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
- Functionschaperone binding / copper ion binding / ferroxidase activityProcessescellular iron ion homeostasis / copper ion transport / transmembrane transportComponentsblood 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
Resource Link UniProtKB ID P00450 UniProtKB Entry Name CERU_HUMAN GenBank Protein ID 180256 GenBank Gene ID M13699 GenAtlas ID CP HGNC ID HGNC:2295 - 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]
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- 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]
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- 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]
Drug Relations
- Drug Relations
DrugBank ID Name Drug group Pharmacological action? Actions Details DB09130 Copper approved, investigational no binder Details DB01373 Calcium nutraceutical unknown Details DB01592 Iron approved unknown Details DB01593 Zinc approved, investigational unknown Details DB06778 Cupric sulfate approved unknown Details DB13257 Ferrous sulfate anhydrous approved no substrate Details DB11134 Cupric oxide approved unknown binder Details DB12965 Silver approved, investigational unknown binder Details DB14487 Zinc acetate approved, investigational unknown Details DB14488 Ferrous gluconate approved unknown Details DB14489 Ferrous succinate approved unknown Details DB14490 Ferrous ascorbate approved unknown Details DB14491 Ferrous fumarate approved unknown Details DB14501 Ferrous glycine sulfate approved unknown Details DB14533 Zinc chloride approved, investigational unknown ligand Details DB14548 Zinc sulfate, unspecified form approved, experimental unknown ligand Details