SOD3

Superoxide dismutase 3, extracellular

Available structures

Ortholog search: PDBe, RCSB

List of PDB id codes
2JLP

Identifiers

Symbols

SOD3 ; EC-SOD

External IDs

OMIM: 185490 MGI: 103181 HomoloGene: 2334 GeneCards: SOD3 Gene

EC number

1.15.1.1

Gene ontology
Molecular function	• superoxide dismutase activity • copper ion binding • protein binding • heparin binding • zinc ion binding
Cellular component	• extracellular region • extracellular space • nucleus • cytoplasm • Golgi lumen • trans-Golgi network • extracellular matrix • extracellular exosome
Biological process	• response to reactive oxygen species • response to hypoxia • removal of superoxide radicals • response to copper ion • oxidation-reduction process
Sources: Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 4:
24.79 – 24.8 Mb

Chr 5:
52.36 – 52.37 Mb

PubMed search

Extracellular superoxide dismutase [Cu-Zn] is an enzyme that in humans is encoded by the SOD3 gene.

This gene encodes a member of the superoxide dismutase (SOD) protein family. SODs are antioxidant enzymes that catalyze the dismutation of two superoxide radicals into hydrogen peroxide and oxygen. The product of this gene is thought to protect the brain, lungs, and other tissues from oxidative stress. The protein is secreted into the extracellular space and forms a glycosylated homotetramer that is anchored to the extracellular matrix (ECM) and cell surfaces through an interaction with heparan sulfate proteoglycan and collagen. A fraction of the protein is cleaved near the C-terminus before secretion to generate circulating tetramers that do not interact with the ECM.^[1]

References

↑ "Entrez Gene: SOD3 superoxide dismutase 3, extracellular".

Zelko IN, Mariani TJ, Folz RJ (2003). "Superoxide dismutase multigene family: a comparison of the CuZn-SOD (SOD1), Mn-SOD (SOD2), and EC-SOD (SOD3) gene structures, evolution, and expression.". Free Radic. Biol. Med. 33 (3): 337–49. doi:10.1016/S0891-5849(02)00905-X. PMID 12126755.
Faraci FM, Didion SP (2005). "Vascular protection: superoxide dismutase isoforms in the vessel wall.". Arterioscler. Thromb. Vasc. Biol. 24 (8): 1367–73. doi:10.1161/01.ATV.0000133604.20182.cf. PMID 15166009.
Adachi T, Ohta H, Yamada H, et al. (1993). "Quantitative analysis of extracellular-superoxide dismutase in serum and urine by ELISA with monoclonal antibody". Clin. Chim. Acta 212 (3): 89–102. doi:10.1016/0009-8981(92)90176-Q. PMID 1477980.
Adachi T, Ohta H, Hayashi K, et al. (1992). "The site of nonenzymic glycation of human extracellular-superoxide dismutase in vitro". Free Radic. Biol. Med. 13 (3): 205–10. doi:10.1016/0891-5849(92)90016-A. PMID 1505778.
Marklund SL (1990). "Expression of extracellular superoxide dismutase by human cell lines". Biochem. J. 266 (1): 213–9. PMC 1131117. PMID 2106874.
Hendrickson DJ, Fisher JH, Jones C, Ho YS (1991). "Regional localization of human extracellular superoxide dismutase gene to 4pter-q21". Genomics 8 (4): 736–8. doi:10.1016/0888-7543(90)90264-U. PMID 2276747.
Hjalmarsson K, Marklund SL, Engström A, Edlund T (1987). "Isolation and sequence of complementary DNA encoding human extracellular superoxide dismutase". Proc. Natl. Acad. Sci. U.S.A. 84 (18): 6340–4. doi:10.1073/pnas.84.18.6340. PMC 299071. PMID 3476950.
Marklund SL (1984). "Extracellular superoxide dismutase in human tissues and human cell lines". J. Clin. Invest. 74 (4): 1398–403. doi:10.1172/JCI111550. PMC 425307. PMID 6541229.
Yamada H, Yamada Y, Adachi T, et al. (1995). "Molecular analysis of extracellular-superoxide dismutase gene associated with high level in serum". Jpn. J. Hum. Genet. 40 (2): 177–84. doi:10.1007/BF01883574. PMID 7662997.
Folz RJ, Crapo JD (1994). "Extracellular superoxide dismutase (SOD3): tissue-specific expression, genomic characterization, and computer-assisted sequence analysis of the human EC SOD gene". Genomics 22 (1): 162–71. doi:10.1006/geno.1994.1357. PMID 7959763.
Sandström J, Nilsson P, Karlsson K, Marklund SL (1994). "10-fold increase in human plasma extracellular superoxide dismutase content caused by a mutation in heparin-binding domain". J. Biol. Chem. 269 (29): 19163–6. PMID 8034674.
Adachi T, Yamada H, Yamada Y, et al. (1996). "Substitution of glycine for arginine-213 in extracellular-superoxide dismutase impairs affinity for heparin and endothelial cell surface". Biochem. J. 313 (1): 235–9. PMC 1216888. PMID 8546689.
Oury TD, Crapo JD, Valnickova Z, Enghild JJ (1996). "Human extracellular superoxide dismutase is a tetramer composed of two disulphide-linked dimers: a simplified, high-yield purification of extracellular superoxide dismutase". Biochem. J. 317 (1): 51–7. PMC 1217485. PMID 8694786.
Adachi T, Morihara N, Yamazaki N, et al. (1997). "An arginine-213 to glycine mutation in human extracellular-superoxide dismutase reduces susceptibility to trypsin-like proteinases". J. Biochem. 120 (1): 184–8. doi:10.1093/oxfordjournals.jbchem.a021383. PMID 8864862.
Bonaldo MF, Lennon G, Soares MB (1997). "Normalization and subtraction: two approaches to facilitate gene discovery". Genome Res. 6 (9): 791–806. doi:10.1101/gr.6.9.791. PMID 8889548.
Enghild JJ, Thogersen IB, Oury TD, et al. (1999). "The heparin-binding domain of extracellular superoxide dismutase is proteolytically processed intracellularly during biosynthesis". J. Biol. Chem. 274 (21): 14818–22. doi:10.1074/jbc.274.21.14818. PMID 10329680.
Bowler RP, Nicks M, Olsen DA, et al. (2002). "Furin proteolytically processes the heparin-binding region of extracellular superoxide dismutase". J. Biol. Chem. 277 (19): 16505–11. doi:10.1074/jbc.M105409200. PMID 11861638.
Yamamoto M, Hara H, Adachi T (2002). "The expression of extracellular-superoxide dismutase is increased by lysophosphatidylcholine in human monocytic U937 cells". Atherosclerosis 163 (2): 223–8. doi:10.1016/S0021-9150(02)00007-2. PMID 12052468.
Serra V, von Zglinicki T, Lorenz M, Saretzki G (2003). "Extracellular superoxide dismutase is a major antioxidant in human fibroblasts and slows telomere shortening". J. Biol. Chem. 278 (9): 6824–30. doi:10.1074/jbc.M207939200. PMID 12475988.

Other oxidoreductases (EC 1.15-1.21)

1.15: Acting on superoxide as acceptor	Superoxide dismutase SOD1 SOD2 SOD3

1.16: Oxidizing metal ions	Ceruloplasmin

1.17: Acting on CH or CH2 groups	Xanthine oxidase Ribonucleotide reductase 4-Hydroxy-3-methylbut-2-enyl diphosphate reductase

1.18: Acting on iron-sulfur proteins as donors	Nitrogenase

1.19: Acting on reduced flavodoxin as donor	Nitrogenase (flavodoxin)

1.20: Acting on phosphorus or arsenic in donors	Glutaredoxin GLRX GLRX2 GLRX3 GLRX5

1.21: Acting on X-H and Y-H to form an X-Y bond	Isopenicillin N synthase Columbamine oxidase Reticuline oxidase Sulochrin oxidase (+)-bisdechlorogeodin-forming (-)-bisdechlorogeodin-forming Aureusidin synthase Tetrahydrocannabinolic acid synthase Cannabidiolic acid synthase Dichlorochromopyrrolate synthase

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SOD3

References

Further reading