[1]	NUCLEOTIDE SEQUENCE [MRNA]. DOI=10.1073/pnas.83.14.5086; PubMed=2873574 [NCBI, ExPASy, EBI, Israel, Japan] 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. DOI=10.1006/bbrc.1995.1437; PubMed=7702601 [NCBI, ExPASy, EBI, Israel, Japan] 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. DOI=10.1016/0014-5793(86)80739-6; PubMed=3755405 [NCBI, ExPASy, EBI, Israel, Japan] 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. DOI=10.1073/pnas.83.10.3257; PubMed=3486416 [NCBI, ExPASy, EBI, Israel, Japan] 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. DOI=10.1073/pnas.81.2.390; PubMed=6582496 [NCBI, ExPASy, EBI, Israel, Japan] 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. DOI=10.1073/pnas.80.1.115; PubMed=6571985 [NCBI, ExPASy, EBI, Israel, Japan] 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. DOI=10.1073/pnas.78.2.790; PubMed=6940148 [NCBI, ExPASy, EBI, Israel, Japan] 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 [NCBI, ExPASy, EBI, Israel, Japan] 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 [NCBI, ExPASy, EBI, Israel, Japan] 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 [NCBI, ExPASy, EBI, Israel, Japan] 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. DOI=10.1146/annurev.nutr.22.012502.114457; PubMed=12055353 [NCBI, ExPASy, EBI, Israel, Japan] 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, AND MASS SPECTROMETRY. TISSUE=Bile; DOI=10.1074/mcp.M400015-MCP200; PubMed=15084671 [NCBI, ExPASy, EBI, Israel, Japan] 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, AND MASS SPECTROMETRY. TISSUE=Plasma; DOI=10.1002/pmic.200300556; PubMed=14760718 [NCBI, ExPASy, EBI, Israel, Japan] 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, AND MASS SPECTROMETRY. TISSUE=Plasma; DOI=10.1021/pr0502065; PubMed=16335952 [NCBI, ExPASy, EBI, Israel, Japan] 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]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-784 AND TYR-787, AND MASS SPECTROMETRY. DOI=10.1016/j.cell.2007.11.025; PubMed=18083107 [NCBI, ExPASy, EBI, Israel, Japan] 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 J.M., Yuan J., Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X., Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.; "Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer."; Cell 131:1190-1203(2007).
[18]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-204, AND MASS SPECTROMETRY. DOI=10.2116/analsci.24.161; PubMed=18187866 [NCBI, ExPASy, EBI, Israel, Japan] 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. 24:161-166(2008).
[19]	GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-138; ASN-358; ASN-397 AND ASN-762, AND MASS SPECTROMETRY. TISSUE=Liver; DOI=10.1021/pr8008012; PubMed=19159218 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[20]	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).
[21]	X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS), METAL-BINDING SITES, AND DISULFIDE BONDS. DOI=10.1107/S090744490604947X; PubMed=17242517 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[22]	VARIANTS THR-63; LEU-477; GLU-544; ILE-551; HIS-793 AND ARG-841. PubMed=15557511 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[23]	CHARACTERIZATION OF VARIANTS THR-63; GLU-544 AND HIS-793. DOI=10.1096/fj.04-3486fje; PubMed=16150804 [NCBI, ExPASy, EBI, Israel, Japan] 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).

Comments

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.
CATALYTIC ACTIVITY: 4 Fe²⁺ + 4 H⁺ + O₂ = 4 Fe³⁺ + 2 H₂O.
COFACTOR: Binds 6 copper ions per monomer.
SUBCELLULAR LOCATION: Secreted.
TISSUE SPECIFICITY: Expressed by the liver and secreted in plasma.
DISEASE: Defects in CP are the cause of aceruloplasminemia (ACERULOP) [MIM:604290]. It is 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.
DISEASE: 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.
SIMILARITY: Contains 3 F5/8 type A domains.
SIMILARITY: Contains 6 plastocyanin-like domains.
WEB RESOURCE: Name=GeneReviews; URL="http://www.genetests.org/query?gene=CP";.
WEB RESOURCE: Name=Wikipedia; Note=Ceruloplasmin entry; URL="http://en.wikipedia.org/wiki/Ceruloplasmin";.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

M13699; AAA51976.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
DQ314867; ABC40726.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
D45045; BAA08085.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
D00025; BAA00019.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X04135; CAA27752.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X04136; CAA27753.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X04137; CAA27754.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X04138; CAA27755.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF132978; AAF02483.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M13536; AAA51975.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
J05506; -; NOT_ANNOTATED_CDS; Genomic_DNA.	[EMBL / GenBank / DDBJ]

IPI00017601; -.

A25443; KUHU.

NP_000087.1; -.

3D structure databases

PDB

1KCW; X-ray; 3.00 A; A=20-1065.	[ExPASy / RCSB / EBI]
2J5W; X-ray; 2.80 A; A=1-1065.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

1KCW; -.
2J5W; -.

PTM databases

P00450; -.

P00450; -.

Enzyme and pathway databases

BRENDA

1.16.3.1; 247.

Pathway_Interaction_DB

hif1_tfpathway; HIF-1-alpha transcription factor network.

2D gel databases

SWISS-2DPAGE

P00450; -.

DOSAC-COBS-2DPAGE

P00450; -.

Siena-2DPAGE

P00450; -.

Organism-specific databases

GC03M150374; -.

HIX0003762; -.

HGNC:2295; CP.

CP.

CAB008591; -.
HPA001834; -.

MIM

117700; gene. [NCBI / EBI]
604290; phenotype. [NCBI / EBI]

Orphanet

48818; Aceruloplasminemia.

PharmGKB

PA24362; -.

Gene expression databases

P00450; -.

P00450; -.

HS_CP; -.

ENSG00000047457; Homo sapiens.

Ontologies

GO:0005615;	Cellular component: extracellular space (traceable author statement from ProtInc).
GO:0005507;	Molecular function: copper ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0004322;	Molecular function: ferroxidase activity (traceable author statement from ProtInc).
GO:0006879;	Biological process: cellular iron ion homeostasis (traceable author statement from ProtInc).
GO:0006825;	Biological process: copper ion transport (inferred from electronic annotation from UniProtKB-KW).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR001117; Cu-oxidase.
IPR011706; Cu-oxidase_2.
IPR011707; Cu-oxidase_3.
IPR002355; Cu_oxidase_Cu_BS.
IPR008972; Cupredoxin.
Graphical view of domain structure.

Gene3D

G3DSA:2.60.40.420; Cupredoxin; 6.

Pfam

PF00394; Cu-oxidase; 1.
PF07731; Cu-oxidase_2; 1.
PF07732; Cu-oxidase_3; 3.
Pfam graphical view of domain structure.

PROSITE

PS00079; MULTICOPPER_OXIDASE1; 3.
PS00080; MULTICOPPER_OXIDASE2; 1.

Proteomic databases

PeptideAtlas

P00450; -.

PRIDE

P00450; -.

Genome annotation databases

Ensembl

ENSG00000047457; Homo sapiens. [Contig view]

GeneID

1356; -.

KEGG

hsa:1356; -.

Phylogenomic databases

HOGENOM

P00450; -.

HOVERGEN

P00450; -.

Other

DrugBank

DB00055; Drotrecogin alfa.

5493; -.

P00450; -.

CP; Homo sapiens.

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Copper; Copper transport; Direct protein sequencing; Disulfide bond; Glycoprotein; Ion transport; Metal-binding; Oxidoreductase; Phosphoprotein; Polymorphism; Repeat; Secreted; Signal; Transport.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 19`	`19`
`CHAIN`	`20 1065`	`1046`	`Ceruloplasmin.`	`PRO_0000002912`
`DOMAIN`	`20 357`	`338`	`F5/8 type A 1.`
`DOMAIN`	`20 200`	`181`	`Plastocyanin-like 1.`
`DOMAIN`	`209 357`	`149`	`Plastocyanin-like 2.`
`DOMAIN`	`370 718`	`349`	`F5/8 type A 2.`
`DOMAIN`	`370 560`	`191`	`Plastocyanin-like 3.`
`DOMAIN`	`570 718`	`149`	`Plastocyanin-like 4.`
`DOMAIN`	`730 1061`	`332`	`F5/8 type A 3.`
`DOMAIN`	`730 900`	`171`	`Plastocyanin-like 5.`
`DOMAIN`	`908 1061`	`154`	`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`	`204 204`		`Phosphoserine.`
`MOD_RES`	`784 784`		`Phosphotyrosine.`
`MOD_RES`	`787 787`		`Phosphotyrosine.`
`CARBOHYD`	`138 138`		`N-linked (GlcNAc...).`
`CARBOHYD`	`358 358`		`N-linked (GlcNAc...).`
`CARBOHYD`	`397 397`		`N-linked (GlcNAc...).`
`CARBOHYD`	`588 588`		`N-linked (GlcNAc...).`
`CARBOHYD`	`762 762`		`N-linked (GlcNAc...).`
`CARBOHYD`	`926 926`		`N-linked (GlcNAc...).`
`DISULFID`	`174 200`		`Probable.`
`DISULFID`	`276 357`		`Probable.`
`DISULFID`	`534 560`		`Probable.`
`DISULFID`	`637 718`		`Probable.`
`DISULFID`	`874 900`		`Probable.`
`VARIANT`	`63 63`	`1`	`I -> T (retained in the ER due to impaired N-glycosylation; may present a vulnerability factor for iron induced oxidative stress in Parkinson disease).`	`VAR_025655`
`VARIANT`	`367 367`	`1`	`R -> C (in dbSNP:rs34624984 [NCBI]).`	`VAR_032815`
`VARIANT`	`477 477`	`1`	`P -> L (in dbSNP:rs35331711 [NCBI]).`	`VAR_025656`
`VARIANT`	`544 544`	`1`	`D -> E (reduced ferroxidase activity; may present a vulnerability factor for iron induced oxidative stress in Parkinson disease; dbSNP:rs701753 [NCBI]).`	`VAR_025657`
`VARIANT`	`551 551`	`1`	`T -> I.`	`VAR_025658`
`VARIANT`	`793 793`	`1`	`R -> H.`	`VAR_025659`
`VARIANT`	`841 841`	`1`	`T -> R.`	`VAR_025660`
`CONFLICT`	`1060 1060`		`E -> EGEYP (in Ref. 6; AAA51975).`
`STRAND`	`21 35`	`15`
`STRAND`	`49 51`	`3`
`HELIX`	`53 56`	`4`
`STRAND`	`65 79`	`15`
`HELIX`	`88 90`	`3`
`STRAND`	`97 100`	`4`
`STRAND`	`104 115`	`12`
`STRAND`	`120 125`	`6`
`HELIX`	`128 130`	`3`
`HELIX`	`141 143`	`3`
`HELIX`	`145 147`	`3`
`STRAND`	`154 160`	`7`
`STRAND`	`173 180`	`8`
`HELIX`	`185 191`	`7`
`STRAND`	`194 200`	`7`
`STRAND`	`205 210`	`6`
`STRAND`	`215 225`	`11`
`HELIX`	`226 228`	`3`
`HELIX`	`232 239`	`8`
`HELIX`	`243 245`	`3`
`HELIX`	`251 256`	`6`
`STRAND`	`258 262`	`5`
`STRAND`	`274 276`	`3`
`STRAND`	`280 287`	`8`
`STRAND`	`295 299`	`5`
`STRAND`	`304 306`	`3`
`STRAND`	`309 316`	`8`
`STRAND`	`321 327`	`7`
`STRAND`	`332 338`	`7`
`HELIX`	`341 345`	`5`
`STRAND`	`349 355`	`7`
`STRAND`	`369 385`	`17`
`TURN`	`392 394`	`3`
`HELIX`	`406 409`	`4`
`STRAND`	`418 430`	`13`
`HELIX`	`441 446`	`6`
`STRAND`	`453 456`	`4`
`STRAND`	`459 467`	`9`
`STRAND`	`469 471`	`3`
`STRAND`	`476 481`	`6`
`HELIX`	`484 486`	`3`
`STRAND`	`514 520`	`7`
`HELIX`	`523 525`	`3`
`STRAND`	`529 531`	`3`
`STRAND`	`533 540`	`8`
`STRAND`	`542 544`	`3`
`HELIX`	`545 551`	`7`
`STRAND`	`554 560`	`7`
`STRAND`	`575 580`	`6`
`STRAND`	`582 586`	`5`
`HELIX`	`587 589`	`3`
`HELIX`	`593 600`	`8`
`HELIX`	`604 606`	`3`
`HELIX`	`612 617`	`6`
`STRAND`	`619 623`	`5`
`STRAND`	`635 637`	`3`
`STRAND`	`642 647`	`6`
`STRAND`	`656 660`	`5`
`STRAND`	`665 667`	`3`
`STRAND`	`670 677`	`8`
`STRAND`	`682 687`	`6`
`STRAND`	`693 699`	`7`
`HELIX`	`702 706`	`5`
`STRAND`	`710 716`	`7`
`STRAND`	`729 745`	`17`
`HELIX`	`750 759`	`10`
`TURN`	`766 768`	`3`
`TURN`	`771 773`	`3`
`STRAND`	`777 789`	`13`
`HELIX`	`800 805`	`6`
`STRAND`	`812 815`	`4`
`STRAND`	`818 826`	`9`
`STRAND`	`828 830`	`3`
`STRAND`	`835 838`	`4`
`STRAND`	`854 860`	`7`
`HELIX`	`863 865`	`3`
`STRAND`	`873 880`	`8`
`HELIX`	`885 890`	`6`
`STRAND`	`894 900`	`7`
`STRAND`	`913 924`	`12`
`HELIX`	`925 927`	`3`
`HELIX`	`931 938`	`8`
`HELIX`	`942 944`	`3`
`HELIX`	`950 955`	`6`
`STRAND`	`957 961`	`5`
`STRAND`	`973 975`	`3`
`STRAND`	`979 986`	`8`
`STRAND`	`994 1000`	`7`
`STRAND`	`1003 1005`	`3`
`TURN`	`1006 1009`	`4`
`STRAND`	`1011 1018`	`8`
`STRAND`	`1023 1028`	`6`
`STRAND`	`1034 1040`	`7`
`HELIX`	`1043 1047`	`5`
`STRAND`	`1051 1057`	`7`

Sequence information

Length: 1065 AA [This is the length of the unprocessed precursor]

Molecular weight: 122205 Da [This is the MW of the unprocessed precursor]

CRC64: 2F2F1294E2D30F58 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MKILILGIFL FLCSTPAWAK EKHYYIGIIE TTWDYASDHG EKKLISVDTE HSNIYLQNGP 

        70         80         90        100        110        120 
DRIGRLYKKA LYLQYTDETF RTTIEKPVWL GFLGPIIKAE TGDKVYVHLK NLASRPYTFH 

       130        140        150        160        170        180 
SHGITYYKEH EGAIYPDNTT DFQRADDKVY PGEQYTYMLL ATEEQSPGEG DGNCVTRIYH 

       190        200        210        220        230        240 
SHIDAPKDIA SGLIGPLIIC KKDSLDKEKE KHIDREFVVM FSVVDENFSW YLEDNIKTYC 

       250        260        270        280        290        300 
SEPEKVDKDN EDFQESNRMY SVNGYTFGSL PGLSMCAEDR VKWYLFGMGN EVDVHAAFFH 

       310        320        330        340        350        360 
GQALTNKNYR IDTINLFPAT LFDAYMVAQN PGEWMLSCQN LNHLKAGLQA FFQVQECNKS 

       370        380        390        400        410        420 
SSKDNIRGKH VRHYYIAAEE IIWNYAPSGI DIFTKENLTA PGSDSAVFFE QGTTRIGGSY 

       430        440        450        460        470        480 
KKLVYREYTD ASFTNRKERG PEEEHLGILG PVIWAEVGDT IRVTFHNKGA YPLSIEPIGV 

       490        500        510        520        530        540 
RFNKNNEGTY YSPNYNPQSR SVPPSASHVA PTETFTYEWT VPKEVGPTNA DPVCLAKMYY 

       550        560        570        580        590        600 
SAVDPTKDIF TGLIGPMKIC KKGSLHANGR QKDVDKEFYL FPTVFDENES LLLEDNIRMF 

       610        620        630        640        650        660 
TTAPDQVDKE DEDFQESNKM HSMNGFMYGN QPGLTMCKGD SVVWYLFSAG NEADVHGIYF 

       670        680        690        700        710        720 
SGNTYLWRGE RRDTANLFPQ TSLTLHMWPD TEGTFNVECL TTDHYTGGMK QKYTVNQCRR 

       730        740        750        760        770        780 
QSEDSTFYLG ERTYYIAAVE VEWDYSPQRE WEKELHHLQE QNVSNAFLDK GEFYIGSKYK 

       790        800        810        820        830        840 
KVVYRQYTDS TFRVPVERKA EEEHLGILGP QLHADVGDKV KIIFKNMATR PYSIHAHGVQ 

       850        860        870        880        890        900 
TESSTVTPTL PGETLTYVWK IPERSGAGTE DSACIPWAYY STVDQVKDLY SGLIGPLIVC 

       910        920        930        940        950        960 
RRPYLKVFNP RRKLEFALLF LVFDENESWY LDDNIKTYSD HPEKVNKDDE EFIESNKMHA 

       970        980        990       1000       1010       1020 
INGRMFGNLQ GLTMHVGDEV NWYLMGMGNE IDLHTVHFHG HSFQYKHRGV YSSDVFDIFP 

      1030       1040       1050       1060 
GTYQTLEMFP RTPGIWLLHC HVTDHIHAGM ETTYTVLQNE DTKSG

P00450 in FASTA format

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	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools