed=19289127; DOI=10.1016/j.jmb.2009.03.026;
Antonyuk S.V., Strange R.W., Marklund S.L., Hasnain S.S.;
"The structure of human extracellular copper-zinc superoxide dismutase
at 1.7 A resolution: insights into heparin and collagen binding.";
J. Mol. Biol. 388:310-326(2009).
[11]
VARIANT GLY-231.
PubMed=8034674;
Sandstrom J., Nilsson P., Karlsson K., Marklund S.L.;
"10-fold increase in human plasma extracellular superoxide dismutase
content caused by a mutation in heparin-binding domain.";
J. Biol. Chem. 269:19163-19166(1994).
[12]
VARIANT GLY-231.
PubMed=7662997; DOI=10.1007/BF01883574;
Yamada H., Yamada Y., Adachi T., Goto H., Ogasawara N., Futenma A.,
Kitano M., Hirano K., Kato K.;
"Molecular analysis of extracellular-superoxide dismutase gene
associated with high level in serum.";
Jpn. J. Hum. Genet. 40:177-184(1995).
[13]
VARIANT GLY-231.
PubMed=8546689; DOI=10.1042/bj3130235;
Adachi T., Yamada H., Yamada Y., Morihara N., Yamazaki N.,
Murakami T., Futenma A., Kato K., Hirano K.;
"Substitution of glycine for arginine-213 in extracellular-superoxide
dismutase impairs affinity for heparin and endothelial cell surface.";
Biochem. J. 313:235-239(1996).
[14]
VARIANT GLY-231.
PubMed=8864862; DOI=10.1093/oxfordjournals.jbchem.a021383;
Adachi T., Morihara N., Yamazaki N., Yamada H., Futenma A., Kato K.,
Hirano K.;
"An arginine-213 to glycine mutation in human extracellular-superoxide
dismutase reduces susceptibility to trypsin-like proteinases.";
J. Biochem. 120:184-188(1996).
-!- FUNCTION: Protect the extracellular space from toxic effect of
reactive oxygen intermediates by converting superoxide radicals
into hydrogen peroxide and oxygen.
-!- 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};
-!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:19289127}.
-!- INTERACTION:
Q9Y2W7:KCNIP3; NbExp=4; IntAct=EBI-10195782, EBI-751501;
O43765:SGTA; NbExp=3; IntAct=EBI-10195782, EBI-347996;
-!- SUBCELLULAR LOCATION: Secreted, extracellular space. Note=99% of
EC-SOD is anchored to heparan sulfate proteoglycans in the tissue
interstitium, and 1% is located in the vasculature in equilibrium
between the plasma and the endothelium.
-!- TISSUE SPECIFICITY: Expressed in blood vessels, heart, lung,
kidney and placenta. Major SOD isoenzyme in extracellular fluids
such as plasma, lymph and synovial fluid.
-!- POLYMORPHISM: The variant Gly-231 which is found in about 2.2% of
individual displays a 10-fold increased plasma EC-SOD content due
to reduced heparin-binding affinity and thus the impairment of its
binding ability to endothelial cell surface.
{ECO:0000269|PubMed:7662997, ECO:0000269|PubMed:8034674,
ECO:0000269|PubMed:8546689}.
-!- SIMILARITY: Belongs to the Cu-Zn superoxide dismutase family.
{ECO:0000305}.
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/sod3/";
-!- WEB RESOURCE: Name=Wikipedia; Note=Superoxide dismutase entry;
URL="https://en.wikipedia.org/wiki/Superoxide_dismutase";
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; J02947; AAA66000.1; -; mRNA.
EMBL; U10116; AAA62278.1; -; Genomic_DNA.
EMBL; CR541853; CAG46651.1; -; mRNA.
EMBL; AY787834; AAV40827.1; -; Genomic_DNA.
EMBL; BC014418; AAH14418.1; -; mRNA.
CCDS; CCDS3430.1; -.
PIR; A28301; DSHUEC.
RefSeq; NP_003093.2; NM_003102.2.
UniGene; Hs.2420; -.
PDB; 2JLP; X-ray; 1.70 A; A/B/C/D=19-240.
PDBsum; 2JLP; -.
ProteinModelPortal; P08294; -.
SMR; P08294; -.
BioGrid; 112532; 1.
IntAct; P08294; 9.
STRING; 9606.ENSP00000371554; -.
BindingDB; P08294; -.
ChEMBL; CHEMBL2069159; -.
iPTMnet; P08294; -.
PhosphoSitePlus; P08294; -.
BioMuta; SOD3; -.
DMDM; 108885292; -.
EPD; P08294; -.
MaxQB; P08294; -.
PaxDb; P08294; -.
PeptideAtlas; P08294; -.
PRIDE; P08294; -.
ProteomicsDB; 52104; -.
DNASU; 6649; -.
Ensembl; ENST00000382120; ENSP00000371554; ENSG00000109610.
GeneID; 6649; -.
KEGG; hsa:6649; -.
UCSC; uc003gqz.4; human.
CTD; 6649; -.
DisGeNET; 6649; -.
EuPathDB; HostDB:ENSG00000109610.5; -.
GeneCards; SOD3; -.
HGNC; HGNC:11181; SOD3.
HPA; HPA042110; -.
MIM; 185490; gene.
neXtProt; NX_P08294; -.
OpenTargets; ENSG00000109610; -.
PharmGKB; PA36018; -.
eggNOG; KOG0441; Eukaryota.
eggNOG; COG2032; LUCA.
GeneTree; ENSGT00530000063226; -.
HOGENOM; HOG000263447; -.
HOVERGEN; HBG000062; -.
InParanoid; P08294; -.
KO; K16627; -.
OMA; EQEDDMG; -.
OrthoDB; EOG091G13ID; -.
PhylomeDB; P08294; -.
TreeFam; TF105133; -.
BioCyc; MetaCyc:HS03242-MONOMER; -.
Reactome; R-HSA-3299685; Detoxification of Reactive Oxygen Species.
ChiTaRS; SOD3; human.
EvolutionaryTrace; P08294; -.
GeneWiki; SOD3; -.
GenomeRNAi; 6649; -.
PMAP-CutDB; P08294; -.
PRO; PR:P08294; -.
Proteomes; UP000005640; Chromosome 4.
Bgee; ENSG00000109610; -.
CleanEx; HS_SOD3; -.
ExpressionAtlas; P08294; baseline and differential.
Genevisible; P08294; HS.
GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0005576; C:extracellular region; HDA:BHF-UCL.
GO; GO:0005615; C:extracellular space; HDA:BHF-UCL.
GO; GO:0005796; C:Golgi lumen; TAS:Reactome.
GO; GO:0005634; C:nucleus; IEA:Ensembl.
GO; GO:0005507; F:copper ion binding; IBA:GO_Central.
GO; GO:0008201; F:heparin binding; IEA:UniProtKB-KW.
GO; GO:0004784; F:superoxide dismutase activity; IBA:GO_Central.
GO; GO:0008270; F:zinc ion binding; IBA:GO_Central.
GO; GO:0034599; P:cellular response to oxidative stress; TAS:Reactome.
GO; GO:0046688; P:response to copper ion; IEA:Ensembl.
GO; GO:0001666; P:response to hypoxia; IEA:Ensembl.
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; Glycation; Glycoprotein;
Heparin-binding; Metal-binding; Oxidoreductase; Polymorphism;
Reference proteome; Secreted; Signal; Zinc.
SIGNAL 1 18
CHAIN 19 240 Extracellular superoxide dismutase [Cu-
Zn].
/FTId=PRO_0000032855.
METAL 114 114 Copper; catalytic.
METAL 116 116 Copper; catalytic.
METAL 131 131 Copper; catalytic.
METAL 131 131 Zinc; structural.
METAL 139 139 Zinc; structural.
METAL 142 142 Zinc; structural.
METAL 145 145 Zinc; structural.
METAL 181 181 Copper; catalytic.
SITE 41 41 Not glycated.
SITE 92 92 Not glycated.
SITE 238 238 Not glycated.
CARBOHYD 107 107 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:16335952,
ECO:0000269|PubMed:19159218}.
CARBOHYD 229 229 N-linked (Glc) (glycation) lysine; in
vitro.
CARBOHYD 230 230 N-linked (Glc) (glycation) lysine; in
vitro.
DISULFID 63 208 {ECO:0000269|PubMed:19289127}.
DISULFID 125 207 {ECO:0000269|PubMed:19289127}.
VARIANT 58 58 A -> T (in dbSNP:rs2536512).
{ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:3476950,
ECO:0000269|PubMed:7959763,
ECO:0000269|Ref.3, ECO:0000269|Ref.4}.
/FTId=VAR_020776.
VARIANT 91 91 A -> T (in dbSNP:rs17879876).
{ECO:0000269|Ref.4}.
/FTId=VAR_020777.
VARIANT 231 231 R -> G (in dbSNP:rs1799895).
{ECO:0000269|PubMed:7662997,
ECO:0000269|PubMed:8034674,
ECO:0000269|PubMed:8546689,
ECO:0000269|PubMed:8864862,
ECO:0000269|Ref.4}.
/FTId=VAR_014705.
STRAND 59 67 {ECO:0000244|PDB:2JLP}.
STRAND 79 88 {ECO:0000244|PDB:2JLP}.
STRAND 93 100 {ECO:0000244|PDB:2JLP}.
STRAND 104 117 {ECO:0000244|PDB:2JLP}.
HELIX 124 128 {ECO:0000244|PDB:2JLP}.
STRAND 145 152 {ECO:0000244|PDB:2JLP}.
STRAND 155 164 {ECO:0000244|PDB:2JLP}.
STRAND 166 169 {ECO:0000244|PDB:2JLP}.
STRAND 176 183 {ECO:0000244|PDB:2JLP}.
STRAND 190 192 {ECO:0000244|PDB:2JLP}.
HELIX 195 198 {ECO:0000244|PDB:2JLP}.
STRAND 204 209 {ECO:0000244|PDB:2JLP}.
HELIX 216 222 {ECO:0000244|PDB:2JLP}.
SEQUENCE 240 AA; 25851 MW; 585B8DEBFC506CF4 CRC64;
MLALLCSCLL LAAGASDAWT GEDSAEPNSD SAEWIRDMYA KVTEIWQEVM QRRDDDGALH
AACQVQPSAT LDAAQPRVTG VVLFRQLAPR AKLDAFFALE GFPTEPNSSS RAIHVHQFGD
LSQGCESTGP HYNPLAVPHP QHPGDFGNFA VRDGSLWRYR AGLAASLAGP HSIVGRAVVV
HAGEDDLGRG GNQASVENGN AGRRLACCVV GVCGPGLWER QAREHSERKK RRRESECKAA


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