Cp ceruloplasmin [Rattus norvegicus (Norway rat)] - Gene

Summary

Official Symbol: Cpprovided by RGD
Official Full Name: ceruloplasminprovided by RGD
Primary source: RGD:2387
See related: EnsemblRapid:ENSRNOG00000011913 AllianceGenome:RGD:2387
Gene type: protein coding
RefSeq status: VALIDATED
Organism: Rattus norvegicus
Lineage: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; Murinae; Rattus
Also known as: CERP
Summary: Enables copper ion binding activity. Involved in several processes, including female pregnancy; gland development; and response to copper ion. Located in extracellular space. Is anchored component of plasma membrane. Used to study brain edema and iron metabolism disease. Biomarker of Wilson disease; brain ischemia; heart disease; and hyperthyroidism. Human ortholog(s) of this gene implicated in aceruloplasminemia; epilepsy; and hemosiderosis. Orthologous to human CP (ceruloplasmin). [provided by Alliance of Genome Resources, Apr 2022]
Expression: Biased expression in Liver (RPKM 6726.9), Spleen (RPKM 532.4) and 2 other tissues See more
Orthologs: human mouse all
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Genomic context

Location:: 2q24

Exon count:: 22

Annotation release	Status	Assembly	Chr	Location
RS_2024_02	current	GRCr8 (GCF_036323735.1)	2	NC_086020.1 (104368336..104427119)
RS_2023_06	previous assembly	mRatBN7.2 (GCF_015227675.2)	2	NC_051337.1 (102439433..102498075)
106	previous assembly	Rnor_6.0 (GCF_000001895.5)	2	NC_005101.4 (104744249..104803034)

Chromosome 2 - NC_086020.1 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

Expression

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See details

Project title: A rat RNA-Seq transcriptomic BodyMap across 11 organs and 4 developmental stages A rat RNA-Seq transcriptomic BodyMap across 11 organs and 4 developmental stages
Description: 320 RNA samples isolated from 11 organs (adrenal gland, brain, heart, kidney, liver, lung, muscle, spleen, thymus, and testes or uterus) from both sexes of Fischer 344 rats across four developmental stages (2-, 6-, 21-, and 104-weeks-old)
BioProject: PRJNA238328
Publication: PMID 24510058
Analysis date: Mon Jun 6 17:44:12 2016

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

Urine exosomal CP, observed to increase prior to proteinuria, makes it a potential urinary biomarker to diagnose early kidney disease.
Title: Urine exosomal ceruloplasmin: a potential early biomarker of underlying kidney disease.
This study found that CP was expressed on neurons and astrocytes in both cortex and basal ganglia after Intracerebral Hemorrhage.
Title: Brain Ceruloplasmin Expression After Experimental Intracerebral Hemorrhage and Protection Against Iron-Induced Brain Injury.
Data suggest beta-glucuronidase and bilitranslocase in vascular endothelium are involved in changes in endothelium-independent vaso-relaxation induced by dietary antioxidants; here, using in vitro studies with thoracic aorta rings in oxidative stress, glucuronides of dietary supplement antioxidant hydroxytyrosol (HT) are deconjugated by beta-glucuronidase before HT is taken up by vascular endothelium via bilitranslocase.
Title: Involvement of bilitranslocase and beta-glucuronidase in the vascular protection by hydroxytyrosol and its glucuronide metabolites in oxidative stress conditions.
these results suggest that genetically determined Cp levels can alter susceptibility to Crescentic glomerulonephritis through macrophage function and propose a new role for Cp in early macrophage activation.
Title: Identification of Ceruloplasmin as a Gene that Affects Susceptibility to Glomerulonephritis Through Macrophage Function.
Ferroportin 1 and CP colocalize in the rat brain.
Title: Ceruloplasmin is Involved in the Nigral Iron Accumulation of 6-OHDA-Lesioned Rats.
Cerebral ischemia inhibited ceruloplasmin expression in the cortex and hippocampus of rats. The decrease of Cp might be involved in iron deposition in neurons.
Title: An inhibition of ceruloplasmin expression induced by cerebral ischemia in the cortex and hippocampus of rats.
Data show there was no significant difference detected in hepatic and hippocampus iron levels in response to increased serum ceruloplasmin between control and copper-intoxicated rats.
Title: Hepatic and hippocampus iron status is not altered in response to increased serum ceruloplasmin and serum "free" copper in Wistar rat model for non-Wilsonian brain copper toxicosis.
FOX activity was present in rat cytosol, and was partly inhibited by anti-Heph antibody.
Title: Immunoreactive hephaestin and ferroxidase activity are present in the cytosolic fraction of rat enterocytes.
Liver copper loading increases metallation of the Cp protein, leading to increased production of the holo enzyme.
Title: Serum ceruloplasmin protein expression and activity increases in iron-deficient rats and is further enhanced by higher dietary copper intake.
Insulin downregulat CP mRNA levels and attenuates CP secretion in rat liver cells.
Title: Ceruloplasmin expression in rat liver cells is attenuated by insulin: role of FoxO transcription factors.

Submit: New GeneRIF Correction See all GeneRIFs (22)

Interactions

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Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

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Markers

RH141500 (e-PCR)
- UniSTS:223494

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

D2Wox54 (e-PCR)
- UniSTS:240051

D2Wox55 (e-PCR)
- UniSTS:240052

Gene Ontology Provided by RGD

Function	Evidence Code	Pubs
enables copper ion binding	IDA Inferred from Direct Assay more info	PubMed
enables copper ion binding	IEA Inferred from Electronic Annotation more info
enables copper ion binding	ISO Inferred from Sequence Orthology more info
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	IEA Inferred from Electronic Annotation 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 female pregnancy	IEP Inferred from Expression Pattern more info	PubMed
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 intracellular iron ion homeostasis	TAS Traceable Author Statement more info	PubMed
involved_in iron ion transport	IBA Inferred from Biological aspect of Ancestor more info
involved_in lactation	IEP Inferred from Expression Pattern more info	PubMed
involved_in liver development	IEP Inferred from Expression Pattern more info	PubMed
involved_in lung development	IEP Inferred from Expression Pattern more info	PubMed
involved_in mammary gland involution	IEP Inferred from Expression Pattern more info	PubMed
involved_in plasma membrane copper ion transport	TAS Traceable Author Statement more info	PubMed
involved_in response to copper ion	IDA Inferred from Direct Assay more info	PubMed
involved_in response to nutrient	IEP Inferred from Expression Pattern more info	PubMed

Component	Evidence Code	Pubs
located_in cell surface	IDA Inferred from Direct Assay more info	PubMed
located_in extracellular region	IEA Inferred from Electronic Annotation more info
located_in extracellular space	IDA Inferred from Direct Assay more info	PubMed
located_in extracellular space	ISO Inferred from Sequence Orthology 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: bilitranslocase; ceruloplasmin (ferroxidase); cuproxidase ceruloplasmin; ferroxidase ceruloplasmin; glutathione peroxidase ceruloplasmin; glutathione-dependent peroxiredoxin ceruloplasmin

NP_001257890.1

EC 1.11.1.27

EC 1.11.1.9

EC 1.16.3.1

EC 1.16.3.4

NP_036664.2

EC 1.11.1.27

EC 1.11.1.9

EC 1.16.3.1

EC 1.16.3.4

XP_063137357.1

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_001270961.1 → NP_001257890.1 ceruloplasmin isoform 2 precursor

See identical proteins and their annotated locations for NP_001257890.1

Status: VALIDATED

Description

Transcript Variant: This variant (2) lacks an exon and contains two alternate 3' exons compared to variant 1. The resulting protein (isoform 2), which is longer and has a distinct C-terminus compared to isoform 1, is a glycosylphosphatidylinositol-anchored form.

Source sequence(s)

JAXUCZ010000002

UniProtKB/TrEMBL

A0A8I6A708, A6IHC3, Q9JL97

Related

ENSRNOP00000089330.1, ENSRNOT00000119964.2

Conserved Domains (5) summary

cd04225
Location:726 → 896

CuRO_5_ceruloplasmin; The fifth cupredoxin domain of Ceruloplasmin

cd11012
Location:907 → 1051

CuRO_6_ceruloplasmin; The sixth 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:369 → 566

Cupredoxin; Cupredoxin superfamily
NM_012532.2 → NP_036664.2 ceruloplasmin isoform 1 precursor

See identical proteins and their annotated locations for NP_036664.2

Status: VALIDATED

Description

Transcript Variant: This variant (1) represents the longer transcript and encodes a secreted protein (isoform 1).

Source sequence(s)

JAXUCZ010000002

UniProtKB/Swiss-Prot

P13635, Q64719

UniProtKB/TrEMBL

A6IHC4, G3V7K3

Related

ENSRNOP00000016083.4, ENSRNOT00000016083.7

Conserved Domains (5) summary

cd04225
Location:726 → 896

CuRO_5_ceruloplasmin; The fifth cupredoxin domain of Ceruloplasmin

cd11012
Location:907 → 1051

CuRO_6_ceruloplasmin; The sixth 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:369 → 566

Cupredoxin; Cupredoxin superfamily