CERU_HUMAN
ID CERU_HUMAN Reviewed; 1065 AA.
AC P00450; Q14063; Q2PP18; Q9UKS4;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 13-AUG-1987, sequence version 1.
DT 03-AUG-2022, entry version 232.
DE RecName: Full=Ceruloplasmin;
DE EC=1.16.3.1;
DE AltName: Full=Ferroxidase;
DE Flags: Precursor;
GN Name=CP;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2873574; DOI=10.1073/pnas.83.14.5086;
RA Koschinsky M.L., Funk W.D., van Oost B.A., McGillivray R.T.A.;
RT "Complete cDNA sequence of human preceruloplasmin.";
RL Proc. Natl. Acad. Sci. U.S.A. 83:5086-5090(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RG NHLBI resequencing and genotyping service (RS&G);
RL Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-1006.
RX PubMed=7702601; DOI=10.1006/bbrc.1995.1437;
RA Daimon M., Yamatani K., Igarashi M., Fukase N., Kawanami T., Kato T.,
RA Tominaga M., Sasaki H.;
RT "Fine structure of the human ceruloplasmin gene.";
RL Biochem. Biophys. Res. Commun. 208:1028-1035(1995).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-40; 549-599; 784-829 AND 919-952.
RX PubMed=3755405; DOI=10.1016/0014-5793(86)80739-6;
RA Mercer J.F.B., Grimes A.;
RT "Isolation of a human ceruloplasmin cDNA clone that includes the N-terminal
RT leader sequence.";
RL FEBS Lett. 203:185-190(1986).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-22.
RA Bingle C.D.;
RT "Cloning and functional analysis of the human ceruloplasmin gene minimal
RT promoter.";
RL Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 218-1065.
RX PubMed=3486416; DOI=10.1073/pnas.83.10.3257;
RA Yang F., Naylor S.L., Lum J.B., Cutshaw S., McCombs J.L., Naberhaus K.H.,
RA McGill J.R., Adrian G.S., Moore C.M., Barnett D.R., Bowman B.H.;
RT "Characterization, mapping, and expression of the human ceruloplasmin
RT gene.";
RL Proc. Natl. Acad. Sci. U.S.A. 83:3257-3261(1986).
RN [7]
RP PROTEIN SEQUENCE OF 20-1065.
RX PubMed=6582496; DOI=10.1073/pnas.81.2.390;
RA Takahashi N., Ortel T.L., Putnam F.W.;
RT "Single-chain structure of human ceruloplasmin: the complete amino acid
RT sequence of the whole molecule.";
RL Proc. Natl. Acad. Sci. U.S.A. 81:390-394(1984).
RN [8]
RP PROTEIN SEQUENCE OF 158-333; 518-724 AND 858-1065.
RX PubMed=6571985; DOI=10.1073/pnas.80.1.115;
RA Takahashi N., Bauman R.A., Ortel T.L., Dwulet F.E., Wang C.-C.,
RA Putnam F.W.;
RT "Internal triplication in the structure of human ceruloplasmin.";
RL Proc. Natl. Acad. Sci. U.S.A. 80:115-119(1983).
RN [9]
RP PROTEIN SEQUENCE OF 501-905.
RX PubMed=6940148; DOI=10.1073/pnas.78.2.790;
RA Dwulet F.E., Putnam F.W.;
RT "Complete amino acid sequence of a 50,000-dalton fragment of human
RT ceruloplasmin.";
RL Proc. Natl. Acad. Sci. U.S.A. 78:790-794(1981).
RN [10]
RP PROTEIN SEQUENCE OF 907-1065.
RX PubMed=6987229; DOI=10.1016/s0021-9258(19)85822-2;
RA Kingston I.B., Kingston B.L., Putnam F.W.;
RT "Primary structure of a histidine-rich proteolytic fragment of human
RT ceruloplasmin. I. Amino acid sequence of the cyanogen bromide peptides.";
RL J. Biol. Chem. 255:2878-2885(1980).
RN [11]
RP PROTEIN SEQUENCE OF 907-1065.
RX PubMed=6987230; DOI=10.1016/s0021-9258(19)85823-4;
RA Kingston I.B., Kingston B.L., Putnam F.W.;
RT "Primary structure of a histidine-rich proteolytic fragment of human
RT ceruloplasmin. II. Amino acid sequence of the tryptic peptides.";
RL J. Biol. Chem. 255:2886-2896(1980).
RN [12]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1007-1061.
RX PubMed=2355023; DOI=10.1016/s0021-9258(18)87015-6;
RA Yang F.M., Friedrichs W.E., Cupples R.L., Banifacio M.J., Sanford J.A.,
RA Horton W.A., Bowman B.H.;
RT "Human ceruloplasmin. Tissue-specific expression of transcripts produced by
RT alternative splicing.";
RL J. Biol. Chem. 265:10780-10785(1990).
RN [13]
RP REVIEW.
RX PubMed=12055353; DOI=10.1146/annurev.nutr.22.012502.114457;
RA Hellman N.E., Gitlin J.D.;
RT "Ceruloplasmin metabolism and function.";
RL Annu. Rev. Nutr. 22:439-458(2002).
RN [14]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-138.
RC TISSUE=Bile;
RX PubMed=15084671; DOI=10.1074/mcp.m400015-mcp200;
RA Kristiansen T.Z., Bunkenborg J., Gronborg M., Molina H., Thuluvath P.J.,
RA Argani P., Goggins M.G., Maitra A., Pandey A.;
RT "A proteomic analysis of human bile.";
RL Mol. Cell. Proteomics 3:715-728(2004).
RN [15]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-138; ASN-397 AND ASN-762.
RC TISSUE=Plasma;
RX PubMed=14760718; DOI=10.1002/pmic.200300556;
RA Bunkenborg J., Pilch B.J., Podtelejnikov A.V., Wisniewski J.R.;
RT "Screening for N-glycosylated proteins by liquid chromatography mass
RT spectrometry.";
RL Proteomics 4:454-465(2004).
RN [16]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-138; ASN-358; ASN-397; ASN-588;
RP ASN-762 AND ASN-926.
RC TISSUE=Plasma;
RX PubMed=16335952; DOI=10.1021/pr0502065;
RA Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J.,
RA Smith R.D.;
RT "Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
RT hydrazide chemistry, and mass spectrometry.";
RL J. Proteome Res. 4:2070-2080(2005).
RN [17]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-138; ASN-358; ASN-397 AND
RP ASN-762.
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of multiple
RT enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [18]
RP GLYCOSYLATION AT ASN-138; ASN-358; ASN-397 AND ASN-762.
RX PubMed=19139490; DOI=10.1074/mcp.m800504-mcp200;
RA Jia W., Lu Z., Fu Y., Wang H.P., Wang L.H., Chi H., Yuan Z.F., Zheng Z.B.,
RA Song L.N., Han H.H., Liang Y.M., Wang J.L., Cai Y., Zhang Y.K., Deng Y.L.,
RA Ying W.T., He S.M., Qian X.H.;
RT "A strategy for precise and large scale identification of core fucosylated
RT glycoproteins.";
RL Mol. Cell. Proteomics 8:913-923(2009).
RN [19]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-138; ASN-358 AND ASN-397, AND
RP STRUCTURE OF CARBOHYDRATES.
RC TISSUE=Cerebrospinal fluid;
RX PubMed=19838169; DOI=10.1038/nmeth.1392;
RA Nilsson J., Rueetschi U., Halim A., Hesse C., Carlsohn E., Brinkmalm G.,
RA Larson G.;
RT "Enrichment of glycopeptides for glycan structure and attachment site
RT identification.";
RL Nat. Methods 6:809-811(2009).
RN [20]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [21]
RP PHOSPHORYLATION AT SER-722.
RX PubMed=26091039; DOI=10.1016/j.cell.2015.05.028;
RA Tagliabracci V.S., Wiley S.E., Guo X., Kinch L.N., Durrant E., Wen J.,
RA Xiao J., Cui J., Nguyen K.B., Engel J.L., Coon J.J., Grishin N.,
RA Pinna L.A., Pagliarini D.J., Dixon J.E.;
RT "A single kinase generates the majority of the secreted phosphoproteome.";
RL Cell 161:1619-1632(2015).
RN [22]
RP X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS), DISULFIDE BONDS, AND METAL-BINDING
RP SITES.
RA Zaitseva I., Zaitsev V., Card G., Moshkov K., Bax B., Ralph A., Lindley P.;
RT "The X-ray structure of human serum ceruloplasmin at 3.1 A: nature of the
RT copper centres.";
RL J. Biol. Inorg. Chem. 1:15-23(1996).
RN [23]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS), METAL-BINDING SITES, AND DISULFIDE
RP BONDS.
RX PubMed=17242517; DOI=10.1107/s090744490604947x;
RA Bento I., Peixoto C., Zaitsev V.N., Lindley P.F.;
RT "Ceruloplasmin revisited: structural and functional roles of various metal
RT cation-binding sites.";
RL Acta Crystallogr. D 63:240-248(2007).
RN [24]
RP VARIANTS THR-63; LEU-477; GLU-544; ILE-551; HIS-793 AND ARG-841.
RX PubMed=15557511; DOI=10.1212/01.wnl.0000144276.29988.c3;
RA Hochstrasser H., Bauer P., Walter U., Behnke S., Spiegel J., Csoti I.,
RA Zeiler B., Bornemann A., Pahnke J., Becker G., Riess O., Berg D.;
RT "Ceruloplasmin gene variations and substantia nigra hyperechogenicity in
RT Parkinson disease.";
RL Neurology 63:1912-1917(2004).
RN [25]
RP CHARACTERIZATION OF VARIANTS THR-63; GLU-544 AND HIS-793.
RX PubMed=16150804; DOI=10.1096/fj.04-3486fje;
RA Hochstrasser H., Tomiuk J., Walter U., Behnke S., Spiegel J., Krueger R.,
RA Becker G., Riess O., Berg D.;
RT "Functional relevance of ceruloplasmin mutations in Parkinson's disease.";
RL FASEB J. 19:1851-1853(2005).
CC -!- FUNCTION: Ceruloplasmin is a blue, copper-binding (6-7 atoms per
CC molecule) glycoprotein. It has ferroxidase activity oxidizing Fe(2+) to
CC Fe(3+) without releasing radical oxygen species. It is involved in iron
CC transport across the cell membrane. Provides Cu(2+) ions for the
CC ascorbate-mediated deaminase degradation of the heparan sulfate chains
CC of GPC1. May also play a role in fetal lung development or pulmonary
CC antioxidant defense (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4 Fe(2+) + 4 H(+) + O2 = 4 Fe(3+) + 2 H2O;
CC Xref=Rhea:RHEA:11148, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034; EC=1.16.3.1;
CC -!- COFACTOR:
CC Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC Note=Binds 6 Cu cations per monomer.;
CC -!- SUBCELLULAR LOCATION: Secreted. Note=Colocalizes with GCP1 in secretory
CC intracellular compartments. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed by the liver and secreted in plasma.
CC -!- DISEASE: Aceruloplasminemia (ACERULOP) [MIM:604290]: An autosomal
CC recessive disorder of iron metabolism characterized by iron
CC accumulation in the brain as well as visceral organs. Clinical features
CC consist of the triad of retinal degeneration, diabetes mellitus and
CC neurological disturbances. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Note=Ceruloplasmin levels are decreased in Wilson disease, in
CC which copper cannot be incorporated into ceruloplasmin in liver because
CC of defects in the copper-transporting ATPase 2.
CC -!- SIMILARITY: Belongs to the multicopper oxidase family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Wikipedia; Note=Ceruloplasmin entry;
CC URL="https://en.wikipedia.org/wiki/Ceruloplasmin";
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DR EMBL; M13699; AAA51976.1; -; mRNA.
DR EMBL; DQ314867; ABC40726.1; -; Genomic_DNA.
DR EMBL; D45045; BAA08085.1; -; Genomic_DNA.
DR EMBL; D00025; BAA00019.1; -; mRNA.
DR EMBL; X04135; CAA27752.1; -; mRNA.
DR EMBL; X04136; CAA27753.1; -; mRNA.
DR EMBL; X04137; CAA27754.1; -; mRNA.
DR EMBL; X04138; CAA27755.1; -; mRNA.
DR EMBL; AF132978; AAF02483.1; -; Genomic_DNA.
DR EMBL; M13536; AAA51975.1; -; mRNA.
DR EMBL; J05506; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS3141.1; -.
DR PIR; A25443; KUHU.
DR RefSeq; NP_000087.1; NM_000096.3.
DR PDB; 1KCW; X-ray; 3.00 A; A=20-1065.
DR PDB; 2J5W; X-ray; 2.80 A; A=1-1065.
DR PDB; 4EJX; X-ray; 4.69 A; A=1-1065.
DR PDB; 4ENZ; X-ray; 2.60 A; A=1-1065.
DR PDBsum; 1KCW; -.
DR PDBsum; 2J5W; -.
DR PDBsum; 4EJX; -.
DR PDBsum; 4ENZ; -.
DR AlphaFoldDB; P00450; -.
DR PCDDB; P00450; -.
DR SASBDB; P00450; -.
DR SMR; P00450; -.
DR BioGRID; 107748; 60.
DR CORUM; P00450; -.
DR IntAct; P00450; 13.
DR MINT; P00450; -.
DR STRING; 9606.ENSP00000264613; -.
DR DrugBank; DB01373; Calcium.
DR DrugBank; DB09130; Copper.
DR DrugBank; DB11134; Cupric oxide.
DR DrugBank; DB06778; Cupric sulfate.
DR DrugBank; DB14490; Ferrous ascorbate.
DR DrugBank; DB14491; Ferrous fumarate.
DR DrugBank; DB14488; Ferrous gluconate.
DR DrugBank; DB14501; Ferrous glycine sulfate.
DR DrugBank; DB14489; Ferrous succinate.
DR DrugBank; DB13257; Ferrous sulfate anhydrous.
DR DrugBank; DB01592; Iron.
DR DrugBank; DB12965; Silver.
DR DrugBank; DB01593; Zinc.
DR DrugBank; DB14487; Zinc acetate.
DR DrugBank; DB14533; Zinc chloride.
DR DrugBank; DB14548; Zinc sulfate, unspecified form.
DR TCDB; 8.A.105.1.2; the multi-copper-containing ferroxidase (mcfo) family.
DR CarbonylDB; P00450; -.
DR GlyConnect; 85; 71 N-Linked glycans (5 sites), 1 O-Linked glycan (1 site).
DR GlyGen; P00450; 13 sites, 89 N-linked glycans (6 sites), 2 O-linked glycans (5 sites).
DR iPTMnet; P00450; -.
DR PhosphoSitePlus; P00450; -.
DR BioMuta; CP; -.
DR DMDM; 116117; -.
DR DOSAC-COBS-2DPAGE; P00450; -.
DR SWISS-2DPAGE; P00450; -.
DR CPTAC; CPTAC-660; -.
DR CPTAC; non-CPTAC-1093; -.
DR CPTAC; non-CPTAC-1094; -.
DR CPTAC; non-CPTAC-1095; -.
DR EPD; P00450; -.
DR jPOST; P00450; -.
DR MassIVE; P00450; -.
DR MaxQB; P00450; -.
DR PaxDb; P00450; -.
DR PeptideAtlas; P00450; -.
DR PRIDE; P00450; -.
DR ProteomicsDB; 51251; -.
DR Antibodypedia; 861; 389 antibodies from 35 providers.
DR DNASU; 1356; -.
DR Ensembl; ENST00000264613.11; ENSP00000264613.6; ENSG00000047457.14.
DR GeneID; 1356; -.
DR KEGG; hsa:1356; -.
DR UCSC; uc003ewy.6; human.
DR CTD; 1356; -.
DR DisGeNET; 1356; -.
DR GeneCards; CP; -.
DR GeneReviews; CP; -.
DR HGNC; HGNC:2295; CP.
DR HPA; ENSG00000047457; Tissue enriched (liver).
DR MalaCards; CP; -.
DR MIM; 117700; gene.
DR MIM; 604290; phenotype.
DR neXtProt; NX_P00450; -.
DR Orphanet; 48818; Aceruloplasminemia.
DR PharmGKB; PA26815; -.
DR VEuPathDB; HostDB:ENSG00000047457; -.
DR eggNOG; KOG1263; Eukaryota.
DR InParanoid; P00450; -.
DR OrthoDB; 454773at2759; -.
DR PhylomeDB; P00450; -.
DR TreeFam; TF329807; -.
DR BioCyc; MetaCyc:HS00590-MON; -.
DR BRENDA; 1.16.3.1; 2681.
DR PathwayCommons; P00450; -.
DR Reactome; R-HSA-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR Reactome; R-HSA-425410; Metal ion SLC transporters.
DR Reactome; R-HSA-5619049; Defective SLC40A1 causes hemochromatosis 4 (HFE4) (macrophages).
DR Reactome; R-HSA-5619060; Defective CP causes aceruloplasminemia (ACERULOP).
DR Reactome; R-HSA-8957275; Post-translational protein phosphorylation.
DR Reactome; R-HSA-917937; Iron uptake and transport.
DR SABIO-RK; P00450; -.
DR SignaLink; P00450; -.
DR SIGNOR; P00450; -.
DR BioGRID-ORCS; 1356; 9 hits in 1069 CRISPR screens.
DR ChiTaRS; CP; human.
DR EvolutionaryTrace; P00450; -.
DR GeneWiki; Ceruloplasmin; -.
DR GenomeRNAi; 1356; -.
DR Pharos; P00450; Tbio.
DR PRO; PR:P00450; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; P00450; protein.
DR Bgee; ENSG00000047457; Expressed in right lobe of liver and 154 other tissues.
DR ExpressionAtlas; P00450; baseline and differential.
DR Genevisible; P00450; HS.
DR GO; GO:0072562; C:blood microparticle; HDA:UniProtKB.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; IDA:BHF-UCL.
DR GO; GO:0005765; C:lysosomal membrane; HDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0051087; F:chaperone binding; IPI:BHF-UCL.
DR GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR GO; GO:0004322; F:ferroxidase activity; TAS:Reactome.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0006879; P:cellular iron ion homeostasis; TAS:Reactome.
DR GO; GO:0006825; P:copper ion transport; IEA:UniProtKB-KW.
DR GO; GO:0055072; P:iron ion homeostasis; IBA:GO_Central.
DR GO; GO:0006826; P:iron ion transport; IBA:GO_Central.
DR Gene3D; 2.60.40.420; -; 5.
DR InterPro; IPR001117; Cu-oxidase.
DR InterPro; IPR011706; Cu-oxidase_C.
DR InterPro; IPR045087; Cu-oxidase_fam.
DR InterPro; IPR011707; Cu-oxidase_N.
DR InterPro; IPR033138; Cu_oxidase_CS.
DR InterPro; IPR002355; Cu_oxidase_Cu_BS.
DR InterPro; IPR008972; Cupredoxin.
DR PANTHER; PTHR11709; PTHR11709; 3.
DR Pfam; PF00394; Cu-oxidase; 1.
DR Pfam; PF07731; Cu-oxidase_2; 1.
DR Pfam; PF07732; Cu-oxidase_3; 2.
DR SUPFAM; SSF49503; SSF49503; 6.
DR PROSITE; PS00079; MULTICOPPER_OXIDASE1; 3.
DR PROSITE; PS00080; MULTICOPPER_OXIDASE2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Copper; Copper transport; Direct protein sequencing;
KW Disulfide bond; Glycoprotein; Ion transport; Metal-binding; Oxidoreductase;
KW Phosphoprotein; Reference proteome; Repeat; Secreted; Signal; Transport.
FT SIGNAL 1..19
FT /evidence="ECO:0000269|PubMed:6582496"
FT CHAIN 20..1065
FT /note="Ceruloplasmin"
FT /id="PRO_0000002912"
FT DOMAIN 20..357
FT /note="F5/8 type A 1"
FT DOMAIN 20..200
FT /note="Plastocyanin-like 1"
FT DOMAIN 209..357
FT /note="Plastocyanin-like 2"
FT DOMAIN 370..718
FT /note="F5/8 type A 2"
FT DOMAIN 370..560
FT /note="Plastocyanin-like 3"
FT DOMAIN 570..718
FT /note="Plastocyanin-like 4"
FT DOMAIN 730..1061
FT /note="F5/8 type A 3"
FT DOMAIN 730..900
FT /note="Plastocyanin-like 5"
FT DOMAIN 908..1061
FT /note="Plastocyanin-like 6"
FT BINDING 120
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="1"
FT /note="type 2 copper site"
FT BINDING 122
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="2"
FT /note="type 3 copper site"
FT BINDING 180
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="2"
FT /note="type 3 copper site"
FT BINDING 182
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="3"
FT /note="type 3 copper site"
FT BINDING 295
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="4"
FT /note="type 1 copper site"
FT BINDING 338
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="4"
FT /note="type 1 copper site"
FT BINDING 343
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="4"
FT /note="type 1 copper site"
FT BINDING 656
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="5"
FT /note="type 1 copper site"
FT BINDING 699
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="5"
FT /note="type 1 copper site"
FT BINDING 704
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="5"
FT /note="type 1 copper site"
FT BINDING 709
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="5"
FT /note="type 1 copper site"
FT BINDING 994
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="6"
FT /note="type 1 copper site"
FT BINDING 997
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="1"
FT /note="type 2 copper site"
FT BINDING 999
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="3"
FT /note="type 3 copper site"
FT BINDING 1039
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="3"
FT /note="type 3 copper site"
FT BINDING 1040
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="6"
FT /note="type 1 copper site"
FT BINDING 1041
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="2"
FT /note="type 3 copper site"
FT BINDING 1045
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="6"
FT /note="type 1 copper site"
FT BINDING 1050
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="6"
FT /note="type 1 copper site"
FT MOD_RES 722
FT /note="Phosphoserine; by FAM20C"
FT /evidence="ECO:0000269|PubMed:26091039"
FT CARBOHYD 138
FT /note="N-linked (GlcNAc...) (complex) asparagine"
FT /evidence="ECO:0000269|PubMed:14760718,
FT ECO:0000269|PubMed:15084671, ECO:0000269|PubMed:16335952,
FT ECO:0000269|PubMed:19139490, ECO:0000269|PubMed:19159218,
FT ECO:0000269|PubMed:19838169"
FT CARBOHYD 358
FT /note="N-linked (GlcNAc...) (complex) asparagine"
FT /evidence="ECO:0000269|PubMed:16335952,
FT ECO:0000269|PubMed:19139490, ECO:0000269|PubMed:19159218,
FT ECO:0000269|PubMed:19838169"
FT CARBOHYD 397
FT /note="N-linked (GlcNAc...) (complex) asparagine"
FT /evidence="ECO:0000269|PubMed:14760718,
FT ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19139490,
FT ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:19838169"
FT CARBOHYD 588
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16335952"
FT CARBOHYD 762
FT /note="N-linked (GlcNAc...) (complex) asparagine"
FT /evidence="ECO:0000269|PubMed:14760718,
FT ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19139490,
FT ECO:0000269|PubMed:19159218"
FT CARBOHYD 926
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16335952"
FT DISULFID 174..200
FT /evidence="ECO:0000305"
FT DISULFID 276..357
FT /evidence="ECO:0000305"
FT DISULFID 534..560
FT /evidence="ECO:0000305"
FT DISULFID 637..718
FT /evidence="ECO:0000305"
FT DISULFID 874..900
FT /evidence="ECO:0000305"
FT VARIANT 63
FT /note="I -> T (retained in the ER due to impaired N-
FT glycosylation; may present a vulnerability factor for iron
FT induced oxidative stress in Parkinson disease;
FT dbSNP:rs759185877)"
FT /evidence="ECO:0000269|PubMed:15557511,
FT ECO:0000269|PubMed:16150804"
FT /id="VAR_025655"
FT VARIANT 367
FT /note="R -> C (in dbSNP:rs34624984)"
FT /id="VAR_032815"
FT VARIANT 477
FT /note="P -> L (in dbSNP:rs35331711)"
FT /evidence="ECO:0000269|PubMed:15557511"
FT /id="VAR_025656"
FT VARIANT 544
FT /note="D -> E (reduced ferroxidase activity; may present a
FT vulnerability factor for iron induced oxidative stress in
FT Parkinson disease; dbSNP:rs701753)"
FT /evidence="ECO:0000269|PubMed:15557511,
FT ECO:0000269|PubMed:16150804"
FT /id="VAR_025657"
FT VARIANT 551
FT /note="T -> I (in dbSNP:rs61733458)"
FT /evidence="ECO:0000269|PubMed:15557511"
FT /id="VAR_025658"
FT VARIANT 793
FT /note="R -> H (in dbSNP:rs115552500)"
FT /evidence="ECO:0000269|PubMed:15557511,
FT ECO:0000269|PubMed:16150804"
FT /id="VAR_025659"
FT VARIANT 841
FT /note="T -> R (in dbSNP:rs56033670)"
FT /evidence="ECO:0000269|PubMed:15557511"
FT /id="VAR_025660"
FT CONFLICT 1060
FT /note="E -> EGEYP (in Ref. 6; AAA51975)"
FT /evidence="ECO:0000305"
FT STRAND 21..36
FT /evidence="ECO:0007829|PDB:4ENZ"
FT TURN 49..52
FT /evidence="ECO:0007829|PDB:4ENZ"
FT HELIX 53..56
FT /evidence="ECO:0007829|PDB:4ENZ"
FT STRAND 58..61
FT /evidence="ECO:0007829|PDB:1KCW"
FT STRAND 65..79
FT /evidence="ECO:0007829|PDB:4ENZ"
FT STRAND 82..84
FT /evidence="ECO:0007829|PDB:1KCW"
FT HELIX 88..90
FT /evidence="ECO:0007829|PDB:4ENZ"
FT STRAND 97..100
FT /evidence="ECO:0007829|PDB:4ENZ"
FT STRAND 104..111
FT /evidence="ECO:0007829|PDB:4ENZ"
FT STRAND 113..115
FT /evidence="ECO:0007829|PDB:4ENZ"
FT STRAND 120..125
FT /evidence="ECO:0007829|PDB:4ENZ"
FT HELIX 128..130
FT /evidence="ECO:0007829|PDB:4ENZ"
FT HELIX 141..144
FT /evidence="ECO:0007829|PDB:4ENZ"
FT HELIX 145..147
FT /evidence="ECO:0007829|PDB:4ENZ"
FT STRAND 154..160
FT /evidence="ECO:0007829|PDB:4ENZ"
FT STRAND 173..180
FT /evidence="ECO:0007829|PDB:4ENZ"
FT HELIX 185..190
FT /evidence="ECO:0007829|PDB:4ENZ"
FT STRAND 194..200
FT /evidence="ECO:0007829|PDB:4ENZ"
FT STRAND 205..210
FT /evidence="ECO:0007829|PDB:2J5W"
FT STRAND 214..225
FT /evidence="ECO:0007829|PDB:4ENZ"
FT HELIX 226..228
FT /evidence="ECO:0007829|PDB:4ENZ"
FT HELIX 232..239
FT /evidence="ECO:0007829|PDB:4ENZ"
FT HELIX 243..245
FT /evidence="ECO:0007829|PDB:4ENZ"
FT HELIX 251..257
FT /evidence="ECO:0007829|PDB:4ENZ"
FT STRAND 258..262
FT /evidence="ECO:0007829|PDB:4ENZ"
FT STRAND 274..276
FT /evidence="ECO:0007829|PDB:4ENZ"
FT STRAND 280..287
FT /evidence="ECO:0007829|PDB:4ENZ"
FT STRAND 295..301
FT /evidence="ECO:0007829|PDB:4ENZ"
FT STRAND 304..306
FT /evidence="ECO:0007829|PDB:4ENZ"
FT STRAND 309..312
FT /evidence="ECO:0007829|PDB:4ENZ"
FT STRAND 321..327
FT /evidence="ECO:0007829|PDB:4ENZ"
FT STRAND 332..338
FT /evidence="ECO:0007829|PDB:4ENZ"
FT HELIX 341..344
FT /evidence="ECO:0007829|PDB:4ENZ"
FT TURN 345..347
FT /evidence="ECO:0007829|PDB:4ENZ"
FT STRAND 349..355
FT /evidence="ECO:0007829|PDB:4ENZ"
FT STRAND 367..385
FT /evidence="ECO:0007829|PDB:4ENZ"
FT TURN 392..394
FT /evidence="ECO:0007829|PDB:4ENZ"
FT STRAND 401..403
FT /evidence="ECO:0007829|PDB:1KCW"
FT HELIX 406..409
FT /evidence="ECO:0007829|PDB:4ENZ"
FT STRAND 412..414
FT /evidence="ECO:0007829|PDB:1KCW"
FT STRAND 418..427
FT /evidence="ECO:0007829|PDB:4ENZ"
FT STRAND 429..435
FT /evidence="ECO:0007829|PDB:4ENZ"
FT HELIX 444..446
FT /evidence="ECO:0007829|PDB:4ENZ"
FT STRAND 453..456
FT /evidence="ECO:0007829|PDB:4ENZ"
FT STRAND 459..471
FT /evidence="ECO:0007829|PDB:4ENZ"
FT STRAND 476..481
FT /evidence="ECO:0007829|PDB:4ENZ"
FT HELIX 484..486
FT /evidence="ECO:0007829|PDB:4ENZ"
FT STRAND 514..520
FT /evidence="ECO:0007829|PDB:4ENZ"
FT TURN 523..525
FT /evidence="ECO:0007829|PDB:4ENZ"
FT STRAND 529..531
FT /evidence="ECO:0007829|PDB:2J5W"
FT STRAND 533..540
FT /evidence="ECO:0007829|PDB:4ENZ"
FT STRAND 542..544
FT /evidence="ECO:0007829|PDB:2J5W"
FT HELIX 545..551
FT /evidence="ECO:0007829|PDB:4ENZ"
FT STRAND 554..560
FT /evidence="ECO:0007829|PDB:4ENZ"
FT STRAND 575..580
FT /evidence="ECO:0007829|PDB:4ENZ"
FT STRAND 582..586
FT /evidence="ECO:0007829|PDB:4ENZ"
FT HELIX 587..589
FT /evidence="ECO:0007829|PDB:4ENZ"
FT HELIX 593..600
FT /evidence="ECO:0007829|PDB:4ENZ"
FT HELIX 604..606
FT /evidence="ECO:0007829|PDB:4ENZ"
FT HELIX 612..617
FT /evidence="ECO:0007829|PDB:4ENZ"
FT STRAND 619..623
FT /evidence="ECO:0007829|PDB:4ENZ"
FT STRAND 635..637
FT /evidence="ECO:0007829|PDB:4ENZ"
FT STRAND 642..647
FT /evidence="ECO:0007829|PDB:4ENZ"
FT STRAND 656..660
FT /evidence="ECO:0007829|PDB:4ENZ"
FT STRAND 665..667
FT /evidence="ECO:0007829|PDB:4ENZ"
FT STRAND 670..677
FT /evidence="ECO:0007829|PDB:4ENZ"
FT STRAND 682..687
FT /evidence="ECO:0007829|PDB:4ENZ"
FT STRAND 693..699
FT /evidence="ECO:0007829|PDB:4ENZ"
FT HELIX 702..706
FT /evidence="ECO:0007829|PDB:4ENZ"
FT STRAND 710..716
FT /evidence="ECO:0007829|PDB:4ENZ"
FT STRAND 729..745
FT /evidence="ECO:0007829|PDB:4ENZ"
FT HELIX 750..759
FT /evidence="ECO:0007829|PDB:4ENZ"
FT TURN 766..768
FT /evidence="ECO:0007829|PDB:4ENZ"
FT TURN 771..773
FT /evidence="ECO:0007829|PDB:4ENZ"
FT STRAND 777..789
FT /evidence="ECO:0007829|PDB:4ENZ"
FT HELIX 800..805
FT /evidence="ECO:0007829|PDB:4ENZ"
FT STRAND 812..815
FT /evidence="ECO:0007829|PDB:4ENZ"
FT STRAND 818..826
FT /evidence="ECO:0007829|PDB:4ENZ"
FT STRAND 828..830
FT /evidence="ECO:0007829|PDB:4ENZ"
FT STRAND 835..838
FT /evidence="ECO:0007829|PDB:4ENZ"
FT STRAND 842..844
FT /evidence="ECO:0007829|PDB:1KCW"
FT STRAND 854..860
FT /evidence="ECO:0007829|PDB:4ENZ"
FT HELIX 863..865
FT /evidence="ECO:0007829|PDB:4ENZ"
FT STRAND 869..871
FT /evidence="ECO:0007829|PDB:1KCW"
FT STRAND 873..880
FT /evidence="ECO:0007829|PDB:4ENZ"
FT HELIX 885..890
FT /evidence="ECO:0007829|PDB:4ENZ"
FT STRAND 894..900
FT /evidence="ECO:0007829|PDB:4ENZ"
FT STRAND 913..924
FT /evidence="ECO:0007829|PDB:4ENZ"
FT HELIX 925..927
FT /evidence="ECO:0007829|PDB:4ENZ"
FT HELIX 931..938
FT /evidence="ECO:0007829|PDB:4ENZ"
FT HELIX 942..944
FT /evidence="ECO:0007829|PDB:4ENZ"
FT HELIX 950..955
FT /evidence="ECO:0007829|PDB:4ENZ"
FT STRAND 957..961
FT /evidence="ECO:0007829|PDB:4ENZ"
FT STRAND 973..975
FT /evidence="ECO:0007829|PDB:4ENZ"
FT STRAND 979..986
FT /evidence="ECO:0007829|PDB:4ENZ"
FT STRAND 994..998
FT /evidence="ECO:0007829|PDB:4ENZ"
FT STRAND 1003..1006
FT /evidence="ECO:0007829|PDB:4ENZ"
FT HELIX 1007..1009
FT /evidence="ECO:0007829|PDB:4ENZ"
FT STRAND 1011..1018
FT /evidence="ECO:0007829|PDB:4ENZ"
FT STRAND 1023..1028
FT /evidence="ECO:0007829|PDB:4ENZ"
FT STRAND 1034..1040
FT /evidence="ECO:0007829|PDB:4ENZ"
FT HELIX 1043..1047
FT /evidence="ECO:0007829|PDB:4ENZ"
FT STRAND 1051..1057
FT /evidence="ECO:0007829|PDB:4ENZ"
SQ 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
