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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.By similarity1 Publication

Catalytic activityi

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

Cofactori

Cu cationNote: Binds 6 Cu cations 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
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 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
Complete GO annotation...

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.
InParanoidiP13635.

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

        10         20         30         40         50
MKFLLLSALL FLHSSLAWTR EKHYYIGITE AVWDYASGSE EKELISVDTE
60 70 80 90 100
QSNFYLRNGP DRIGRKYKKA LYSEYTDGTF TKTIDKPAWL GFLGPVIKAE
110 120 130 140 150
VGDKVSVHVK NFASRPYTFH AHGVTYTKAN EGAIYPDNTT DFQRADDKLF
160 170 180 190 200
PGQQYLYVLR ANEPSPGEGD SNCVTRIYHS HVDAPKDIAS GLIGPLILCK
210 220 230 240 250
KGSLHKEKEE NIDQEFVLMF SVVDENLSWY LEDNIKTFCS EPEKVDKDNE
260 270 280 290 300
DFQESNRMYS INGYTFGSLP GLSMCAEDRV KWYLFGMGNE VDVHSELFHG
310 320 330 340 350
QALTSKNYHT DIINLFPATL IDVSMVAQNP GVWMLSCQNL NHLKAGLQAF
360 370 380 390 400
FQVRDCNKPS PDDDIQDRHV RHYYIAAEET IWDYAPSGTD TFTGENFTSL
410 420 430 440 450
GSDSRVFFEQ GATRIGGSYK KLVYREYTDD SFTNRKERGP DEEHLGILGP
460 470 480 490 500
VIWAEVGDII RVTFHNKGQF PLSIQPMGVR FTKENEGTYY GPDGRSSKQA
510 520 530 540 550
SHVAPKETFT YEWTVPKEMG PTYADPVCLS KMYYSGVDLT KDIFTGLIGP
560 570 580 590 600
MKICKKGSLL ADGRQKDVDK EFYLFATVFD ENESLLLDDN IRMFTTAPEN
610 620 630 640 650
VDKEDEDFQE SNKMHSMNGF MYGNLPGLNM CLGESIVWYL FSAGNEADVH
660 670 680 690 700
GIYFSGNTYL SKGERRDTAN LFPHKSLTLL MTPDTEGSFD VECLTTDHYT
710 720 730 740 750
GGMKQKYTVN QCKGQFEDVT LYQGERTYYI AAVEVEWDYS PSRDWEMELH
760 770 780 790 800
HLQEQNVSNA FLDKEEFFIG SKYKKVVYRE FTDSTFREQV KRRAEEEHLG
810 820 830 840 850
MLGPLIHADV GAKVKVVFKN MATRPYSIHA HGVKTKSSTV APTLPGEVRT
860 870 880 890 900
YIWQIPERSG AGTEDSPCIP WAYYSTVDRV KDLYSGLIGP LIVCRKSYVK
910 920 930 940 950
VFNPKKKMEF SLLFLVFDEN ESWYLDDNIN TYPDHPEKDN KDNEEFIESN
960 970 980 990 1000
KMHAINGKMF GNLQGLTMHV GDEVNWYVMA MGNEIDLHTV HFHGHSFQYK
1010 1020 1030 1040 1050
HRGIHSSDVF DFFPGTYQTL EMFPQTPGTW LLHCHVTDHI HAGMVTTYTV

LPNQETKSG
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.Curated

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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.
InParanoidi P13635.

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: November 26, 2014
This is version 116 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