Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q5MY95 (ENTP8_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 82. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·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
Gene names
Name:ENTPD8
ORF Names:UNQ2492/PRO5779
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length495 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Canalicular ectonucleoside NTPDase responsible for the main hepatic NTPDase activity. Ectonucleoside NTPDases catalyze the hydrolysis of gamma- and beta-phosphate residues of nucleotides, playing a central role in concentration of extracellular nucleotides. Has activity toward ATP, ADP, UTP and UDP, but not toward AMP. Ref.1 Ref.2

Catalytic activity

A nucleoside 5'-triphosphate + 2 H2O = a nucleoside 5'-phosphate + 2 phosphate. Ref.1 Ref.2

Cofactor

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

Enzyme regulation

Not inhibited by ARL 67156. Ref.6

Subcellular location

Cell membrane; Multi-pass membrane protein By similarity.

Domain

The transmembranous domains are involved in regulation of enzyme activity. Ref.1

Post-translational modification

N-glycosylated. Ref.1

Sequence similarities

Belongs to the GDA1/CD39 NTPase family.

Biophysicochemical properties

Kinetic parameters:

KM=81 µM for ATP Ref.2

KM=137 µM for ADP

KM=480 µM for UTP

KM=241 µM for UDP

Vmax=790 nmol/min/mg enzyme with ATP as substrate

Vmax=163 nmol/min/mg enzyme with ADP as substrate

Vmax=1100 nmol/min/mg enzyme with UTP as substrate

Vmax=110 nmol/min/mg enzyme with UDP as substrate

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q5MY95-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q5MY95-2)

The sequence of this isoform differs from the canonical sequence as follows:
     351-387: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 495495Ectonucleoside triphosphate diphosphohydrolase 8
PRO_0000306882

Regions

Topological domain1 – 88Cytoplasmic Potential
Transmembrane9 – 2921Helical; Potential
Topological domain30 – 471442Extracellular Potential
Transmembrane472 – 49221Helical; Potential
Topological domain493 – 4953Cytoplasmic Potential

Sites

Active site1681Proton acceptor By similarity

Amino acid modifications

Glycosylation671N-linked (GlcNAc...) Potential
Glycosylation3041N-linked (GlcNAc...) Potential
Glycosylation3631N-linked (GlcNAc...) Potential
Disulfide bond78 ↔ 102 By similarity
Disulfide bond246 ↔ 292 By similarity
Disulfide bond329 ↔ 335 By similarity
Disulfide bond381 ↔ 403 By similarity

Natural variations

Alternative sequence351 – 38737Missing in isoform 2.
VSP_028559
Natural variant621L → P. Ref.1 Ref.2 Ref.3 Ref.5
Corresponds to variant rs6606582 [ dbSNP | Ensembl ].
VAR_035339
Natural variant4281E → K.
Corresponds to variant rs61491031 [ dbSNP | Ensembl ].
VAR_061385

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified October 2, 2007. Version 2.
Checksum: 030200E15F662D82

FASTA49553,904
        10         20         30         40         50         60 
MGLSRKEQVF LALLGASGVS GLTALILLLV EATSVLLPTD IKFGIVFDAG SSHTSLFLYQ 

        70         80         90        100        110        120 
WLANKENGTG VVSQALACQV EGPGISSYTS NAAQAGESLQ GCLEEALVLI PEAQHRKTPT 

       130        140        150        160        170        180 
FLGATAGMRL LSRKNSSQAR DIFAAVTQVL GRSPVDFWGA ELLAGQAEGA FGWITVNYGL 

       190        200        210        220        230        240 
GTLVKYSFTG EWIQPPEEML VGALDMGGAS TQITFVPGGP ILDKSTQADF RLYGSDYSVY 

       250        260        270        280        290        300 
THSYLCFGRD QMLSRLLVGL VQSRPAALLR HPCYLSGYQT TLALGPLYES PCVHATPPLS 

       310        320        330        340        350        360 
LPQNLTVEGT GNPGACVSAI RELFNFSSCQ GQEDCAFDGV YQPPLRGQFY AFSNFYYTFH 

       370        380        390        400        410        420 
FLNLTSRQPL STVNATIWEF CQRPWKLVEA SYPGQDRWLR DYCASGLYIL TLLHEGYGFS 

       430        440        450        460        470        480 
EETWPSLEFR KQAGGVDIGW TLGYMLNLTG MIPADAPAQW RAESYGVWVA KVVFMVLALV 

       490 
AVVGAALVQL FWLQD 

« Hide

Isoform 2 [UniParc].

Checksum: C2BEDCB65064B6B3
Show »

FASTA45849,393

References

« Hide 'large scale' references
[1]"Molecular cloning and characterization of expressed human ecto-nucleoside triphosphate diphosphohydrolase 8 (E-NTPDase 8) and its soluble extracellular domain."
Knowles A.F., Li C.
Biochemistry 45:7323-7333(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, ENZYME ACTIVITY, DOMAIN, GLYCOSYLATION, VARIANT PRO-62.
[2]"Cloning, purification, and identification of the liver canalicular ecto-ATPase as NTPDase8."
Fausther M., Lecka J., Kukulski F., Levesque S.A., Pelletier J., Zimmermann H., Dranoff J.A., Sevigny J.
Am. J. Physiol. 292:G785-G795(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, ENZYME ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, VARIANT PRO-62.
Tissue: Liver.
[3]"The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment."
Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J., Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P., Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E. expand/collapse author list , Heldens S., Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.
Genome Res. 13:2265-2270(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), VARIANT PRO-62.
[4]"DNA sequence and analysis of human chromosome 9."
Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L. expand/collapse author list , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"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] (ISOFORM 2), VARIANT PRO-62.
[6]"Specificity of the ecto-ATPase inhibitor ARL 67156 on human and mouse ectonucleotidases."
Levesque S.A., Lavoie E.G., Lecka J., Bigonnesse F., Sevigny J.
Br. J. Pharmacol. 152:141-150(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: ENZYME REGULATION.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY903953 Transcribed RNA. Translation: AAW83515.1.
AY903954 mRNA. Translation: AAW83516.1.
AY430414 mRNA. Translation: AAR04374.1.
AY359088 mRNA. Translation: AAQ89446.1.
BX322799 Genomic DNA. Translation: CAM24777.1.
BC141810 mRNA. Translation: AAI41811.1.
RefSeqNP_001028285.1. NM_001033113.1.
NP_940987.2. NM_198585.2.
UniGeneHs.512562.

3D structure databases

ProteinModelPortalQ5MY95.
SMRQ5MY95. Positions 41-458.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9606.ENSP00000360561.

Chemistry

BindingDBQ5MY95.
ChEMBLCHEMBL5338.

PTM databases

PhosphoSiteQ5MY95.

Polymorphism databases

DMDM158705943.

Proteomic databases

PaxDbQ5MY95.
PRIDEQ5MY95.

Protocols and materials databases

DNASU377841.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000344119; ENSP00000344089; ENSG00000188833. [Q5MY95-2]
ENST00000371506; ENSP00000360561; ENSG00000188833. [Q5MY95-1]
ENST00000472938; ENSP00000420531; ENSG00000188833. [Q5MY95-1]
GeneID377841.
KEGGhsa:377841.
UCSCuc004cmw.3. human. [Q5MY95-1]
uc004cmx.3. human. [Q5MY95-2]

Organism-specific databases

CTD377841.
GeneCardsGC09M140328.
HGNCHGNC:24860. ENTPD8.
HPAHPA021509.
neXtProtNX_Q5MY95.
PharmGKBPA142671906.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5371.
HOGENOMHOG000059572.
HOVERGENHBG018982.
InParanoidQ5MY95.
KOK01510.
OMAFCQRPWK.
OrthoDBEOG754HPX.
PhylomeDBQ5MY95.
TreeFamTF332859.

Enzyme and pathway databases

SABIO-RKQ5MY95.

Gene expression databases

ArrayExpressQ5MY95.
BgeeQ5MY95.
CleanExHS_ENTPD8.
GenevestigatorQ5MY95.

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

GenomeRNAi377841.
NextBio100687.
PROQ5MY95.

Entry information

Entry nameENTP8_HUMAN
AccessionPrimary (citable) accession number: Q5MY95
Secondary accession number(s): A2BG17, Q6UVZ0
Entry history
Integrated into UniProtKB/Swiss-Prot: October 2, 2007
Last sequence update: October 2, 2007
Last modified: April 16, 2014
This is version 82 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 9

Human chromosome 9: entries, gene names and cross-references to MIM