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Q61147

- CERU_MOUSE

UniProt

Q61147 - CERU_MOUSE

Protein

Ceruloplasmin

Gene

Cp

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 116 (01 Oct 2014)
      Sequence version 2 (04 Dec 2007)
      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. 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.By similarity

    Catalytic activityi

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

    Cofactori

    Binds 6 copper ions per monomer.By similarity

    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 bindingi651 – 6511Copper 5; type 1By similarity
    Metal bindingi694 – 6941Copper 5; type 1By similarity
    Metal bindingi699 – 6991Copper 5; type 1By similarity
    Metal bindingi704 – 7041Copper 5; type 1By similarity
    Metal bindingi989 – 9891Copper 6; type 1By similarity
    Metal bindingi992 – 9921Copper 1; type 2By similarity
    Metal bindingi994 – 9941Copper 3; type 3By similarity
    Metal bindingi1034 – 10341Copper 3; type 3By similarity
    Metal bindingi1035 – 10351Copper 6; type 1By similarity
    Metal bindingi1036 – 10361Copper 2; type 3By similarity
    Metal bindingi1040 – 10401Copper 6; type 1By similarity
    Metal bindingi1045 – 10451Copper 6; type 1By similarity

    GO - Molecular functioni

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

    GO - Biological processi

    1. cellular iron ion homeostasis Source: InterPro
    2. copper ion transport Source: UniProtKB-KW

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Copper transport, Ion transport, Transport

    Keywords - Ligandi

    Copper, Metal-binding

    Enzyme and pathway databases

    ReactomeiREACT_205755. Iron uptake and transport.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ceruloplasmin (EC:1.16.3.1)
    Alternative name(s):
    Ferroxidase
    Gene namesi
    Name:Cp
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 3

    Organism-specific databases

    MGIiMGI:88476. Cp.

    Subcellular locationi

    Secreted
    Note: Colocalizes with GCP1 in secretory intracellular compartments.By similarity

    GO - Cellular componenti

    1. extracellular space Source: MGI
    2. lysosomal membrane Source: Ensembl

    Keywords - Cellular componenti

    Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1919By similarityAdd
    BLAST
    Chaini20 – 10611042CeruloplasminPRO_0000002913Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi138 – 1381N-linked (GlcNAc...)2 Publications
    Disulfide bondi173 ↔ 199By similarity
    Glycosylationi226 – 2261N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi275 ↔ 356By similarity
    Glycosylationi396 – 3961N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi529 ↔ 555By similarity
    Glycosylationi583 – 5831N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi632 ↔ 713By similarity
    Glycosylationi757 – 7571N-linked (GlcNAc...)2 Publications
    Disulfide bondi869 ↔ 895By similarity
    Glycosylationi921 – 9211N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    MaxQBiQ61147.
    PaxDbiQ61147.
    PRIDEiQ61147.

    PTM databases

    PhosphoSiteiQ61147.

    Expressioni

    Tissue specificityi

    Expressed in many tissues, including liver, eye and brain.1 Publication

    Gene expression databases

    ArrayExpressiQ61147.
    BgeeiQ61147.
    CleanExiMM_CP.
    GenevestigatoriQ61147.

    Interactioni

    Protein-protein interaction databases

    IntActiQ61147. 6 interactions.
    MINTiMINT-4090622.

    Structurei

    3D structure databases

    ProteinModelPortaliQ61147.
    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 – 356149Plastocyanin-like 2Add
    BLAST
    Domaini369 – 713345F5/8 type A 2Add
    BLAST
    Domaini369 – 555187Plastocyanin-like 3Add
    BLAST
    Domaini565 – 713149Plastocyanin-like 4Add
    BLAST
    Domaini725 – 1056332F5/8 type A 3Add
    BLAST
    Domaini725 – 895171Plastocyanin-like 5Add
    BLAST
    Domaini903 – 1056154Plastocyanin-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.
    GeneTreeiENSGT00550000074552.
    HOGENOMiHOG000231499.
    HOVERGENiHBG003674.
    KOiK13624.
    OrthoDBiEOG7V49XN.
    PhylomeDBiQ61147.
    TreeFamiTF329807.

    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.

    Q61147-1 [UniParc]FASTAAdd to Basket

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    MKFLLLSTFI FLYSSLALAR DKHYFIGITE AVWDYASGTE EKKLISVDTE     50
    QSNFYLQNGP DRIGRKYKKA LYFEYTDGTF SKTIDKPAWL GFLGPVIKAE 100
    VEDKVYVHLK NLASRIYTFH AHGVTYTKEY EGAVYPDNTT DFQRADDKVL 150
    PGQQYVYVLH ANEPSPGEGD SNCVTRIYHS HVDAPKDIAS GLIGPLILCK 200
    KGSLYKEKEK NIDQEFVLMF SVVDENLSWY LEDNIKTFCS EPEKVDKDNE 250
    DFQESNRMYS INGYTFGSLP GLSMCAADRV KWYLFGMGNE VDVHSAFFHG 300
    QALTSRNYQT DIINLFPATL IDAYMVAQNP GVWMLSCQNL NHLKAGLQAF 350
    FQVRDCNKPS PEDNIQDRHV RHYYIAAEEV IWNYAPSGTD IFTGENLTAL 400
    ESDSRVFFEQ GATRIGGSYK KMAYREYTDG SFTNRKQRGP DEEHLGILGP 450
    VIWAEVGDTI KVTFHNKGQH PLSIQPMGVS FTAENEGTYY GPPGRSSQQA 500
    ASHVAPKETF TYEWTVPKEM GPTYADPVCL SKMYYSGVDP TKDIFTGLIG 550
    PMKICKKGSL LADGRQKDVD KEFYLFPTVF DENESLLLDD NIRMFTTAPD 600
    QVDKEDEDFQ ESNKMHSMNG FMYGNQPGLN MCLGESIVWY LFSAGNEADV 650
    HGIYFSGNTY LSKGERRDTA NLFPHKSLTL LMNPDTKGTF DVECLTTDHY 700
    TGGMKQKYTV NQCQRQFEDF TVYLGERTYY VAAVEVEWDY SPSRAWEKEL 750
    HHLQEQNVSN VFLDKEEFFI GSKYKKVVYR QFTDSSFREQ VKRRAEDEHL 800
    GILGPPIHAN VGDKVKVVFK NMATRPYSIH AHGVKTESST VVPTLPGEVR 850
    TYTWQIPERS GAGREDSACI PWAYYSTVDR VKDLYSGLIG PLIVCRKSYV 900
    KVFSPKKKME FFLLFLVFDE NESWYLDDNI KTYSEHPEKV NKDNEEFLES 950
    NKMHAINGKM FGNLQGLTMH VKDEVNWYVM GMGNEIDLHT VHFHGHSFQY 1000
    KHRGVYSSDV FDLFPGTYQT LEMFPQTPGT WLLHCHVTDH VHAGMATTYT 1050
    VLPVEQETKS G 1061
    Length:1,061
    Mass (Da):121,151
    Last modified:December 4, 2007 - v2
    Checksum:i16A2DAEA4F483886
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti354 – 3541R → Q in AAB07996. (PubMed:8690795)Curated
    Sequence conflicti361 – 3622PE → SK in AAB07996. (PubMed:8690795)Curated
    Sequence conflicti366 – 3683QDR → RGK in AAB07996. (PubMed:8690795)Curated
    Sequence conflicti389 – 3891T → I in AAB07996. (PubMed:8690795)Curated
    Sequence conflicti394 – 3963GEN → EEK in AAB07996. (PubMed:8690795)Curated
    Sequence conflicti400 – 4012LE → SG in AAB07996. (PubMed:8690795)Curated
    Sequence conflicti405 – 4051R → G in AAB07996. (PubMed:8690795)Curated
    Sequence conflicti437 – 4371Q → E in AAB07996. (PubMed:8690795)Curated
    Sequence conflicti471 – 4711P → H in AAB07996. (PubMed:8690795)Curated
    Sequence conflicti495 – 4951R → A in AAB07996. (PubMed:8690795)Curated
    Sequence conflicti537 – 5371G → A in AAB07996. (PubMed:8690795)Curated
    Sequence conflicti597 – 5971T → H in AAB07996. (PubMed:8690795)Curated
    Sequence conflicti627 – 6304PGLN → SWPH in AAB07996. (PubMed:8690795)Curated
    Sequence conflicti662 – 6621S → C in AAB07996. (PubMed:8690795)Curated
    Sequence conflicti666 – 6661R → E in AAB07996. (PubMed:8690795)Curated
    Sequence conflicti732 – 7321A → D in AAB07996. (PubMed:8690795)Curated
    Sequence conflicti796 – 7961E → EE in AAB07996. (PubMed:8690795)Curated
    Sequence conflicti850 – 8501R → A in AAB07996. (PubMed:8690795)Curated
    Sequence conflicti979 – 9791V → L in AAB07996. (PubMed:8690795)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U49430 mRNA. Translation: AAB07996.1.
    BC062957 mRNA. Translation: AAH62957.1.
    CCDSiCCDS38401.1.
    RefSeqiNP_001263177.1. NM_001276248.1.
    NP_031778.2. NM_007752.3.
    UniGeneiMm.13787.

    Genome annotation databases

    EnsembliENSMUST00000091309; ENSMUSP00000088857; ENSMUSG00000003617.
    GeneIDi12870.
    KEGGimmu:12870.
    UCSCiuc008orz.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U49430 mRNA. Translation: AAB07996.1 .
    BC062957 mRNA. Translation: AAH62957.1 .
    CCDSi CCDS38401.1.
    RefSeqi NP_001263177.1. NM_001276248.1.
    NP_031778.2. NM_007752.3.
    UniGenei Mm.13787.

    3D structure databases

    ProteinModelPortali Q61147.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi Q61147. 6 interactions.
    MINTi MINT-4090622.

    PTM databases

    PhosphoSitei Q61147.

    Proteomic databases

    MaxQBi Q61147.
    PaxDbi Q61147.
    PRIDEi Q61147.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000091309 ; ENSMUSP00000088857 ; ENSMUSG00000003617 .
    GeneIDi 12870.
    KEGGi mmu:12870.
    UCSCi uc008orz.1. mouse.

    Organism-specific databases

    CTDi 1356.
    MGIi MGI:88476. Cp.

    Phylogenomic databases

    eggNOGi NOG276067.
    GeneTreei ENSGT00550000074552.
    HOGENOMi HOG000231499.
    HOVERGENi HBG003674.
    KOi K13624.
    OrthoDBi EOG7V49XN.
    PhylomeDBi Q61147.
    TreeFami TF329807.

    Enzyme and pathway databases

    Reactomei REACT_205755. Iron uptake and transport.

    Miscellaneous databases

    ChiTaRSi CP. mouse.
    NextBioi 282456.
    PROi Q61147.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q61147.
    Bgeei Q61147.
    CleanExi MM_CP.
    Genevestigatori Q61147.

    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. "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.

    Entry informationi

    Entry nameiCERU_MOUSE
    AccessioniPrimary (citable) accession number: Q61147
    Secondary accession number(s): Q6P5C8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: December 4, 2007
    Last modified: October 1, 2014
    This is version 116 of the entry and version 2 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. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3