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Extracellular superoxide dismutase [Cu-Zn]

NameExtracellular superoxide dismutase [Cu-Zn]
Synonyms
  • 1.15.1.1
  • EC-SOD
Gene NameSOD3
OrganismHuman
Amino acid sequence
>lcl|BSEQ0019667|Extracellular superoxide dismutase [Cu-Zn]
MLALLCSCLLLAAGASDAWTGEDSAEPNSDSAEWIRDMYAKVTEIWQEVMQRRDDDGALH
AACQVQPSATLDAAQPRVTGVVLFRQLAPRAKLDAFFALEGFPTEPNSSSRAIHVHQFGD
LSQGCESTGPHYNPLAVPHPQHPGDFGNFAVRDGSLWRYRAGLAASLAGPHSIVGRAVVV
HAGEDDLGRGGNQASVENGNAGRRLACCVVGVCGPGLWERQAREHSERKKRRRESECKAA
Number of residues240
Molecular Weight25850.675
Theoretical pINot Available
GO Classification
Functions
  • superoxide dismutase activity
  • heparin binding
  • zinc ion binding
  • copper ion binding
Processes
  • response to hypoxia
  • response to copper ion
  • response to reactive oxygen species
  • removal of superoxide radicals
Components
  • extracellular space
  • extracellular exosome
  • Golgi lumen
  • trans-Golgi network
  • cytoplasm
  • extracellular matrix
  • extracellular region
  • nucleus
General FunctionZinc ion binding
Specific FunctionProtect the extracellular space from toxic effect of reactive oxygen intermediates by converting superoxide radicals into hydrogen peroxide and oxygen.
Pfam Domain Function
Transmembrane RegionsNot Available
GenBank Protein IDNot Available
UniProtKB IDP08294
UniProtKB Entry NameSODE_HUMAN
Cellular LocationSecreted
Gene sequence
>lcl|BSEQ0019668|Extracellular superoxide dismutase [Cu-Zn] (SOD3)
ATGCTGGCGCTACTGTGTTCCTGCCTGCTCCTGGCAGCCGGTGCCTCGGACGCCTGGACG
GGCGAGGACTCGGCGGAGCCCAACTCTGACTCGGCGGAGTGGATCCGAGACATGTACGCC
AAGGTCACGGAGATCTGGCAGGAGGTCATGCAGCGGCGGGACGACGACGGCGCGCTCCAC
GCCGCCTGCCAGGTGCAGCCGTCGGCCACGCTGGACGCCGCGCAGCCCCGGGTGACCGGC
GTCGTCCTCTTCCGGCAGCTTGCGCCCCGCGCCAAGCTCGACGCCTTCTTCGCCCTGGAG
GGCTTCCCGACCGAGCCGAACAGCTCCAGCCGCGCCATCCACGTGCACCAGTTCGGGGAC
CTGAGCCAGGGCTGCGAGTCCACCGGGCCCCACTACAACCCGCTGGCCGTGCCGCACCCG
CAGCACCCGGGCGACTTCGGCAACTTCGCGGTCCGCGACGGCAGCCTCTGGAGGTACCGC
GCCGGCCTGGCCGCCTCGCTCGCGGGCCCGCACTCCATCGTGGGCCGGGCCGTGGTCGTC
CACGCTGGCGAGGACGACCTGGGCCGCGGCGGCAACCAGGCCAGCGTGGAGAACGGGAAC
GCGGGCCGGCGGCTGGCCTGCTGCGTGGTGGGCGTGTGCGGGCCCGGGCTCTGGGAGCGC
CAGGCGCGGGAGCACTCAGAGCGCAAGAAGCGGCGGCGCGAGAGCGAGTGCAAGGCCGCC
TGA
GenBank Gene IDNot Available
GeneCard IDNot Available
GenAtlas IDNot Available
HGNC IDHGNC:11181
Chromosome Location4
LocusNot Available
References
  1. Hjalmarsson K, Marklund SL, Engstrom A, Edlund T: Isolation and sequence of complementary DNA encoding human extracellular superoxide dismutase. Proc Natl Acad Sci U S A. 1987 Sep;84(18):6340-4. 3476950
  2. Folz RJ, Crapo JD: Extracellular superoxide dismutase (SOD3): tissue-specific expression, genomic characterization, and computer-assisted sequence analysis of the human EC SOD gene. Genomics. 1994 Jul 1;22(1):162-71. 7959763
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. 15489334
  4. Adachi T, Ohta H, Hayashi K, Hirano K, Marklund SL: The site of nonenzymic glycation of human extracellular-superoxide dismutase in vitro. Free Radic Biol Med. 1992 Sep;13(3):205-10. 1505778
  5. Nozik-Grayck E, Suliman HB, Piantadosi CA: Extracellular superoxide dismutase. Int J Biochem Cell Biol. 2005 Dec;37(12):2466-71. Epub 2005 Jul 21. 16087389
  6. Liu T, Qian WJ, Gritsenko MA, Camp DG 2nd, Monroe ME, Moore RJ, Smith RD: Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry. J Proteome Res. 2005 Nov-Dec;4(6):2070-80. 16335952
  7. 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. 2009 Feb;8(2):651-61. doi: 10.1021/pr8008012. 19159218
  8. Antonyuk SV, Strange RW, Marklund SL, Hasnain SS: The structure of human extracellular copper-zinc superoxide dismutase at 1.7 A resolution: insights into heparin and collagen binding. J Mol Biol. 2009 May 1;388(2):310-26. doi: 10.1016/j.jmb.2009.03.026. Epub 2009 Mar 14. 19289127
  9. Sandstrom J, Nilsson P, Karlsson K, Marklund SL: 10-fold increase in human plasma extracellular superoxide dismutase content caused by a mutation in heparin-binding domain. J Biol Chem. 1994 Jul 22;269(29):19163-6. 8034674
  10. 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. 1995 Jun;40(2):177-84. 7662997
  11. 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. 1996 Jan 1;313 ( Pt 1):235-9. 8546689
  12. 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. 1996 Jul;120(1):184-8. 8864862