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 11-NOV-2015, entry version 185. 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; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; 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- RT terminal 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 RT minimal 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., RA Naberhaus K.H., McGill J.R., Adrian G.S., Moore C.M., Barnett D.R., RA 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 RT acid 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; 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 RT peptides."; RL J. Biol. Chem. 255:2878-2885(1980). RN [11] RP PROTEIN SEQUENCE OF 907-1065. RX PubMed=6987230; 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; RA Yang F.M., Friedrichs W.E., Cupples R.L., Banifacio M.J., RA Sanford J.A., Horton W.A., Bowman B.H.; RT "Human ceruloplasmin. Tissue-specific expression of transcripts RT produced by 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., RA Thuluvath P.J., 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; RP ASN-588; 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., RA Moore R.J., 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 RT multiple 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., RA Zheng Z.B., Song L.N., Han H.H., Liang Y.M., Wang J.L., Cai Y., RA Zhang Y.K., Deng Y.L., Ying W.T., He S.M., Qian X.H.; RT "A strategy for precise and large scale identification of core RT fucosylated glycoproteins."; RL Mol. Cell. Proteomics 8:913-923(2009). RN [19] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-138; ASN-358 AND ASN-397, RP AND 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., RA Brinkmalm G., 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., RA Wang L., Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human RT liver 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 RT phosphoproteome."; RL Cell 161:1619-1632(2015). RN [22] RP X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS), DISULFIDE BONDS, AND RP METAL-BINDING SITES. RA Zaitseva I., Zaitsev V., Card G., Moshkov K., Bax B., Ralph A., RA Lindley P.; RT "The X-ray structure of human serum ceruloplasmin at 3.1 A: nature of RT the copper centres."; RL J. Biol. Inorg. Chem. 1:15-23(1996). RN [23] RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS), METAL-BINDING SITES, AND RP DISULFIDE 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 RT metal 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 RT in 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., RA Krueger R., Becker G., Riess O., Berg D.; RT "Functional relevance of ceruloplasmin mutations in Parkinson's RT 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 CC Fe(2+) to Fe(3+) without releasing radical oxygen species. It is CC involved in iron transport across the cell membrane. Provides CC Cu(2+) ions for the ascorbate-mediated deaminase degradation of CC the heparan sulfate chains of GPC1. May also play a role in fetal CC lung development or pulmonary antioxidant defense (By similarity). CC {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: 4 Fe(2+) + 4 H(+) + O(2) = 4 Fe(3+) + 2 H(2)O. 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 CC secretory 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 CC features consist of the triad of retinal degeneration, diabetes CC mellitus and neurological disturbances. Note=The disease is caused CC by mutations affecting the gene represented in this entry. CC -!- DISEASE: Note=Ceruloplasmin levels are decreased in Wilson CC disease, in which copper cannot be incorporated into ceruloplasmin CC in liver because of defects in the copper-transporting ATPase 2. CC -!- SIMILARITY: Belongs to the multicopper oxidase family. CC {ECO:0000305}. CC -!- SIMILARITY: Contains 3 F5/8 type A domains. {ECO:0000305}. CC -!- SIMILARITY: Contains 6 plastocyanin-like domains. {ECO:0000305}. CC -!- WEB RESOURCE: Name=Wikipedia; Note=Ceruloplasmin entry; CC URL="https://en.wikipedia.org/wiki/Ceruloplasmin"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 UniGene; Hs.558314; -. 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 ProteinModelPortal; P00450; -. DR BioGrid; 107748; 7. DR IntAct; P00450; 5. DR STRING; 9606.ENSP00000264613; -. DR DrugBank; DB00055; Drotrecogin alfa. DR PhosphoSite; P00450; -. DR UniCarbKB; P00450; -. DR BioMuta; CP; -. DR DMDM; 116117; -. DR DOSAC-COBS-2DPAGE; P00450; -. DR SWISS-2DPAGE; P00450; -. DR MaxQB; P00450; -. DR PaxDb; P00450; -. DR PeptideAtlas; P00450; -. DR PRIDE; P00450; -. DR Ensembl; ENST00000264613; ENSP00000264613; ENSG00000047457. DR GeneID; 1356; -. DR KEGG; hsa:1356; -. DR UCSC; uc003ewy.4; human. DR CTD; 1356; -. DR GeneCards; CP; -. DR GeneReviews; CP; -. DR HGNC; HGNC:2295; CP. DR HPA; CAB008591; -. DR HPA; HPA001834; -. DR MIM; 117700; gene. DR MIM; 604290; phenotype. DR neXtProt; NX_P00450; -. DR Orphanet; 48818; Aceruloplasminemia. DR PharmGKB; PA26815; -. DR eggNOG; KOG1263; Eukaryota. DR eggNOG; COG2132; LUCA. DR HOGENOM; HOG000231499; -. DR HOVERGEN; HBG003674; -. DR InParanoid; P00450; -. DR KO; K13624; -. DR PhylomeDB; P00450; -. DR TreeFam; TF329807; -. DR BioCyc; MetaCyc:HS00590-MONOMER; -. DR BRENDA; 1.16.3.1; 2681. DR Reactome; R-HSA-425410; Metal ion SLC transporters. DR Reactome; R-HSA-917937; Iron uptake and transport. DR SABIO-RK; P00450; -. DR ChiTaRS; CP; human. DR EvolutionaryTrace; P00450; -. DR GeneWiki; Ceruloplasmin; -. DR GenomeRNAi; 1356; -. DR NextBio; 5493; -. DR PMAP-CutDB; P00450; -. DR PRO; PR:P00450; -. DR Proteomes; UP000005640; Chromosome 3. DR Bgee; P00450; -. DR CleanEx; HS_CP; -. DR ExpressionAtlas; P00450; baseline and differential. DR Genevisible; P00450; HS. DR GO; GO:0072562; C:blood microparticle; IDA:UniProtKB. DR GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB. DR GO; GO:0005576; C:extracellular region; NAS:UniProtKB. DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB. DR GO; GO:0005765; C:lysosomal membrane; IDA:UniProtKB. DR GO; GO:0051087; F:chaperone binding; IPI:BHF-UCL. DR GO; GO:0005507; F:copper ion binding; IEA:Ensembl. DR GO; GO:0004322; F:ferroxidase activity; TAS:Reactome. 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:0055085; P:transmembrane transport; TAS:Reactome. DR Gene3D; 2.60.40.420; -; 6. DR InterPro; IPR027150; CP. DR InterPro; IPR001117; Cu-oxidase. DR InterPro; IPR011706; Cu-oxidase_2. DR InterPro; IPR011707; Cu-oxidase_3. DR InterPro; IPR002355; Cu_oxidase_Cu_BS. DR InterPro; IPR008972; Cupredoxin. DR PANTHER; PTHR10127:SF664; PTHR10127:SF664; 1. 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; Complete proteome; Copper; Copper transport; KW Direct protein sequencing; Disulfide bond; Glycoprotein; KW Ion transport; Metal-binding; Oxidoreductase; Phosphoprotein; KW Polymorphism; Reference proteome; Repeat; Secreted; Signal; Transport. FT SIGNAL 1 19 {ECO:0000269|PubMed:6582496}. FT CHAIN 20 1065 Ceruloplasmin. FT /FTId=PRO_0000002912. FT DOMAIN 20 357 F5/8 type A 1. FT DOMAIN 20 200 Plastocyanin-like 1. FT DOMAIN 209 357 Plastocyanin-like 2. FT DOMAIN 370 718 F5/8 type A 2. FT DOMAIN 370 560 Plastocyanin-like 3. FT DOMAIN 570 718 Plastocyanin-like 4. FT DOMAIN 730 1061 F5/8 type A 3. FT DOMAIN 730 900 Plastocyanin-like 5. FT DOMAIN 908 1061 Plastocyanin-like 6. FT METAL 120 120 Copper 1; type 2. FT METAL 122 122 Copper 2; type 3. FT METAL 180 180 Copper 2; type 3. FT METAL 182 182 Copper 3; type 3. FT METAL 295 295 Copper 4; type 1. FT METAL 338 338 Copper 4; type 1. FT METAL 343 343 Copper 4; type 1. FT METAL 656 656 Copper 5; type 1. FT METAL 699 699 Copper 5; type 1. FT METAL 704 704 Copper 5; type 1. FT METAL 709 709 Copper 5; type 1. FT METAL 994 994 Copper 6; type 1. FT METAL 997 997 Copper 1; type 2. FT METAL 999 999 Copper 3; type 3. FT METAL 1039 1039 Copper 3; type 3. FT METAL 1040 1040 Copper 6; type 1. FT METAL 1041 1041 Copper 2; type 3. FT METAL 1045 1045 Copper 6; type 1. FT METAL 1050 1050 Copper 6; type 1. FT MOD_RES 722 722 Phosphoserine; by FAM20C. FT {ECO:0000269|PubMed:26091039}. FT CARBOHYD 138 138 N-linked (GlcNAc...) (complex). FT {ECO:0000269|PubMed:14760718, FT ECO:0000269|PubMed:15084671, FT ECO:0000269|PubMed:16335952, FT ECO:0000269|PubMed:19139490, FT ECO:0000269|PubMed:19159218, FT ECO:0000269|PubMed:19838169}. FT CARBOHYD 358 358 N-linked (GlcNAc...) (complex). FT {ECO:0000269|PubMed:16335952, FT ECO:0000269|PubMed:19139490, FT ECO:0000269|PubMed:19159218, FT ECO:0000269|PubMed:19838169}. FT CARBOHYD 397 397 N-linked (GlcNAc...) (complex). FT {ECO:0000269|PubMed:14760718, FT ECO:0000269|PubMed:16335952, FT ECO:0000269|PubMed:19139490, FT ECO:0000269|PubMed:19159218, FT ECO:0000269|PubMed:19838169}. FT CARBOHYD 588 588 N-linked (GlcNAc...). FT {ECO:0000269|PubMed:16335952}. FT CARBOHYD 762 762 N-linked (GlcNAc...) (complex). FT {ECO:0000269|PubMed:14760718, FT ECO:0000269|PubMed:16335952, FT ECO:0000269|PubMed:19139490, FT ECO:0000269|PubMed:19159218}. FT CARBOHYD 926 926 N-linked (GlcNAc...). FT {ECO:0000269|PubMed:16335952}. FT DISULFID 174 200 {ECO:0000305}. FT DISULFID 276 357 {ECO:0000305}. FT DISULFID 534 560 {ECO:0000305}. FT DISULFID 637 718 {ECO:0000305}. FT DISULFID 874 900 {ECO:0000305}. FT VARIANT 63 63 I -> T (retained in the ER due to FT impaired N-glycosylation; may present a FT vulnerability factor for iron induced FT oxidative stress in Parkinson disease). FT {ECO:0000269|PubMed:15557511, FT ECO:0000269|PubMed:16150804}. FT /FTId=VAR_025655. FT VARIANT 367 367 R -> C (in dbSNP:rs34624984). FT /FTId=VAR_032815. FT VARIANT 477 477 P -> L (in dbSNP:rs35331711). FT {ECO:0000269|PubMed:15557511}. FT /FTId=VAR_025656. FT VARIANT 544 544 D -> E (reduced ferroxidase activity; may FT present a vulnerability factor for iron FT induced oxidative stress in Parkinson FT disease; dbSNP:rs701753). FT {ECO:0000269|PubMed:15557511, FT ECO:0000269|PubMed:16150804}. FT /FTId=VAR_025657. FT VARIANT 551 551 T -> I. {ECO:0000269|PubMed:15557511}. FT /FTId=VAR_025658. FT VARIANT 793 793 R -> H. {ECO:0000269|PubMed:15557511, FT ECO:0000269|PubMed:16150804}. FT /FTId=VAR_025659. FT VARIANT 841 841 T -> R (in dbSNP:rs56033670). FT {ECO:0000269|PubMed:15557511}. FT /FTId=VAR_025660. FT CONFLICT 1060 1060 E -> EGEYP (in Ref. 6; AAA51975). FT {ECO:0000305}. FT STRAND 21 36 {ECO:0000244|PDB:4ENZ}. FT TURN 49 52 {ECO:0000244|PDB:4ENZ}. FT HELIX 53 56 {ECO:0000244|PDB:4ENZ}. FT STRAND 58 61 {ECO:0000244|PDB:1KCW}. FT STRAND 65 79 {ECO:0000244|PDB:4ENZ}. FT STRAND 82 84 {ECO:0000244|PDB:1KCW}. FT HELIX 88 90 {ECO:0000244|PDB:4ENZ}. FT STRAND 97 100 {ECO:0000244|PDB:4ENZ}. FT STRAND 104 111 {ECO:0000244|PDB:4ENZ}. FT STRAND 113 115 {ECO:0000244|PDB:4ENZ}. FT STRAND 120 125 {ECO:0000244|PDB:4ENZ}. FT HELIX 128 130 {ECO:0000244|PDB:4ENZ}. FT HELIX 141 144 {ECO:0000244|PDB:4ENZ}. FT HELIX 145 147 {ECO:0000244|PDB:4ENZ}. FT STRAND 154 160 {ECO:0000244|PDB:4ENZ}. FT STRAND 173 180 {ECO:0000244|PDB:4ENZ}. FT HELIX 185 190 {ECO:0000244|PDB:4ENZ}. FT STRAND 194 200 {ECO:0000244|PDB:4ENZ}. FT STRAND 205 210 {ECO:0000244|PDB:2J5W}. FT STRAND 214 225 {ECO:0000244|PDB:4ENZ}. FT HELIX 226 228 {ECO:0000244|PDB:4ENZ}. FT HELIX 232 239 {ECO:0000244|PDB:4ENZ}. FT HELIX 243 245 {ECO:0000244|PDB:4ENZ}. FT HELIX 251 257 {ECO:0000244|PDB:4ENZ}. FT STRAND 258 262 {ECO:0000244|PDB:4ENZ}. FT STRAND 274 276 {ECO:0000244|PDB:4ENZ}. FT STRAND 280 287 {ECO:0000244|PDB:4ENZ}. FT STRAND 295 301 {ECO:0000244|PDB:4ENZ}. FT STRAND 304 306 {ECO:0000244|PDB:4ENZ}. FT STRAND 309 312 {ECO:0000244|PDB:4ENZ}. FT STRAND 321 327 {ECO:0000244|PDB:4ENZ}. FT STRAND 332 338 {ECO:0000244|PDB:4ENZ}. FT HELIX 341 344 {ECO:0000244|PDB:4ENZ}. FT TURN 345 347 {ECO:0000244|PDB:4ENZ}. FT STRAND 349 355 {ECO:0000244|PDB:4ENZ}. FT STRAND 367 385 {ECO:0000244|PDB:4ENZ}. FT TURN 392 394 {ECO:0000244|PDB:4ENZ}. FT STRAND 401 403 {ECO:0000244|PDB:1KCW}. FT HELIX 406 409 {ECO:0000244|PDB:4ENZ}. FT STRAND 412 414 {ECO:0000244|PDB:1KCW}. FT STRAND 418 427 {ECO:0000244|PDB:4ENZ}. FT STRAND 429 435 {ECO:0000244|PDB:4ENZ}. FT HELIX 444 446 {ECO:0000244|PDB:4ENZ}. FT STRAND 453 456 {ECO:0000244|PDB:4ENZ}. FT STRAND 459 471 {ECO:0000244|PDB:4ENZ}. FT STRAND 476 481 {ECO:0000244|PDB:4ENZ}. FT HELIX 484 486 {ECO:0000244|PDB:4ENZ}. FT STRAND 514 520 {ECO:0000244|PDB:4ENZ}. FT TURN 523 525 {ECO:0000244|PDB:4ENZ}. FT STRAND 529 531 {ECO:0000244|PDB:2J5W}. FT STRAND 533 540 {ECO:0000244|PDB:4ENZ}. FT STRAND 542 544 {ECO:0000244|PDB:2J5W}. FT HELIX 545 551 {ECO:0000244|PDB:4ENZ}. FT STRAND 554 560 {ECO:0000244|PDB:4ENZ}. FT STRAND 575 580 {ECO:0000244|PDB:4ENZ}. FT STRAND 582 586 {ECO:0000244|PDB:4ENZ}. FT HELIX 587 589 {ECO:0000244|PDB:4ENZ}. FT HELIX 593 600 {ECO:0000244|PDB:4ENZ}. FT HELIX 604 606 {ECO:0000244|PDB:4ENZ}. FT HELIX 612 617 {ECO:0000244|PDB:4ENZ}. FT STRAND 619 623 {ECO:0000244|PDB:4ENZ}. FT STRAND 635 637 {ECO:0000244|PDB:4ENZ}. FT STRAND 642 647 {ECO:0000244|PDB:4ENZ}. FT STRAND 656 660 {ECO:0000244|PDB:4ENZ}. FT STRAND 665 667 {ECO:0000244|PDB:4ENZ}. FT STRAND 670 677 {ECO:0000244|PDB:4ENZ}. FT STRAND 682 687 {ECO:0000244|PDB:4ENZ}. FT STRAND 693 699 {ECO:0000244|PDB:4ENZ}. FT HELIX 702 706 {ECO:0000244|PDB:4ENZ}. FT STRAND 710 716 {ECO:0000244|PDB:4ENZ}. FT STRAND 729 745 {ECO:0000244|PDB:4ENZ}. FT HELIX 750 759 {ECO:0000244|PDB:4ENZ}. FT TURN 766 768 {ECO:0000244|PDB:4ENZ}. FT TURN 771 773 {ECO:0000244|PDB:4ENZ}. FT STRAND 777 789 {ECO:0000244|PDB:4ENZ}. FT HELIX 800 805 {ECO:0000244|PDB:4ENZ}. FT STRAND 812 815 {ECO:0000244|PDB:4ENZ}. FT STRAND 818 826 {ECO:0000244|PDB:4ENZ}. FT STRAND 828 830 {ECO:0000244|PDB:4ENZ}. FT STRAND 835 838 {ECO:0000244|PDB:4ENZ}. FT STRAND 842 844 {ECO:0000244|PDB:1KCW}. FT STRAND 854 860 {ECO:0000244|PDB:4ENZ}. FT HELIX 863 865 {ECO:0000244|PDB:4ENZ}. FT STRAND 869 871 {ECO:0000244|PDB:1KCW}. FT STRAND 873 880 {ECO:0000244|PDB:4ENZ}. FT HELIX 885 890 {ECO:0000244|PDB:4ENZ}. FT STRAND 894 900 {ECO:0000244|PDB:4ENZ}. FT STRAND 913 924 {ECO:0000244|PDB:4ENZ}. FT HELIX 925 927 {ECO:0000244|PDB:4ENZ}. FT HELIX 931 938 {ECO:0000244|PDB:4ENZ}. FT HELIX 942 944 {ECO:0000244|PDB:4ENZ}. FT HELIX 950 955 {ECO:0000244|PDB:4ENZ}. FT STRAND 957 961 {ECO:0000244|PDB:4ENZ}. FT STRAND 973 975 {ECO:0000244|PDB:4ENZ}. FT STRAND 979 986 {ECO:0000244|PDB:4ENZ}. FT STRAND 994 998 {ECO:0000244|PDB:4ENZ}. FT STRAND 1003 1006 {ECO:0000244|PDB:4ENZ}. FT HELIX 1007 1009 {ECO:0000244|PDB:4ENZ}. FT STRAND 1011 1018 {ECO:0000244|PDB:4ENZ}. FT STRAND 1023 1028 {ECO:0000244|PDB:4ENZ}. FT STRAND 1034 1040 {ECO:0000244|PDB:4ENZ}. FT HELIX 1043 1047 {ECO:0000244|PDB:4ENZ}. FT STRAND 1051 1057 {ECO:0000244|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 //