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Ceruloplasmin (EC 1.16.3.1) (Ferroxidase)

 CERU_RAT                Reviewed;        1059 AA.
P13635; Q64719;
01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
01-NOV-1997, sequence version 3.
22-NOV-2017, entry version 129.
RecName: Full=Ceruloplasmin;
EC=1.16.3.1;
AltName: Full=Ferroxidase;
Flags: Precursor;
Name=Cp;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
STRAIN=Sprague-Dawley; TISSUE=Liver, and Lung;
PubMed=2332446;
Fleming R.E., Gitlin J.D.;
"Primary structure of rat ceruloplasmin and analysis of tissue-
specific gene expression during development.";
J. Biol. Chem. 265:7701-7707(1990).
[2]
NUCLEOTIDE SEQUENCE [MRNA] OF 257-294; 571-612 AND 823-892.
TISSUE=Liver;
PubMed=3818625;
Aldred A.R., Grimes A., Schreiber G., Mercer J.F.B.;
"Rat ceruloplasmin. Molecular cloning and gene expression in liver,
choroid plexus, yolk sac, placenta, and testis.";
J. Biol. Chem. 262:2875-2878(1987).
[3]
COPPER-BINDING, FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=14707133; DOI=10.1074/jbc.M313678200;
Mani K., Cheng F., Havsmark B., David S., Fransson L.A.;
"Involvement of glycosylphosphatidylinositol-linked ceruloplasmin in
the copper/zinc-nitric oxide-dependent degradation of glypican-1
heparan sulfate in rat C6 glioma cells.";
J. Biol. Chem. 279:12918-12923(2004).
-!- 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. May also play
a role in fetal lung development or pulmonary antioxidant defense.
involved in iron transport across the cell membrane (By
similarity). Provides Cu(2+) ions for the ascorbate-mediated
deaminase degradation of the heparan sulfate chains of GPC1.
{ECO:0000250, ECO:0000269|PubMed:14707133}.
-!- CATALYTIC ACTIVITY: 4 Fe(2+) + 4 H(+) + O(2) = 4 Fe(3+) + 2 H(2)O.
-!- COFACTOR:
Name=Cu cation; Xref=ChEBI:CHEBI:23378;
Note=Binds 6 Cu cations per monomer.;
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:14707133}.
Note=Colocalizes with GCP1 in secretory intracellular
compartments.
-!- TISSUE SPECIFICITY: Synthesized in liver and secreted into the
plasma. Also choroid plexus, yolk sac, placenta, and testis; not
in stomach and small intestine. Fetal lung and liver.
-!- INDUCTION: By inflammation.
-!- SIMILARITY: Belongs to the multicopper oxidase family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAA40914.1; Type=Miscellaneous discrepancy; Note=Wrong order of assembly of the mRNA fragments.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; L33869; AAA40917.1; -; mRNA.
EMBL; M80529; AAB65820.1; -; Genomic_DNA.
EMBL; J02670; AAA40914.1; ALT_SEQ; mRNA.
EMBL; M14102; AAA40915.1; -; mRNA.
PIR; A35210; A35210.
UniGene; Rn.32777; -.
ProteinModelPortal; P13635; -.
SMR; P13635; -.
IntAct; P13635; 1.
STRING; 10116.ENSRNOP00000016083; -.
iPTMnet; P13635; -.
PhosphoSitePlus; P13635; -.
PaxDb; P13635; -.
PRIDE; P13635; -.
UCSC; RGD:2387; rat.
RGD; 2387; Cp.
eggNOG; KOG1263; Eukaryota.
eggNOG; COG2132; LUCA.
HOGENOM; HOG000231499; -.
HOVERGEN; HBG003674; -.
InParanoid; P13635; -.
PRO; PR:P13635; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0046658; C:anchored component of plasma membrane; IDA:RGD.
GO; GO:0072562; C:blood microparticle; ISO:RGD.
GO; GO:0070062; C:extracellular exosome; ISO:RGD.
GO; GO:0005615; C:extracellular space; IDA:RGD.
GO; GO:0005765; C:lysosomal membrane; ISO:RGD.
GO; GO:0051087; F:chaperone binding; ISO:RGD.
GO; GO:0005507; F:copper ion binding; IDA:RGD.
GO; GO:0004322; F:ferroxidase activity; ISO:RGD.
GO; GO:0007568; P:aging; IEP:RGD.
GO; GO:0006879; P:cellular iron ion homeostasis; TAS:RGD.
GO; GO:0001889; P:liver development; IEP:RGD.
GO; GO:0030324; P:lung development; IEP:RGD.
GO; GO:0015679; P:plasma membrane copper ion transport; TAS:RGD.
GO; GO:0046688; P:response to copper ion; IDA:RGD.
GO; GO:0007584; P:response to nutrient; IEP:RGD.
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.
InterPro; IPR024715; Factor_5/8_like.
PANTHER; PTHR44048:SF5; PTHR44048:SF5; 1.
Pfam; PF00394; Cu-oxidase; 1.
Pfam; PF07731; Cu-oxidase_2; 1.
Pfam; PF07732; Cu-oxidase_3; 3.
PIRSF; PIRSF000354; Factors_V_VIII; 1.
SUPFAM; SSF49503; SSF49503; 6.
PROSITE; PS00079; MULTICOPPER_OXIDASE1; 3.
PROSITE; PS00080; MULTICOPPER_OXIDASE2; 1.
1: Evidence at protein level;
Complete proteome; Copper; Copper transport; Disulfide bond;
Glycoprotein; Ion transport; Metal-binding; Oxidoreductase;
Reference proteome; Repeat; Secreted; Signal; Transport.
SIGNAL 1 19 {ECO:0000305}.
CHAIN 20 1059 Ceruloplasmin.
/FTId=PRO_0000002914.
DOMAIN 20 356 F5/8 type A 1.
DOMAIN 20 199 Plastocyanin-like 1.
DOMAIN 208 354 Plastocyanin-like 2.
DOMAIN 369 712 F5/8 type A 2.
DOMAIN 369 554 Plastocyanin-like 3.
DOMAIN 564 710 Plastocyanin-like 4.
DOMAIN 724 1055 F5/8 type A 3.
DOMAIN 724 894 Plastocyanin-like 5.
DOMAIN 902 1051 Plastocyanin-like 6.
METAL 120 120 Copper 1; type 2. {ECO:0000250}.
METAL 122 122 Copper 2; type 3. {ECO:0000250}.
METAL 179 179 Copper 2; type 3. {ECO:0000250}.
METAL 181 181 Copper 3; type 3. {ECO:0000250}.
METAL 294 294 Copper 4; type 1. {ECO:0000250}.
METAL 337 337 Copper 4; type 1. {ECO:0000250}.
METAL 342 342 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 988 988 Copper 6; type 1. {ECO:0000250}.
METAL 991 991 Copper 1; type 2. {ECO:0000250}.
METAL 993 993 Copper 3; type 3. {ECO:0000250}.
METAL 1033 1033 Copper 3; type 3. {ECO:0000250}.
METAL 1034 1034 Copper 6; type 1. {ECO:0000250}.
METAL 1035 1035 Copper 2; type 3. {ECO:0000250}.
METAL 1039 1039 Copper 6; type 1. {ECO:0000250}.
METAL 1044 1044 Copper 6; type 1. {ECO:0000250}.
CARBOHYD 138 138 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 226 226 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 396 396 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}.
DISULFID 173 199 {ECO:0000250}.
DISULFID 275 356 {ECO:0000250}.
DISULFID 528 554 {ECO:0000250}.
DISULFID 631 712 {ECO:0000250}.
DISULFID 868 894 {ECO:0000250}.
CONFLICT 271 271 G -> A (in Ref. 2; AAA40914).
{ECO:0000305}.
CONFLICT 604 605 ED -> DN (in Ref. 2; AAA40914).
{ECO:0000305}.
CONFLICT 823 823 T -> S (in Ref. 2; AAA40915).
{ECO:0000305}.
CONFLICT 833 833 V -> L (in Ref. 2; AAA40915).
{ECO:0000305}.
CONFLICT 868 868 C -> V (in Ref. 2; AAA40915).
{ECO:0000305}.
CONFLICT 891 891 L -> R (in Ref. 2; AAA40915).
{ECO:0000305}.
SEQUENCE 1059 AA; 120841 MW; 12BA3B990A0B95E3 CRC64;
MKFLLLSALL FLHSSLAWTR EKHYYIGITE AVWDYASGSE EKELISVDTE QSNFYLRNGP
DRIGRKYKKA LYSEYTDGTF TKTIDKPAWL GFLGPVIKAE VGDKVSVHVK NFASRPYTFH
AHGVTYTKAN EGAIYPDNTT DFQRADDKLF PGQQYLYVLR ANEPSPGEGD SNCVTRIYHS
HVDAPKDIAS GLIGPLILCK KGSLHKEKEE NIDQEFVLMF SVVDENLSWY LEDNIKTFCS
EPEKVDKDNE DFQESNRMYS INGYTFGSLP GLSMCAEDRV KWYLFGMGNE VDVHSELFHG
QALTSKNYHT DIINLFPATL IDVSMVAQNP GVWMLSCQNL NHLKAGLQAF FQVRDCNKPS
PDDDIQDRHV RHYYIAAEET IWDYAPSGTD TFTGENFTSL GSDSRVFFEQ GATRIGGSYK
KLVYREYTDD SFTNRKERGP DEEHLGILGP VIWAEVGDII RVTFHNKGQF PLSIQPMGVR
FTKENEGTYY GPDGRSSKQA SHVAPKETFT YEWTVPKEMG PTYADPVCLS KMYYSGVDLT
KDIFTGLIGP MKICKKGSLL ADGRQKDVDK EFYLFATVFD ENESLLLDDN IRMFTTAPEN
VDKEDEDFQE SNKMHSMNGF MYGNLPGLNM CLGESIVWYL FSAGNEADVH GIYFSGNTYL
SKGERRDTAN LFPHKSLTLL MTPDTEGSFD VECLTTDHYT GGMKQKYTVN QCKGQFEDVT
LYQGERTYYI AAVEVEWDYS PSRDWEMELH HLQEQNVSNA FLDKEEFFIG SKYKKVVYRE
FTDSTFREQV KRRAEEEHLG MLGPLIHADV GAKVKVVFKN MATRPYSIHA HGVKTKSSTV
APTLPGEVRT YIWQIPERSG AGTEDSPCIP WAYYSTVDRV KDLYSGLIGP LIVCRKSYVK
VFNPKKKMEF SLLFLVFDEN ESWYLDDNIN TYPDHPEKDN KDNEEFIESN KMHAINGKMF
GNLQGLTMHV GDEVNWYVMA MGNEIDLHTV HFHGHSFQYK HRGIHSSDVF DFFPGTYQTL
EMFPQTPGTW LLHCHVTDHI HAGMVTTYTV LPNQETKSG


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