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Protein

Ceruloplasmin

Gene

CP

Organism
Ovis aries (Sheep)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript 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 (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 bindingi180 – 1801Copper 2; type 3By similarity
Metal bindingi182 – 1821Copper 3; type 3By similarity
Metal bindingi295 – 2951Copper 4; type 1By similarity
Metal bindingi338 – 3381Copper 4; type 1By similarity
Metal bindingi343 – 3431Copper 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 bindingi977 – 9771Copper 6; type 1By similarity
Metal bindingi980 – 9801Copper 1; type 2By similarity
Metal bindingi982 – 9821Copper 3; type 3By similarity
Metal bindingi1022 – 10221Copper 3; type 3By similarity
Metal bindingi1023 – 10231Copper 6; type 1By similarity
Metal bindingi1024 – 10241Copper 2; type 3By similarity
Metal bindingi1028 – 10281Copper 6; type 1By similarity
Metal bindingi1033 – 10331Copper 6; type 1By similarity

GO - Molecular functioni

  1. copper ion binding Source: InterPro
  2. ferroxidase activity Source: UniProtKB-EC

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

Names & Taxonomyi

Protein namesi
Recommended name:
Ceruloplasmin (EC:1.16.3.1)
Alternative name(s):
Ferroxidase
Gene namesi
Name:CP
OrganismiOvis aries (Sheep)
Taxonomic identifieri9940 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeCaprinaeOvis
ProteomesiUP000002356 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

  1. extracellular region Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1919Sequence AnalysisAdd
BLAST
Chaini20 – 10481029CeruloplasminPRO_0000227940Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi138 – 1381N-linked (GlcNAc...)Sequence Analysis
Glycosylationi227 – 2271N-linked (GlcNAc...)Sequence Analysis
Glycosylationi556 – 5561N-linked (GlcNAc...)Sequence Analysis
Glycosylationi582 – 5821N-linked (GlcNAc...)Sequence Analysis
Glycosylationi756 – 7561N-linked (GlcNAc...)Sequence Analysis
Glycosylationi920 – 9201N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Glycoprotein

Proteomic databases

PRIDEiQ9XT27.

Expressioni

Tissue specificityi

Expressed by the liver and secreted in plasma. Also expressed in the hypothalamus, spleen and uterus. No expression in the cortex, heart, intestine or kidney.1 Publication

Structurei

3D structure databases

ProteinModelPortaliQ9XT27.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini20 – 357338F5/8 type A 1Add
BLAST
Domaini20 – 200181Plastocyanin-like 1Add
BLAST
Domaini209 – 355147Plastocyanin-like 2Add
BLAST
Domaini370 – 712343F5/8 type A 2Add
BLAST
Domaini370 – 554185Plastocyanin-like 3Add
BLAST
Domaini564 – 710147Plastocyanin-like 4Add
BLAST
Domaini724 – 1044321F5/8 type A 3Add
BLAST
Domaini724 – 894171Plastocyanin-like 5Add
BLAST
Domaini902 – 1040139Plastocyanin-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

HOVERGENiHBG003674.
KOiK13624.

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.

Q9XT27-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKIFLLCIFL ILCGTSVWAK DKHYYIGIIE TAWNYASDHA EKKLISVDTE
60 70 80 90 100
HSNIYLQNGP NRIGSVYKKA VYLQYTDENF RTVIEKPVWL GFLGPIIKAE
110 120 130 140 150
TGDKVYVHLK NFASRPYTFH AHGLTYYKEH EGAIYPDNTT DLQKADDKVQ
160 170 180 190 200
PGEQCLYILH ANPEQGPGEE DSNCVTRIYH SHIDAPKDIA SGLIGPLIHC
210 220 230 240 250
KKDSLDEEKE KNIDKEFVVM FSVVDENLSW YLEENIKTYC SEPEKVEQDN
260 270 280 290 300
EDFQESNRMY SVNGYAFGSL PGLSMCAEDR VKWYLFGMGN EIDVHAAFFH
310 320 330 340 350
GQVLTSKNYR VDTINLFPAT LFDAFMVAQN PGQWMLSCQN LNHLKAGLQA
360 370 380 390 400
FFWVQDCKKS SSEDNIHGKN VRHYYIAAEE VIWNYAPSGI DAFTKENLRA
410 420 430 440 450
PGSASEAFFE QGPTRIGGSY KKLVYREYTD ASFSNQKERG PEEEHLGILG
460 470 480 490 500
PVIAAEVGDT IRVTFHNKAA HPLSIEPIGV RVDKNNEGTY YSPTGSGPPP
510 520 530 540 550
SGSHVAPKGT FTYEWTVPKE VGPTYKDPVC LAKMYYSGST KDIFTGLIGP
560 570 580 590 600
MKICRNGSLL ANGRLKNVDK EFYLFPTVFD ENESLLLDDN IKMFTTAPDQ
610 620 630 640 650
VDKENEDFQE SNKMHSMNGF MYGNQPGLSM CQGDSVMWYL FSAGNEVDIH
660 670 680 690 700
GIYFSGNTYL SRGERRDTAN LFPQTSLSLF MQPDTAGTFD VECLTTDHYT
710 720 730 740 750
GGMKQKYTVS QCGQRSEDLY LYLGERTYYI AAVEVEWDYS PSRKWEKELH
760 770 780 790 800
HLQEQNLSNA FLDKEEFYIG SKYKKVVYRQ FTDSTFQVPV ERKGEEEHLG
810 820 830 840 850
ILGPQLHADV GDKVNIIFKN MATRPYSIHA HGVKTESSTV TPTAPGETRT
860 870 880 890 900
YIWKIPERSG AGMGDSPCIP WVYYSTVDRV KDLFSGLIGP LIVCRKHYLK
910 920 930 940 950
VSNPIKKLEF SLLFLVFDEN ESWYLDDNIK TYSDHPEKVD KANEEFMESN
960 970 980 990 1000
KMHAINGRMF GNLQGLTMHV GNEVDLHSVH FHGHSFQYQH RGIYTSDVFD
1010 1020 1030 1040
LFPGTYQTLE MTPKTPGIWL LHCHVTDHIH AGMETTYTVL PNEEIKSG
Length:1,048
Mass (Da):119,126
Last modified:November 1, 1999 - v1
Checksum:i925F16D7B0549CBB
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF134814 mRNA. Translation: AAD41477.1.
RefSeqiNP_001009733.1. NM_001009733.1.
UniGeneiOar.706.

Genome annotation databases

GeneIDi443053.
KEGGioas:443053.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF134814 mRNA. Translation: AAD41477.1.
RefSeqiNP_001009733.1. NM_001009733.1.
UniGeneiOar.706.

3D structure databases

ProteinModelPortaliQ9XT27.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiQ9XT27.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi443053.
KEGGioas:443053.

Organism-specific databases

CTDi1356.

Phylogenomic databases

HOVERGENiHBG003674.
KOiK13624.

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]
ProtoNetiSearch...

Publicationsi

  1. "Cloning and expression analysis of the sheep ceruloplasmin cDNA."
    Lockhart P.J., Mercer J.F.B.
    Gene 236:251-257(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
    Tissue: Liver.

Entry informationi

Entry nameiCERU_SHEEP
AccessioniPrimary (citable) accession number: Q9XT27
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 21, 2006
Last sequence update: November 1, 1999
Last modified: January 7, 2015
This is version 69 of the entry and version 1 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.