ID CERU_HUMAN STANDARD; PRT; 1065 AA. AC P00450; Q14063; DT 21-JUL-1986 (Rel. 01, Created) DT 13-AUG-1987 (Rel. 05, Last sequence update) DT 30-MAY-2000 (Rel. 39, Last annotation update) DE Ceruloplasmin precursor (EC 1.16.3.1) (Ferroxidase). GN CP. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=86259737; PubMed=2873574; 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 SEQUENCE OF 1-1006 FROM N.A. RX MEDLINE=95217183; PubMed=7702601; RA Daimon M., Yamatani K., Igarashi M., Fukase N., Kawanami T., RA Kato T., Tominaga M., Sasaki H.; RT "Fine structure of human ceruloplasmin gene."; RL Biochem. Biophys. Res. Commun. 208:1028-1035(1995). RN [3] RP SEQUENCE OF 1-40; 549-599; 784-829 AND 919-952 FROM N.A. RX MEDLINE=86275241; PubMed=3755405; 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 [4] RP SEQUENCE OF 218-1065 FROM N.A. RX MEDLINE=86205876; PubMed=3486416; 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 [5] RP SEQUENCE OF 20-1065. RX MEDLINE=84119493; PubMed=6582496; 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 [6] RP SEQUENCE OF 158-333; 518-724 AND 858-1065. RX MEDLINE=83117800; PubMed=6571985; 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 [7] RP SEQUENCE OF 501-905. RX MEDLINE=81199407; PubMed=6940148; 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 [8] RP SEQUENCE OF 907-1065. RX MEDLINE=80137543; 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 [9] RP SEQUENCE OF 907-1065. RX MEDLINE=80137544; 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 [10] RP SEQUENCE OF 1007-1061 FROM N.A. RX MEDLINE=90285218; 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 [11] RP X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS). 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). CC -!- FUNCTION: CERULOPLASMIN IS A BLUE, COPPER-BINDING (6-7 ATOMS PER CC MOLECULE) GLYCOPROTEIN FOUND IN PLASMA. FOUR POSSIBLE FUNCTIONS CC ARE FERROXIDASE ACTIVITY, AMINE OXIDASE ACTIVITY, COPPER TRANSPORT CC AND HOMEOSTASIS, AND SUPEROXIDE DISMUTASE ACTIVITY. CC -!- CATALYTIC ACTIVITY: 4 FE(2+) + 4 H(+) + O(2) = 4 FE(3+) + 2 H(2)O. CC -!- COFACTOR: BINDS 6 CU-IONS PER MOLECULE. THIS PROTEIN BELONGS TO CC THE MULTICOPPER OXIDASES WHICH CONTAIN THREE DISTINCT CU CENTERS CC KNOWN AS TYPE 1 OR BLUE, TYPE 2 OR NORMAL, AND TYPE 3 OR COUPLED CC BINUCLEAR. CC -!- TISSUE SPECIFICITY: SYNTHESIZED IN LIVER AND SECRETED INTO THE CC PLASMA. CC -!- DISEASE: CERULOPLASMIN IS DEFICIENT IN WILSON'S DISEASE. CC -!- SIMILARITY: CONTAINS 3 F5/8 TYPE A DOMAINS; EACH IS COMPOSED OF CC 2 PLASTOCYANIN-LIKE REPEATS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M13699; AAA51976.1; -. DR EMBL; D45045; BAA08085.1; -. DR EMBL; D45044; BAA08084.1; -. DR EMBL; D45028; BAA08084.1; JOINED. DR EMBL; D45029; BAA08084.1; JOINED. DR EMBL; D45030; BAA08084.1; JOINED. DR EMBL; D45031; BAA08084.1; JOINED. DR EMBL; D45032; BAA08084.1; JOINED. DR EMBL; D45033; BAA08084.1; JOINED. DR EMBL; D45034; BAA08084.1; JOINED. DR EMBL; D45035; BAA08084.1; JOINED. DR EMBL; D45036; BAA08084.1; JOINED. DR EMBL; D45037; BAA08084.1; JOINED. DR EMBL; D45038; BAA08084.1; JOINED. DR EMBL; D45039; BAA08084.1; JOINED. DR EMBL; D45040; BAA08084.1; JOINED. DR EMBL; D45041; BAA08084.1; JOINED. DR EMBL; D45042; BAA08084.1; JOINED. DR EMBL; D45043; BAA08084.1; JOINED. DR EMBL; D00025; BAA00019.1; -. DR EMBL; X04135; CAA27752.1; -. DR EMBL; X04136; CAA27753.1; -. DR EMBL; X04137; CAA27754.1; -. DR EMBL; X04138; CAA27755.1; -. DR EMBL; M13536; AAA51975.1; -. DR EMBL; J05506; -; NOT_ANNOTATED_CDS. DR PIR; A25443; KUHU. DR PIR; A24165; A24165. DR PDB; 1KCW; 12-FEB-97. DR GlycoSuiteDB; P00450; -. DR SWISS-2DPAGE; P00450; HUMAN. DR Siena-2DPAGE; P00450; -. DR MIM; 117700; -. DR MIM; 604290; -. DR InterPro; IPR001117; Cu-oxidase. DR InterPro; IPR002355; MultiCu_oxidse2. DR Pfam; PF00394; Cu-oxidase; 3. DR PROSITE; PS00079; MULTICOPPER_OXIDASE1; 3. DR PROSITE; PS00080; MULTICOPPER_OXIDASE2; 1. KW Oxidoreductase; Copper; Metal-binding; Glycoprotein; Plasma; Repeat; KW Signal; Polymorphism; 3D-structure. FT SIGNAL 1 19 FT CHAIN 20 1065 CERULOPLASMIN. 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 CARBOHYD 138 138 N-LINKED (GLCNAC...). FT CARBOHYD 358 358 N-LINKED (GLCNAC...). FT CARBOHYD 397 397 N-LINKED (GLCNAC...). FT CARBOHYD 762 762 N-LINKED (GLCNAC...). FT DISULFID 174 200 PROBABLE. FT DISULFID 276 357 PROBABLE. FT DISULFID 534 560 PROBABLE. FT DISULFID 637 718 PROBABLE. FT DISULFID 874 900 PROBABLE. FT METAL 120 120 COPPER (TYPE 2) (BY SIMILARITY). FT METAL 122 122 COPPER (TYPE 3) (BY SIMILARITY). FT METAL 180 180 COPPER (TYPE 3) (BY SIMILARITY). FT METAL 182 182 COPPER (TYPE 3) (BY SIMILARITY). FT METAL 994 994 COPPER (TYPE 1) (BY SIMILARITY). FT METAL 997 997 COPPER (TYPE 2) (BY SIMILARITY). FT METAL 999 999 COPPER (TYPE 3) (BY SIMILARITY). FT METAL 1039 1039 COPPER (TYPE 3) (BY SIMILARITY). FT METAL 1040 1040 COPPER (TYPE 1) (BY SIMILARITY). FT METAL 1041 1041 COPPER (TYPE 3) (BY SIMILARITY). FT METAL 1045 1045 COPPER (TYPE 1) (BY SIMILARITY). FT METAL 1050 1050 COPPER (TYPE 1) (BY SIMILARITY). FT VARIANT 79 79 T -> G. FT /FTId=VAR_001043. FT VARIANT 449 449 L -> G. FT /FTId=VAR_001044. FT CONFLICT 1060 1060 E -> EGEYP (IN REF. 4). 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 //