Ceruloplasmin precursor - Mus musculus (Mouse)

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Q61147 (CERU_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 103. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Ceruloplasmin
EC=1.16.3.1

Alternative name(s):
Ferroxidase

Gene names

Name:

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	1061 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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.
Catalytic activity	4 Fe²⁺ + 4 H⁺ + O₂ = 4 Fe³⁺ + 2 H₂O.
Cofactor	Binds 6 copper ions per monomer By similarity.
Subcellular location	Secreted. Note: Colocalizes with GCP1 in secretory intracellular compartments By similarity.
Tissue specificity	Expressed in many tissues, including liver, eye and brain. Ref.1
Sequence similarities	Belongs to the multicopper oxidase family. Contains 3 F5/8 type A domains. Contains 6 plastocyanin-like domains.

Ontologies

Keywords
Biological process	Copper transport Ion transport Transport
Cellular component	Secreted
Domain	Repeat Signal
Ligand	Copper Metal-binding
Molecular function	Oxidoreductase
PTM	Disulfide bond Glycoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cellular iron ion homeostasis Inferred from electronic annotation. Source: InterPro copper ion transport Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	extracellular space Inferred from direct assay PubMed 16436657. Source: MGI
Molecular_function	copper ion binding Inferred from direct assay PubMed 15634671 PubMed 16436657. Source: MGI ferroxidase activity Inferred from direct assay PubMed 16436657. Source: MGI
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 19

By similarity

Chain

20 – 1061

1042

Ceruloplasmin

PRO_0000002913

Regions

Domain

20 – 356

337

F5/8 type A 1

Domain

20 – 199

180

Plastocyanin-like 1

Domain

208 – 356

149

Plastocyanin-like 2

Domain

369 – 713

345

F5/8 type A 2

Domain

369 – 555

187

Plastocyanin-like 3

Domain

565 – 713

149

Plastocyanin-like 4

Domain

725 – 1056

332

F5/8 type A 3

Domain

725 – 895

171

Plastocyanin-like 5

Domain

903 – 1056

154

Plastocyanin-like 6

Sites

Metal binding

120

Copper 1; type 2 By similarity

Metal binding

122

Copper 2; type 3 By similarity

Metal binding

179

Copper 2; type 3 By similarity

Metal binding

181

Copper 3; type 3 By similarity

Metal binding

294

Copper 4; type 1 By similarity

Metal binding

337

Copper 4; type 1 By similarity

Metal binding

342

Copper 4; type 1 By similarity

Metal binding

651

Copper 5; type 1 By similarity

Metal binding

694

Copper 5; type 1 By similarity

Metal binding

699

Copper 5; type 1 By similarity

Metal binding

704

Copper 5; type 1 By similarity

Metal binding

989

Copper 6; type 1 By similarity

Metal binding

992

Copper 1; type 2 By similarity

Metal binding

994

Copper 3; type 3 By similarity

Metal binding

1034

Copper 3; type 3 By similarity

Metal binding

1035

Copper 6; type 1 By similarity

Metal binding

1036

Copper 2; type 3 By similarity

Metal binding

1040

Copper 6; type 1 By similarity

Metal binding

1045

Copper 6; type 1 By similarity

Amino acid modifications

Glycosylation

138

N-linked (GlcNAc...) Ref.3 Ref.4

Glycosylation

226

N-linked (GlcNAc...) Potential

Glycosylation

396

N-linked (GlcNAc...) Potential

Glycosylation

583

N-linked (GlcNAc...) Potential

Glycosylation

757

N-linked (GlcNAc...) Ref.3 Ref.4

Glycosylation

921

N-linked (GlcNAc...) Potential

Disulfide bond

173 ↔ 199

By similarity

Disulfide bond

275 ↔ 356

By similarity

Disulfide bond

529 ↔ 555

By similarity

Disulfide bond

632 ↔ 713

By similarity

Disulfide bond

869 ↔ 895

By similarity

Experimental info

Sequence conflict

354

R → Q in AAB07996. Ref.1

Sequence conflict

361 – 362

PE → SK in AAB07996. Ref.1

Sequence conflict

366 – 368

QDR → RGK in AAB07996. Ref.1

Sequence conflict

389

T → I in AAB07996. Ref.1

Sequence conflict

394 – 396

GEN → EEK in AAB07996. Ref.1

Sequence conflict

400 – 401

LE → SG in AAB07996. Ref.1

Sequence conflict

405

R → G in AAB07996. Ref.1

Sequence conflict

437

Q → E in AAB07996. Ref.1

Sequence conflict

471

P → H in AAB07996. Ref.1

Sequence conflict

495

R → A in AAB07996. Ref.1

Sequence conflict

537

G → A in AAB07996. Ref.1

Sequence conflict

597

T → H in AAB07996. Ref.1

Sequence conflict

627 – 630

PGLN → SWPH in AAB07996. Ref.1

Sequence conflict

662

S → C in AAB07996. Ref.1

Sequence conflict

666

R → E in AAB07996. Ref.1

Sequence conflict

732

A → D in AAB07996. Ref.1

Sequence conflict

796

E → EE in AAB07996. Ref.1

Sequence conflict

850

R → A in AAB07996. Ref.1

Sequence conflict

979

V → L in AAB07996. Ref.1

Sequences

Sequence

Length

Mass (Da)

Tools

Q61147 [UniParc].

Last modified December 4, 2007. Version 2.
Checksum: 16A2DAEA4F483886
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FASTA

1,061

121,151

        10         20         30         40         50         60 
MKFLLLSTFI FLYSSLALAR DKHYFIGITE AVWDYASGTE EKKLISVDTE QSNFYLQNGP 

        70         80         90        100        110        120 
DRIGRKYKKA LYFEYTDGTF SKTIDKPAWL GFLGPVIKAE VEDKVYVHLK NLASRIYTFH 

       130        140        150        160        170        180 
AHGVTYTKEY EGAVYPDNTT DFQRADDKVL PGQQYVYVLH ANEPSPGEGD SNCVTRIYHS 

       190        200        210        220        230        240 
HVDAPKDIAS GLIGPLILCK KGSLYKEKEK NIDQEFVLMF SVVDENLSWY LEDNIKTFCS 

       250        260        270        280        290        300 
EPEKVDKDNE DFQESNRMYS INGYTFGSLP GLSMCAADRV KWYLFGMGNE VDVHSAFFHG 

       310        320        330        340        350        360 
QALTSRNYQT DIINLFPATL IDAYMVAQNP GVWMLSCQNL NHLKAGLQAF FQVRDCNKPS 

       370        380        390        400        410        420 
PEDNIQDRHV RHYYIAAEEV IWNYAPSGTD IFTGENLTAL ESDSRVFFEQ GATRIGGSYK 

       430        440        450        460        470        480 
KMAYREYTDG SFTNRKQRGP DEEHLGILGP VIWAEVGDTI KVTFHNKGQH PLSIQPMGVS 

       490        500        510        520        530        540 
FTAENEGTYY GPPGRSSQQA ASHVAPKETF TYEWTVPKEM GPTYADPVCL SKMYYSGVDP 

       550        560        570        580        590        600 
TKDIFTGLIG PMKICKKGSL LADGRQKDVD KEFYLFPTVF DENESLLLDD NIRMFTTAPD 

       610        620        630        640        650        660 
QVDKEDEDFQ ESNKMHSMNG FMYGNQPGLN MCLGESIVWY LFSAGNEADV HGIYFSGNTY 

       670        680        690        700        710        720 
LSKGERRDTA NLFPHKSLTL LMNPDTKGTF DVECLTTDHY TGGMKQKYTV NQCQRQFEDF 

       730        740        750        760        770        780 
TVYLGERTYY VAAVEVEWDY SPSRAWEKEL HHLQEQNVSN VFLDKEEFFI GSKYKKVVYR 

       790        800        810        820        830        840 
QFTDSSFREQ VKRRAEDEHL GILGPPIHAN VGDKVKVVFK NMATRPYSIH AHGVKTESST 

       850        860        870        880        890        900 
VVPTLPGEVR TYTWQIPERS GAGREDSACI PWAYYSTVDR VKDLYSGLIG PLIVCRKSYV 

       910        920        930        940        950        960 
KVFSPKKKME FFLLFLVFDE NESWYLDDNI KTYSEHPEKV NKDNEEFLES NKMHAINGKM 

       970        980        990       1000       1010       1020 
FGNLQGLTMH VKDEVNWYVM GMGNEIDLHT VHFHGHSFQY KHRGVYSSDV FDLFPGTYQT 

      1030       1040       1050       1060 
LEMFPQTPGT WLLHCHVTDH VHAGMATTYT VLPVEQETKS G

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Ceruloplasmin gene expression in the murine central nervous system." Klomp L.W.J., Farhangrazi Z.S., Dugan L.L., Gitlin J.D. J. Clin. Invest. 98:207-215(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
[2]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6. Tissue: Eye.
[3]	"Proteome-wide characterization of N-glycosylation events by diagonal chromatography." Ghesquiere B., Van Damme J., Martens L., Vandekerckhove J., Gevaert K. J. Proteome Res. 5:2438-2447(2006) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-138 AND ASN-757, MASS SPECTROMETRY. Strain: C57BL/6. Tissue: Plasma.
[4]	"Enhanced analysis of the mouse plasma proteome using cysteine-containing tryptic glycopeptides." Bernhard O.K., Kapp E.A., Simpson R.J. J. Proteome Res. 6:987-995(2007) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-138 AND ASN-757, MASS SPECTROMETRY. Strain: C57BL/6. Tissue: Plasma.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U49430 mRNA. Translation: AAB07996.1. BC062957 mRNA. Translation: AAH62957.1.
IPI	IPI00117831.
RefSeq	NP_001036076.1. NM_001042611.1. NP_031778.2. NM_007752.3.
UniGene	Mm.13787.
3D structure databases
ProteinModelPortal	Q61147.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q61147. 1 interaction.
PTM databases
PhosphoSite	Q61147.
Proteomic databases
PaxDb	Q61147.
PRIDE	Q61147.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000091309; ENSMUSP00000088857; ENSMUSG00000003617.
GeneID	12870.
KEGG	mmu:12870.
UCSC	uc008orz.1. mouse.
Organism-specific databases
CTD	1356.
MGI	MGI:88476. Cp.
Phylogenomic databases
eggNOG	NOG276067.
GeneTree	ENSGT00550000074552.
HOGENOM	HOG000231499.
HOVERGEN	HBG003674.
KO	K13624.
OrthoDB	EOG4WH8K0.
Gene expression databases
ArrayExpress	Q61147.
Bgee	Q61147.
CleanEx	MM_CP.
Genevestigator	Q61147.
GermOnline	ENSMUSG00000003617. Mus musculus.
Family and domain databases
Gene3D	2.60.40.420. 6 hits.
InterPro	IPR027150. CP. IPR001117. Cu-oxidase. IPR011706. Cu-oxidase_2. IPR011707. Cu-oxidase_3. IPR002355. Cu_oxidase_Cu_BS. IPR008972. Cupredoxin. [Graphical view]
PANTHER	PTHR10127:SF89. PTHR10127:SF89. 1 hit.
Pfam	PF00394. Cu-oxidase. 1 hit. PF07731. Cu-oxidase_2. 1 hit. PF07732. Cu-oxidase_3. 3 hits. [Graphical view]
SUPFAM	SSF49503. Cupredoxin. 6 hits.
PROSITE	PS00079. MULTICOPPER_OXIDASE1. 3 hits. PS00080. MULTICOPPER_OXIDASE2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	CP. mouse.
NextBio	282456.
SOURCE	Search...

Entry information

Entry name

CERU_MOUSE

Accession

Primary (citable) accession number: Q61147
Secondary accession number(s): Q6P5C8

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	December 4, 2007
Last modified:	May 1, 2013
This is version 103 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents