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Q61147

- CERU_MOUSE

UniProt

Q61147 - CERU_MOUSE

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Protein

Ceruloplasmin

Gene

Cp

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 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. 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

Cu cationBy similarityNote: Binds 6 Cu cations 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
Complete GO annotation...

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.
REACT_251299. Metal ion SLC transporters.

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. blood microparticle Source: Ensembl
  2. extracellular space Source: MGI
  3. extracellular vesicular exosome Source: Ensembl
  4. lysosomal membrane Source: Ensembl
Complete GO annotation...

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

BgeeiQ61147.
CleanExiMM_CP.
ExpressionAtlasiQ61147. baseline and differential.
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.
InParanoidiQ61147.
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

« Hide

        10         20         30         40         50
MKFLLLSTFI FLYSSLALAR DKHYFIGITE AVWDYASGTE EKKLISVDTE
60 70 80 90 100
QSNFYLQNGP DRIGRKYKKA LYFEYTDGTF SKTIDKPAWL GFLGPVIKAE
110 120 130 140 150
VEDKVYVHLK NLASRIYTFH AHGVTYTKEY EGAVYPDNTT DFQRADDKVL
160 170 180 190 200
PGQQYVYVLH ANEPSPGEGD SNCVTRIYHS HVDAPKDIAS GLIGPLILCK
210 220 230 240 250
KGSLYKEKEK NIDQEFVLMF SVVDENLSWY LEDNIKTFCS EPEKVDKDNE
260 270 280 290 300
DFQESNRMYS INGYTFGSLP GLSMCAADRV KWYLFGMGNE VDVHSAFFHG
310 320 330 340 350
QALTSRNYQT DIINLFPATL IDAYMVAQNP GVWMLSCQNL NHLKAGLQAF
360 370 380 390 400
FQVRDCNKPS PEDNIQDRHV RHYYIAAEEV IWNYAPSGTD IFTGENLTAL
410 420 430 440 450
ESDSRVFFEQ GATRIGGSYK KMAYREYTDG SFTNRKQRGP DEEHLGILGP
460 470 480 490 500
VIWAEVGDTI KVTFHNKGQH PLSIQPMGVS FTAENEGTYY GPPGRSSQQA
510 520 530 540 550
ASHVAPKETF TYEWTVPKEM GPTYADPVCL SKMYYSGVDP TKDIFTGLIG
560 570 580 590 600
PMKICKKGSL LADGRQKDVD KEFYLFPTVF DENESLLLDD NIRMFTTAPD
610 620 630 640 650
QVDKEDEDFQ ESNKMHSMNG FMYGNQPGLN MCLGESIVWY LFSAGNEADV
660 670 680 690 700
HGIYFSGNTY LSKGERRDTA NLFPHKSLTL LMNPDTKGTF DVECLTTDHY
710 720 730 740 750
TGGMKQKYTV NQCQRQFEDF TVYLGERTYY VAAVEVEWDY SPSRAWEKEL
760 770 780 790 800
HHLQEQNVSN VFLDKEEFFI GSKYKKVVYR QFTDSSFREQ VKRRAEDEHL
810 820 830 840 850
GILGPPIHAN VGDKVKVVFK NMATRPYSIH AHGVKTESST VVPTLPGEVR
860 870 880 890 900
TYTWQIPERS GAGREDSACI PWAYYSTVDR VKDLYSGLIG PLIVCRKSYV
910 920 930 940 950
KVFSPKKKME FFLLFLVFDE NESWYLDDNI KTYSEHPEKV NKDNEEFLES
960 970 980 990 1000
NKMHAINGKM FGNLQGLTMH VKDEVNWYVM GMGNEIDLHT VHFHGHSFQY
1010 1020 1030 1040 1050
KHRGVYSSDV FDLFPGTYQT LEMFPQTPGT WLLHCHVTDH VHAGMATTYT
1060
VLPVEQETKS G
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.
InParanoidi Q61147.
KOi K13624.
OrthoDBi EOG7V49XN.
PhylomeDBi Q61147.
TreeFami TF329807.

Enzyme and pathway databases

Reactomei REACT_205755. Iron uptake and transport.
REACT_251299. Metal ion SLC transporters.

Miscellaneous databases

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

Gene expression databases

Bgeei Q61147.
CleanExi MM_CP.
ExpressionAtlasi Q61147. baseline and differential.
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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 118 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