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P97687 (ENTP1_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 99. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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 1

Short name=NTPDase 1
EC=3.6.1.5
Alternative name(s):
Ecto-ATP diphosphohydrolase 1
Short name=Ecto-ATPDase 1
Short name=Ecto-ATPase 1
Ecto-apyrase
Lymphoid cell activation antigen
CD_antigen=CD39
Gene names
Name:Entpd1
Synonyms:Cd39
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length511 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

In the nervous system, could hydrolyze ATP and other nucleotides to regulate purinergic neurotransmission. Could also be implicated in the prevention of platelet aggregation by hydrolyzing platelet-activating ADP to AMP. Hydrolyzes ATP and ADP equally well. Ref.1

Catalytic activity

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

Cofactor

Ca2+ or Mg2+. Ref.1

Subunit structure

Homodimer; disulfide-linked By similarity. Ref.4

Subcellular location

Membrane; Multi-pass membrane protein Potential.

Tissue specificity

Expressed in primary neurons and astrocytes, kidney, liver, muscle, thymus, lung and spleen. Ref.1

Post-translational modification

N-glycosylated. Ref.1

Sequence similarities

Belongs to the GDA1/CD39 NTPase family.

Ontologies

Keywords
   Cellular componentMembrane
   DomainTransmembrane
Transmembrane helix
   LigandATP-binding
Calcium
Magnesium
Nucleotide-binding
   Molecular functionHydrolase
   PTMDisulfide bond
Glycoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Cellular_componentintegral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

hydrolase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 511511Ectonucleoside triphosphate diphosphohydrolase 1
PRO_0000209904

Regions

Topological domain1 – 1616Cytoplasmic Potential
Transmembrane17 – 3721Helical; Potential
Topological domain38 – 478441Extracellular Potential
Transmembrane479 – 49921Helical; Potential
Topological domain500 – 51112Cytoplasmic Potential
Region46 – 171126N-terminal lobe
Region205 – 441237C-terminal lobe

Sites

Active site1741Proton acceptor By similarity

Amino acid modifications

Glycosylation731N-linked (GlcNAc...) Potential
Glycosylation2261N-linked (GlcNAc...) Potential
Glycosylation2911N-linked (GlcNAc...) Potential
Glycosylation3331N-linked (GlcNAc...) Potential
Glycosylation3741N-linked (GlcNAc...) Potential
Glycosylation4291N-linked (GlcNAc...) Potential
Glycosylation4581N-linked (GlcNAc...) Potential
Disulfide bond84 ↔ 108 Ref.4
Disulfide bond254 ↔ 300 Ref.4
Disulfide bond281 ↔ 324 Ref.4
Disulfide bond337 ↔ 342 Ref.4
Disulfide bond391 ↔ 414 Ref.4

Experimental info

Sequence conflict3321F → L Ref.2

Secondary structure

....................................................................... 511
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P97687 [UniParc].

Last modified May 1, 1997. Version 1.
Checksum: 4CC123D3E644C193

FASTA51157,408
        10         20         30         40         50         60 
MEDIKDSKVK RFCSKNILII LGFSSVLAVI ALIAVGLTHN KPLPENVKYG IVLDAGSSHT 

        70         80         90        100        110        120 
NLYIYKWPAE KENDTGVVQL LEECQVKGPG ISKYAQKTDE IAAYLAECMK MSTERIPASK 

       130        140        150        160        170        180 
QHQTPVYLGA TAGMRLLRME SKQSADEVLA AVSRSLKSYP FDFQGAKIIT GQEEGAYGWI 

       190        200        210        220        230        240 
TINYLLGRFT QEQSWLNFIS DSQKQATFGA LDLGGSSTQV TFVPLNQTLE APETSLQFRL 

       250        260        270        280        290        300 
YGTDYTVYTH SFLCYGKDQA LWQKLAQDIQ VSSGGILKDP CFYPGYKKVV NVSELYGTPC 

       310        320        330        340        350        360 
TKRFEKKLPF NQFQVQGTGD YEQCHQSILK FFNNSHCPYS QCAFNGVFLP PLQGSFGAFS 

       370        380        390        400        410        420 
AFYFVMDFFK KMANDSVSSQ EKMTEITKNF CSKPWEEVKA SYPTVKEKYL SEYCFSGTYI 

       430        440        450        460        470        480 
LSLLLQGYNF TGTSWDQIHF MGKIKDSNAG WTLGYMLNLT NMIPAEQPLS PPLPHSTYIS 

       490        500        510 
LMVLFSLVLV AMVITGLFIF SKPSYFWKEA V 

« Hide

References

[1]"Characterization of brain ecto-apyrase: evidence for only one ecto-apyrase (CD39) gene."
Wang T.-F., Rosenberg P.A., Guidotti G.
Brain Res. Mol. Brain Res. 47:295-302(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, FUNCTION, COFACTOR, GLYCOSYLATION, TISSUE SPECIFICITY.
Strain: Sprague-Dawley.
Tissue: Brain and Hippocampus.
[2]"Evidence for alternative splicing of ecto-ATPase associated with termination of purinergic transmission."
Vlajkovic S.M., Housley G.D., Greenwood D., Thorne P.R.
Brain Res. Mol. Brain Res. 73:85-92(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Wistar.
Tissue: Cochlea.
[3]"An ecto-ATPase and an ecto-ATP diphosphohydrolase are expressed in rat brain."
Kegel B., Braun N., Heine P., Maliszewski C.R., Zimmermann H.
Neuropharmacology 36:1189-1200(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 432-511.
Strain: Sprague-Dawley.
Tissue: Brain.
[4]"Crystallographic evidence for a domain motion in rat nucleoside triphosphate diphosphohydrolase (NTPDase) 1."
Zebisch M., Krauss M., Schafer P., Strater N.
J. Mol. Biol. 415:288-306(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 38-477, DISULFIDE BONDS.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U81295 mRNA. Translation: AAC53195.1.
Y15685 mRNA. Translation: CAA75730.1.
RefSeqNP_072109.1. NM_022587.1.
UniGeneRn.17491.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3ZX0X-ray2.50A/B/C/D38-477[»]
3ZX2X-ray1.81A/B/C/D38-477[»]
3ZX3X-ray1.70A/B/C/D38-477[»]
ProteinModelPortalP97687.
ModBaseSearch...
MobiDBSearch...

Chemistry

BindingDBP97687.
ChEMBLCHEMBL2767.

PTM databases

PhosphoSiteP97687.

Proteomic databases

PRIDEP97687.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID64519.
KEGGrno:64519.

Organism-specific databases

CTD953.
RGD69265. Entpd1.

Phylogenomic databases

HOVERGENHBG018982.
KOK01510.
PhylomeDBP97687.

Gene expression databases

GenevestigatorP97687.

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

NextBio613322.
PROP97687.

Entry information

Entry nameENTP1_RAT
AccessionPrimary (citable) accession number: P97687
Entry history
Integrated into UniProtKB/Swiss-Prot: June 20, 2001
Last sequence update: May 1, 1997
Last modified: April 16, 2014
This is version 99 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references