A0A0D9QZB3 · A0A0D9QZB3_CHLSB

Function

function

Cyclic nucleotide phosphodiesterase with a dual specificity for the second messengers cAMP and cGMP, which are key regulators of many important physiological processes. Has a preference for cGMP as a substrate.

Catalytic activity

Cofactor

Protein has several cofactor binding sites:
Mg2+ (UniProtKB | Rhea| CHEBI:18420 )

Zn2+ (UniProtKB | Rhea| CHEBI:29105 )

a divalent metal cation (UniProtKB | Rhea| CHEBI:60240 )

Note: Binds 2 divalent metal cations per subunit. Site 1 may preferentially bind zinc ions, while site 2 has a preference for magnesium and/or manganese ions.

Features

Showing features for active site, binding site.

TypeIDPosition(s)Description
Active site223Proton donor
Binding site223-227AMP (UniProtKB | ChEBI)
Binding site227Zn2+ 1 (UniProtKB | ChEBI)
Binding site263Zn2+ 1 (UniProtKB | ChEBI)
Binding site264AMP (UniProtKB | ChEBI)
Binding site264Zn2+ 2 (UniProtKB | ChEBI)
Binding site264Zn2+ 1 (UniProtKB | ChEBI)
Binding site370AMP (UniProtKB | ChEBI)
Binding site370Zn2+ 1 (UniProtKB | ChEBI)
Binding site421AMP (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytosol
Cellular Componentneuronal cell body
Molecular Functioncalmodulin-activated 3',5'-cyclic-GMP phosphodiesterase activity
Molecular Functioncalmodulin-activated dual specificity 3',5'-cyclic-GMP, 3',5'-cyclic-AMP phosphodiesterase activity
Molecular Functionmetal ion binding
Biological Processcellular response to granulocyte macrophage colony-stimulating factor stimulus
Biological Processcellular response to macrophage colony-stimulating factor stimulus
Biological Processdopamine catabolic process
Biological Processlocomotory behavior
Biological Processmonocyte differentiation
Biological Processresponse to amphetamine
Biological Processserotonin metabolic process
Biological Processsignal transduction
Biological Processvisual learning

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Phosphodiesterase
  • EC number

Gene names

    • Name
      PDE1B

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Cercopithecidae > Cercopithecinae > Chlorocebus

Accessions

  • Primary accession
    A0A0D9QZB3

Proteomes

Subcellular Location

PTM/Processing

Keywords

Expression

Gene expression databases

Interaction

Subunit

Homodimer.

Protein-protein interaction databases

Family & Domains

Features

Showing features for region, coiled coil, domain, compositional bias.

TypeIDPosition(s)Description
Region1-20Disordered
Coiled coil39-91
Domain146-503PDEase
Region447-473Disordered
Compositional bias450-464Polar residues
Region494-536Disordered

Sequence similarities

Belongs to the cyclic nucleotide phosphodiesterase family. PDE1 subfamily.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    536
  • Mass (Da)
    61,365
  • Last updated
    2015-05-27 v1
  • Checksum
    5B0F82829574B9C6
MELSPRSPPEMLEESDCPSPLELKSAPSKKMWIKLRSLLRYMVKQLENGEVNIEELKKNLEYTASLLEAVYIDETRQILDTEDELQELRSDAVPSEVRDWLASTFTQQARAKGRRAEEKPKFRSIVHAVQAGIFVERMFRRTYTSVGPTYSTAVLNCFKNLDLWCFDVFSLNRAADDHALRTIVFELLTRHNLISRFKIPTVFLMSFLDALETGYGKYKNPYHNQIHAADVTQTVHCFLLRTGMVHCLSEIEVLAIIFAAAIHDYEHTGTTNSFHIQTKSECAILYNDRSVLENHHISSVFRLMQDDELNIFINLTKDEFVELRALVIEMVLATDMSCHFQQVKTMKTALQQLERIDKPKALSLLLHAADISHPTKQWSVHSRWTKALMEEFFRQGDKEAELGLPFSPLCDRTSTLVAQSQIGFIDFIVEPTFSVLTDVAEKSVQPLADEDSKSKNQPSFQWRQPSLDVEVGDPNPDVVSFRSTWIKHIQENKQKWKERAASGITNQMSIDELSPCDEEAPPSPAEDEHNQNGNLD

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias450-464Polar residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AQIB01022982
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.

Genome annotation databases

Similar Proteins

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