Ceruloplasmin

Details

Name
Ceruloplasmin
Synonyms
  • 1.16.3.1
  • Ferroxidase
Gene Name
CP
Organism
Humans
Amino acid sequence
>lcl|BSEQ0010796|Ceruloplasmin
MKILILGIFLFLCSTPAWAKEKHYYIGIIETTWDYASDHGEKKLISVDTEHSNIYLQNGP
DRIGRLYKKALYLQYTDETFRTTIEKPVWLGFLGPIIKAETGDKVYVHLKNLASRPYTFH
SHGITYYKEHEGAIYPDNTTDFQRADDKVYPGEQYTYMLLATEEQSPGEGDGNCVTRIYH
SHIDAPKDIASGLIGPLIICKKDSLDKEKEKHIDREFVVMFSVVDENFSWYLEDNIKTYC
SEPEKVDKDNEDFQESNRMYSVNGYTFGSLPGLSMCAEDRVKWYLFGMGNEVDVHAAFFH
GQALTNKNYRIDTINLFPATLFDAYMVAQNPGEWMLSCQNLNHLKAGLQAFFQVQECNKS
SSKDNIRGKHVRHYYIAAEEIIWNYAPSGIDIFTKENLTAPGSDSAVFFEQGTTRIGGSY
KKLVYREYTDASFTNRKERGPEEEHLGILGPVIWAEVGDTIRVTFHNKGAYPLSIEPIGV
RFNKNNEGTYYSPNYNPQSRSVPPSASHVAPTETFTYEWTVPKEVGPTNADPVCLAKMYY
SAVDPTKDIFTGLIGPMKICKKGSLHANGRQKDVDKEFYLFPTVFDENESLLLEDNIRMF
TTAPDQVDKEDEDFQESNKMHSMNGFMYGNQPGLTMCKGDSVVWYLFSAGNEADVHGIYF
SGNTYLWRGERRDTANLFPQTSLTLHMWPDTEGTFNVECLTTDHYTGGMKQKYTVNQCRR
QSEDSTFYLGERTYYIAAVEVEWDYSPQREWEKELHHLQEQNVSNAFLDKGEFYIGSKYK
KVVYRQYTDSTFRVPVERKAEEEHLGILGPQLHADVGDKVKIIFKNMATRPYSIHAHGVQ
TESSTVTPTLPGETLTYVWKIPERSGAGTEDSACIPWAYYSTVDQVKDLYSGLIGPLIVC
RRPYLKVFNPRRKLEFALLFLVFDENESWYLDDNIKTYSDHPEKVNKDDEEFIESNKMHA
INGRMFGNLQGLTMHVGDEVNWYLMGMGNEIDLHTVHFHGHSFQYKHRGVYSSDVFDIFP
GTYQTLEMFPRTPGIWLLHCHVTDHIHAGMETTYTVLQNEDTKSG
Number of residues
1065
Molecular Weight
122204.45
Theoretical pI
5.5
GO Classification
Functions
chaperone binding / copper ion binding / ferroxidase activity
Processes
cellular iron ion homeostasis / copper ion transport / transmembrane transport
Components
blood microparticle / extracellular exosome / extracellular region / extracellular space / lysosomal membrane
General Function
Ferroxidase 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).
Pfam Domain Function
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
3q23-q25
External Identifiers
ResourceLink
UniProtKB IDP00450
UniProtKB Entry NameCERU_HUMAN
GenBank Protein ID180256
GenBank Gene IDM13699
GenAtlas IDCP
HGNC IDHGNC:2295
General References
  1. 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]
  2. 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]
  3. 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]
  4. 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]
  5. 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]
  6. 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]
  7. 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]
  8. 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]
  9. 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]
  10. 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]
  11. Hellman NE, Gitlin JD: Ceruloplasmin metabolism and function. Annu Rev Nutr. 2002;22:439-58. Epub 2002 Apr 4. [PubMed:12055353]
  12. 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]
  13. 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]
  14. 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]
  15. 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]
  16. 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. [PubMed:19139490]
  17. 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]
  18. 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. [PubMed:24275569]
  19. 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. [PubMed:26091039]
  20. 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]
  21. 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]
  22. 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]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB00055Drotrecogin alfaapproved, investigational, withdrawnunknownDetails
DB09130Copperapproved, investigationalnobinderDetails
DB01373Calciumapproved, nutraceuticalunknownDetails
DB01592IronapprovedunknownDetails
DB01593Zincapproved, investigationalunknownDetails
DB06778Cupric sulfateapprovedunknownDetails
DB13257Ferrous sulfate anhydrousapprovedyessubstrateDetails
DB11134Cupric oxideapprovedunknownbinderDetails
DB12965Silverapproved, investigationalunknownbinderDetails
DB14487Zinc acetateapproved, investigationalunknownDetails
DB14488Ferrous gluconateapprovedunknownDetails
DB14489Ferrous succinateapprovedunknownDetails
DB14490Ferrous ascorbateapprovedunknownDetails
DB14491Ferrous fumarateapprovedunknownDetails
DB14501Ferrous glycine sulfateapprovedunknownDetails
DB14533Zinc chlorideapproved, investigationalunknownDetails