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Ceruloplasmin (EC 1.16.3.1) (Ferroxidase)

 CERU_MOUSE              Reviewed;        1061 AA.
Q61147; Q6P5C8;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
04-DEC-2007, sequence version 2.
20-JUN-2018, entry version 146.
RecName: Full=Ceruloplasmin;
EC=1.16.3.1;
AltName: Full=Ferroxidase;
Flags: Precursor;
Name=Cp;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
PubMed=8690795; DOI=10.1172/JCI118768;
Klomp L.W.J., Farhangrazi Z.S., Dugan L.L., Gitlin J.D.;
"Ceruloplasmin gene expression in the murine central nervous system.";
J. Clin. Invest. 98:207-215(1996).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Eye;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[3]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-138 AND ASN-757.
STRAIN=C57BL/6J; TISSUE=Plasma;
PubMed=16944957; DOI=10.1021/pr060186m;
Ghesquiere B., Van Damme J., Martens L., Vandekerckhove J.,
Gevaert K.;
"Proteome-wide characterization of N-glycosylation events by diagonal
chromatography.";
J. Proteome Res. 5:2438-2447(2006).
[4]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-138 AND ASN-757.
STRAIN=C57BL/6J; TISSUE=Plasma;
PubMed=17330941; DOI=10.1021/pr0604559;
Bernhard O.K., Kapp E.A., Simpson R.J.;
"Enhanced analysis of the mouse plasma proteome using cysteine-
containing tryptic glycopeptides.";
J. Proteome Res. 6:987-995(2007).
[5]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
Pancreas, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- 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. Provides
Cu(2+) ions for the ascorbate-mediated deaminase degradation of
the heparan sulfate chains of GPC1. May also play a role in fetal
lung development or pulmonary antioxidant defense (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. Note=Colocalizes with GCP1 in
secretory intracellular compartments. {ECO:0000250}.
-!- TISSUE SPECIFICITY: Expressed in many tissues, including liver,
eye and brain. {ECO:0000269|PubMed:8690795}.
-!- SIMILARITY: Belongs to the multicopper oxidase family.
{ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; U49430; AAB07996.1; -; mRNA.
EMBL; BC062957; AAH62957.1; -; mRNA.
CCDS; CCDS38401.1; -.
RefSeq; NP_001263177.1; NM_001276248.1.
RefSeq; NP_031778.2; NM_007752.3.
UniGene; Mm.13787; -.
ProteinModelPortal; Q61147; -.
SMR; Q61147; -.
BioGrid; 198851; 1.
IntAct; Q61147; 6.
MINT; Q61147; -.
STRING; 10090.ENSMUSP00000103965; -.
GlyConnect; 689; -.
iPTMnet; Q61147; -.
PhosphoSitePlus; Q61147; -.
SwissPalm; Q61147; -.
MaxQB; Q61147; -.
PaxDb; Q61147; -.
PeptideAtlas; Q61147; -.
PRIDE; Q61147; -.
Ensembl; ENSMUST00000091309; ENSMUSP00000088857; ENSMUSG00000003617.
GeneID; 12870; -.
KEGG; mmu:12870; -.
UCSC; uc008orz.2; mouse.
CTD; 1356; -.
MGI; MGI:88476; Cp.
eggNOG; KOG1263; Eukaryota.
eggNOG; COG2132; LUCA.
GeneTree; ENSGT00910000143988; -.
HOGENOM; HOG000231499; -.
HOVERGEN; HBG003674; -.
InParanoid; Q61147; -.
KO; K13624; -.
PhylomeDB; Q61147; -.
TreeFam; TF329807; -.
BRENDA; 1.16.3.1; 3474.
Reactome; R-MMU-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
Reactome; R-MMU-425410; Metal ion SLC transporters.
Reactome; R-MMU-8957275; Post-translational protein phosphorylation.
Reactome; R-MMU-917937; Iron uptake and transport.
ChiTaRS; Cp; mouse.
PRO; PR:Q61147; -.
Proteomes; UP000000589; Chromosome 3.
Bgee; ENSMUSG00000003617; -.
CleanEx; MM_CP; -.
ExpressionAtlas; Q61147; baseline and differential.
Genevisible; Q61147; MM.
GO; GO:0046658; C:anchored component of plasma membrane; ISO:MGI.
GO; GO:0005615; C:extracellular space; IDA:MGI.
GO; GO:0051087; F:chaperone binding; ISO:MGI.
GO; GO:0005507; F:copper ion binding; IDA:MGI.
GO; GO:0004322; F:ferroxidase activity; IDA:MGI.
GO; GO:0006879; P:cellular iron ion homeostasis; IEA:InterPro.
GO; GO:0006825; P:copper ion transport; IEA:UniProtKB-KW.
GO; GO:0046688; P:response to copper ion; ISO:MGI.
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:0000250}.
CHAIN 20 1061 Ceruloplasmin.
/FTId=PRO_0000002913.
DOMAIN 20 356 F5/8 type A 1.
DOMAIN 20 199 Plastocyanin-like 1.
DOMAIN 208 356 Plastocyanin-like 2.
DOMAIN 369 713 F5/8 type A 2.
DOMAIN 369 555 Plastocyanin-like 3.
DOMAIN 565 713 Plastocyanin-like 4.
DOMAIN 725 1056 F5/8 type A 3.
DOMAIN 725 895 Plastocyanin-like 5.
DOMAIN 903 1056 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 651 651 Copper 5; type 1. {ECO:0000250}.
METAL 694 694 Copper 5; type 1. {ECO:0000250}.
METAL 699 699 Copper 5; type 1. {ECO:0000250}.
METAL 704 704 Copper 5; type 1. {ECO:0000250}.
METAL 989 989 Copper 6; type 1. {ECO:0000250}.
METAL 992 992 Copper 1; type 2. {ECO:0000250}.
METAL 994 994 Copper 3; type 3. {ECO:0000250}.
METAL 1034 1034 Copper 3; type 3. {ECO:0000250}.
METAL 1035 1035 Copper 6; type 1. {ECO:0000250}.
METAL 1036 1036 Copper 2; type 3. {ECO:0000250}.
METAL 1040 1040 Copper 6; type 1. {ECO:0000250}.
METAL 1045 1045 Copper 6; type 1. {ECO:0000250}.
CARBOHYD 138 138 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:16944957,
ECO:0000269|PubMed:17330941}.
CARBOHYD 226 226 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 396 396 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 583 583 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 757 757 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:16944957,
ECO:0000269|PubMed:17330941}.
CARBOHYD 921 921 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 173 199 {ECO:0000250}.
DISULFID 275 356 {ECO:0000250}.
DISULFID 529 555 {ECO:0000250}.
DISULFID 632 713 {ECO:0000250}.
DISULFID 869 895 {ECO:0000250}.
CONFLICT 354 354 R -> Q (in Ref. 1; AAB07996).
{ECO:0000305}.
CONFLICT 361 362 PE -> SK (in Ref. 1; AAB07996).
{ECO:0000305}.
CONFLICT 366 368 QDR -> RGK (in Ref. 1; AAB07996).
{ECO:0000305}.
CONFLICT 389 389 T -> I (in Ref. 1; AAB07996).
{ECO:0000305}.
CONFLICT 394 396 GEN -> EEK (in Ref. 1; AAB07996).
{ECO:0000305}.
CONFLICT 400 401 LE -> SG (in Ref. 1; AAB07996).
{ECO:0000305}.
CONFLICT 405 405 R -> G (in Ref. 1; AAB07996).
{ECO:0000305}.
CONFLICT 437 437 Q -> E (in Ref. 1; AAB07996).
{ECO:0000305}.
CONFLICT 471 471 P -> H (in Ref. 1; AAB07996).
{ECO:0000305}.
CONFLICT 495 495 R -> A (in Ref. 1; AAB07996).
{ECO:0000305}.
CONFLICT 537 537 G -> A (in Ref. 1; AAB07996).
{ECO:0000305}.
CONFLICT 597 597 T -> H (in Ref. 1; AAB07996).
{ECO:0000305}.
CONFLICT 627 630 PGLN -> SWPH (in Ref. 1; AAB07996).
{ECO:0000305}.
CONFLICT 662 662 S -> C (in Ref. 1; AAB07996).
{ECO:0000305}.
CONFLICT 666 666 R -> E (in Ref. 1; AAB07996).
{ECO:0000305}.
CONFLICT 732 732 A -> D (in Ref. 1; AAB07996).
{ECO:0000305}.
CONFLICT 796 796 E -> EE (in Ref. 1; AAB07996).
{ECO:0000305}.
CONFLICT 850 850 R -> A (in Ref. 1; AAB07996).
{ECO:0000305}.
CONFLICT 979 979 V -> L (in Ref. 1; AAB07996).
{ECO:0000305}.
SEQUENCE 1061 AA; 121151 MW; 16A2DAEA4F483886 CRC64;
MKFLLLSTFI FLYSSLALAR DKHYFIGITE AVWDYASGTE EKKLISVDTE QSNFYLQNGP
DRIGRKYKKA LYFEYTDGTF SKTIDKPAWL GFLGPVIKAE VEDKVYVHLK NLASRIYTFH
AHGVTYTKEY EGAVYPDNTT DFQRADDKVL PGQQYVYVLH ANEPSPGEGD SNCVTRIYHS
HVDAPKDIAS GLIGPLILCK KGSLYKEKEK NIDQEFVLMF SVVDENLSWY LEDNIKTFCS
EPEKVDKDNE DFQESNRMYS INGYTFGSLP GLSMCAADRV KWYLFGMGNE VDVHSAFFHG
QALTSRNYQT DIINLFPATL IDAYMVAQNP GVWMLSCQNL NHLKAGLQAF FQVRDCNKPS
PEDNIQDRHV RHYYIAAEEV IWNYAPSGTD IFTGENLTAL ESDSRVFFEQ GATRIGGSYK
KMAYREYTDG SFTNRKQRGP DEEHLGILGP VIWAEVGDTI KVTFHNKGQH PLSIQPMGVS
FTAENEGTYY GPPGRSSQQA ASHVAPKETF TYEWTVPKEM GPTYADPVCL SKMYYSGVDP
TKDIFTGLIG PMKICKKGSL LADGRQKDVD KEFYLFPTVF DENESLLLDD NIRMFTTAPD
QVDKEDEDFQ ESNKMHSMNG FMYGNQPGLN MCLGESIVWY LFSAGNEADV HGIYFSGNTY
LSKGERRDTA NLFPHKSLTL LMNPDTKGTF DVECLTTDHY TGGMKQKYTV NQCQRQFEDF
TVYLGERTYY VAAVEVEWDY SPSRAWEKEL HHLQEQNVSN VFLDKEEFFI GSKYKKVVYR
QFTDSSFREQ VKRRAEDEHL GILGPPIHAN VGDKVKVVFK NMATRPYSIH AHGVKTESST
VVPTLPGEVR TYTWQIPERS GAGREDSACI PWAYYSTVDR VKDLYSGLIG PLIVCRKSYV
KVFSPKKKME FFLLFLVFDE NESWYLDDNI KTYSEHPEKV NKDNEEFLES NKMHAINGKM
FGNLQGLTMH VKDEVNWYVM GMGNEIDLHT VHFHGHSFQY KHRGVYSSDV FDLFPGTYQT
LEMFPQTPGT WLLHCHVTDH VHAGMATTYT VLPVEQETKS G


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