G3V450 · G3V450_HUMAN

  • Protein
    nucleoside diphosphate phosphatase
  • Gene
    ENTPD5
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    4/5

Function

function

Hydrolyzes nucleoside diphosphates with a preference for GDP, IDP and UDP compared to ADP and CDP. In the lumen of the endoplasmic reticulum, hydrolyzes UDP that acts as an end-product feedback inhibitor of the UDP-Glc:glycoprotein glucosyltransferases. UMP can be transported back by an UDP-sugar antiporter to the cytosol where it is consumed to regenerate UDP-glucose. Therefore, it positively regulates protein reglucosylation by clearing UDP from the ER lumen and by promoting the regeneration of UDP-glucose. Protein reglucosylation is essential to proper glycoprotein folding and quality control in the ER.

Catalytic activity

Cofactor

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

Mg2+ (UniProtKB | Rhea| CHEBI:18420 )

Pathway

Protein modification; protein glycosylation.

Features

Showing features for active site, binding site.

TypeIDPosition(s)Description
Active site172Proton acceptor
Binding site202-206ATP (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentextracellular region
Molecular FunctionATP binding
Molecular Functionhydrolase activity

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    nucleoside diphosphate phosphatase
  • EC number
  • Alternative names
    • Guanosine-diphosphatase ENTPD5
    • Uridine-diphosphatase ENTPD5

Gene names

    • Name
      ENTPD5

Organism names

  • Taxonomic identifier
  • Organism
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo

Accessions

  • Primary accession
    G3V450

Proteomes

Organism-specific databases

Subcellular Location

Keywords

Disease & Variants

Genetic variation databases

PTM/Processing

Features

Showing features for signal, chain.

TypeIDPosition(s)Description
Signal1-20
ChainPRO_500345729921-211nucleoside diphosphate phosphatase

Keywords

Proteomic databases

Expression

Gene expression databases

Interaction

Subunit

Monomer; active form. Homodimer; disulfide-linked. Homodimers are enzymatically inactive.

Structure

Family & Domains

Sequence similarities

Belongs to the GDA1/CD39 NTPase family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Fragment
  • Length
    211
  • Mass (Da)
    22,969
  • Last updated
    2011-11-16 v1
  • Checksum
    3FA17DF3A4BE2C48
MATSWGTVFFMLVVSCVCSAVSHRNQQTWFEGIFLSSMCPINVSASTLYGIMFDAGSTGTRIHVYTFVQKMPGQLPILEGEVFDSVKPGLSAFVDQPKQGAETVQGLLEVAKDSIPRSHWKKTPVVLKATAGLRLLPEHKAKALLFEVKEIFRKSPFLVPKGSVSIMDGSDEGILAWVTVNFLTGQLHGHRQETVGTLDLGGASTQITFLP

Computationally mapped potential isoform sequences

There are 4 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
O75356ENTP5_HUMANENTPD5428
H0YJH1H0YJH1_HUMANENTPD580
G3V3Y0G3V3Y0_HUMANENTPD591
G3V4I0G3V4I0_HUMANENTPD5407

Features

Showing features for non-terminal residue.

TypeIDPosition(s)Description
Non-terminal residue211

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AC005480
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
AC005484
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.

Genome annotation databases

Similar Proteins

Disclaimer

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