SOD3

SOD3
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 2JLP
Identifiers
Aliases	SOD3, EC-SOD, superoxide dismutase 3, extracellular, superoxide dismutase 3
External IDs	OMIM: 185490; MGI: 103181; HomoloGene: 2334; GeneCards: SOD3; OMA:SOD3 - orthologs
Gene location (Human) Chr. Chromosome 4 (human)[1] Band 4p15.2 Start 24,789,912 bp[1] End 24,800,842 bp[1]
Gene location (Mouse) Chr. Chromosome 5 (mouse)[2] Band 5 C1|5 27.92 cM Start 52,521,133 bp[2] End 52,528,760 bp[2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in Descending thoracic aorta right uterine tube ascending aorta right coronary artery popliteal artery tibial arteries left coronary artery gastric mucosa canal of the cervix right lung Top expressed in choroid plexus of fourth ventricle ascending aorta right kidney aortic valve lactiferous gland human kidney right lung brown adipose tissue adrenal gland ankle More reference expression data BioGPS More reference expression data
Gene ontology Molecular function heparin binding zinc ion binding metal ion binding antioxidant activity protein binding oxidoreductase activity copper ion binding superoxide dismutase activity superoxide dismutase copper chaperone activity Cellular component cytoplasm extracellular matrix Golgi lumen extracellular exosome nucleus extracellular space extracellular region collagen-containing extracellular matrix Biological process response to hypoxia response to copper ion response to oxidative stress superoxide metabolic process cellular response to oxidative stress removal of superoxide radicals cellular oxidant detoxification positive regulation of catalytic activity Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 6649 20657 Ensembl ENSG00000109610 ENSMUSG00000072941 UniProt P08294 O09164 RefSeq (mRNA) NM_003102 NM_011435 RefSeq (protein) NP_003093 NP_035565 Location (UCSC) Chr 4: 24.79 – 24.8 Mb Chr 5: 52.52 – 52.53 Mb PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

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.^[5]

Among black garden ants (Lasius niger), the lifespan of queens is an order of magnitude greater than that of workers despite no systematic nucleotide sequence difference between them.^[6] The SOD3 gene was found to be the most differentially over-expressed gene in the brains of queen vs worker ants. This finding raises the possibility that SOD3 antioxidant activity plays a key role in the striking longevity of social insect queens.^[6]

References

1. GRCh38: Ensembl release 89: ENSG00000109610 – Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000072941 – Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. "Entrez Gene: SOD3 superoxide dismutase 3, extracellular".
6. Lucas ER, Keller L. Elevated expression of ageing and immunity genes in queens of the black garden ant. Exp Gerontol. 2018 Jul 15;108:92-98. doi: 10.1016/j.exger.2018.03.020. Epub 2018 Apr 3. PMID: 29625209

Further reading

• Zelko IN, Mariani TJ, Folz RJ (August 2002). "Superoxide dismutase multigene family: a comparison of the CuZn-SOD (SOD1), Mn-SOD (SOD2), and EC-SOD (SOD3) gene structures, evolution, and expression". Free Radical Biology & Medicine. 33 (3): 337–49. doi:10.1016/S0891-5849(02)00905-X. PMID 12126755.
• Faraci FM, Didion SP (August 2004). "Vascular protection: superoxide dismutase isoforms in the vessel wall". Arteriosclerosis, Thrombosis, and Vascular Biology. 24 (8): 1367–73. doi:10.1161/01.ATV.0000133604.20182.cf. PMID 15166009.
• Adachi T, Ohta H, Yamada H, Futenma A, Kato K, Hirano K (November 1992). "Quantitative analysis of extracellular-superoxide dismutase in serum and urine by ELISA with monoclonal antibody". Clinica Chimica Acta; International Journal of Clinical Chemistry. 212 (3): 89–102. doi:10.1016/0009-8981(92)90176-Q. PMID 1477980.
• Adachi T, Ohta H, Hayashi K, Hirano K, Marklund SL (September 1992). "The site of nonenzymic glycation of human extracellular-superoxide dismutase in vitro". Free Radical Biology & Medicine. 13 (3): 205–10. doi:10.1016/0891-5849(92)90016-A. PMID 1505778.
• Marklund SL (February 1990). "Expression of extracellular superoxide dismutase by human cell lines". The Biochemical Journal. 266 (1): 213–9. doi:10.1042/bj2660213. PMC 1131117. PMID 2106874.
• Hendrickson DJ, Fisher JH, Jones C, Ho YS (December 1990). "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 (September 1987). "Isolation and sequence of complementary DNA encoding human extracellular superoxide dismutase". Proceedings of the National Academy of Sciences of the United States of America. 84 (18): 6340–4. Bibcode:1987PNAS...84.6340H. doi:10.1073/pnas.84.18.6340. PMC 299071. PMID 3476950.
• Marklund SL (October 1984). "Extracellular superoxide dismutase in human tissues and human cell lines". The Journal of Clinical Investigation. 74 (4): 1398–403. doi:10.1172/JCI111550. PMC 425307. PMID 6541229.
• Yamada H, Yamada Y, Adachi T, Goto H, Ogasawara N, Futenma A, Kitano M, Hirano K, Kato K (June 1995). "Molecular analysis of extracellular-superoxide dismutase gene associated with high level in serum". The Japanese Journal of Human Genetics. 40 (2): 177–84. doi:10.1007/BF01883574. PMID 7662997.
• Folz RJ, Crapo JD (July 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 (July 1994). "10-fold increase in human plasma extracellular superoxide dismutase content caused by a mutation in heparin-binding domain". The Journal of Biological Chemistry. 269 (29): 19163–6. doi:10.1016/S0021-9258(17)32289-5. PMID 8034674.
• Adachi T, Yamada H, Yamada Y, Morihara N, Yamazaki N, Murakami T, Futenma A, Kato K, Hirano K (January 1996). "Substitution of glycine for arginine-213 in extracellular-superoxide dismutase impairs affinity for heparin and endothelial cell surface". The Biochemical Journal. 313 ( Pt 1) (1): 235–9. doi:10.1042/bj3130235. PMC 1216888. PMID 8546689.
• Oury TD, Crapo JD, Valnickova Z, Enghild JJ (July 1996). "Human extracellular superoxide dismutase is a tetramer composed of two disulphide-linked dimers: a simplified, high-yield purification of extracellular superoxide dismutase". The Biochemical Journal. 317 ( Pt 1) (1): 51–7. doi:10.1042/bj3170051. PMC 1217485. PMID 8694786.
• Adachi T, Morihara N, Yamazaki N, Yamada H, Futenma A, Kato K, Hirano K (July 1996). "An arginine-213 to glycine mutation in human extracellular-superoxide dismutase reduces susceptibility to trypsin-like proteinases". Journal of Biochemistry. 120 (1): 184–8. doi:10.1093/oxfordjournals.jbchem.a021383. PMID 8864862.
• Bonaldo MF, Lennon G, Soares MB (September 1996). "Normalization and subtraction: two approaches to facilitate gene discovery". Genome Research. 6 (9): 791–806. doi:10.1101/gr.6.9.791. PMID 8889548.
• Enghild JJ, Thogersen IB, Oury TD, Valnickova Z, Hojrup P, Crapo JD (May 1999). "The heparin-binding domain of extracellular superoxide dismutase is proteolytically processed intracellularly during biosynthesis". The Journal of Biological Chemistry. 274 (21): 14818–22. doi:10.1074/jbc.274.21.14818. PMID 10329680.
• Bowler RP, Nicks M, Olsen DA, Thøgersen IB, Valnickova Z, Højrup P, Franzusoff A, Enghild JJ, Crapo JD (May 2002). "Furin proteolytically processes the heparin-binding region of extracellular superoxide dismutase". The Journal of Biological Chemistry. 277 (19): 16505–11. doi:10.1074/jbc.M105409200. PMID 11861638.
• Yamamoto M, Hara H, Adachi T (August 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 (February 2003). "Extracellular superoxide dismutase is a major antioxidant in human fibroblasts and slows telomere shortening". The Journal of Biological Chemistry. 278 (9): 6824–30. doi:10.1074/jbc.M207939200. PMID 12475988.