A0A7L0SFM2 · A0A7L0SFM2_PODPO

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.

Caution

The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

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

Ca2+ (UniProtKB | Rhea| CHEBI:29108 )

Features

Showing features for active site, binding site.

Type
IDPosition(s)Description
Active site159Proton acceptor
Binding site206-210ATP (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
      PODPOD_R07460

Organism names

  • Taxonomic identifier
  • Strain
    • B10K-DU-009-04
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Archelosauria > Archosauria > Dinosauria > Saurischia > Theropoda > Coelurosauria > Aves > Neognathae > Neoaves > Mirandornithes > Podicipediformes > Podicipedidae > Podilymbus

Accessions

  • Primary accession
    A0A7L0SFM2

Proteomes

Subcellular Location

Membrane, caveola
Membrane
; Multi-pass membrane protein

Features

Showing features for transmembrane.

TypeIDPosition(s)Description
Transmembrane470-492Helical

Keywords

  • Cellular component

PTM/Processing

Features

Showing features for signal, chain.

Type
IDPosition(s)Description
Signal1-21
ChainPRO_502961654922-503Ectonucleoside triphosphate diphosphohydrolase 1

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
    Fragment
  • Length
    503
  • Mass (Da)
    56,239
  • Last updated
    2021-04-07 v1
  • Checksum
    5603BAF395385A03
KILLILGFLSILAVIALIAVAVTQNKPLPKNIKYGIVLDAGSSHTNLYVYEWPAEKENDTGVVQQVEVCKVEGPGISGYSHATEKAGPSLAQCLLQAEEVIPSQQHQETPIYLGATAGMRLLSLENKSAADKVLSSVEKTLRSAPFNFQGARIISGQEEGAYGWITINYLLGNFKQVLYQWQSGWKKLLHSLKSISETSGALDLGGASTQITFVPNELHSESPENLLYFRLYGKDYIVYTHSFLCYGKDQALQQKLARDLQASTSNSSLLDPCFHQGYQRTVNISELFKNPCTSAKKKQFPFSQLYIQGEGDYQKCRRNIQKLFNKTDCPYSRCSFNGIYLPSLQGDFGAFSAFYFVMNFLNLTSEQSPVALEKVASAIEHFCARPWHEVKTAYLQIKEKYLSEYCFSGAYILSLLQNGYEFTEKNWQRIHFLGKIGSSDAGWTLGYMLNLTNMIPAEEPAVPPLSYGSYVALMVLCSLVLVSVLLFVWLLFHKPKCLQKGIV

Features

Showing features for non-terminal residue.

TypeIDPosition(s)Description
Non-terminal residue1
Non-terminal residue503

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
VXAO01000008
EMBL· GenBank· DDBJ
NXL41156.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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