Ceruloplasmin
Details
- Name
- Ceruloplasmin
- Kind
- protein
- Synonyms
- Cuproxidase ceruloplasmin
- Ferroxidase ceruloplasmin
- Glutathione peroxidase ceruloplasmin
- Glutathione-dependent peroxiredoxin ceruloplasmin
- Gene Name
- CP
- UniProtKB Entry
- P00450Swiss-Prot
- Organism
- Humans
- NCBI Taxonomy ID
- 9606
- Amino acid sequence
>lcl|BSEQ0055645|Ceruloplasmin MKILILGIFLFLCSTPAWAKEKHYYIGIIETTWDYASDHGEKKLISVDTEHSNIYLQNGP DRIGRLYKKALYLQYTDETFRTTIEKPVWLGFLGPIIKAETGDKVYVHLKNLASRPYTFH SHGITYYKEHEGAIYPDNTTDFQRADDKVYPGEQYTYMLLATEEQSPGEGDGNCVTRIYH SHIDAPKDIASGLIGPLIICKKDSLDKEKEKHIDREFVVMFSVVDENFSWYLEDNIKTYC SEPEKVDKDNEDFQESNRMYSVNGYTFGSLPGLSMCAEDRVKWYLFGMGNEVDVHAAFFH GQALTNKNYRIDTINLFPATLFDAYMVAQNPGEWMLSCQNLNHLKAGLQAFFQVQECNKS SSKDNIRGKHVRHYYIAAEEIIWNYAPSGIDIFTKENLTAPGSDSAVFFEQGTTRIGGSY KKLVYREYTDASFTNRKERGPEEEHLGILGPVIWAEVGDTIRVTFHNKGAYPLSIEPIGV RFNKNNEGTYYSPNYNPQSRSVPPSASHVAPTETFTYEWTVPKEVGPTNADPVCLAKMYY SAVEPTKDIFTGLIGPMKICKKGSLHANGRQKDVDKEFYLFPTVFDENESLLLEDNIRMF TTAPDQVDKEDEDFQESNKMHSMNGFMYGNQPGLTMCKGDSVVWYLFSAGNEADVHGIYF SGNTYLWRGERRDTANLFPQTSLTLHMWPDTEGTFNVECLTTDHYTGGMKQKYTVNQCRR QSEDSTFYLGERTYYIAAVEVEWDYSPQREWEKELHHLQEQNVSNAFLDKGEFYIGSKYK KVVYRQYTDSTFRVPVERKAEEEHLGILGPQLHADVGDKVKIIFKNMATRPYSIHAHGVQ TESSTVTPTLPGETLTYVWKIPERSGAGTEDSACIPWAYYSTVDQVKDLYSGLIGPLIVC RRPYLKVFNPRRKLEFALLFLVFDENESWYLDDNIKTYSDHPEKVNKDDEEFIESNKMHA INGRMFGNLQGLTMHVGDEVNWYLMGMGNEIDLHTVHFHGHSFQYKHRGVYSSDVFDIFP GTYQTLEMFPRTPGIWLLHCHVTDHIHAGMETTYTVLQNEDTKSG
- Number of residues
- 1065
- Molecular Weight
- 122218.48
- Theoretical pI
- 5.5
- GO Classification
- Functionsglutathione peroxidase activity / oxidoreductase activity / oxidoreductase activity, acting on metal ions, oxygen as acceptor / phospholipid-hydroperoxide glutathione peroxidase activity / protein-folding chaperone bindingProcessesintracellular copper ion homeostasis / intracellular iron ion homeostasis / iron ion transportComponentsendoplasmic reticulum lumen / plasma membrane
- General Function
- Multifunctional blue, copper-binding (6-7 atoms per molecule) glycoprotein. It has ferroxidase activity oxidizing Fe(2+) to Fe(3+) without releasing radical oxygen species. It is involved in iron transport across the cell membrane (PubMed:16150804). Copper ions provide a large number of enzymatic activites. Oxidizes highly toxic ferrous ions to the ferric state for further incorporation onto apo-transferrins, catalyzes Cu(+) oxidation and promotes the oxidation of biogenic amines such as norepinephrin and serotonin (PubMed:14623105, PubMed:4643313, PubMed:5912351). Provides Cu(2+) ions for the ascorbate-mediated deaminase degradation of the heparan sulfate chains of GPC1 (By similarity). Has glutathione peroxidase-like activity, can remove both hydrogen peroxide and lipid hydroperoxide in the presence of thiols (PubMed:10481051). Also shows NO-oxidase and NO2 synthase activities that determine endocrine NO homeostasis (PubMed:16906150)
- Specific Function
- copper ion binding
- Pfam Domain Function
- Signal Regions
- 1-19
- Transmembrane Regions
- Not Available
- Cellular Location
- Secreted
- Gene sequence
>lcl|BSEQ0010797|Ceruloplasmin (CP) ATGAAGATTTTGATACTTGGTATTTTTCTGTTTTTATGTAGTACCCCAGCCTGGGCGAAA GAAAAGCATTATTACATTGGAATTATTGAAACGACTTGGGATTATGCCTCTGACCATGGG GAAAAGAAACTTATTTCTGTTGACACGGAACATTCCAATATCTATCTTCAAAATGGCCCA GATAGAATTGGGAGACTATATAAGAAGGCCCTTTATCTTCAGTACACAGATGAAACCTTT AGGACAACTATAGAAAAACCGGTCTGGCTTGGGTTTTTAGGCCCTATTATCAAAGCTGAA ACTGGAGATAAAGTTTATGTACACTTAAAAAACCTTGCCTCTAGGCCCTACACCTTTCAT TCACATGGAATAACTTACTATAAGGAACATGAGGGGGCCATCTACCCTGATAACACCACA GATTTTCAAAGAGCAGATGACAAAGTATATCCAGGAGAGCAGTATACATACATGTTGCTT GCCACTGAAGAACAAAGTCCTGGGGAAGGAGATGGCAATTGTGTGACTAGGATTTACCAT TCCCACATTGATGCTCCAAAAGATATTGCCTCAGGACTCATCGGACCTTTAATAATCTGT AAAAAAGATTCTCTAGATAAAGAAAAAGAAAAACATATTGACCGAGAATTTGTGGTGATG TTTTCTGTGGTGGATGAAAATTTCAGCTGGTACCTAGAAGACAACATTAAAACCTACTGC TCAGAACCAGAGAAAGTTGACAAAGACAACGAAGACTTCCAGGAGAGTAACAGAATGTAT TCTGTGAATGGATACACTTTTGGAAGTCTCCCAGGACTCTCCATGTGTGCTGAAGACAGA GTAAAATGGTACCTTTTTGGTATGGGTAATGAAGTTGATGTGCACGCAGCTTTCTTTCAC GGGCAAGCACTGACTAACAAGAACTACCGTATTGACACAATCAACCTCTTTCCTGCTACC CTGTTTGATGCTTATATGGTGGCCCAGAACCCTGGAGAATGGATGCTCAGCTGTCAGAAT CTAAACCATCTGAAAGCCGGTTTGCAAGCCTTTTTCCAGGTCCAGGAGTGTAACAAGTCT TCATCAAAGGATAATATCCGTGGGAAGCATGTTAGACACTACTACATTGCCGCTGAGGAA ATCATCTGGAACTATGCTCCCTCTGGTATAGACATCTTCACTAAAGAAAACTTAACAGCA CCTGGAAGTGACTCAGCGGTGTTTTTTGAACAAGGTACCACAAGAATTGGAGGCTCTTAT AAAAAGCTGGTTTATCGTGAGTACACAGATGCCTCCTTCACAAATCGAAAGGAGAGAGGC CCTGAAGAAGAGCATCTTGGCATCCTGGGTCCTGTCATTTGGGCAGAGGTGGGAGACACC ATCAGAGTAACCTTCCATAACAAAGGAGCATATCCCCTCAGTATTGAGCCGATTGGGGTG AGATTCAATAAGAACAACGAGGGCACATACTATTCCCCAAATTACAACCCCCAGAGCAGA AGTGTGCCTCCTTCAGCCTCCCATGTGGCACCCACAGAAACATTCACCTATGAATGGACT GTCCCCAAAGAAGTAGGACCCACTAATGCAGATCCTGTGTGTCTAGCTAAGATGTATTAT TCTGCTGTGGATCCCACTAAAGATATATTCACTGGGCTTATTGGGCCAATGAAAATATGC AAGAAAGGAAGTTTACATGCAAATGGGAGACAGAAAGATGTAGACAAGGAATTCTATTTG TTTCCTACAGTATTTGATGAGAATGAGAGTTTACTCCTGGAAGATAATATTAGAATGTTT ACAACTGCACCTGATCAGGTGGATAAGGAAGATGAAGACTTTCAGGAATCTAATAAAATG CACTCCATGAATGGATTCATGTATGGGAATCAGCCGGGTCTCACTATGTGCAAAGGAGAT TCGGTCGTGTGGTACTTATTCAGCGCCGGAAATGAGGCCGATGTACATGGAATATACTTT TCAGGAAACACATATCTGTGGAGAGGAGAACGGAGAGACACAGCAAACCTCTTCCCTCAA ACAAGTCTTACGCTCCACATGTGGCCTGACACAGAGGGGACTTTTAATGTTGAATGCCTT ACAACTGATCATTACACAGGCGGCATGAAGCAAAAATATACTGTGAACCAATGCAGGCGG CAGTCTGAGGATTCCACCTTCTACCTGGGAGAGAGGACATACTATATCGCAGCAGTGGAG GTGGAATGGGATTATTCCCCACAAAGGGAGTGGGAAAAGGAGCTGCATCATTTACAAGAG CAGAATGTTTCAAATGCATTTTTAGATAAGGGAGAGTTTTACATAGGCTCAAAGTACAAG AAAGTTGTGTATCGGCAGTATACTGATAGCACATTCCGTGTTCCAGTGGAGAGAAAAGCT GAAGAAGAACATCTGGGAATTCTAGGTCCACAACTTCATGCAGATGTTGGAGACAAAGTC AAAATTATCTTTAAAAACATGGCCACAAGGCCCTACTCAATACATGCCCATGGGGTACAA ACAGAGAGTTCTACAGTTACTCCAACATTACCAGGTGAAACTCTCACTTACGTATGGAAA ATCCCAGAAAGATCTGGAGCTGGAACAGAGGATTCTGCTTGTATTCCATGGGCTTATTAT TCAACTGTGGATCAAGTTAAGGACCTCTACAGTGGATTAATTGGCCCCCTGATTGTTTGT CGAAGACCTTACTTGAAAGTATTCAATCCCAGAAGGAAACTGGAATTTGCCCTTCTGTTT CTAGTTTTTGATGAGAATGAATCTTGGTACTTAGATGACAACATCAAAACATACTCTGAT CACCCCGAGAAAGTAAACAAAGATGATGAGGAATTCATAGAAAGCAATAAAATGCATGCT ATTAATGGAAGAATGTTTGGAAACCTACAAGGCCTCACAATGCACGTGGGAGATGAAGTC AACTGGTATCTGATGGGAATGGGCAATGAAATAGACTTACACACTGTACATTTTCACGGC CATAGCTTCCAATACAAGCACAGGGGAGTTTATAGTTCTGATGTCTTTGACATTTTCCCT GGAACATACCAAACCCTAGAAATGTTTCCAAGAACACCTGGAATTTGGTTACTCCACTGC CATGTGACCGACCACATTCATGCTGGAATGGAAACCACTTACACCGTTCTACAAAATGAA GACACCAAATCTGGCTGA
- Chromosome Location
- 3
- Locus
- 3q24-q25.1
- External Identifiers
Resource Link UniProtKB ID P00450 UniProtKB Entry Name CERU_HUMAN GenBank Protein ID 180256 GenBank Gene ID M13699 GeneCard ID CP GenAtlas ID CP HGNC ID HGNC:2295 PDB ID(s) 1KCW, 2J5W, 4EJX, 4ENZ KEGG ID hsa:1356 NCBI Gene ID 1356 - General References
- Koschinsky ML, Funk WD, van Oost BA, MacGillivray RT: Complete cDNA sequence of human preceruloplasmin. Proc Natl Acad Sci U S A. 1986 Jul;83(14):5086-90. [Article]
- Daimon M, Yamatani K, Igarashi M, Fukase N, Kawanami T, Kato T, Tominaga M, Sasaki H: Fine structure of the human ceruloplasmin gene. Biochem Biophys Res Commun. 1995 Mar 28;208(3):1028-35. [Article]
- Mercer JF, Grimes A: Isolation of a human ceruloplasmin cDNA clone that includes the N-terminal leader sequence. FEBS Lett. 1986 Jul 28;203(2):185-90. [Article]
- Yang F, Naylor SL, Lum JB, Cutshaw S, McCombs JL, Naberhaus KH, McGill JR, Adrian GS, Moore CM, Barnett DR, et al.: Characterization, mapping, and expression of the human ceruloplasmin gene. Proc Natl Acad Sci U S A. 1986 May;83(10):3257-61. [Article]
- Takahashi N, Ortel TL, Putnam FW: Single-chain structure of human ceruloplasmin: the complete amino acid sequence of the whole molecule. Proc Natl Acad Sci U S A. 1984 Jan;81(2):390-4. [Article]
- Takahashi N, Bauman RA, Ortel TL, Dwulet FE, Wang CC, Putnam FW: Internal triplication in the structure of human ceruloplasmin. Proc Natl Acad Sci U S A. 1983 Jan;80(1):115-9. [Article]
- Dwulet FE, Putnam FW: Complete amino acid sequence of a 50,000-dalton fragment of human ceruloplasmin. Proc Natl Acad Sci U S A. 1981 Feb;78(2):790-4. [Article]
- Kingston IB, Kingston BL, Putnam FW: Primary structure of a histidine-rich proteolytic fragment of human ceruloplasmin. I. Amino acid sequence of the cyanogen bromide peptides. J Biol Chem. 1980 Apr 10;255(7):2878-85. [Article]
- Kingston IB, Kingston BL, Putnam FW: Primary structure of a histidine-rich proteolytic fragment of human ceruloplasmin. II. Amino acid sequence of the tryptic peptides. J Biol Chem. 1980 Apr 10;255(7):2886-96. [Article]
- Yang FM, Friedrichs WE, Cupples RL, Bonifacio MJ, Sanford JA, Horton WA, Bowman BH: Human ceruloplasmin. Tissue-specific expression of transcripts produced by alternative splicing. J Biol Chem. 1990 Jun 25;265(18):10780-5. [Article]
- Hellman NE, Gitlin JD: Ceruloplasmin metabolism and function. Annu Rev Nutr. 2002;22:439-58. Epub 2002 Apr 4. [Article]
- Kristiansen TZ, Bunkenborg J, Gronborg M, Molina H, Thuluvath PJ, Argani P, Goggins MG, Maitra A, Pandey A: A proteomic analysis of human bile. Mol Cell Proteomics. 2004 Jul;3(7):715-28. Epub 2004 Apr 14. [Article]
- Bunkenborg J, Pilch BJ, Podtelejnikov AV, Wisniewski JR: Screening for N-glycosylated proteins by liquid chromatography mass spectrometry. Proteomics. 2004 Feb;4(2):454-65. [Article]
- 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. [Article]
- 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. [Article]
- Jia W, Lu Z, Fu Y, Wang HP, Wang LH, Chi H, Yuan ZF, Zheng ZB, Song LN, Han HH, Liang YM, Wang JL, Cai Y, Zhang YK, Deng YL, Ying WT, He SM, Qian XH: A strategy for precise and large scale identification of core fucosylated glycoproteins. Mol Cell Proteomics. 2009 May;8(5):913-23. doi: 10.1074/mcp.M800504-MCP200. Epub 2009 Jan 12. [Article]
- Nilsson J, Ruetschi U, Halim A, Hesse C, Carlsohn E, Brinkmalm G, Larson G: Enrichment of glycopeptides for glycan structure and attachment site identification. Nat Methods. 2009 Nov;6(11):809-11. doi: 10.1038/nmeth.1392. Epub 2009 Oct 18. [Article]
- Bian Y, Song C, Cheng K, Dong M, Wang F, Huang J, Sun D, Wang L, Ye M, Zou H: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome. J Proteomics. 2014 Jan 16;96:253-62. doi: 10.1016/j.jprot.2013.11.014. Epub 2013 Nov 22. [Article]
- Tagliabracci VS, Wiley SE, Guo X, Kinch LN, Durrant E, Wen J, Xiao J, Cui J, Nguyen KB, Engel JL, Coon JJ, Grishin N, Pinna LA, Pagliarini DJ, Dixon JE: A Single Kinase Generates the Majority of the Secreted Phosphoproteome. Cell. 2015 Jun 18;161(7):1619-32. doi: 10.1016/j.cell.2015.05.028. [Article]
- Bento I, Peixoto C, Zaitsev VN, Lindley PF: Ceruloplasmin revisited: structural and functional roles of various metal cation-binding sites. Acta Crystallogr D Biol Crystallogr. 2007 Feb;63(Pt 2):240-8. Epub 2007 Jan 16. [Article]
- Hochstrasser H, Bauer P, Walter U, Behnke S, Spiegel J, Csoti I, Zeiler B, Bornemann A, Pahnke J, Becker G, Riess O, Berg D: Ceruloplasmin gene variations and substantia nigra hyperechogenicity in Parkinson disease. Neurology. 2004 Nov 23;63(10):1912-7. [Article]
- Hochstrasser H, Tomiuk J, Walter U, Behnke S, Spiegel J, Kruger R, Becker G, Riess O, Berg D: Functional relevance of ceruloplasmin mutations in Parkinson's disease. FASEB J. 2005 Nov;19(13):1851-3. Epub 2005 Sep 8. [Article]
Associated Data
- Drug Relations
Drug Drug group Pharmacological action? Type Actions Details Copper approved, investigational no carrier binder Details Calcium nutraceutical unknown target Details Iron approved unknown target Details Zinc approved, investigational unknown target Details Cupric sulfate approved unknown transporter Details Ferrous sulfate anhydrous approved no enzyme substrate Details Cupric oxide approved unknown carrier binder Details Silver approved, investigational unknown target binder Details Zinc acetate approved, investigational unknown target Details Ferrous gluconate approved unknown target Details Ferrous succinate approved unknown target Details Ferrous ascorbate approved unknown target Details Ferrous fumarate approved unknown target Details Ferrous glycine sulfate approved unknown target Details Zinc chloride approved, investigational unknown target ligand Details Zinc sulfate, unspecified form approved, experimental unknown target ligand Details Manganese cation approved, nutraceutical unknown carrier binder Details