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Q61147 (CERU_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 114. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ceruloplasmin

EC=1.16.3.1
Alternative name(s):
Ferroxidase
Gene names
Name:Cp
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length1061 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919 By similarity
Chain20 – 10611042Ceruloplasmin
PRO_0000002913

Regions

Domain20 – 356337F5/8 type A 1
Domain20 – 199180Plastocyanin-like 1
Domain208 – 356149Plastocyanin-like 2
Domain369 – 713345F5/8 type A 2
Domain369 – 555187Plastocyanin-like 3
Domain565 – 713149Plastocyanin-like 4
Domain725 – 1056332F5/8 type A 3
Domain725 – 895171Plastocyanin-like 5
Domain903 – 1056154Plastocyanin-like 6

Sites

Metal binding1201Copper 1; type 2 By similarity
Metal binding1221Copper 2; type 3 By similarity
Metal binding1791Copper 2; type 3 By similarity
Metal binding1811Copper 3; type 3 By similarity
Metal binding2941Copper 4; type 1 By similarity
Metal binding3371Copper 4; type 1 By similarity
Metal binding3421Copper 4; type 1 By similarity
Metal binding6511Copper 5; type 1 By similarity
Metal binding6941Copper 5; type 1 By similarity
Metal binding6991Copper 5; type 1 By similarity
Metal binding7041Copper 5; type 1 By similarity
Metal binding9891Copper 6; type 1 By similarity
Metal binding9921Copper 1; type 2 By similarity
Metal binding9941Copper 3; type 3 By similarity
Metal binding10341Copper 3; type 3 By similarity
Metal binding10351Copper 6; type 1 By similarity
Metal binding10361Copper 2; type 3 By similarity
Metal binding10401Copper 6; type 1 By similarity
Metal binding10451Copper 6; type 1 By similarity

Amino acid modifications

Glycosylation1381N-linked (GlcNAc...) Ref.3 Ref.4
Glycosylation2261N-linked (GlcNAc...) Potential
Glycosylation3961N-linked (GlcNAc...) Potential
Glycosylation5831N-linked (GlcNAc...) Potential
Glycosylation7571N-linked (GlcNAc...) Ref.3 Ref.4
Glycosylation9211N-linked (GlcNAc...) Potential
Disulfide bond173 ↔ 199 By similarity
Disulfide bond275 ↔ 356 By similarity
Disulfide bond529 ↔ 555 By similarity
Disulfide bond632 ↔ 713 By similarity
Disulfide bond869 ↔ 895 By similarity

Experimental info

Sequence conflict3541R → Q in AAB07996. Ref.1
Sequence conflict361 – 3622PE → SK in AAB07996. Ref.1
Sequence conflict366 – 3683QDR → RGK in AAB07996. Ref.1
Sequence conflict3891T → I in AAB07996. Ref.1
Sequence conflict394 – 3963GEN → EEK in AAB07996. Ref.1
Sequence conflict400 – 4012LE → SG in AAB07996. Ref.1
Sequence conflict4051R → G in AAB07996. Ref.1
Sequence conflict4371Q → E in AAB07996. Ref.1
Sequence conflict4711P → H in AAB07996. Ref.1
Sequence conflict4951R → A in AAB07996. Ref.1
Sequence conflict5371G → A in AAB07996. Ref.1
Sequence conflict5971T → H in AAB07996. Ref.1
Sequence conflict627 – 6304PGLN → SWPH in AAB07996. Ref.1
Sequence conflict6621S → C in AAB07996. Ref.1
Sequence conflict6661R → E in AAB07996. Ref.1
Sequence conflict7321A → D in AAB07996. Ref.1
Sequence conflict7961E → EE in AAB07996. Ref.1
Sequence conflict8501R → A in AAB07996. Ref.1
Sequence conflict9791V → L in AAB07996. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q61147 [UniParc].

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

FASTA1,061121,151
        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' 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.
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.
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.
CCDSCCDS38401.1.
RefSeqNP_001263177.1. NM_001276248.1.
NP_031778.2. NM_007752.3.
UniGeneMm.13787.

3D structure databases

ProteinModelPortalQ61147.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ61147. 6 interactions.
MINTMINT-4090622.

PTM databases

PhosphoSiteQ61147.

Proteomic databases

MaxQBQ61147.
PaxDbQ61147.
PRIDEQ61147.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000091309; ENSMUSP00000088857; ENSMUSG00000003617.
GeneID12870.
KEGGmmu:12870.
UCSCuc008orz.1. mouse.

Organism-specific databases

CTD1356.
MGIMGI:88476. Cp.

Phylogenomic databases

eggNOGNOG276067.
GeneTreeENSGT00550000074552.
HOGENOMHOG000231499.
HOVERGENHBG003674.
KOK13624.
OrthoDBEOG7V49XN.
PhylomeDBQ61147.
TreeFamTF329807.

Gene expression databases

ArrayExpressQ61147.
BgeeQ61147.
CleanExMM_CP.
GenevestigatorQ61147.

Family and domain databases

Gene3D2.60.40.420. 6 hits.
InterProIPR027150. CP.
IPR001117. Cu-oxidase.
IPR011706. Cu-oxidase_2.
IPR011707. Cu-oxidase_3.
IPR002355. Cu_oxidase_Cu_BS.
IPR008972. Cupredoxin.
[Graphical view]
PANTHERPTHR10127:SF294. PTHR10127:SF294. 1 hit.
PfamPF00394. Cu-oxidase. 1 hit.
PF07731. Cu-oxidase_2. 1 hit.
PF07732. Cu-oxidase_3. 3 hits.
[Graphical view]
SUPFAMSSF49503. SSF49503. 6 hits.
PROSITEPS00079. MULTICOPPER_OXIDASE1. 3 hits.
PS00080. MULTICOPPER_OXIDASE2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSCP. mouse.
NextBio282456.
PROQ61147.
SOURCESearch...

Entry information

Entry nameCERU_MOUSE
AccessionPrimary (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: July 9, 2014
This is version 114 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

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