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Ceruloplasmin (EC 1.16.3.1) (Ferroxidase)

 CERU_SHEEP              Reviewed;        1048 AA.
Q9XT27;
21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
01-NOV-1999, sequence version 1.
25-OCT-2017, entry version 77.
RecName: Full=Ceruloplasmin;
EC=1.16.3.1;
AltName: Full=Ferroxidase;
Flags: Precursor;
Name=CP;
Ovis aries (Sheep).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
Pecora; Bovidae; Caprinae; Ovis.
NCBI_TaxID=9940;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
TISSUE=Liver;
PubMed=10452945; DOI=10.1016/S0378-1119(99)00276-0;
Lockhart P.J., Mercer J.F.B.;
"Cloning and expression analysis of the sheep ceruloplasmin cDNA.";
Gene 236:251-257(1999).
-!- 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 (By
similarity). {ECO:0000250}.
-!- CATALYTIC ACTIVITY: 4 Fe(2+) + 4 H(+) + O(2) = 4 Fe(3+) + 2 H(2)O.
-!- COFACTOR:
Name=Cu cation; Xref=ChEBI:CHEBI:23378; Evidence={ECO:0000250};
Note=Binds 6 Cu cations per monomer. {ECO:0000250};
-!- SUBCELLULAR LOCATION: Secreted.
-!- TISSUE SPECIFICITY: Expressed by the liver and secreted in plasma.
Also expressed in the hypothalamus, spleen and uterus. No
expression in the cortex, heart, intestine or kidney.
{ECO:0000269|PubMed:10452945}.
-!- SIMILARITY: Belongs to the multicopper oxidase family.
{ECO:0000305}.
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EMBL; AF134814; AAD41477.1; -; mRNA.
RefSeq; NP_001009733.1; NM_001009733.1.
UniGene; Oar.706; -.
ProteinModelPortal; Q9XT27; -.
SMR; Q9XT27; -.
PRIDE; Q9XT27; -.
GeneID; 443053; -.
KEGG; oas:443053; -.
CTD; 1356; -.
HOVERGEN; HBG003674; -.
KO; K13624; -.
Proteomes; UP000002356; Unplaced.
GO; GO:0005623; C:cell; IEA:GOC.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0005507; F:copper ion binding; IEA:InterPro.
GO; GO:0004322; F:ferroxidase activity; IEA:UniProtKB-EC.
GO; GO:0006879; P:cellular iron ion homeostasis; IEA:InterPro.
GO; GO:0006825; P:copper ion transport; IEA:UniProtKB-KW.
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; 3.
SUPFAM; SSF49503; SSF49503; 6.
PROSITE; PS00079; MULTICOPPER_OXIDASE1; 3.
PROSITE; PS00080; MULTICOPPER_OXIDASE2; 1.
2: Evidence at transcript level;
Complete proteome; Copper; Copper transport; Glycoprotein;
Ion transport; Metal-binding; Oxidoreductase; Phosphoprotein;
Reference proteome; Repeat; Secreted; Signal; Transport.
SIGNAL 1 19 {ECO:0000255}.
CHAIN 20 1048 Ceruloplasmin.
/FTId=PRO_0000227940.
DOMAIN 20 357 F5/8 type A 1.
DOMAIN 20 200 Plastocyanin-like 1.
DOMAIN 209 355 Plastocyanin-like 2.
DOMAIN 370 712 F5/8 type A 2.
DOMAIN 370 554 Plastocyanin-like 3.
DOMAIN 564 710 Plastocyanin-like 4.
DOMAIN 724 1044 F5/8 type A 3.
DOMAIN 724 894 Plastocyanin-like 5.
DOMAIN 902 1040 Plastocyanin-like 6.
METAL 120 120 Copper 1; type 2. {ECO:0000250}.
METAL 122 122 Copper 2; type 3. {ECO:0000250}.
METAL 180 180 Copper 2; type 3. {ECO:0000250}.
METAL 182 182 Copper 3; type 3. {ECO:0000250}.
METAL 295 295 Copper 4; type 1. {ECO:0000250}.
METAL 338 338 Copper 4; type 1. {ECO:0000250}.
METAL 343 343 Copper 4; type 1. {ECO:0000250}.
METAL 650 650 Copper 5; type 1. {ECO:0000250}.
METAL 693 693 Copper 5; type 1. {ECO:0000250}.
METAL 698 698 Copper 5; type 1. {ECO:0000250}.
METAL 703 703 Copper 5; type 1. {ECO:0000250}.
METAL 977 977 Copper 6; type 1. {ECO:0000250}.
METAL 980 980 Copper 1; type 2. {ECO:0000250}.
METAL 982 982 Copper 3; type 3. {ECO:0000250}.
METAL 1022 1022 Copper 3; type 3. {ECO:0000250}.
METAL 1023 1023 Copper 6; type 1. {ECO:0000250}.
METAL 1024 1024 Copper 2; type 3. {ECO:0000250}.
METAL 1028 1028 Copper 6; type 1. {ECO:0000250}.
METAL 1033 1033 Copper 6; type 1. {ECO:0000250}.
MOD_RES 716 716 Phosphoserine.
{ECO:0000250|UniProtKB:P00450}.
CARBOHYD 138 138 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 227 227 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 556 556 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 582 582 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 756 756 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 920 920 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
SEQUENCE 1048 AA; 119126 MW; 925F16D7B0549CBB CRC64;
MKIFLLCIFL ILCGTSVWAK DKHYYIGIIE TAWNYASDHA EKKLISVDTE HSNIYLQNGP
NRIGSVYKKA VYLQYTDENF RTVIEKPVWL GFLGPIIKAE TGDKVYVHLK NFASRPYTFH
AHGLTYYKEH EGAIYPDNTT DLQKADDKVQ PGEQCLYILH ANPEQGPGEE DSNCVTRIYH
SHIDAPKDIA SGLIGPLIHC KKDSLDEEKE KNIDKEFVVM FSVVDENLSW YLEENIKTYC
SEPEKVEQDN EDFQESNRMY SVNGYAFGSL PGLSMCAEDR VKWYLFGMGN EIDVHAAFFH
GQVLTSKNYR VDTINLFPAT LFDAFMVAQN PGQWMLSCQN LNHLKAGLQA FFWVQDCKKS
SSEDNIHGKN VRHYYIAAEE VIWNYAPSGI DAFTKENLRA PGSASEAFFE QGPTRIGGSY
KKLVYREYTD ASFSNQKERG PEEEHLGILG PVIAAEVGDT IRVTFHNKAA HPLSIEPIGV
RVDKNNEGTY YSPTGSGPPP SGSHVAPKGT FTYEWTVPKE VGPTYKDPVC LAKMYYSGST
KDIFTGLIGP MKICRNGSLL ANGRLKNVDK EFYLFPTVFD ENESLLLDDN IKMFTTAPDQ
VDKENEDFQE SNKMHSMNGF MYGNQPGLSM CQGDSVMWYL FSAGNEVDIH GIYFSGNTYL
SRGERRDTAN LFPQTSLSLF MQPDTAGTFD VECLTTDHYT GGMKQKYTVS QCGQRSEDLY
LYLGERTYYI AAVEVEWDYS PSRKWEKELH HLQEQNLSNA FLDKEEFYIG SKYKKVVYRQ
FTDSTFQVPV ERKGEEEHLG ILGPQLHADV GDKVNIIFKN MATRPYSIHA HGVKTESSTV
TPTAPGETRT YIWKIPERSG AGMGDSPCIP WVYYSTVDRV KDLFSGLIGP LIVCRKHYLK
VSNPIKKLEF SLLFLVFDEN ESWYLDDNIK TYSDHPEKVD KANEEFMESN KMHAINGRMF
GNLQGLTMHV GNEVDLHSVH FHGHSFQYQH RGIYTSDVFD LFPGTYQTLE MTPKTPGIWL
LHCHVTDHIH AGMETTYTVL PNEEIKSG


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