A0A6J2LMX7 · A0A6J2LMX7_9CHIR

Function

function

Catalyzes the hydrolysis of both di- and triphosphate nucleotides (NDPs and NTPs) and hydrolyze NTPs to nucleotide monophosphates (NMPs) in two distinct successive phosphate-releasing steps, with NDPs as intermediates and participates in the regulation of extracellular levels of nucleotides. By hydrolyzing proinflammatory ATP and platelet-activating ADP to AMP, it blocks platelet aggregation and supports blood flow.

Catalytic activity

  • ITP + 2 H2O = IMP + 2 phosphate + 2 H+
    This reaction proceeds in the forward direction.
  • UTP + 2 H2O = UMP + 2 phosphate + 2 H+
    This reaction proceeds in the forward direction.
  • ADP + H2O = AMP + phosphate + H+
    This reaction proceeds in the forward direction.
  • ATP + 2 H2O = AMP + 2 phosphate + 2 H+
    This reaction proceeds in the forward direction.
  • ATP + H2O = ADP + phosphate + H+
    This reaction proceeds in the forward direction.
  • CDP + H2O = CMP + phosphate + H+
    This reaction proceeds in the forward direction.
  • CTP + 2 H2O = CMP + 2 phosphate + 2 H+
    This reaction proceeds in the forward direction.
  • CTP + H2O = CDP + phosphate + H+
    This reaction proceeds in the forward direction.
  • GDP + H2O = GMP + phosphate + H+
    This reaction proceeds in the forward direction.
  • GTP + 2 H2O = GMP + 2 phosphate + 2 H+
    This reaction proceeds in the forward direction.
  • GTP + H2O = GDP + phosphate + H+
    This reaction proceeds in the forward direction.
  • IDP + H2O = IMP + phosphate + H+
    This reaction proceeds in the forward direction.
  • ITP + H2O = IDP + phosphate + H+
    This reaction proceeds in the forward direction.
  • UDP + H2O = UMP + phosphate + H+
    This reaction proceeds in the forward direction.
  • UTP + H2O = UDP + phosphate + H+
    This reaction proceeds in the forward direction.
  • a ribonucleoside 5'-diphosphate + H2O = a ribonucleoside 5'-phosphate + phosphate + H+
    This reaction proceeds in the forward direction.
  • a ribonucleoside 5'-triphosphate + 2 H2O = a ribonucleoside 5'-phosphate + 2 phosphate + 2 H+
    This reaction proceeds in the forward direction.
    EC:3.6.1.5 (UniProtKB | ENZYME | Rhea)
  • a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-diphosphate + phosphate + H+
    This reaction proceeds in the forward direction.

Cofactor

Protein has several cofactor binding sites:
Ca2+ (UniProtKB | Rhea| CHEBI:29108 )

Mg2+ (UniProtKB | Rhea| CHEBI:18420 )

Features

Showing features for active site, binding site.

Type
IDPosition(s)Description
Active site174Proton acceptor
Binding site216-220ATP (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentplasma membrane
Molecular FunctionATP binding
Molecular Functionhydrolase activity

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Ectonucleoside triphosphate diphosphohydrolase 1
  • EC number
  • Alternative names
    • ATP diphosphohydrolase
    • Ecto-ATP diphosphohydrolase 1
    • Ecto-apyrase
    • Lymphoid cell activation antigen
    • Nucleoside triphosphate diphosphohydrolase 1

Gene names

    • Name
      ENTPD1
    • ORF names
      HJG60_004477

Organism names

  • Taxonomic identifier
  • Strain
    • Bat1K_MPI-CBG_1
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Laurasiatheria > Chiroptera > Yangochiroptera > Phyllostomidae > Phyllostominae > Phyllostomus

Accessions

  • Primary accession
    A0A6J2LMX7

Proteomes

Subcellular Location

Membrane, caveola
Membrane
; Multi-pass membrane protein

Features

Showing features for transmembrane.

TypeIDPosition(s)Description
Transmembrane17-37Helical
Transmembrane477-499Helical

Keywords

  • Cellular component

PTM/Processing

Keywords

Interaction

Subunit

Homodimer; disulfide-linked.

Family & Domains

Sequence similarities

Belongs to the GDA1/CD39 NTPase family.

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    510
  • Mass (Da)
    58,041
  • Last updated
    2020-10-07 v1
  • Checksum
    C48E513B74FF321E
MEDVKDSGLKGFCSRNILIILGFSFIMAVIALIAVGLTQNKALPENVKYGIVLDAGSSHTTLYIYKWPAEKENDTGVVNQIHECKVKGPGISQYAHKTSDLDIYLTACMEKARKVIPISQHHETPVYLGATAGMRLLRLENEWVADNVLAVIRDVLDSYPFDFRGARIISGGEEGAYGWITVNYLLGKFTKKLRWLNLMSYGNESQETYGALDLGGASTQITFVPQNQATESPQNALYFRLYGKDYNVYTHSFLCYGKDQALLQKIAKDIQATNRTIQDPCFNHGYSRVMNVNDLYNSTCTWKFKKPLPFNQLEILGTGNFEECQKSVIALFNTSQCPYSRCAFNEIFLPQLQGQFGAFSAYYYVMKFLNLTSEETLSQEKMIDTIKNFCSRPWKELKMNFGDVKEKYLSEYCFSGTYIISLLQEGYHFTPDNWKTIHFMGQIRDTDVGWTLGYMLNLTNMIPAEQPMSTPLPYSTYVFLMVLFSLILIAVVLIGLIIFHKPSCFWKDMV

Computationally mapped potential isoform sequences

There are 3 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
A0A7E6DUQ9A0A7E6DUQ9_9CHIRENTPD1508
A0A7E6DVC1A0A7E6DVC1_9CHIRENTPD1402
A0A7E6DVN6A0A7E6DVN6_9CHIRENTPD1518

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
JABVXQ010000005
EMBL· GenBank· DDBJ
KAF6108533.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

Any 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. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
Help