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ceruloplasmin; ferroxidase (CP)
Function:
- oxidizes Fe+2 to Fe+3 without releasing oxygen radicals
- essential for transferrin binding of iron
- binds copper (6-7 atoms per molecule)
- but not a transport protein for copper
- involved in iron transport across the cell membrane
4 Fe+2 + 4 H+ + O2 = 4 Fe+3 + 2 H2O
Cofactor: binds 6 copper ions per monomer
Structure:
- glycoprotein
- belongs to the multicopper oxidase family
- contains 3 F5/8 type A domains
- contains 6 plastocyanin-like domains
Compartment: secreted
Expression:
- expressed by the liver & secreted into plasma
Pathology:
- defects in CP are the cause of aceruloplasminemia
- ceruloplasmin levels are decreased in Wilson's disease
- copper cannot be incorporated into ceruloplasmin in liver due to a defect in copper transporting ATPase-2
Notes:
- blue protein
Related
ceruloplasmin in serum
General
acute phase protein
alpha 2 globulin
glycoprotein
metalloprotein
oxidoreductase
phosphoprotein
Properties
SIZE: entity length = 1065 aa
MW = 122 kD
COMPARTMENT: plasma
MOTIF: signal sequence {1-19}
F5/8 type A 1 {20-357}
MOTIF: Plastocyanin-like 1 {20-200}
copper [Cu]-binding site
SITE: 120-120
MOTIF: histidine residue (3)
copper [Cu]-binding site
SITE: 122-122
MOTIF: histidine residue (3)
N-glycosylation site {N138}
cysteine residue {C174}
MODIFICATION: cysteine residue {C200}
copper [Cu]-binding site
SITE: 180-180
MOTIF: histidine residue (3)
copper [Cu]-binding site
SITE: 182-182
MOTIF: histidine residue (3)
cysteine residue {C200}
MODIFICATION: cysteine residue {C174}
Ser phosphorylation site {S204}
Plastocyanin-like 2 {209-357}
cysteine residue {C276}
MODIFICATION: cysteine residue {C357}
copper [Cu]-binding site
SITE: 295-295
MOTIF: histidine residue (3)
copper [Cu]-binding site
SITE: 338-338
MOTIF: histidine residue (3)
copper [Cu]-binding site
SITE: 343-343
MOTIF: histidine residue (3)
cysteine residue {C357}
MODIFICATION: cysteine residue {C276}
N-glycosylation site {N358}
F5/8 type A 2 {370-718}
MOTIF: Plastocyanin-like 3 {370-560}
N-glycosylation site {N397}
cysteine residue {C534}
MODIFICATION: cysteine residue {C560}
cysteine residue {C560}
MODIFICATION: cysteine residue {C534}
Plastocyanin-like 4 {570-718}
N-glycosylation site {N588}
cysteine residue {C637}
MODIFICATION: cysteine residue {C718}
copper [Cu]-binding site
SITE: 656-656
MOTIF: histidine residue (3)
copper [Cu]-binding site
SITE: 699-699
MOTIF: histidine residue (3)
copper [Cu]-binding site
SITE: 704-704
MOTIF: histidine residue (3)
copper [Cu]-binding site
SITE: 709-709
MOTIF: histidine residue (3)
cysteine residue {C718}
MODIFICATION: cysteine residue {C637}
F5/8 type A 3 {730-1061}
MOTIF: Plastocyanin-like 5 {730-900}
N-glycosylation site {N762}
Tyr phosphorylation site {Y784}
Tyr phosphorylation site {Y787}
cysteine residue {C874}
MODIFICATION: cysteine residue {C900}
cysteine residue {C900}
MODIFICATION: cysteine residue {C874}
Plastocyanin-like 6 {908-1061}
N-glycosylation site {N926}
copper [Cu]-binding site
SITE: 994-994
MOTIF: histidine residue (3)
copper [Cu]-binding site
SITE: 997-997
MOTIF: histidine residue (3)
copper [Cu]-binding site
SITE: 999-999
MOTIF: histidine residue (3)
copper [Cu]-binding site
SITE: 1039-1039
MOTIF: histidine residue (3)
copper [Cu]-binding site
SITE: 1040-1040
MOTIF: histidine residue (3)
copper [Cu]-binding site
SITE: 1041-1041
MOTIF: histidine residue (3)
copper [Cu]-binding site
SITE: 1045-1045
MOTIF: histidine residue (3)
copper [Cu]-binding site
SITE: 1050-1050
MOTIF: histidine residue (3)
MISC-INFO: CONCENTRATION 20-40 MG/DL
Database Correlations
OMIM correlations
MORBIDMAP 117700
UniProt P00450
PFAM correlations
Entrez Gene 1356
Kegg hsa:1356
ENZYME 1.16.3.1
References
- Tietz Fundamentals of Clinical Chemistry 3rd ed, WB
Saunders, 1987 pg 331
- Principles of Biochemistry 6th ed., White, Handler,
Smith, Hill, & Lehman (eds.) McGraw-Hill, NY 1978,
pg 408 (MW)
- UniProt :accession P00450
- GeneReviews
http://www.ncbi.nlm.nih.gov/sites/genetests/lab/gene/CP
- Wikipedia; Note: ceruloplasmin entry
http://en.wikipedia.org/wiki/ceruloplasmin