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P13635 (CERU_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 113. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length1059 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. May also play a role in fetal lung development or pulmonary antioxidant defense. involved in iron transport across the cell membrane By similarity. Provides Cu2+ ions for the ascorbate-mediated deaminase degradation of the heparan sulfate chains of GPC1. Ref.3

Catalytic activity

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

Cofactor

Binds 6 copper ions per monomer.

Subcellular location

Secreted. Note: Colocalizes with GCP1 in secretory intracellular compartments. Ref.3

Tissue specificity

Synthesized in liver and secreted into the plasma. Also choroid plexus, yolk sac, placenta, and testis; not in stomach and small intestine. Fetal lung and liver.

Induction

By inflammation.

Sequence similarities

Belongs to the multicopper oxidase family.

Contains 3 F5/8 type A domains.

Contains 6 plastocyanin-like domains.

Sequence caution

The sequence AAA40914.1 differs from that shown. Reason: Wrong order of assembly of the mRNA fragments.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919 Probable
Chain20 – 10591040Ceruloplasmin
PRO_0000002914

Regions

Domain20 – 356337F5/8 type A 1
Domain20 – 199180Plastocyanin-like 1
Domain208 – 354147Plastocyanin-like 2
Domain369 – 712344F5/8 type A 2
Domain369 – 554186Plastocyanin-like 3
Domain564 – 710147Plastocyanin-like 4
Domain724 – 1055332F5/8 type A 3
Domain724 – 894171Plastocyanin-like 5
Domain902 – 1051150Plastocyanin-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 binding6501Copper 5; type 1 By similarity
Metal binding6931Copper 5; type 1 By similarity
Metal binding6981Copper 5; type 1 By similarity
Metal binding7031Copper 5; type 1 By similarity
Metal binding9881Copper 6; type 1 By similarity
Metal binding9911Copper 1; type 2 By similarity
Metal binding9931Copper 3; type 3 By similarity
Metal binding10331Copper 3; type 3 By similarity
Metal binding10341Copper 6; type 1 By similarity
Metal binding10351Copper 2; type 3 By similarity
Metal binding10391Copper 6; type 1 By similarity
Metal binding10441Copper 6; type 1 By similarity

Amino acid modifications

Glycosylation1381N-linked (GlcNAc...) Potential
Glycosylation2261N-linked (GlcNAc...) Potential
Glycosylation3961N-linked (GlcNAc...) Potential
Glycosylation5821N-linked (GlcNAc...) Potential
Glycosylation7561N-linked (GlcNAc...) Potential
Glycosylation9201N-linked (GlcNAc...) Potential
Disulfide bond173 ↔ 199 By similarity
Disulfide bond275 ↔ 356 By similarity
Disulfide bond528 ↔ 554 By similarity
Disulfide bond631 ↔ 712 By similarity
Disulfide bond868 ↔ 894 By similarity

Experimental info

Sequence conflict2711G → A in AAA40914. Ref.2
Sequence conflict604 – 6052ED → DN in AAA40914. Ref.2
Sequence conflict8231T → S in AAA40915. Ref.2
Sequence conflict8331V → L in AAA40915. Ref.2
Sequence conflict8681C → V in AAA40915. Ref.2
Sequence conflict8911L → R in AAA40915. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P13635 [UniParc].

Last modified November 1, 1997. Version 3.
Checksum: 12BA3B990A0B95E3

FASTA1,059120,841
        10         20         30         40         50         60 
MKFLLLSALL FLHSSLAWTR EKHYYIGITE AVWDYASGSE EKELISVDTE QSNFYLRNGP 

        70         80         90        100        110        120 
DRIGRKYKKA LYSEYTDGTF TKTIDKPAWL GFLGPVIKAE VGDKVSVHVK NFASRPYTFH 

       130        140        150        160        170        180 
AHGVTYTKAN EGAIYPDNTT DFQRADDKLF PGQQYLYVLR ANEPSPGEGD SNCVTRIYHS 

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

       250        260        270        280        290        300 
EPEKVDKDNE DFQESNRMYS INGYTFGSLP GLSMCAEDRV KWYLFGMGNE VDVHSELFHG 

       310        320        330        340        350        360 
QALTSKNYHT DIINLFPATL IDVSMVAQNP GVWMLSCQNL NHLKAGLQAF FQVRDCNKPS 

       370        380        390        400        410        420 
PDDDIQDRHV RHYYIAAEET IWDYAPSGTD TFTGENFTSL GSDSRVFFEQ GATRIGGSYK 

       430        440        450        460        470        480 
KLVYREYTDD SFTNRKERGP DEEHLGILGP VIWAEVGDII RVTFHNKGQF PLSIQPMGVR 

       490        500        510        520        530        540 
FTKENEGTYY GPDGRSSKQA SHVAPKETFT YEWTVPKEMG PTYADPVCLS KMYYSGVDLT 

       550        560        570        580        590        600 
KDIFTGLIGP MKICKKGSLL ADGRQKDVDK EFYLFATVFD ENESLLLDDN IRMFTTAPEN 

       610        620        630        640        650        660 
VDKEDEDFQE SNKMHSMNGF MYGNLPGLNM CLGESIVWYL FSAGNEADVH GIYFSGNTYL 

       670        680        690        700        710        720 
SKGERRDTAN LFPHKSLTLL MTPDTEGSFD VECLTTDHYT GGMKQKYTVN QCKGQFEDVT 

       730        740        750        760        770        780 
LYQGERTYYI AAVEVEWDYS PSRDWEMELH HLQEQNVSNA FLDKEEFFIG SKYKKVVYRE 

       790        800        810        820        830        840 
FTDSTFREQV KRRAEEEHLG MLGPLIHADV GAKVKVVFKN MATRPYSIHA HGVKTKSSTV 

       850        860        870        880        890        900 
APTLPGEVRT YIWQIPERSG AGTEDSPCIP WAYYSTVDRV KDLYSGLIGP LIVCRKSYVK 

       910        920        930        940        950        960 
VFNPKKKMEF SLLFLVFDEN ESWYLDDNIN TYPDHPEKDN KDNEEFIESN KMHAINGKMF 

       970        980        990       1000       1010       1020 
GNLQGLTMHV GDEVNWYVMA MGNEIDLHTV HFHGHSFQYK HRGIHSSDVF DFFPGTYQTL 

      1030       1040       1050 
EMFPQTPGTW LLHCHVTDHI HAGMVTTYTV LPNQETKSG 

« Hide

References

[1]"Primary structure of rat ceruloplasmin and analysis of tissue-specific gene expression during development."
Fleming R.E., Gitlin J.D.
J. Biol. Chem. 265:7701-7707(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
Strain: Sprague-Dawley.
Tissue: Liver and Lung.
[2]"Rat ceruloplasmin. Molecular cloning and gene expression in liver, choroid plexus, yolk sac, placenta, and testis."
Aldred A.R., Grimes A., Schreiber G., Mercer J.F.B.
J. Biol. Chem. 262:2875-2878(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 257-294; 571-612 AND 823-892.
Tissue: Liver.
[3]"Involvement of glycosylphosphatidylinositol-linked ceruloplasmin in the copper/zinc-nitric oxide-dependent degradation of glypican-1 heparan sulfate in rat C6 glioma cells."
Mani K., Cheng F., Havsmark B., David S., Fransson L.A.
J. Biol. Chem. 279:12918-12923(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: COPPER-BINDING, FUNCTION, SUBCELLULAR LOCATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L33869 mRNA. Translation: AAA40917.1.
M80529 Genomic DNA. Translation: AAB65820.1.
J02670 mRNA. Translation: AAA40914.1. Sequence problems.
M14102 mRNA. Translation: AAA40915.1.
PIRA35210.
UniGeneRn.32777.

3D structure databases

ProteinModelPortalP13635.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP13635. 1 interaction.

PTM databases

PhosphoSiteP13635.

Proteomic databases

PaxDbP13635.
PRIDEP13635.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

UCSCRGD:2387. rat.

Organism-specific databases

RGD2387. Cp.

Phylogenomic databases

eggNOGNOG276067.
HOGENOMHOG000231499.
HOVERGENHBG003674.

Gene expression databases

GenevestigatorP13635.

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

NextBio602829.
PROP13635.

Entry information

Entry nameCERU_RAT
AccessionPrimary (citable) accession number: P13635
Secondary accession number(s): Q64719
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: November 1, 1997
Last modified: June 11, 2014
This is version 113 of the entry and version 3 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