Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Ceruloplasmin

Gene

Cp

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Ceruloplasmin is a blue, copper-binding (6-7 atoms per molecule) glycoprotein. It has ferroxidase activity oxidizing Fe2+ to Fe3+ without releasing radical oxygen species. It is involved in iron transport across the cell membrane. Provides Cu2+ 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).By similarity

Catalytic activityi

4 Fe2+ + 4 H+ + O2 = 4 Fe3+ + 2 H2O.

Cofactori

Cu cationBy similarityNote: Binds 6 Cu cations per monomer.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi120Copper 1; type 2By similarity1
Metal bindingi122Copper 2; type 3By similarity1
Metal bindingi179Copper 2; type 3By similarity1
Metal bindingi181Copper 3; type 3By similarity1
Metal bindingi294Copper 4; type 1By similarity1
Metal bindingi337Copper 4; type 1By similarity1
Metal bindingi342Copper 4; type 1By similarity1
Metal bindingi651Copper 5; type 1By similarity1
Metal bindingi694Copper 5; type 1By similarity1
Metal bindingi699Copper 5; type 1By similarity1
Metal bindingi704Copper 5; type 1By similarity1
Metal bindingi989Copper 6; type 1By similarity1
Metal bindingi992Copper 1; type 2By similarity1
Metal bindingi994Copper 3; type 3By similarity1
Metal bindingi1034Copper 3; type 3By similarity1
Metal bindingi1035Copper 6; type 1By similarity1
Metal bindingi1036Copper 2; type 3By similarity1
Metal bindingi1040Copper 6; type 1By similarity1
Metal bindingi1045Copper 6; type 1By similarity1

GO - Molecular functioni

  • chaperone binding Source: MGI
  • copper ion binding Source: MGI
  • ferroxidase activity Source: MGI

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Copper transport, Ion transport, Transport

Keywords - Ligandi

Copper, Metal-binding

Enzyme and pathway databases

BRENDAi1.16.3.1. 3474.
ReactomeiR-MMU-425410. Metal ion SLC transporters.
R-MMU-917937. Iron uptake and transport.

Names & Taxonomyi

Protein namesi
Recommended name:
Ceruloplasmin (EC:1.16.3.1)
Alternative name(s):
Ferroxidase
Gene namesi
Name:Cp
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 3

Organism-specific databases

MGIiMGI:88476. Cp.

Subcellular locationi

  • Secreted

  • Note: Colocalizes with GCP1 in secretory intracellular compartments.By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 19By similarityAdd BLAST19
ChainiPRO_000000291320 – 1061CeruloplasminAdd BLAST1042

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi138N-linked (GlcNAc...)2 Publications1
Disulfide bondi173 ↔ 199By similarity
Glycosylationi226N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi275 ↔ 356By similarity
Glycosylationi396N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi529 ↔ 555By similarity
Glycosylationi583N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi632 ↔ 713By similarity
Glycosylationi757N-linked (GlcNAc...)2 Publications1
Disulfide bondi869 ↔ 895By similarity
Glycosylationi921N-linked (GlcNAc...)Sequence analysis1

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiQ61147.
PaxDbiQ61147.
PeptideAtlasiQ61147.
PRIDEiQ61147.

PTM databases

iPTMnetiQ61147.
PhosphoSitePlusiQ61147.
SwissPalmiQ61147.

Expressioni

Tissue specificityi

Expressed in many tissues, including liver, eye and brain.1 Publication

Gene expression databases

BgeeiENSMUSG00000003617.
CleanExiMM_CP.
ExpressionAtlasiQ61147. baseline and differential.
GenevisibleiQ61147. MM.

Interactioni

GO - Molecular functioni

Protein-protein interaction databases

IntActiQ61147. 6 interactors.
MINTiMINT-4090622.
STRINGi10090.ENSMUSP00000103965.

Structurei

3D structure databases

ProteinModelPortaliQ61147.
SMRiQ61147.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini20 – 356F5/8 type A 1Add BLAST337
Domaini20 – 199Plastocyanin-like 1Add BLAST180
Domaini208 – 356Plastocyanin-like 2Add BLAST149
Domaini369 – 713F5/8 type A 2Add BLAST345
Domaini369 – 555Plastocyanin-like 3Add BLAST187
Domaini565 – 713Plastocyanin-like 4Add BLAST149
Domaini725 – 1056F5/8 type A 3Add BLAST332
Domaini725 – 895Plastocyanin-like 5Add BLAST171
Domaini903 – 1056Plastocyanin-like 6Add BLAST154

Sequence similaritiesi

Belongs to the multicopper oxidase family.Curated
Contains 3 F5/8 type A domains.Curated
Contains 6 plastocyanin-like domains.Curated

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiKOG1263. Eukaryota.
COG2132. LUCA.
GeneTreeiENSGT00550000074552.
HOGENOMiHOG000231499.
HOVERGENiHBG003674.
InParanoidiQ61147.
KOiK13624.
PhylomeDBiQ61147.
TreeFamiTF329807.

Family and domain databases

Gene3Di2.60.40.420. 6 hits.
InterProiIPR027150. CP.
IPR001117. Cu-oxidase.
IPR011706. Cu-oxidase_2.
IPR011707. Cu-oxidase_3.
IPR033138. Cu_oxidase_CS.
IPR002355. Cu_oxidase_Cu_BS.
IPR008972. Cupredoxin.
[Graphical view]
PANTHERiPTHR10127:SF664. PTHR10127:SF664. 1 hit.
PfamiPF00394. Cu-oxidase. 1 hit.
PF07731. Cu-oxidase_2. 1 hit.
PF07732. Cu-oxidase_3. 3 hits.
[Graphical view]
SUPFAMiSSF49503. SSF49503. 6 hits.
PROSITEiPS00079. MULTICOPPER_OXIDASE1. 3 hits.
PS00080. MULTICOPPER_OXIDASE2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q61147-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKFLLLSTFI FLYSSLALAR DKHYFIGITE AVWDYASGTE EKKLISVDTE
60 70 80 90 100
QSNFYLQNGP DRIGRKYKKA LYFEYTDGTF SKTIDKPAWL GFLGPVIKAE
110 120 130 140 150
VEDKVYVHLK NLASRIYTFH AHGVTYTKEY EGAVYPDNTT DFQRADDKVL
160 170 180 190 200
PGQQYVYVLH ANEPSPGEGD SNCVTRIYHS HVDAPKDIAS GLIGPLILCK
210 220 230 240 250
KGSLYKEKEK NIDQEFVLMF SVVDENLSWY LEDNIKTFCS EPEKVDKDNE
260 270 280 290 300
DFQESNRMYS INGYTFGSLP GLSMCAADRV KWYLFGMGNE VDVHSAFFHG
310 320 330 340 350
QALTSRNYQT DIINLFPATL IDAYMVAQNP GVWMLSCQNL NHLKAGLQAF
360 370 380 390 400
FQVRDCNKPS PEDNIQDRHV RHYYIAAEEV IWNYAPSGTD IFTGENLTAL
410 420 430 440 450
ESDSRVFFEQ GATRIGGSYK KMAYREYTDG SFTNRKQRGP DEEHLGILGP
460 470 480 490 500
VIWAEVGDTI KVTFHNKGQH PLSIQPMGVS FTAENEGTYY GPPGRSSQQA
510 520 530 540 550
ASHVAPKETF TYEWTVPKEM GPTYADPVCL SKMYYSGVDP TKDIFTGLIG
560 570 580 590 600
PMKICKKGSL LADGRQKDVD KEFYLFPTVF DENESLLLDD NIRMFTTAPD
610 620 630 640 650
QVDKEDEDFQ ESNKMHSMNG FMYGNQPGLN MCLGESIVWY LFSAGNEADV
660 670 680 690 700
HGIYFSGNTY LSKGERRDTA NLFPHKSLTL LMNPDTKGTF DVECLTTDHY
710 720 730 740 750
TGGMKQKYTV NQCQRQFEDF TVYLGERTYY VAAVEVEWDY SPSRAWEKEL
760 770 780 790 800
HHLQEQNVSN VFLDKEEFFI GSKYKKVVYR QFTDSSFREQ VKRRAEDEHL
810 820 830 840 850
GILGPPIHAN VGDKVKVVFK NMATRPYSIH AHGVKTESST VVPTLPGEVR
860 870 880 890 900
TYTWQIPERS GAGREDSACI PWAYYSTVDR VKDLYSGLIG PLIVCRKSYV
910 920 930 940 950
KVFSPKKKME FFLLFLVFDE NESWYLDDNI KTYSEHPEKV NKDNEEFLES
960 970 980 990 1000
NKMHAINGKM FGNLQGLTMH VKDEVNWYVM GMGNEIDLHT VHFHGHSFQY
1010 1020 1030 1040 1050
KHRGVYSSDV FDLFPGTYQT LEMFPQTPGT WLLHCHVTDH VHAGMATTYT
1060
VLPVEQETKS G
Length:1,061
Mass (Da):121,151
Last modified:December 4, 2007 - v2
Checksum:i16A2DAEA4F483886
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti354R → Q in AAB07996 (PubMed:8690795).Curated1
Sequence conflicti361 – 362PE → SK in AAB07996 (PubMed:8690795).Curated2
Sequence conflicti366 – 368QDR → RGK in AAB07996 (PubMed:8690795).Curated3
Sequence conflicti389T → I in AAB07996 (PubMed:8690795).Curated1
Sequence conflicti394 – 396GEN → EEK in AAB07996 (PubMed:8690795).Curated3
Sequence conflicti400 – 401LE → SG in AAB07996 (PubMed:8690795).Curated2
Sequence conflicti405R → G in AAB07996 (PubMed:8690795).Curated1
Sequence conflicti437Q → E in AAB07996 (PubMed:8690795).Curated1
Sequence conflicti471P → H in AAB07996 (PubMed:8690795).Curated1
Sequence conflicti495R → A in AAB07996 (PubMed:8690795).Curated1
Sequence conflicti537G → A in AAB07996 (PubMed:8690795).Curated1
Sequence conflicti597T → H in AAB07996 (PubMed:8690795).Curated1
Sequence conflicti627 – 630PGLN → SWPH in AAB07996 (PubMed:8690795).Curated4
Sequence conflicti662S → C in AAB07996 (PubMed:8690795).Curated1
Sequence conflicti666R → E in AAB07996 (PubMed:8690795).Curated1
Sequence conflicti732A → D in AAB07996 (PubMed:8690795).Curated1
Sequence conflicti796E → EE in AAB07996 (PubMed:8690795).Curated1
Sequence conflicti850R → A in AAB07996 (PubMed:8690795).Curated1
Sequence conflicti979V → L in AAB07996 (PubMed:8690795).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U49430 mRNA. Translation: AAB07996.1.
BC062957 mRNA. Translation: AAH62957.1.
CCDSiCCDS38401.1.
RefSeqiNP_001263177.1. NM_001276248.1.
NP_031778.2. NM_007752.3.
UniGeneiMm.13787.

Genome annotation databases

EnsembliENSMUST00000091309; ENSMUSP00000088857; ENSMUSG00000003617.
GeneIDi12870.
KEGGimmu:12870.
UCSCiuc008orz.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U49430 mRNA. Translation: AAB07996.1.
BC062957 mRNA. Translation: AAH62957.1.
CCDSiCCDS38401.1.
RefSeqiNP_001263177.1. NM_001276248.1.
NP_031778.2. NM_007752.3.
UniGeneiMm.13787.

3D structure databases

ProteinModelPortaliQ61147.
SMRiQ61147.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ61147. 6 interactors.
MINTiMINT-4090622.
STRINGi10090.ENSMUSP00000103965.

PTM databases

iPTMnetiQ61147.
PhosphoSitePlusiQ61147.
SwissPalmiQ61147.

Proteomic databases

MaxQBiQ61147.
PaxDbiQ61147.
PeptideAtlasiQ61147.
PRIDEiQ61147.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000091309; ENSMUSP00000088857; ENSMUSG00000003617.
GeneIDi12870.
KEGGimmu:12870.
UCSCiuc008orz.2. mouse.

Organism-specific databases

CTDi1356.
MGIiMGI:88476. Cp.

Phylogenomic databases

eggNOGiKOG1263. Eukaryota.
COG2132. LUCA.
GeneTreeiENSGT00550000074552.
HOGENOMiHOG000231499.
HOVERGENiHBG003674.
InParanoidiQ61147.
KOiK13624.
PhylomeDBiQ61147.
TreeFamiTF329807.

Enzyme and pathway databases

BRENDAi1.16.3.1. 3474.
ReactomeiR-MMU-425410. Metal ion SLC transporters.
R-MMU-917937. Iron uptake and transport.

Miscellaneous databases

ChiTaRSiCp. mouse.
PROiQ61147.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000003617.
CleanExiMM_CP.
ExpressionAtlasiQ61147. baseline and differential.
GenevisibleiQ61147. MM.

Family and domain databases

Gene3Di2.60.40.420. 6 hits.
InterProiIPR027150. CP.
IPR001117. Cu-oxidase.
IPR011706. Cu-oxidase_2.
IPR011707. Cu-oxidase_3.
IPR033138. Cu_oxidase_CS.
IPR002355. Cu_oxidase_Cu_BS.
IPR008972. Cupredoxin.
[Graphical view]
PANTHERiPTHR10127:SF664. PTHR10127:SF664. 1 hit.
PfamiPF00394. Cu-oxidase. 1 hit.
PF07731. Cu-oxidase_2. 1 hit.
PF07732. Cu-oxidase_3. 3 hits.
[Graphical view]
SUPFAMiSSF49503. SSF49503. 6 hits.
PROSITEiPS00079. MULTICOPPER_OXIDASE1. 3 hits.
PS00080. MULTICOPPER_OXIDASE2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiCERU_MOUSE
AccessioniPrimary (citable) accession number: Q61147
Secondary accession number(s): Q6P5C8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: December 4, 2007
Last modified: November 2, 2016
This is version 134 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.