Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Ceruloplasmin (EC 1.16.3.1) (Ferroxidase)

 CERU_HUMAN              Reviewed;        1065 AA.
P00450; Q14063; Q2PP18; Q9UKS4;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
13-AUG-1987, sequence version 1.
05-DEC-2018, entry version 212.
RecName: Full=Ceruloplasmin;
EC=1.16.3.1;
AltName: Full=Ferroxidase;
Flags: Precursor;
Name=CP;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2873574; DOI=10.1073/pnas.83.14.5086;
Koschinsky M.L., Funk W.D., van Oost B.A., McGillivray R.T.A.;
"Complete cDNA sequence of human preceruloplasmin.";
Proc. Natl. Acad. Sci. U.S.A. 83:5086-5090(1986).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
NHLBI resequencing and genotyping service (RS&G);
Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-1006.
PubMed=7702601; DOI=10.1006/bbrc.1995.1437;
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. 208:1028-1035(1995).
[4]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-40; 549-599; 784-829 AND 919-952.
PubMed=3755405; DOI=10.1016/0014-5793(86)80739-6;
Mercer J.F.B., Grimes A.;
"Isolation of a human ceruloplasmin cDNA clone that includes the N-
terminal leader sequence.";
FEBS Lett. 203:185-190(1986).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-22.
Bingle C.D.;
"Cloning and functional analysis of the human ceruloplasmin gene
minimal promoter.";
Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 218-1065.
PubMed=3486416; DOI=10.1073/pnas.83.10.3257;
Yang F., Naylor S.L., Lum J.B., Cutshaw S., McCombs J.L.,
Naberhaus K.H., McGill J.R., Adrian G.S., Moore C.M., Barnett D.R.,
Bowman B.H.;
"Characterization, mapping, and expression of the human ceruloplasmin
gene.";
Proc. Natl. Acad. Sci. U.S.A. 83:3257-3261(1986).
[7]
PROTEIN SEQUENCE OF 20-1065.
PubMed=6582496; DOI=10.1073/pnas.81.2.390;
Takahashi N., Ortel T.L., Putnam F.W.;
"Single-chain structure of human ceruloplasmin: the complete amino
acid sequence of the whole molecule.";
Proc. Natl. Acad. Sci. U.S.A. 81:390-394(1984).
[8]
PROTEIN SEQUENCE OF 158-333; 518-724 AND 858-1065.
PubMed=6571985; DOI=10.1073/pnas.80.1.115;
Takahashi N., Bauman R.A., Ortel T.L., Dwulet F.E., Wang C.-C.,
Putnam F.W.;
"Internal triplication in the structure of human ceruloplasmin.";
Proc. Natl. Acad. Sci. U.S.A. 80:115-119(1983).
[9]
PROTEIN SEQUENCE OF 501-905.
PubMed=6940148; DOI=10.1073/pnas.78.2.790;
Dwulet F.E., Putnam F.W.;
"Complete amino acid sequence of a 50,000-dalton fragment of human
ceruloplasmin.";
Proc. Natl. Acad. Sci. U.S.A. 78:790-794(1981).
[10]
PROTEIN SEQUENCE OF 907-1065.
PubMed=6987229;
Kingston I.B., Kingston B.L., Putnam F.W.;
"Primary structure of a histidine-rich proteolytic fragment of human
ceruloplasmin. I. Amino acid sequence of the cyanogen bromide
peptides.";
J. Biol. Chem. 255:2878-2885(1980).
[11]
PROTEIN SEQUENCE OF 907-1065.
PubMed=6987230;
Kingston I.B., Kingston B.L., Putnam F.W.;
"Primary structure of a histidine-rich proteolytic fragment of human
ceruloplasmin. II. Amino acid sequence of the tryptic peptides.";
J. Biol. Chem. 255:2886-2896(1980).
[12]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1007-1061.
PubMed=2355023;
Yang F.M., Friedrichs W.E., Cupples R.L., Banifacio M.J.,
Sanford J.A., Horton W.A., Bowman B.H.;
"Human ceruloplasmin. Tissue-specific expression of transcripts
produced by alternative splicing.";
J. Biol. Chem. 265:10780-10785(1990).
[13]
REVIEW.
PubMed=12055353; DOI=10.1146/annurev.nutr.22.012502.114457;
Hellman N.E., Gitlin J.D.;
"Ceruloplasmin metabolism and function.";
Annu. Rev. Nutr. 22:439-458(2002).
[14]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-138.
TISSUE=Bile;
PubMed=15084671; DOI=10.1074/mcp.M400015-MCP200;
Kristiansen T.Z., Bunkenborg J., Gronborg M., Molina H.,
Thuluvath P.J., Argani P., Goggins M.G., Maitra A., Pandey A.;
"A proteomic analysis of human bile.";
Mol. Cell. Proteomics 3:715-728(2004).
[15]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-138; ASN-397 AND ASN-762.
TISSUE=Plasma;
PubMed=14760718; DOI=10.1002/pmic.200300556;
Bunkenborg J., Pilch B.J., Podtelejnikov A.V., Wisniewski J.R.;
"Screening for N-glycosylated proteins by liquid chromatography mass
spectrometry.";
Proteomics 4:454-465(2004).
[16]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-138; ASN-358; ASN-397;
ASN-588; ASN-762 AND ASN-926.
TISSUE=Plasma;
PubMed=16335952; DOI=10.1021/pr0502065;
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,
Moore R.J., Smith R.D.;
"Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
hydrazide chemistry, and mass spectrometry.";
J. Proteome Res. 4:2070-2080(2005).
[17]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-138; ASN-358; ASN-397 AND
ASN-762.
TISSUE=Liver;
PubMed=19159218; DOI=10.1021/pr8008012;
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. 8:651-661(2009).
[18]
GLYCOSYLATION AT ASN-138; ASN-358; ASN-397 AND ASN-762.
PubMed=19139490; DOI=10.1074/mcp.M800504-MCP200;
Jia W., Lu Z., Fu Y., Wang H.P., Wang L.H., Chi H., Yuan Z.F.,
Zheng Z.B., Song L.N., Han H.H., Liang Y.M., Wang J.L., Cai Y.,
Zhang Y.K., Deng Y.L., Ying W.T., He S.M., Qian X.H.;
"A strategy for precise and large scale identification of core
fucosylated glycoproteins.";
Mol. Cell. Proteomics 8:913-923(2009).
[19]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-138; ASN-358 AND ASN-397,
AND STRUCTURE OF CARBOHYDRATES.
TISSUE=Cerebrospinal fluid;
PubMed=19838169; DOI=10.1038/nmeth.1392;
Nilsson J., Rueetschi U., Halim A., Hesse C., Carlsohn E.,
Brinkmalm G., Larson G.;
"Enrichment of glycopeptides for glycan structure and attachment site
identification.";
Nat. Methods 6:809-811(2009).
[20]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
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 96:253-262(2014).
[21]
PHOSPHORYLATION AT SER-722.
PubMed=26091039; DOI=10.1016/j.cell.2015.05.028;
Tagliabracci V.S., Wiley S.E., Guo X., Kinch L.N., Durrant E., Wen J.,
Xiao J., Cui J., Nguyen K.B., Engel J.L., Coon J.J., Grishin N.,
Pinna L.A., Pagliarini D.J., Dixon J.E.;
"A single kinase generates the majority of the secreted
phosphoproteome.";
Cell 161:1619-1632(2015).
[22]
X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS), DISULFIDE BONDS, AND
METAL-BINDING SITES.
Zaitseva I., Zaitsev V., Card G., Moshkov K., Bax B., Ralph A.,
Lindley P.;
"The X-ray structure of human serum ceruloplasmin at 3.1 A: nature of
the copper centres.";
J. Biol. Inorg. Chem. 1:15-23(1996).
[23]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS), METAL-BINDING SITES, AND
DISULFIDE BONDS.
PubMed=17242517; DOI=10.1107/S090744490604947X;
Bento I., Peixoto C., Zaitsev V.N., Lindley P.F.;
"Ceruloplasmin revisited: structural and functional roles of various
metal cation-binding sites.";
Acta Crystallogr. D 63:240-248(2007).
[24]
VARIANTS THR-63; LEU-477; GLU-544; ILE-551; HIS-793 AND ARG-841.
PubMed=15557511; DOI=10.1212/01.WNL.0000144276.29988.C3;
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 63:1912-1917(2004).
[25]
CHARACTERIZATION OF VARIANTS THR-63; GLU-544 AND HIS-793.
PubMed=16150804; DOI=10.1096/fj.04-3486fje;
Hochstrasser H., Tomiuk J., Walter U., Behnke S., Spiegel J.,
Krueger R., Becker G., Riess O., Berg D.;
"Functional relevance of ceruloplasmin mutations in Parkinson's
disease.";
FASEB J. 19:1851-1853(2005).
-!- 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).
{ECO:0000250}.
-!- CATALYTIC ACTIVITY:
Reaction=4 Fe(2+) + 4 H(+) + O2 = 4 Fe(3+) + 2 H2O;
Xref=Rhea:RHEA:11148, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
ChEBI:CHEBI:15379, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034;
EC=1.16.3.1;
-!- COFACTOR:
Name=Cu cation; Xref=ChEBI:CHEBI:23378;
Note=Binds 6 Cu cations per monomer.;
-!- SUBCELLULAR LOCATION: Secreted. Note=Colocalizes with GCP1 in
secretory intracellular compartments. {ECO:0000250}.
-!- TISSUE SPECIFICITY: Expressed by the liver and secreted in plasma.
-!- DISEASE: Aceruloplasminemia (ACERULOP) [MIM:604290]: An autosomal
recessive disorder of iron metabolism characterized by iron
accumulation in the brain as well as visceral organs. Clinical
features consist of the triad of retinal degeneration, diabetes
mellitus and neurological disturbances. Note=The disease is caused
by mutations affecting the gene represented in this entry.
-!- DISEASE: Note=Ceruloplasmin levels are decreased in Wilson
disease, in which copper cannot be incorporated into ceruloplasmin
in liver because of defects in the copper-transporting ATPase 2.
-!- SIMILARITY: Belongs to the multicopper oxidase family.
{ECO:0000305}.
-!- WEB RESOURCE: Name=Wikipedia; Note=Ceruloplasmin entry;
URL="https://en.wikipedia.org/wiki/Ceruloplasmin";
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; M13699; AAA51976.1; -; mRNA.
EMBL; DQ314867; ABC40726.1; -; Genomic_DNA.
EMBL; D45045; BAA08085.1; -; Genomic_DNA.
EMBL; D00025; BAA00019.1; -; mRNA.
EMBL; X04135; CAA27752.1; -; mRNA.
EMBL; X04136; CAA27753.1; -; mRNA.
EMBL; X04137; CAA27754.1; -; mRNA.
EMBL; X04138; CAA27755.1; -; mRNA.
EMBL; AF132978; AAF02483.1; -; Genomic_DNA.
EMBL; M13536; AAA51975.1; -; mRNA.
EMBL; J05506; -; NOT_ANNOTATED_CDS; Genomic_DNA.
CCDS; CCDS3141.1; -.
PIR; A25443; KUHU.
RefSeq; NP_000087.1; NM_000096.3.
UniGene; Hs.558314; -.
PDB; 1KCW; X-ray; 3.00 A; A=20-1065.
PDB; 2J5W; X-ray; 2.80 A; A=1-1065.
PDB; 4EJX; X-ray; 4.69 A; A=1-1065.
PDB; 4ENZ; X-ray; 2.60 A; A=1-1065.
PDBsum; 1KCW; -.
PDBsum; 2J5W; -.
PDBsum; 4EJX; -.
PDBsum; 4ENZ; -.
ProteinModelPortal; P00450; -.
SMR; P00450; -.
BioGrid; 107748; 10.
CORUM; P00450; -.
IntAct; P00450; 5.
STRING; 9606.ENSP00000264613; -.
DrugBank; DB00055; Drotrecogin alfa.
TCDB; 8.A.105.1.2; the multi-copper-containing ferrooxidase (mcfo) family.
CarbonylDB; P00450; -.
GlyConnect; 85; -.
iPTMnet; P00450; -.
PhosphoSitePlus; P00450; -.
UniCarbKB; P00450; -.
BioMuta; CP; -.
DMDM; 116117; -.
DOSAC-COBS-2DPAGE; P00450; -.
SWISS-2DPAGE; P00450; -.
EPD; P00450; -.
MaxQB; P00450; -.
PaxDb; P00450; -.
PeptideAtlas; P00450; -.
PRIDE; P00450; -.
ProteomicsDB; 51251; -.
Ensembl; ENST00000264613; ENSP00000264613; ENSG00000047457.
GeneID; 1356; -.
KEGG; hsa:1356; -.
UCSC; uc003ewy.6; human.
CTD; 1356; -.
DisGeNET; 1356; -.
EuPathDB; HostDB:ENSG00000047457.13; -.
GeneCards; CP; -.
GeneReviews; CP; -.
HGNC; HGNC:2295; CP.
HPA; CAB008591; -.
HPA; HPA001834; -.
MalaCards; CP; -.
MIM; 117700; gene.
MIM; 604290; phenotype.
neXtProt; NX_P00450; -.
Orphanet; 48818; Aceruloplasminemia.
PharmGKB; PA26815; -.
eggNOG; KOG1263; Eukaryota.
eggNOG; COG2132; LUCA.
HOGENOM; HOG000231499; -.
HOVERGEN; HBG003674; -.
InParanoid; P00450; -.
KO; K13624; -.
OrthoDB; EOG091G00QL; -.
PhylomeDB; P00450; -.
TreeFam; TF329807; -.
BioCyc; MetaCyc:HS00590-MONOMER; -.
BRENDA; 1.16.3.1; 2681.
Reactome; R-HSA-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
Reactome; R-HSA-425410; Metal ion SLC transporters.
Reactome; R-HSA-5619060; Defective CP causes aceruloplasminemia (ACERULOP).
Reactome; R-HSA-8957275; Post-translational protein phosphorylation.
Reactome; R-HSA-917937; Iron uptake and transport.
SABIO-RK; P00450; -.
SIGNOR; P00450; -.
ChiTaRS; CP; human.
EvolutionaryTrace; P00450; -.
GeneWiki; Ceruloplasmin; -.
GenomeRNAi; 1356; -.
PMAP-CutDB; P00450; -.
PRO; PR:P00450; -.
Proteomes; UP000005640; Chromosome 3.
Bgee; ENSG00000047457; Expressed in 185 organ(s), highest expression level in liver.
CleanEx; HS_CP; -.
ExpressionAtlas; P00450; baseline and differential.
Genevisible; P00450; HS.
GO; GO:0072562; C:blood microparticle; HDA:UniProtKB.
GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005615; C:extracellular space; IDA:BHF-UCL.
GO; GO:0005765; C:lysosomal membrane; HDA:UniProtKB.
GO; GO:0051087; F:chaperone binding; IPI:BHF-UCL.
GO; GO:0005507; F:copper ion binding; IEA:InterPro.
GO; GO:0004322; F:ferroxidase activity; TAS:Reactome.
GO; GO:0016722; F:oxidoreductase activity, oxidizing metal ions; IBA:GO_Central.
GO; GO:0006879; P:cellular iron ion homeostasis; TAS:Reactome.
GO; GO:0044267; P:cellular protein metabolic process; TAS:Reactome.
GO; GO:0006825; P:copper ion transport; IEA:UniProtKB-KW.
GO; GO:0043687; P:post-translational protein modification; TAS:Reactome.
Gene3D; 2.60.40.420; -; 6.
InterPro; IPR027150; CP.
InterPro; IPR001117; Cu-oxidase.
InterPro; IPR011706; Cu-oxidase_2.
InterPro; IPR011707; Cu-oxidase_3.
InterPro; IPR033138; Cu_oxidase_CS.
InterPro; IPR002355; Cu_oxidase_Cu_BS.
InterPro; IPR008972; Cupredoxin.
PANTHER; PTHR44048:SF5; PTHR44048:SF5; 1.
Pfam; PF00394; Cu-oxidase; 1.
Pfam; PF07731; Cu-oxidase_2; 1.
Pfam; PF07732; Cu-oxidase_3; 2.
SUPFAM; SSF49503; SSF49503; 6.
PROSITE; PS00079; MULTICOPPER_OXIDASE1; 3.
PROSITE; PS00080; MULTICOPPER_OXIDASE2; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Copper; Copper transport;
Direct protein sequencing; Disulfide bond; Glycoprotein;
Ion transport; Metal-binding; Oxidoreductase; Phosphoprotein;
Polymorphism; Reference proteome; Repeat; Secreted; Signal; Transport.
SIGNAL 1 19 {ECO:0000269|PubMed:6582496}.
CHAIN 20 1065 Ceruloplasmin.
/FTId=PRO_0000002912.
DOMAIN 20 357 F5/8 type A 1.
DOMAIN 20 200 Plastocyanin-like 1.
DOMAIN 209 357 Plastocyanin-like 2.
DOMAIN 370 718 F5/8 type A 2.
DOMAIN 370 560 Plastocyanin-like 3.
DOMAIN 570 718 Plastocyanin-like 4.
DOMAIN 730 1061 F5/8 type A 3.
DOMAIN 730 900 Plastocyanin-like 5.
DOMAIN 908 1061 Plastocyanin-like 6.
METAL 120 120 Copper 1; type 2.
METAL 122 122 Copper 2; type 3.
METAL 180 180 Copper 2; type 3.
METAL 182 182 Copper 3; type 3.
METAL 295 295 Copper 4; type 1.
METAL 338 338 Copper 4; type 1.
METAL 343 343 Copper 4; type 1.
METAL 656 656 Copper 5; type 1.
METAL 699 699 Copper 5; type 1.
METAL 704 704 Copper 5; type 1.
METAL 709 709 Copper 5; type 1.
METAL 994 994 Copper 6; type 1.
METAL 997 997 Copper 1; type 2.
METAL 999 999 Copper 3; type 3.
METAL 1039 1039 Copper 3; type 3.
METAL 1040 1040 Copper 6; type 1.
METAL 1041 1041 Copper 2; type 3.
METAL 1045 1045 Copper 6; type 1.
METAL 1050 1050 Copper 6; type 1.
MOD_RES 722 722 Phosphoserine; by FAM20C.
{ECO:0000269|PubMed:26091039}.
CARBOHYD 138 138 N-linked (GlcNAc...) (complex)
asparagine. {ECO:0000269|PubMed:14760718,
ECO:0000269|PubMed:15084671,
ECO:0000269|PubMed:16335952,
ECO:0000269|PubMed:19139490,
ECO:0000269|PubMed:19159218,
ECO:0000269|PubMed:19838169}.
CARBOHYD 358 358 N-linked (GlcNAc...) (complex)
asparagine. {ECO:0000269|PubMed:16335952,
ECO:0000269|PubMed:19139490,
ECO:0000269|PubMed:19159218,
ECO:0000269|PubMed:19838169}.
CARBOHYD 397 397 N-linked (GlcNAc...) (complex)
asparagine. {ECO:0000269|PubMed:14760718,
ECO:0000269|PubMed:16335952,
ECO:0000269|PubMed:19139490,
ECO:0000269|PubMed:19159218,
ECO:0000269|PubMed:19838169}.
CARBOHYD 588 588 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:16335952}.
CARBOHYD 762 762 N-linked (GlcNAc...) (complex)
asparagine. {ECO:0000269|PubMed:14760718,
ECO:0000269|PubMed:16335952,
ECO:0000269|PubMed:19139490,
ECO:0000269|PubMed:19159218}.
CARBOHYD 926 926 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:16335952}.
DISULFID 174 200 {ECO:0000305}.
DISULFID 276 357 {ECO:0000305}.
DISULFID 534 560 {ECO:0000305}.
DISULFID 637 718 {ECO:0000305}.
DISULFID 874 900 {ECO:0000305}.
VARIANT 63 63 I -> T (retained in the ER due to
impaired N-glycosylation; may present a
vulnerability factor for iron induced
oxidative stress in Parkinson disease).
{ECO:0000269|PubMed:15557511,
ECO:0000269|PubMed:16150804}.
/FTId=VAR_025655.
VARIANT 367 367 R -> C (in dbSNP:rs34624984).
/FTId=VAR_032815.
VARIANT 477 477 P -> L (in dbSNP:rs35331711).
{ECO:0000269|PubMed:15557511}.
/FTId=VAR_025656.
VARIANT 544 544 D -> E (reduced ferroxidase activity; may
present a vulnerability factor for iron
induced oxidative stress in Parkinson
disease; dbSNP:rs701753).
{ECO:0000269|PubMed:15557511,
ECO:0000269|PubMed:16150804}.
/FTId=VAR_025657.
VARIANT 551 551 T -> I. {ECO:0000269|PubMed:15557511}.
/FTId=VAR_025658.
VARIANT 793 793 R -> H. {ECO:0000269|PubMed:15557511,
ECO:0000269|PubMed:16150804}.
/FTId=VAR_025659.
VARIANT 841 841 T -> R (in dbSNP:rs56033670).
{ECO:0000269|PubMed:15557511}.
/FTId=VAR_025660.
CONFLICT 1060 1060 E -> EGEYP (in Ref. 6; AAA51975).
{ECO:0000305}.
STRAND 21 36 {ECO:0000244|PDB:4ENZ}.
TURN 49 52 {ECO:0000244|PDB:4ENZ}.
HELIX 53 56 {ECO:0000244|PDB:4ENZ}.
STRAND 58 61 {ECO:0000244|PDB:1KCW}.
STRAND 65 79 {ECO:0000244|PDB:4ENZ}.
STRAND 82 84 {ECO:0000244|PDB:1KCW}.
HELIX 88 90 {ECO:0000244|PDB:4ENZ}.
STRAND 97 100 {ECO:0000244|PDB:4ENZ}.
STRAND 104 111 {ECO:0000244|PDB:4ENZ}.
STRAND 113 115 {ECO:0000244|PDB:4ENZ}.
STRAND 120 125 {ECO:0000244|PDB:4ENZ}.
HELIX 128 130 {ECO:0000244|PDB:4ENZ}.
HELIX 141 144 {ECO:0000244|PDB:4ENZ}.
HELIX 145 147 {ECO:0000244|PDB:4ENZ}.
STRAND 154 160 {ECO:0000244|PDB:4ENZ}.
STRAND 173 180 {ECO:0000244|PDB:4ENZ}.
HELIX 185 190 {ECO:0000244|PDB:4ENZ}.
STRAND 194 200 {ECO:0000244|PDB:4ENZ}.
STRAND 205 210 {ECO:0000244|PDB:2J5W}.
STRAND 214 225 {ECO:0000244|PDB:4ENZ}.
HELIX 226 228 {ECO:0000244|PDB:4ENZ}.
HELIX 232 239 {ECO:0000244|PDB:4ENZ}.
HELIX 243 245 {ECO:0000244|PDB:4ENZ}.
HELIX 251 257 {ECO:0000244|PDB:4ENZ}.
STRAND 258 262 {ECO:0000244|PDB:4ENZ}.
STRAND 274 276 {ECO:0000244|PDB:4ENZ}.
STRAND 280 287 {ECO:0000244|PDB:4ENZ}.
STRAND 295 301 {ECO:0000244|PDB:4ENZ}.
STRAND 304 306 {ECO:0000244|PDB:4ENZ}.
STRAND 309 312 {ECO:0000244|PDB:4ENZ}.
STRAND 321 327 {ECO:0000244|PDB:4ENZ}.
STRAND 332 338 {ECO:0000244|PDB:4ENZ}.
HELIX 341 344 {ECO:0000244|PDB:4ENZ}.
TURN 345 347 {ECO:0000244|PDB:4ENZ}.
STRAND 349 355 {ECO:0000244|PDB:4ENZ}.
STRAND 367 385 {ECO:0000244|PDB:4ENZ}.
TURN 392 394 {ECO:0000244|PDB:4ENZ}.
STRAND 401 403 {ECO:0000244|PDB:1KCW}.
HELIX 406 409 {ECO:0000244|PDB:4ENZ}.
STRAND 412 414 {ECO:0000244|PDB:1KCW}.
STRAND 418 427 {ECO:0000244|PDB:4ENZ}.
STRAND 429 435 {ECO:0000244|PDB:4ENZ}.
HELIX 444 446 {ECO:0000244|PDB:4ENZ}.
STRAND 453 456 {ECO:0000244|PDB:4ENZ}.
STRAND 459 471 {ECO:0000244|PDB:4ENZ}.
STRAND 476 481 {ECO:0000244|PDB:4ENZ}.
HELIX 484 486 {ECO:0000244|PDB:4ENZ}.
STRAND 514 520 {ECO:0000244|PDB:4ENZ}.
TURN 523 525 {ECO:0000244|PDB:4ENZ}.
STRAND 529 531 {ECO:0000244|PDB:2J5W}.
STRAND 533 540 {ECO:0000244|PDB:4ENZ}.
STRAND 542 544 {ECO:0000244|PDB:2J5W}.
HELIX 545 551 {ECO:0000244|PDB:4ENZ}.
STRAND 554 560 {ECO:0000244|PDB:4ENZ}.
STRAND 575 580 {ECO:0000244|PDB:4ENZ}.
STRAND 582 586 {ECO:0000244|PDB:4ENZ}.
HELIX 587 589 {ECO:0000244|PDB:4ENZ}.
HELIX 593 600 {ECO:0000244|PDB:4ENZ}.
HELIX 604 606 {ECO:0000244|PDB:4ENZ}.
HELIX 612 617 {ECO:0000244|PDB:4ENZ}.
STRAND 619 623 {ECO:0000244|PDB:4ENZ}.
STRAND 635 637 {ECO:0000244|PDB:4ENZ}.
STRAND 642 647 {ECO:0000244|PDB:4ENZ}.
STRAND 656 660 {ECO:0000244|PDB:4ENZ}.
STRAND 665 667 {ECO:0000244|PDB:4ENZ}.
STRAND 670 677 {ECO:0000244|PDB:4ENZ}.
STRAND 682 687 {ECO:0000244|PDB:4ENZ}.
STRAND 693 699 {ECO:0000244|PDB:4ENZ}.
HELIX 702 706 {ECO:0000244|PDB:4ENZ}.
STRAND 710 716 {ECO:0000244|PDB:4ENZ}.
STRAND 729 745 {ECO:0000244|PDB:4ENZ}.
HELIX 750 759 {ECO:0000244|PDB:4ENZ}.
TURN 766 768 {ECO:0000244|PDB:4ENZ}.
TURN 771 773 {ECO:0000244|PDB:4ENZ}.
STRAND 777 789 {ECO:0000244|PDB:4ENZ}.
HELIX 800 805 {ECO:0000244|PDB:4ENZ}.
STRAND 812 815 {ECO:0000244|PDB:4ENZ}.
STRAND 818 826 {ECO:0000244|PDB:4ENZ}.
STRAND 828 830 {ECO:0000244|PDB:4ENZ}.
STRAND 835 838 {ECO:0000244|PDB:4ENZ}.
STRAND 842 844 {ECO:0000244|PDB:1KCW}.
STRAND 854 860 {ECO:0000244|PDB:4ENZ}.
HELIX 863 865 {ECO:0000244|PDB:4ENZ}.
STRAND 869 871 {ECO:0000244|PDB:1KCW}.
STRAND 873 880 {ECO:0000244|PDB:4ENZ}.
HELIX 885 890 {ECO:0000244|PDB:4ENZ}.
STRAND 894 900 {ECO:0000244|PDB:4ENZ}.
STRAND 913 924 {ECO:0000244|PDB:4ENZ}.
HELIX 925 927 {ECO:0000244|PDB:4ENZ}.
HELIX 931 938 {ECO:0000244|PDB:4ENZ}.
HELIX 942 944 {ECO:0000244|PDB:4ENZ}.
HELIX 950 955 {ECO:0000244|PDB:4ENZ}.
STRAND 957 961 {ECO:0000244|PDB:4ENZ}.
STRAND 973 975 {ECO:0000244|PDB:4ENZ}.
STRAND 979 986 {ECO:0000244|PDB:4ENZ}.
STRAND 994 998 {ECO:0000244|PDB:4ENZ}.
STRAND 1003 1006 {ECO:0000244|PDB:4ENZ}.
HELIX 1007 1009 {ECO:0000244|PDB:4ENZ}.
STRAND 1011 1018 {ECO:0000244|PDB:4ENZ}.
STRAND 1023 1028 {ECO:0000244|PDB:4ENZ}.
STRAND 1034 1040 {ECO:0000244|PDB:4ENZ}.
HELIX 1043 1047 {ECO:0000244|PDB:4ENZ}.
STRAND 1051 1057 {ECO:0000244|PDB:4ENZ}.
SEQUENCE 1065 AA; 122205 MW; 2F2F1294E2D30F58 CRC64;
MKILILGIFL FLCSTPAWAK EKHYYIGIIE TTWDYASDHG EKKLISVDTE HSNIYLQNGP
DRIGRLYKKA LYLQYTDETF RTTIEKPVWL GFLGPIIKAE TGDKVYVHLK NLASRPYTFH
SHGITYYKEH EGAIYPDNTT DFQRADDKVY PGEQYTYMLL ATEEQSPGEG DGNCVTRIYH
SHIDAPKDIA SGLIGPLIIC KKDSLDKEKE KHIDREFVVM FSVVDENFSW YLEDNIKTYC
SEPEKVDKDN EDFQESNRMY SVNGYTFGSL PGLSMCAEDR VKWYLFGMGN EVDVHAAFFH
GQALTNKNYR IDTINLFPAT LFDAYMVAQN PGEWMLSCQN LNHLKAGLQA FFQVQECNKS
SSKDNIRGKH VRHYYIAAEE IIWNYAPSGI DIFTKENLTA PGSDSAVFFE QGTTRIGGSY
KKLVYREYTD ASFTNRKERG PEEEHLGILG PVIWAEVGDT IRVTFHNKGA YPLSIEPIGV
RFNKNNEGTY YSPNYNPQSR SVPPSASHVA PTETFTYEWT VPKEVGPTNA DPVCLAKMYY
SAVDPTKDIF TGLIGPMKIC KKGSLHANGR QKDVDKEFYL FPTVFDENES LLLEDNIRMF
TTAPDQVDKE DEDFQESNKM HSMNGFMYGN QPGLTMCKGD SVVWYLFSAG NEADVHGIYF
SGNTYLWRGE RRDTANLFPQ TSLTLHMWPD TEGTFNVECL TTDHYTGGMK QKYTVNQCRR
QSEDSTFYLG ERTYYIAAVE VEWDYSPQRE WEKELHHLQE QNVSNAFLDK GEFYIGSKYK
KVVYRQYTDS TFRVPVERKA EEEHLGILGP QLHADVGDKV KIIFKNMATR PYSIHAHGVQ
TESSTVTPTL PGETLTYVWK IPERSGAGTE DSACIPWAYY STVDQVKDLY SGLIGPLIVC
RRPYLKVFNP RRKLEFALLF LVFDENESWY LDDNIKTYSD HPEKVNKDDE EFIESNKMHA
INGRMFGNLQ GLTMHVGDEV NWYLMGMGNE IDLHTVHFHG HSFQYKHRGV YSSDVFDIFP
GTYQTLEMFP RTPGIWLLHC HVTDHIHAGM ETTYTVLQNE DTKSG


Related products :

Catalog number Product name Quantity
678 CERULOPLASMIN (FERROXIDASE), SERUM 1
40-374-130011 Rat Ceruloplasmin - EC. Ferroxidase. CP-2 ELISA_Kits
18-272-196724 Ceruloplasmin - Goat polyclonal to Ceruloplasmin; EC 1.16.3.1; Ferroxidase Polyclonal 1 mg
15-288-20074F Ceruloplasmin - EC 1.16.3.1; Ferroxidase Polyclonal 0.1 mg
CP20 CP Gene ceruloplasmin (ferroxidase)
E1381514 Ceruloplasmin (Ferroxidase) (CP) ELISA Kit 1
15-288-20074F Ceruloplasmin - EC 1.16.3.1; Ferroxidase Polyclonal 0.05 mg
40-288-20074F Human Ceruloplasmin - EC. Ferroxidase. CP-2 ELISA_Kits
CSB-E17811r Rat ceruloplasmin (ferroxidase) (CP)ELISA kit SpeciesRat 96T
U0909r CLIA Ceruloplasmin,Cp,Ferroxidase,Rat,Rattus norvegicus 96T
E0909r ELISA Ceruloplasmin,Cp,Ferroxidase,Rat,Rattus norvegicus 96T
E0909r ELISA kit Ceruloplasmin,Cp,Ferroxidase,Rat,Rattus norvegicus 96T
E0909m ELISA kit Ceruloplasmin,Cp,Ferroxidase,Mouse,Mus musculus 96T
U0909m CLIA Ceruloplasmin,Cp,Ferroxidase,Mouse,Mus musculus 96T
E0909m ELISA Ceruloplasmin,Cp,Ferroxidase,Mouse,Mus musculus 96T
U0909h CLIA Ceruloplasmin,CP,Ferroxidase,Homo sapiens,Human 96T
E0909h ELISA Ceruloplasmin,CP,Ferroxidase,Homo sapiens,Human 96T
E0909h ELISA kit Ceruloplasmin,CP,Ferroxidase,Homo sapiens,Human 96T
CSB-EL005874RA Rat ceruloplasmin (ferroxidase) (CP)ELISA kit, Species Rat, Sample Type serum, plasma 96T
CSB-EL005911HU Human ceruloplasmin (ferroxidase) pseudogene (CPP) ELISA kit, Species Human, Sample Type serum, plasma 96T
orb82123 Human Plasma Ceruloplasmin protein Ceruloplasmin is a purified protein_bioactive peptide. For research use only. 1 mg
orb21969 Goat Serum Against Human Ceruloplasmin Polyclonal Precipitating polyclonal goat antiserum to human alpha-2 ceruloplasmin. Alpha-2 ceruloplasmin is copper containing alpha-2 glycoprotein with a molecul 1 ml
LF-MA0159 anti-Ceruloplasmin (3B11), Mouse monoclonal to Ceruloplasmin, Isotype IgG1, Host Mouse 100 ul
AS06120 Multicopper Ferroxidase (394_646) 0.2 ml
gen13150 CERU_HUMAN Ferroxidase ELISA tesk kit 1


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur | Gentaur





GENTAUR Ltd.
Unicorn House, Station Cl
Hertfordshire, Potters Bar EN6 1TL
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017
RIB 30004 00187 00010092253 10
BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG
IBAN FR76 3000 4001 8700 0100 9225 310
france@gentaur.com | Gentaur | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: +49 0241 40 08 90 86, +49 0241 95 78 94 78, +49 0241 40 08 90 86
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur | Gentaur