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P13635

- CERU_RAT

UniProt

P13635 - CERU_RAT

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Protein

Ceruloplasmin

Gene
Cp
Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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 GPC1.1 Publication

Catalytic activityi

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

Cofactori

Binds 6 copper ions per monomer.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi120 – 1201Copper 1; type 2 By similarity
Metal bindingi122 – 1221Copper 2; type 3 By similarity
Metal bindingi179 – 1791Copper 2; type 3 By similarity
Metal bindingi181 – 1811Copper 3; type 3 By similarity
Metal bindingi294 – 2941Copper 4; type 1 By similarity
Metal bindingi337 – 3371Copper 4; type 1 By similarity
Metal bindingi342 – 3421Copper 4; type 1 By similarity
Metal bindingi650 – 6501Copper 5; type 1 By similarity
Metal bindingi693 – 6931Copper 5; type 1 By similarity
Metal bindingi698 – 6981Copper 5; type 1 By similarity
Metal bindingi703 – 7031Copper 5; type 1 By similarity
Metal bindingi988 – 9881Copper 6; type 1 By similarity
Metal bindingi991 – 9911Copper 1; type 2 By similarity
Metal bindingi993 – 9931Copper 3; type 3 By similarity
Metal bindingi1033 – 10331Copper 3; type 3 By similarity
Metal bindingi1034 – 10341Copper 6; type 1 By similarity
Metal bindingi1035 – 10351Copper 2; type 3 By similarity
Metal bindingi1039 – 10391Copper 6; type 1 By similarity
Metal bindingi1044 – 10441Copper 6; type 1 By similarity

GO - Molecular functioni

  1. copper ion binding Source: RGD
  2. ferroxidase activity Source: RGD

GO - Biological processi

  1. aging Source: RGD
  2. cellular iron ion homeostasis Source: RGD
  3. liver development Source: RGD
  4. lung development Source: RGD
  5. plasma membrane copper ion transport Source: RGD
  6. response to copper ion Source: RGD
  7. response to nutrient Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Copper transport, Ion transport, Transport

Keywords - Ligandi

Copper, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Ceruloplasmin (EC:1.16.3.1)
Alternative name(s):
Ferroxidase
Gene namesi
Name:Cp
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Unplaced

Organism-specific databases

RGDi2387. Cp.

Subcellular locationi

Secreted
Note: Colocalizes with GCP1 in secretory intracellular compartments.1 Publication

GO - Cellular componenti

  1. anchored component of plasma membrane Source: RGD
  2. extracellular space Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1919 InferredAdd
BLAST
Chaini20 – 10591040CeruloplasminPRO_0000002914Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi138 – 1381N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi173 ↔ 199 By similarity
Glycosylationi226 – 2261N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi275 ↔ 356 By similarity
Glycosylationi396 – 3961N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi528 ↔ 554 By similarity
Glycosylationi582 – 5821N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi631 ↔ 712 By similarity
Glycosylationi756 – 7561N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi868 ↔ 894 By similarity
Glycosylationi920 – 9201N-linked (GlcNAc...) Reviewed prediction

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiP13635.
PRIDEiP13635.

PTM databases

PhosphoSiteiP13635.

Expressioni

Tissue specificityi

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.

Inductioni

By inflammation.

Gene expression databases

GenevestigatoriP13635.

Interactioni

Protein-protein interaction databases

IntActiP13635. 1 interaction.

Structurei

3D structure databases

ProteinModelPortaliP13635.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini20 – 356337F5/8 type A 1Add
BLAST
Domaini20 – 199180Plastocyanin-like 1Add
BLAST
Domaini208 – 354147Plastocyanin-like 2Add
BLAST
Domaini369 – 712344F5/8 type A 2Add
BLAST
Domaini369 – 554186Plastocyanin-like 3Add
BLAST
Domaini564 – 710147Plastocyanin-like 4Add
BLAST
Domaini724 – 1055332F5/8 type A 3Add
BLAST
Domaini724 – 894171Plastocyanin-like 5Add
BLAST
Domaini902 – 1051150Plastocyanin-like 6Add
BLAST

Sequence similaritiesi

Contains 3 F5/8 type A domains.

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiNOG276067.
HOGENOMiHOG000231499.
HOVERGENiHBG003674.

Family and domain databases

Gene3Di2.60.40.420. 6 hits.
InterProiIPR027150. CP.
IPR001117. Cu-oxidase.
IPR011706. Cu-oxidase_2.
IPR011707. Cu-oxidase_3.
IPR002355. Cu_oxidase_Cu_BS.
IPR008972. Cupredoxin.
[Graphical view]
PANTHERiPTHR10127:SF294. PTHR10127:SF294. 1 hit.
PfamiPF00394. Cu-oxidase. 1 hit.
PF07731. Cu-oxidase_2. 1 hit.
PF07732. Cu-oxidase_3. 3 hits.
[Graphical view]
SUPFAMiSSF49503. SSF49503. 6 hits.
PROSITEiPS00079. MULTICOPPER_OXIDASE1. 3 hits.
PS00080. MULTICOPPER_OXIDASE2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P13635-1 [UniParc]FASTAAdd to Basket

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MKFLLLSALL FLHSSLAWTR EKHYYIGITE AVWDYASGSE EKELISVDTE     50
QSNFYLRNGP DRIGRKYKKA LYSEYTDGTF TKTIDKPAWL GFLGPVIKAE 100
VGDKVSVHVK NFASRPYTFH AHGVTYTKAN EGAIYPDNTT DFQRADDKLF 150
PGQQYLYVLR ANEPSPGEGD SNCVTRIYHS HVDAPKDIAS GLIGPLILCK 200
KGSLHKEKEE NIDQEFVLMF SVVDENLSWY LEDNIKTFCS EPEKVDKDNE 250
DFQESNRMYS INGYTFGSLP GLSMCAEDRV KWYLFGMGNE VDVHSELFHG 300
QALTSKNYHT DIINLFPATL IDVSMVAQNP GVWMLSCQNL NHLKAGLQAF 350
FQVRDCNKPS PDDDIQDRHV RHYYIAAEET IWDYAPSGTD TFTGENFTSL 400
GSDSRVFFEQ GATRIGGSYK KLVYREYTDD SFTNRKERGP DEEHLGILGP 450
VIWAEVGDII RVTFHNKGQF PLSIQPMGVR FTKENEGTYY GPDGRSSKQA 500
SHVAPKETFT YEWTVPKEMG PTYADPVCLS KMYYSGVDLT KDIFTGLIGP 550
MKICKKGSLL ADGRQKDVDK EFYLFATVFD ENESLLLDDN IRMFTTAPEN 600
VDKEDEDFQE SNKMHSMNGF MYGNLPGLNM CLGESIVWYL FSAGNEADVH 650
GIYFSGNTYL SKGERRDTAN LFPHKSLTLL MTPDTEGSFD VECLTTDHYT 700
GGMKQKYTVN QCKGQFEDVT LYQGERTYYI AAVEVEWDYS PSRDWEMELH 750
HLQEQNVSNA FLDKEEFFIG SKYKKVVYRE FTDSTFREQV KRRAEEEHLG 800
MLGPLIHADV GAKVKVVFKN MATRPYSIHA HGVKTKSSTV APTLPGEVRT 850
YIWQIPERSG AGTEDSPCIP WAYYSTVDRV KDLYSGLIGP LIVCRKSYVK 900
VFNPKKKMEF SLLFLVFDEN ESWYLDDNIN TYPDHPEKDN KDNEEFIESN 950
KMHAINGKMF GNLQGLTMHV GDEVNWYVMA MGNEIDLHTV HFHGHSFQYK 1000
HRGIHSSDVF DFFPGTYQTL EMFPQTPGTW LLHCHVTDHI HAGMVTTYTV 1050
LPNQETKSG 1059
Length:1,059
Mass (Da):120,841
Last modified:November 1, 1997 - v3
Checksum:i12BA3B990A0B95E3
GO

Sequence cautioni

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

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti271 – 2711G → A in AAA40914. 1 Publication
Sequence conflicti604 – 6052ED → DN in AAA40914. 1 Publication
Sequence conflicti823 – 8231T → S in AAA40915. 1 Publication
Sequence conflicti833 – 8331V → L in AAA40915. 1 Publication
Sequence conflicti868 – 8681C → V in AAA40915. 1 Publication
Sequence conflicti891 – 8911L → R in AAA40915. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L33869 mRNA. Translation: AAA40917.1.
M80529 Genomic DNA. Translation: AAB65820.1.
J02670 mRNA. Translation: AAA40914.1. Sequence problems.
M14102 mRNA. Translation: AAA40915.1.
PIRiA35210.
UniGeneiRn.32777.

Genome annotation databases

UCSCiRGD:2387. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L33869 mRNA. Translation: AAA40917.1 .
M80529 Genomic DNA. Translation: AAB65820.1 .
J02670 mRNA. Translation: AAA40914.1 . Sequence problems.
M14102 mRNA. Translation: AAA40915.1 .
PIRi A35210.
UniGenei Rn.32777.

3D structure databases

ProteinModelPortali P13635.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi P13635. 1 interaction.

PTM databases

PhosphoSitei P13635.

Proteomic databases

PaxDbi P13635.
PRIDEi P13635.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

UCSCi RGD:2387. rat.

Organism-specific databases

RGDi 2387. Cp.

Phylogenomic databases

eggNOGi NOG276067.
HOGENOMi HOG000231499.
HOVERGENi HBG003674.

Miscellaneous databases

NextBioi 602829.
PROi P13635.

Gene expression databases

Genevestigatori P13635.

Family and domain databases

Gene3Di 2.60.40.420. 6 hits.
InterProi IPR027150. CP.
IPR001117. Cu-oxidase.
IPR011706. Cu-oxidase_2.
IPR011707. Cu-oxidase_3.
IPR002355. Cu_oxidase_Cu_BS.
IPR008972. Cupredoxin.
[Graphical view ]
PANTHERi PTHR10127:SF294. PTHR10127:SF294. 1 hit.
Pfami PF00394. Cu-oxidase. 1 hit.
PF07731. Cu-oxidase_2. 1 hit.
PF07732. Cu-oxidase_3. 3 hits.
[Graphical view ]
SUPFAMi SSF49503. SSF49503. 6 hits.
PROSITEi PS00079. MULTICOPPER_OXIDASE1. 3 hits.
PS00080. MULTICOPPER_OXIDASE2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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.

Entry informationi

Entry nameiCERU_RAT
AccessioniPrimary (citable) accession number: P13635
Secondary accession number(s): Q64719
Entry historyi
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 statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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