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O93295 (ENTP8_CHICK) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 88. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ectonucleoside triphosphate diphosphohydrolase 8

Short name=E-NTPDase 8
Short name=NTPDase 8
Short name=NTPDase8
EC=3.6.1.5
Alternative name(s):
Liver ecto-ATP diphosphohydrolase
Gene names
Name:ENTPD8
OrganismGallus gallus (Chicken) [Reference proteome]
Taxonomic identifier9031 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiTestudines + Archosauria groupArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalliformesPhasianidaePhasianinaeGallus

Protein attributes

Sequence length493 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Canalicular ectonucleoside NTPDase responsible for the main hepatic NTPDase activity. Ectonucleoside ATPases catalyze the hydrolysis of gamma- and beta-phosphate residues of nucleotides, playing a central role in concentration of extracellular nucleotides. Ref.2 Ref.4

Catalytic activity

A nucleoside 5'-triphosphate + 2 H2O = a nucleoside 5'-phosphate + 2 phosphate. Ref.2

Cofactor

Ca2+ or Mg2+. Has lower efficiency with Mg2+ By similarity.

Subcellular location

Cell membrane; Multi-pass membrane protein Ref.2.

Post-translational modification

N-glycosylated.

Sequence similarities

Belongs to the GDA1/CD39 NTPase family.

Biophysicochemical properties

Kinetic parameters:

KM=0.51 mM for ATP Ref.2

KM=5.3 mM for ADP

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 493493Ectonucleoside triphosphate diphosphohydrolase 8
PRO_0000209905

Regions

Topological domain1 – 77Cytoplasmic Potential
Transmembrane8 – 2821Helical; Potential
Topological domain29 – 463435Extracellular Potential
Transmembrane464 – 48623Helical; Potential
Topological domain487 – 4937Cytoplasmic Potential

Sites

Active site1661Proton acceptor By similarity

Amino acid modifications

Glycosylation651N-linked (GlcNAc...) Potential
Glycosylation791N-linked (GlcNAc...) Potential
Glycosylation1331N-linked (GlcNAc...) Potential
Glycosylation2231N-linked (GlcNAc...) Potential
Glycosylation2341N-linked (GlcNAc...) Potential
Glycosylation2671N-linked (GlcNAc...) Potential
Glycosylation3241N-linked (GlcNAc...) Potential
Glycosylation3301N-linked (GlcNAc...) Potential
Glycosylation3611N-linked (GlcNAc...) Potential
Glycosylation3721N-linked (GlcNAc...) Potential
Glycosylation3821N-linked (GlcNAc...) Potential
Glycosylation4451N-linked (GlcNAc...) Potential
Disulfide bond76 ↔ 100 By similarity
Disulfide bond244 ↔ 291 By similarity
Disulfide bond327 ↔ 333 By similarity
Disulfide bond379 ↔ 401 By similarity

Experimental info

Sequence conflict161C → W AA sequence Ref.3
Sequence conflict211I → G AA sequence Ref.1
Sequence conflict278 – 2803RRI → QEN in AAL25086. Ref.2
Sequence conflict3161P → R in AAL25086. Ref.2
Sequence conflict3251L → F in AAL25086. Ref.2
Sequence conflict461 – 4622HE → QQ in AAL25086. Ref.2

Sequences

Sequence LengthMass (Da)Tools
O93295 [UniParc].

Last modified November 1, 1998. Version 1.
Checksum: F14FF4C3AA2F3603

FASTA49354,035
        10         20         30         40         50         60 
MEYKGKVVAG LLTATCVFSI IALILSAVDV KDVFLPPGTK YGLVFDAGST HTALYVYQWP 

        70         80         90        100        110        120 
ADKENGTGIV SQVESCTVNG SGISSYADDP AGAGASLKPC LDKAMAVIPV EQQWQTPTYL 

       130        140        150        160        170        180 
GATAGMRLLR EQNSTKAEQV FAEVSKAIRE FPVDFRGAQI LTGNEEGSFG WITVNYLLET 

       190        200        210        220        230        240 
LIKFSFAGKW EHPQNTEVLG ALDLGGASTQ ITFQPGVTIE DKNTSVLFRL YGTNYSLYTH 

       250        260        270        280        290        300 
SYLCYGQIQA SKRLMAALHQ DGSYVQNISH PCYPKGYRRI ITIAEIYDSP CVPTPSMLSP 

       310        320        330        340        350        360 
AQILTVTGTG NPAACPTAIL KLFNLTCGAN RTCGFDGVYQ PPVRGQFFAF AGFYYTFSFL 

       370        380        390        400        410        420 
NLTGQQSLSH VNATVWDFCN KNWSELVETF PQNKEHLHTY CVVGLYILTL LVDGYKFDEH 

       430        440        450        460        470        480 
TWSNIHFSQK AGNADIGWTL GFMLNLTNMI PTEALEHVKG HEPSLWAGAI SFIVLAIVAG 

       490 
LVAILLQCFW KSK 

« Hide

References

[1]"Molecular cloning of the chicken oviduct ecto-ATP-diphosphohydrolase."
Nagy A.K., Knowles A.F., Nagami G.T.
J. Biol. Chem. 273:16043-16049(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 1-21 AND 150-156.
Tissue: Oviduct.
[2]"Purification, characterization, cloning, and expression of the chicken liver ecto-ATP-diphosphohydrolase."
Knowles A.F., Nagy A.K., Strobel R.S., Wu-Weis M.
Eur. J. Biochem. 269:2373-2382(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, ENZYME ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION.
Tissue: Liver.
[3]"Immunolocalization of the ecto-ATPase and ecto-apyrase in chicken gizzard and stomach. Purification and N-terminal sequence of the stomach ecto-apyrase."
Lewis-Carl S., Kirley T.L.
J. Biol. Chem. 272:23645-23652(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-17.
Tissue: Stomach.
[4]"Either the carboxyl- or the amino-terminal region of the human ecto-ATPase (E-NTPDase 2) confers detergent and temperature sensitivity to the chicken ecto-ATP-diphosphohydrolase (E-NTPDase 8)."
Mukasa T., Lee Y., Knowles A.F.
Biochemistry 44:11160-11170(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF041355 mRNA. Translation: AAC26491.1.
AF426405 mRNA. Translation: AAL25086.1.
RefSeqNP_989578.1. NM_204247.1.
UniGeneGga.49226.

3D structure databases

ProteinModelPortalO93295.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9031.ENSGALP00000014500.

Proteomic databases

PaxDbO93295.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID374095.
KEGGgga:374095.

Organism-specific databases

CTD377841.

Phylogenomic databases

eggNOGCOG5371.
HOGENOMHOG000059572.
HOVERGENHBG018982.
InParanoidQ90X66.
KOK01510.
PhylomeDBO93295.

Family and domain databases

InterProIPR000407. GDA1_CD39_NTPase.
[Graphical view]
PANTHERPTHR11782. PTHR11782. 1 hit.
PfamPF01150. GDA1_CD39. 1 hit.
[Graphical view]
PROSITEPS01238. GDA1_CD39_NTPASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio20813614.
PROO93295.

Entry information

Entry nameENTP8_CHICK
AccessionPrimary (citable) accession number: O93295
Secondary accession number(s): Q90X66
Entry history
Integrated into UniProtKB/Swiss-Prot: June 20, 2001
Last sequence update: November 1, 1998
Last modified: April 16, 2014
This is version 88 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families