|Gene:||CP||Accession Number: HS00590 (MetaCyc)|
Species: Homo sapiens
Ceruloplasmin is a circulating copper protein found in vertebrate plasma, which belongs to the family of multicopper oxidases together with ascorbate oxidase and laccases. In humans it accounts for 95% of plasma copper.
The enzyme plays an important role in iron metabolism and homeostasis by its capacity to oxidize Fe2+ to Fe3+, which allows the subsequent incorporation of the latter into proteins such as apotransferrin and lactoferrin [Pulina02]. The protein was also shown to have an antioxidant activity because of its ability to scavenge superoxide radicals [Cogalgil02].
The enzyme contains six domains that are arranged in three pairs with a pseudo-ternary axis [Vachette02]. Incorporation of copper into newly synthesized apoceruloplasmin results in a detectable conformational change in the protein [Hellman02].
cDNA clones encoding the human enzyme have been isolated and sequenced [Mercer86, Koschinsky86], and the CP gene has been mapped and its structure studied [Daimon95, Yang86]. mRNA was detected in human liver, macrophages, and lymphocytes [Yang86].
|Map Position: [149,776,320 <- 149,824,558]|
Relationship Links: InterPro:IN-FAMILY:IPR001117 , InterPro:IN-FAMILY:IPR002355 , InterPro:IN-FAMILY:IPR008972 , InterPro:IN-FAMILY:IPR011706 , InterPro:IN-FAMILY:IPR011707 , InterPro:IN-FAMILY:IPR027150 , Panther:IN-FAMILY:PTHR10127:SF89 , PDB:Structure:1KCW , PDB:Structure:2J5W , PDB:Structure:4EJX , PDB:Structure:4ENZ , Pfam:IN-FAMILY:PF00394 , Pfam:IN-FAMILY:PF07731 , Pfam:IN-FAMILY:PF07732 , Prosite:IN-FAMILY:PS00079 , Prosite:IN-FAMILY:PS00080
Enzymatic reaction of: ferroxidase (ceruloplasmin)
EC Number: 18.104.22.168
The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.
The reaction is physiologically favored in the direction shown.
Cogalgil02: Cogalgil S, Taysi S (2002). "Levels of antioxidant proteins and soluble intercellular adhesion molecule-1 in serum of patients with rheumatoid arthritis." Ann Clin Lab Sci 32(3);264-70. PMID: 12175089
Daimon95: Daimon M, Yamatani K, Igarashi M, Fukase N, Kawanami T, Kato T, Tominaga M, Sasaki H (1995). "Fine structure of the human ceruloplasmin gene." Biochem Biophys Res Commun 208(3);1028-35. PMID: 7702601
Harris95a: Harris ZL, Takahashi Y, Miyajima H, Serizawa M, MacGillivray RT, Gitlin JD (1995). "Aceruloplasminemia: molecular characterization of this disorder of iron metabolism." Proc Natl Acad Sci U S A 92(7);2539-43. PMID: 7708681
Pulina02: Pulina MO, Zakharova ET, Sokolov AV, Shavlovski MM, Bass MG, Solovyov KV, Kokryakov VN, Vasilyev VB (2002). "Studies of the ceruloplasmin-lactoferrin complex." Biochem Cell Biol 80(1);35-9. PMID: 11908641
Vachette02: Vachette P, Dainese E, Vasyliev VB, Di Muro P, Beltramini M, Svergun DI, De Filippis V, Salvato B (2002). "A key structural role for active site type 3 copper ions in human ceruloplasmin." J Biol Chem 277(43);40823-31. PMID: 12177070
Yang86: Yang F, Naylor SL, Lum JB, Cutshaw S, McCombs JL, Naberhaus KH, McGill JR, Adrian GS, Moore CM, Barnett DR (1986). "Characterization, mapping, and expression of the human ceruloplasmin gene." Proc Natl Acad Sci U S A 83(10);3257-61. PMID: 3486416
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