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Identification
HMDB Protein ID HMDBP00472
Secondary Accession Numbers
  • 5712
Name Ceruloplasmin
Synonyms
  1. Ferroxidase
Gene Name CP
Protein Type Unknown
Biological Properties
General Function Involved in oxidoreductase activity
Specific Function Ceruloplasmin is a 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. Provides Cu(2+) ions for the ascorbate-mediated deaminase degradation of the heparan sulfate chains of GPC1. May also play a role in fetal lung development or pulmonary antioxidant defense (By similarity).
Pathways
  • Porphyrin and chlorophyll metabolism
Reactions
Fe2+ + Hydrogen Ion + Oxygen → Fe3+ + Water details
GO Classification
Biological Process
cellular iron ion homeostasis
copper ion transport
transmembrane transport
Cellular Component
extracellular space
Function
ion binding
cation binding
metal ion binding
binding
catalytic activity
transition metal ion binding
oxidoreductase activity
copper ion binding
Molecular Function
ferroxidase activity
copper ion binding
Process
metabolic process
oxidation reduction
Cellular Location
  1. Secreted
Gene Properties
Chromosome Location 3
Locus 3q23-q25
SNPs CP
Gene Sequence
>3198 bp
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
CGAAGACCTTACTTGAAAGTATTCAATCCCAGAAGGAAGCTGGAATTTGCCCTTCTGTTT
CTAGTTTTTGATGAGAATGAATCTTGGTACTTAGATGACAACATCAAAACATACTCTGAT
CACCCCGAGAAAGTAAACAAAGATGATGAGGAATTCATAGAAAGCAATAAAATGCATGCT
ATTAATGGAAGAATGTTTGGAAACCTACAAGGCCTCACAATGCACGTGGGAGATGAAGTC
AACTGGTATCTGATGGGAATGGGCAATGAAATAGACTTACACACTGTACATTTTCACGGC
CATAGCTTCCAATACAAGCACAGGGGAGTTTATAGTTCTGATGTCTTTGACATTTTCCCT
GGAACATACCAAACCCTAGAAATGTTTCCAAGAACACCTGGAATTTGGTTACTCCACTGC
CATGTGACCGACCACATTCATGCTGGAATGGAAACCACTTACACCGTTCTACAAAATGAA
GACACCAAATCTGGCTGA
Protein Properties
Number of Residues 1065
Molecular Weight 122204.45
Theoretical pI 5.716
Pfam Domain Function
Signals Not Available
Transmembrane Regions Not Available
Protein Sequence
>Ceruloplasmin
MKILILGIFLFLCSTPAWAKEKHYYIGIIETTWDYASDHGEKKLISVDTEHSNIYLQNGP
DRIGRLYKKALYLQYTDETFRTTIEKPVWLGFLGPIIKAETGDKVYVHLKNLASRPYTFH
SHGITYYKEHEGAIYPDNTTDFQRADDKVYPGEQYTYMLLATEEQSPGEGDGNCVTRIYH
SHIDAPKDIASGLIGPLIICKKDSLDKEKEKHIDREFVVMFSVVDENFSWYLEDNIKTYC
SEPEKVDKDNEDFQESNRMYSVNGYTFGSLPGLSMCAEDRVKWYLFGMGNEVDVHAAFFH
GQALTNKNYRIDTINLFPATLFDAYMVAQNPGEWMLSCQNLNHLKAGLQAFFQVQECNKS
SSKDNIRGKHVRHYYIAAEEIIWNYAPSGIDIFTKENLTAPGSDSAVFFEQGTTRIGGSY
KKLVYREYTDASFTNRKERGPEEEHLGILGPVIWAEVGDTIRVTFHNKGAYPLSIEPIGV
RFNKNNEGTYYSPNYNPQSRSVPPSASHVAPTETFTYEWTVPKEVGPTNADPVCLAKMYY
SAVDPTKDIFTGLIGPMKICKKGSLHANGRQKDVDKEFYLFPTVFDENESLLLEDNIRMF
TTAPDQVDKEDEDFQESNKMHSMNGFMYGNQPGLTMCKGDSVVWYLFSAGNEADVHGIYF
SGNTYLWRGERRDTANLFPQTSLTLHMWPDTEGTFNVECLTTDHYTGGMKQKYTVNQCRR
QSEDSTFYLGERTYYIAAVEVEWDYSPQREWEKELHHLQEQNVSNAFLDKGEFYIGSKYK
KVVYRQYTDSTFRVPVERKAEEEHLGILGPQLHADVGDKVKIIFKNMATRPYSIHAHGVQ
TESSTVTPTLPGETLTYVWKIPERSGAGTEDSACIPWAYYSTVDQVKDLYSGLIGPLIVC
RRPYLKVFNPRRKLEFALLFLVFDENESWYLDDNIKTYSDHPEKVNKDDEEFIESNKMHA
INGRMFGNLQGLTMHVGDEVNWYLMGMGNEIDLHTVHFHGHSFQYKHRGVYSSDVFDIFP
GTYQTLEMFPRTPGIWLLHCHVTDHIHAGMETTYTVLQNEDTKSG
GenBank ID Protein 180256
UniProtKB/Swiss-Prot ID P00450
UniProtKB/Swiss-Prot Entry Name CERU_HUMAN
PDB IDs
GenBank Gene ID M13699
GeneCard ID CP
GenAtlas ID CP
HGNC ID HGNC:2295
References
General References
  1. 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. [PubMed:19159218 ]
  2. Imami K, Sugiyama N, Kyono Y, Tomita M, Ishihama Y: Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column. Anal Sci. 2008 Jan;24(1):161-6. [PubMed:18187866 ]
  3. Rikova K, Guo A, Zeng Q, Possemato A, Yu J, Haack H, Nardone J, Lee K, Reeves C, Li Y, Hu Y, Tan Z, Stokes M, Sullivan L, Mitchell J, Wetzel R, Macneill J, Ren JM, Yuan J, Bakalarski CE, Villen J, Kornhauser JM, Smith B, Li D, Zhou X, Gygi SP, Gu TL, Polakiewicz RD, Rush J, Comb MJ: Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer. Cell. 2007 Dec 14;131(6):1190-203. [PubMed:18083107 ]
  4. 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. [PubMed:16335952 ]
  5. 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. [PubMed:14760718 ]
  6. 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. [PubMed:15084671 ]
  7. 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. [PubMed:2873574 ]
  8. 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. [PubMed:7702601 ]
  9. 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. [PubMed:3755405 ]
  10. 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. [PubMed:3486416 ]
  11. 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. [PubMed:6582496 ]
  12. 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. [PubMed:6571985 ]
  13. 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. [PubMed:6940148 ]
  14. 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. [PubMed:6987229 ]
  15. 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. [PubMed:6987230 ]
  16. 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. [PubMed:2355023 ]
  17. Hellman NE, Gitlin JD: Ceruloplasmin metabolism and function. Annu Rev Nutr. 2002;22:439-58. Epub 2002 Apr 4. [PubMed:12055353 ]
  18. 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. [PubMed:19838169 ]
  19. 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. [PubMed:17242517 ]
  20. 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. [PubMed:15557511 ]
  21. 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. [PubMed:16150804 ]