CERU_MOUSE
ID CERU_MOUSE Reviewed; 1061 AA.
AC Q61147; Q6P5C8;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 04-DEC-2007, sequence version 2.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=Ceruloplasmin;
DE EC=1.16.3.1;
DE AltName: Full=Ferroxidase;
DE Flags: Precursor;
GN Name=Cp;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX PubMed=8690795; DOI=10.1172/jci118768;
RA Klomp L.W.J., Farhangrazi Z.S., Dugan L.L., Gitlin J.D.;
RT "Ceruloplasmin gene expression in the murine central nervous system.";
RL J. Clin. Invest. 98:207-215(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Eye;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-138 AND ASN-757.
RC STRAIN=C57BL/6J; TISSUE=Plasma;
RX PubMed=16944957; DOI=10.1021/pr060186m;
RA Ghesquiere B., Van Damme J., Martens L., Vandekerckhove J., Gevaert K.;
RT "Proteome-wide characterization of N-glycosylation events by diagonal
RT chromatography.";
RL J. Proteome Res. 5:2438-2447(2006).
RN [4]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-138 AND ASN-757.
RC STRAIN=C57BL/6J; TISSUE=Plasma;
RX PubMed=17330941; DOI=10.1021/pr0604559;
RA Bernhard O.K., Kapp E.A., Simpson R.J.;
RT "Enhanced analysis of the mouse plasma proteome using cysteine-containing
RT tryptic glycopeptides.";
RL J. Proteome Res. 6:987-995(2007).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Ceruloplasmin is a blue, copper-binding (6-7 atoms per
CC molecule) glycoprotein. It has ferroxidase activity oxidizing Fe(2+) to
CC Fe(3+) without releasing radical oxygen species. It is involved in iron
CC transport across the cell membrane. Provides Cu(2+) ions for the
CC ascorbate-mediated deaminase degradation of the heparan sulfate chains
CC of GPC1. May also play a role in fetal lung development or pulmonary
CC antioxidant defense (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4 Fe(2+) + 4 H(+) + O2 = 4 Fe(3+) + 2 H2O;
CC Xref=Rhea:RHEA:11148, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034; EC=1.16.3.1;
CC -!- COFACTOR:
CC Name=Cu cation; Xref=ChEBI:CHEBI:23378; Evidence={ECO:0000250};
CC Note=Binds 6 Cu cations per monomer. {ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Secreted. Note=Colocalizes with GCP1 in secretory
CC intracellular compartments. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in many tissues, including liver, eye and
CC brain. {ECO:0000269|PubMed:8690795}.
CC -!- SIMILARITY: Belongs to the multicopper oxidase family. {ECO:0000305}.
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DR EMBL; U49430; AAB07996.1; -; mRNA.
DR EMBL; BC062957; AAH62957.1; -; mRNA.
DR CCDS; CCDS38401.1; -.
DR RefSeq; NP_001263177.1; NM_001276248.1.
DR RefSeq; NP_031778.2; NM_007752.3.
DR AlphaFoldDB; Q61147; -.
DR SMR; Q61147; -.
DR BioGRID; 198851; 5.
DR IntAct; Q61147; 1.
DR STRING; 10090.ENSMUSP00000088857; -.
DR GlyConnect; 689; 2 N-Linked glycans (1 site).
DR GlyGen; Q61147; 6 sites, 4 N-linked glycans (1 site).
DR iPTMnet; Q61147; -.
DR PhosphoSitePlus; Q61147; -.
DR SwissPalm; Q61147; -.
DR CPTAC; non-CPTAC-3505; -.
DR CPTAC; non-CPTAC-5587; -.
DR jPOST; Q61147; -.
DR MaxQB; Q61147; -.
DR PaxDb; Q61147; -.
DR PeptideAtlas; Q61147; -.
DR PRIDE; Q61147; -.
DR ProteomicsDB; 280077; -.
DR Antibodypedia; 861; 389 antibodies from 35 providers.
DR DNASU; 12870; -.
DR Ensembl; ENSMUST00000091309; ENSMUSP00000088857; ENSMUSG00000003617.
DR GeneID; 12870; -.
DR KEGG; mmu:12870; -.
DR UCSC; uc008orz.2; mouse.
DR CTD; 1356; -.
DR MGI; MGI:88476; Cp.
DR VEuPathDB; HostDB:ENSMUSG00000003617; -.
DR eggNOG; KOG1263; Eukaryota.
DR GeneTree; ENSGT00940000155866; -.
DR InParanoid; Q61147; -.
DR OMA; VCRRHYM; -.
DR PhylomeDB; Q61147; -.
DR TreeFam; TF329807; -.
DR BRENDA; 1.16.3.1; 3474.
DR Reactome; R-MMU-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR Reactome; R-MMU-425410; Metal ion SLC transporters.
DR Reactome; R-MMU-8957275; Post-translational protein phosphorylation.
DR Reactome; R-MMU-917937; Iron uptake and transport.
DR BioGRID-ORCS; 12870; 1 hit in 76 CRISPR screens.
DR ChiTaRS; Cp; mouse.
DR PRO; PR:Q61147; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q61147; protein.
DR Bgee; ENSMUSG00000003617; Expressed in left lobe of liver and 194 other tissues.
DR ExpressionAtlas; Q61147; baseline and differential.
DR Genevisible; Q61147; MM.
DR GO; GO:0046658; C:anchored component of plasma membrane; ISO:MGI.
DR GO; GO:0005615; C:extracellular space; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0051087; F:chaperone binding; ISO:MGI.
DR GO; GO:0005507; F:copper ion binding; IDA:MGI.
DR GO; GO:0004322; F:ferroxidase activity; IDA:MGI.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0006825; P:copper ion transport; IEA:UniProtKB-KW.
DR GO; GO:0055072; P:iron ion homeostasis; IBA:GO_Central.
DR GO; GO:0006826; P:iron ion transport; IBA:GO_Central.
DR GO; GO:0046688; P:response to copper ion; ISO:MGI.
DR Gene3D; 2.60.40.420; -; 5.
DR InterPro; IPR001117; Cu-oxidase.
DR InterPro; IPR011706; Cu-oxidase_C.
DR InterPro; IPR045087; Cu-oxidase_fam.
DR InterPro; IPR011707; Cu-oxidase_N.
DR InterPro; IPR033138; Cu_oxidase_CS.
DR InterPro; IPR002355; Cu_oxidase_Cu_BS.
DR InterPro; IPR008972; Cupredoxin.
DR InterPro; IPR024715; Factor_5/8-like.
DR PANTHER; PTHR11709; PTHR11709; 3.
DR Pfam; PF00394; Cu-oxidase; 1.
DR Pfam; PF07731; Cu-oxidase_2; 1.
DR Pfam; PF07732; Cu-oxidase_3; 3.
DR PIRSF; PIRSF000354; Factors_V_VIII; 1.
DR SUPFAM; SSF49503; SSF49503; 6.
DR PROSITE; PS00079; MULTICOPPER_OXIDASE1; 3.
DR PROSITE; PS00080; MULTICOPPER_OXIDASE2; 1.
PE 1: Evidence at protein level;
KW Copper; Copper transport; Disulfide bond; Glycoprotein; Ion transport;
KW Metal-binding; Oxidoreductase; Reference proteome; Repeat; Secreted;
KW Signal; Transport.
FT SIGNAL 1..19
FT /evidence="ECO:0000250"
FT CHAIN 20..1061
FT /note="Ceruloplasmin"
FT /id="PRO_0000002913"
FT DOMAIN 20..356
FT /note="F5/8 type A 1"
FT DOMAIN 20..199
FT /note="Plastocyanin-like 1"
FT DOMAIN 208..356
FT /note="Plastocyanin-like 2"
FT DOMAIN 369..713
FT /note="F5/8 type A 2"
FT DOMAIN 369..555
FT /note="Plastocyanin-like 3"
FT DOMAIN 565..713
FT /note="Plastocyanin-like 4"
FT DOMAIN 725..1056
FT /note="F5/8 type A 3"
FT DOMAIN 725..895
FT /note="Plastocyanin-like 5"
FT DOMAIN 903..1056
FT /note="Plastocyanin-like 6"
FT BINDING 120
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="1"
FT /note="type 2 copper site"
FT /evidence="ECO:0000250"
FT BINDING 122
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="2"
FT /note="type 3 copper site"
FT /evidence="ECO:0000250"
FT BINDING 179
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="2"
FT /note="type 3 copper site"
FT /evidence="ECO:0000250"
FT BINDING 181
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="3"
FT /note="type 3 copper site"
FT /evidence="ECO:0000250"
FT BINDING 294
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="4"
FT /note="type 1 copper site"
FT /evidence="ECO:0000250"
FT BINDING 337
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="4"
FT /note="type 1 copper site"
FT /evidence="ECO:0000250"
FT BINDING 342
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="4"
FT /note="type 1 copper site"
FT /evidence="ECO:0000250"
FT BINDING 651
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="5"
FT /note="type 1 copper site"
FT /evidence="ECO:0000250"
FT BINDING 694
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="5"
FT /note="type 1 copper site"
FT /evidence="ECO:0000250"
FT BINDING 699
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="5"
FT /note="type 1 copper site"
FT /evidence="ECO:0000250"
FT BINDING 704
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="5"
FT /note="type 1 copper site"
FT /evidence="ECO:0000250"
FT BINDING 989
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="6"
FT /note="type 1 copper site"
FT /evidence="ECO:0000250"
FT BINDING 992
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="1"
FT /note="type 2 copper site"
FT /evidence="ECO:0000250"
FT BINDING 994
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="3"
FT /note="type 3 copper site"
FT /evidence="ECO:0000250"
FT BINDING 1034
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="3"
FT /note="type 3 copper site"
FT /evidence="ECO:0000250"
FT BINDING 1035
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="6"
FT /note="type 1 copper site"
FT /evidence="ECO:0000250"
FT BINDING 1036
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="2"
FT /note="type 3 copper site"
FT /evidence="ECO:0000250"
FT BINDING 1040
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="6"
FT /note="type 1 copper site"
FT /evidence="ECO:0000250"
FT BINDING 1045
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="6"
FT /note="type 1 copper site"
FT /evidence="ECO:0000250"
FT CARBOHYD 138
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16944957,
FT ECO:0000269|PubMed:17330941"
FT CARBOHYD 226
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 396
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 583
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 757
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16944957,
FT ECO:0000269|PubMed:17330941"
FT CARBOHYD 921
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 173..199
FT /evidence="ECO:0000250"
FT DISULFID 275..356
FT /evidence="ECO:0000250"
FT DISULFID 529..555
FT /evidence="ECO:0000250"
FT DISULFID 632..713
FT /evidence="ECO:0000250"
FT DISULFID 869..895
FT /evidence="ECO:0000250"
FT CONFLICT 354
FT /note="R -> Q (in Ref. 1; AAB07996)"
FT /evidence="ECO:0000305"
FT CONFLICT 361..362
FT /note="PE -> SK (in Ref. 1; AAB07996)"
FT /evidence="ECO:0000305"
FT CONFLICT 366..368
FT /note="QDR -> RGK (in Ref. 1; AAB07996)"
FT /evidence="ECO:0000305"
FT CONFLICT 389
FT /note="T -> I (in Ref. 1; AAB07996)"
FT /evidence="ECO:0000305"
FT CONFLICT 394..396
FT /note="GEN -> EEK (in Ref. 1; AAB07996)"
FT /evidence="ECO:0000305"
FT CONFLICT 400..401
FT /note="LE -> SG (in Ref. 1; AAB07996)"
FT /evidence="ECO:0000305"
FT CONFLICT 405
FT /note="R -> G (in Ref. 1; AAB07996)"
FT /evidence="ECO:0000305"
FT CONFLICT 437
FT /note="Q -> E (in Ref. 1; AAB07996)"
FT /evidence="ECO:0000305"
FT CONFLICT 471
FT /note="P -> H (in Ref. 1; AAB07996)"
FT /evidence="ECO:0000305"
FT CONFLICT 495
FT /note="R -> A (in Ref. 1; AAB07996)"
FT /evidence="ECO:0000305"
FT CONFLICT 537
FT /note="G -> A (in Ref. 1; AAB07996)"
FT /evidence="ECO:0000305"
FT CONFLICT 597
FT /note="T -> H (in Ref. 1; AAB07996)"
FT /evidence="ECO:0000305"
FT CONFLICT 627..630
FT /note="PGLN -> SWPH (in Ref. 1; AAB07996)"
FT /evidence="ECO:0000305"
FT CONFLICT 662
FT /note="S -> C (in Ref. 1; AAB07996)"
FT /evidence="ECO:0000305"
FT CONFLICT 666
FT /note="R -> E (in Ref. 1; AAB07996)"
FT /evidence="ECO:0000305"
FT CONFLICT 732
FT /note="A -> D (in Ref. 1; AAB07996)"
FT /evidence="ECO:0000305"
FT CONFLICT 796
FT /note="E -> EE (in Ref. 1; AAB07996)"
FT /evidence="ECO:0000305"
FT CONFLICT 850
FT /note="R -> A (in Ref. 1; AAB07996)"
FT /evidence="ECO:0000305"
FT CONFLICT 979
FT /note="V -> L (in Ref. 1; AAB07996)"
FT /evidence="ECO:0000305"
SQ 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
