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P13635

- CERU_RAT

UniProt

P13635 - CERU_RAT

Protein

Ceruloplasmin

Gene

Cp

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 114 (01 Oct 2014)
      Sequence version 3 (01 Nov 1997)
      Previous versions | rss
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    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.By similarity1 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 2By similarity
    Metal bindingi122 – 1221Copper 2; type 3By similarity
    Metal bindingi179 – 1791Copper 2; type 3By similarity
    Metal bindingi181 – 1811Copper 3; type 3By similarity
    Metal bindingi294 – 2941Copper 4; type 1By similarity
    Metal bindingi337 – 3371Copper 4; type 1By similarity
    Metal bindingi342 – 3421Copper 4; type 1By similarity
    Metal bindingi650 – 6501Copper 5; type 1By similarity
    Metal bindingi693 – 6931Copper 5; type 1By similarity
    Metal bindingi698 – 6981Copper 5; type 1By similarity
    Metal bindingi703 – 7031Copper 5; type 1By similarity
    Metal bindingi988 – 9881Copper 6; type 1By similarity
    Metal bindingi991 – 9911Copper 1; type 2By similarity
    Metal bindingi993 – 9931Copper 3; type 3By similarity
    Metal bindingi1033 – 10331Copper 3; type 3By similarity
    Metal bindingi1034 – 10341Copper 6; type 1By similarity
    Metal bindingi1035 – 10351Copper 2; type 3By similarity
    Metal bindingi1039 – 10391Copper 6; type 1By similarity
    Metal bindingi1044 – 10441Copper 6; type 1By 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

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

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Secreted

    PTM / Processingi

    Molecule processing

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

    Amino acid modifications

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

    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.
    ModBaseiSearch...
    MobiDBiSearch...

    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

    Belongs to the multicopper oxidase family.Curated
    Contains 3 F5/8 type A domains.Curated
    Contains 6 plastocyanin-like domains.Curated

    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

    « Hide

    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.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti271 – 2711G → A in AAA40914. (PubMed:3818625)Curated
    Sequence conflicti604 – 6052ED → DN in AAA40914. (PubMed:3818625)Curated
    Sequence conflicti823 – 8231T → S in AAA40915. (PubMed:3818625)Curated
    Sequence conflicti833 – 8331V → L in AAA40915. (PubMed:3818625)Curated
    Sequence conflicti868 – 8681C → V in AAA40915. (PubMed:3818625)Curated
    Sequence conflicti891 – 8911L → R in AAA40915. (PubMed:3818625)Curated

    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: October 1, 2014
    This is version 114 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