Cp ceruloplasmin [Mus musculus (house mouse)] - Gene

Summary

Official Symbol: Cpprovided by MGI
Official Full Name: ceruloplasminprovided by MGI
Primary source: MGI:MGI:88476
See related: Ensembl:ENSMUSG00000003617 AllianceGenome:MGI:88476
Gene type: protein coding
RefSeq status: REVIEWED
Organism: Mus musculus
Lineage: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; Murinae; Mus; Mus
Also known as: D3Ertd555e
Summary: The protein encoded by this gene is a copper-containing glycoprotein found soluble in the serum and GPI-anchored in other tissues. It oxidizes Fe(II) to Fe(III) and is proposed to play an important role in iron homeostasis. In humans mutations of this gene cause aceruloplasminemia, which is characterized by retinal degeneration, diabetes, anemia and neurological symptoms. In mouse deficiency of this gene in combination with a deficiency of its homolog hephaestin causes retinal degeneration and serves as a pathophysiological model for aceruloplasminemia and age-related macular degeneration. Alternative splicing results in multiple transcript variants that encode different protein isoforms. [provided by RefSeq, Jan 2013]
Expression: Biased expression in liver adult (RPKM 26.7), liver E18 (RPKM 23.8) and 8 other tissues See more
Orthologs: human all
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Genomic context

Location:: 3 A2; 3 6.1 cM

Exon count:: 21

Annotation release	Status	Assembly	Chr	Location
RS_2024_02	current	GRCm39 (GCF_000001635.27)	3	NC_000069.7 (20011097..20063914)
108.20200622	previous assembly	GRCm38.p6 (GCF_000001635.26)	3	NC_000069.6 (19956933..20009750)

Chromosome 3 - NC_000069.7 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Go to reference sequence details

Genomic Sequence:

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

Ceruloplasmin-deficient mice show changes in PTM profiles of proteins involved in messenger RNA processing and neuronal projections and synaptic processes.
Title: Ceruloplasmin-deficient mice show changes in PTM profiles of proteins involved in messenger RNA processing and neuronal projections and synaptic processes.
The Placental Ferroxidase Zyklopen Is Not Essential for Iron Transport to the Fetus in Mice.
Title: The Placental Ferroxidase Zyklopen Is Not Essential for Iron Transport to the Fetus in Mice.
This study concluded that even when the ferroportin expression is high, ceruloplasmin remains a limiting factor in the release of iron to the extracellular environment.
Title: Functional iron deficiency in toxic milk mutant mice (tx-J) despite high hepatic ferroportin: a critical role of decreased GPI-ceruloplasmin expression in liver macrophages.
HEPH and CP are not essential for intestinal iron absorption but are required for proper systemic iron distribution.
Title: Severe Iron Metabolism Defects in Mice With Double Knockout of the Multicopper Ferroxidases Hephaestin and Ceruloplasmin.
results suggest that ablation of hephaestin and ceruloplasmin could lead to severe systemic iron deficiency and local tissue iron overload, which disrupt the whole body iron homeostasis and impact on tissue functions
Title: Deletion of hephaestin and ceruloplasmin induces a serious systemic iron deficiency and disrupts iron homeostasis.
Ceruloplasmin regulates reelin processing, cofilin phosphorylation and neuronal organization in the developing brain.
Title: The ferroxidase ceruloplasmin influences Reelin processing, cofilin phosphorylation and neuronal organization in the developing brain.
Results show that both HEPH and CP are expressed in subcutaneous adipose tissue. Ablation of either MCF leads to a compensatory increase in the other, which contributes to the balance of iron status. However, ablation of both induces severe iron deposition in adipocytes and displays disordered carbohydrate metabolism characterized as type 2 diabetes.
Title: Ablation of hephaestin and ceruloplasmin results in iron accumulation in adipocytes and type 2 diabetes.
We thus used hephaestin (Heph) and ceruloplasmin (Cp) single-knockout mice and Heph/Cp double-knockout mice to investigate the roles of multicopper ferroxidases(MCF) in pancreatic iron homeostasis. We found that both HEPH and CP were expressed in the mouse pancreas, and that ablation of either MCF had limited effect on the pancreatic iron levels.
Title: Ceruloplasmin and hephaestin jointly protect the exocrine pancreas against oxidative damage by facilitating iron efflux.
Hephaestin and ceruloplasmin have roles in facilitating iron metabolism in the mouse kidney
Title: Hephaestin and ceruloplasmin facilitate iron metabolism in the mouse kidney.
In D-galactosamine-sensitized mice CP+Cu(II) increased the LPS-induced lethality from 54 to 100%, while administration of antibodies against MIF prevented the lethal effect. The enhancement by CP+Cu(II) of the pro-inflammatory signal of MIF is discussed
Title: Interaction of macrophage migration inhibitory factor with ceruloplasmin: role of labile copper ions.

Submit: New GeneRIF Correction See all GeneRIFs (37)

Variation

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Alleles

Alleles of this type are documented at Mouse Genome Informatics (MGI)

Chemically induced (ENU) (1)
Endonuclease-mediated (3) 1 citation
Spontaneous (2) 1 citation
Targeted (6) 1 citation

Interactions

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Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

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Markers

Cp (e-PCR), detects polymorphism
- UniSTS:141386

CP-000F (e-PCR)
- UniSTS:36019

AU022691 (e-PCR)
- UniSTS:167366

Gene Ontology Provided by MGI

Function	Evidence Code	Pubs
enables copper ion binding	IDA Inferred from Direct Assay more info	PubMed
enables copper ion binding	ISO Inferred from Sequence Orthology more info
enables ferroxidase activity	IDA Inferred from Direct Assay more info	PubMed
enables ferroxidase activity	ISO Inferred from Sequence Orthology more info
enables ferroxidase activity	ISS Inferred from Sequence or Structural Similarity more info
enables glutathione peroxidase activity	ISO Inferred from Sequence Orthology more info
enables glutathione peroxidase activity	ISS Inferred from Sequence or Structural Similarity more info
enables oxidoreductase activity	IBA Inferred from Biological aspect of Ancestor more info
enables oxidoreductase activity, acting on metal ions, oxygen as acceptor	ISO Inferred from Sequence Orthology more info
enables oxidoreductase activity, acting on metal ions, oxygen as acceptor	ISS Inferred from Sequence or Structural Similarity more info
enables phospholipid-hydroperoxide glutathione peroxidase activity	ISO Inferred from Sequence Orthology more info
enables phospholipid-hydroperoxide glutathione peroxidase activity	ISS Inferred from Sequence or Structural Similarity more info
enables protein-folding chaperone binding	ISO Inferred from Sequence Orthology more info

Process	Evidence Code	Pubs
involved_in cellular oxidant detoxification	IEA Inferred from Electronic Annotation more info
involved_in intracellular copper ion homeostasis	ISO Inferred from Sequence Orthology more info
involved_in intracellular copper ion homeostasis	ISS Inferred from Sequence or Structural Similarity more info
involved_in intracellular iron ion homeostasis	ISO Inferred from Sequence Orthology more info
involved_in intracellular iron ion homeostasis	ISS Inferred from Sequence or Structural Similarity more info
involved_in iron ion transport	IBA Inferred from Biological aspect of Ancestor more info
involved_in response to copper ion	ISO Inferred from Sequence Orthology more info

Component	Evidence Code	Pubs
located_in cell surface	ISO Inferred from Sequence Orthology more info
located_in extracellular space	HDA more info	PubMed
located_in extracellular space	IDA Inferred from Direct Assay more info	PubMed
located_in extracellular space	ISO Inferred from Sequence Orthology more info
located_in extracellular space	ISS Inferred from Sequence or Structural Similarity more info
is_active_in plasma membrane	IBA Inferred from Biological aspect of Ancestor more info

General protein information

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Preferred Names: ceruloplasmin

Names: cuproxidase ceruloplasmin; ferroxidase; ferroxidase ceruloplasmin; glutathione peroxidase ceruloplasmin; glutathione-dependent peroxiredoxin ceruloplasmin

NP_001263177.1

EC 1.11.1.27

EC 1.11.1.9

EC 1.16.3.1

EC 1.16.3.4

NP_001263179.1

EC 1.11.1.27

EC 1.11.1.9

EC 1.16.3.1

EC 1.16.3.4

NP_001361606.1

EC 1.11.1.27

EC 1.11.1.9

EC 1.16.3.1

EC 1.16.3.4

NP_001396575.1

EC 1.11.1.27

EC 1.11.1.9

EC 1.16.3.1

EC 1.16.3.4

NP_001396576.1

EC 1.11.1.27

EC 1.11.1.9

EC 1.16.3.1

EC 1.16.3.4

NP_001396577.1

EC 1.11.1.27

EC 1.11.1.9

EC 1.16.3.1

EC 1.16.3.4

NP_001396578.1

EC 1.11.1.27

EC 1.11.1.9

EC 1.16.3.1

EC 1.16.3.4

NP_001396579.1

EC 1.11.1.27

EC 1.11.1.9

EC 1.16.3.1

EC 1.16.3.4

NP_001396580.1

EC 1.11.1.27

EC 1.11.1.9

EC 1.16.3.1

EC 1.16.3.4

NP_031778.2

EC 1.11.1.27

EC 1.11.1.9

EC 1.16.3.1

EC 1.16.3.4

NCBI Reference Sequences (RefSeq)

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RefSeqs maintained independently of Annotated Genomes

These reference sequences exist independently of genome builds. Explain

These reference sequences are curated independently of the genome annotation cycle, so their versions may not match the RefSeq versions in the current genome build. Identify version mismatches by comparing the version of the RefSeq in this section to the one reported in Genomic regions, transcripts, and products above.

mRNA and Protein(s)

NM_001276248.2 → NP_001263177.1 ceruloplasmin isoform c precursor

See identical proteins and their annotated locations for NP_001263177.1

Status: REVIEWED

Source sequence(s)

AC079442

Consensus CDS

CCDS71227.1

UniProtKB/TrEMBL

G3X8Q5

Related

ENSMUSP00000103964.2, ENSMUST00000108328.8

Conserved Domains (5) summary

cd04224
Location:369 → 566

CuRO_3_ceruloplasmin; The third cupredoxin domain of Ceruloplasmin

cd04225
Location:726 → 896

CuRO_5_ceruloplasmin; The fifth cupredoxin domain of Ceruloplasmin

cd11021
Location:213 → 353

CuRO_2_ceruloplasmin; The second cupredoxin domain of Ceruloplasmin

cd11022
Location:569 → 712

CuRO_4_ceruloplasmin; The fourth cupredoxin domain of Ceruloplasmin

cl19115
Location:22 → 201

Cupredoxin; Cupredoxin superfamily
NM_001276250.2 → NP_001263179.1 ceruloplasmin isoform c precursor

See identical proteins and their annotated locations for NP_001263179.1

Status: REVIEWED

Source sequence(s)

AC079442

Consensus CDS

CCDS71227.1

UniProtKB/TrEMBL

G3X8Q5

Related

ENSMUSP00000003714.7, ENSMUST00000003714.13

Conserved Domains (5) summary

cd04224
Location:369 → 566

CuRO_3_ceruloplasmin; The third cupredoxin domain of Ceruloplasmin

cd04225
Location:726 → 896

CuRO_5_ceruloplasmin; The fifth cupredoxin domain of Ceruloplasmin

cd11021
Location:213 → 353

CuRO_2_ceruloplasmin; The second cupredoxin domain of Ceruloplasmin

cd11022
Location:569 → 712

CuRO_4_ceruloplasmin; The fourth cupredoxin domain of Ceruloplasmin

cl19115
Location:22 → 201

Cupredoxin; Cupredoxin superfamily
NM_001374677.1 → NP_001361606.1 ceruloplasmin isoform d precursor

Status: REVIEWED

Source sequence(s)

AC079442

Consensus CDS

CCDS89616.1

UniProtKB/TrEMBL

G3X9T8

Related

ENSMUSP00000103961.3, ENSMUST00000108325.9

Conserved Domains (5) summary

cd04224
Location:369 → 566

CuRO_3_ceruloplasmin; The third cupredoxin domain of Ceruloplasmin

cd04225
Location:726 → 896

CuRO_5_ceruloplasmin; The fifth cupredoxin domain of Ceruloplasmin

cd11021
Location:213 → 353

CuRO_2_ceruloplasmin; The second cupredoxin domain of Ceruloplasmin

cd11022
Location:569 → 712

CuRO_4_ceruloplasmin; The fourth cupredoxin domain of Ceruloplasmin

cl19115
Location:22 → 201

Cupredoxin; Cupredoxin superfamily
NM_001409646.1 → NP_001396575.1 ceruloplasmin isoform a precursor

Status: REVIEWED

Source sequence(s)

AC079442

UniProtKB/TrEMBL

E9PZD8

Related

ENSMUSP00000103965.2, ENSMUST00000108329.8
NM_001409647.1 → NP_001396576.1 ceruloplasmin isoform a precursor

Status: REVIEWED

Source sequence(s)

AC079442

UniProtKB/TrEMBL

E9PZD8
NM_001409648.1 → NP_001396577.1 ceruloplasmin isoform e precursor

Status: REVIEWED

Source sequence(s)

AC079442
NM_001409649.1 → NP_001396578.1 ceruloplasmin isoform f precursor

Status: REVIEWED

Source sequence(s)

AC079442
NM_001409650.1 → NP_001396579.1 ceruloplasmin isoform g precursor

Status: REVIEWED

Source sequence(s)

AC079442
NM_001409651.1 → NP_001396580.1 ceruloplasmin isoform h precursor

Status: REVIEWED

Source sequence(s)

AC079442
NM_007752.4 → NP_031778.2 ceruloplasmin isoform b precursor

See identical proteins and their annotated locations for NP_031778.2

Status: REVIEWED

Source sequence(s)

AC079442

Consensus CDS

CCDS38401.1

UniProtKB/Swiss-Prot

Q61147, Q6P5C8

Related

ENSMUSP00000088857.6, ENSMUST00000091309.12

Conserved Domains (5) summary

cd04224
Location:369 → 567

CuRO_3_ceruloplasmin; The third cupredoxin domain of Ceruloplasmin

cd04225
Location:727 → 897

CuRO_5_ceruloplasmin; The fifth cupredoxin domain of Ceruloplasmin

cd11021
Location:213 → 353

CuRO_2_ceruloplasmin; The second cupredoxin domain of Ceruloplasmin

cd11022
Location:570 → 713

CuRO_4_ceruloplasmin; The fourth cupredoxin domain of Ceruloplasmin

cl19115
Location:22 → 201

Cupredoxin; Cupredoxin superfamily

RefSeqs of Annotated Genomes: GCF_000001635.27-RS_2024_02

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference GRCm39 C57BL/6J

Genomic

NC_000069.7 Reference GRCm39 C57BL/6J

Range

20011097..20063914

Download

GenBank, FASTA, Sequence Viewer (Graphics)

RNA

XR_004941272.1 RNA Sequence
XR_004941273.1 RNA Sequence

Suppressed Reference Sequence(s)

The following Reference Sequences have been suppressed. Explain

NM_001042611.1: Suppressed sequence

Description

NM_001042611.1: This RefSeq was permanently suppressed because currently there is insufficient support for the transcript and the protein.