A0A384D762 · A0A384D762_URSMA

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 site211Proton donor
Binding site211-215AMP (UniProtKB | ChEBI)
Binding site215Zn2+ 1 (UniProtKB | ChEBI)
Binding site251Zn2+ 1 (UniProtKB | ChEBI)
Binding site252AMP (UniProtKB | ChEBI)
Binding site252Zn2+ 1 (UniProtKB | ChEBI)
Binding site252Zn2+ 2 (UniProtKB | ChEBI)
Binding site358AMP (UniProtKB | ChEBI)
Binding site358Zn2+ 1 (UniProtKB | ChEBI)
Binding site409AMP (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

Accessions

  • Primary accession
    A0A384D762

Proteomes

Subcellular Location

PTM/Processing

Keywords

Interaction

Subunit

Homodimer.

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain, region.

TypeIDPosition(s)Description
Domain134-491PDEase
Region484-524Disordered

Sequence similarities

Belongs to the cyclic nucleotide phosphodiesterase family. PDE1 subfamily.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    524
  • Mass (Da)
    60,193
  • Last updated
    2018-11-07 v1
  • Checksum
    A8806765A055CCC4
MQTRRPLLHLDSGWRRQALVGLKATRLRYMVKQLENGEVDIEELKKNLEYTASLLEAVYIDETRQILDTEDELQELRSDAVPSEVRDWLASTFTQQARAKGRRAEEKPKFRSIVHAVQAGIFVERMFRRTYTSVGPTYSTVVLNCLKNLDLWCFDVFSLNRAADDHALRTIVFELLTRHNLISRFKIPTVFLMTFLDALETGYGKYKNPYHNQIHAADVTQTVHCFLLRTGMVHCLSEIEVLAIIFAAAIHDYEHTGTTNSFHIQTKSECAILYNDRSVLENHHISSVFRMMQDDEMNIFINLTRDEFVELRALVIEMVLATDMSCHFQQVKCMKTALQQLERIDKSKALSLLLHAADISHPTKQWSVHSRWTKALMEEFFRQGDKEAELGLPFSPLCDRTSTLVAQSQIGFIDFIVEPTFSVLTDVAEKSVQPLVDEDSKSKTQPSFQWRQPSLDVEVGDPNPDVVSFRSTWTKYIQENKQKWKERAASGVTNQMSIDELSPCEEEALPSPAEDEHNQNGNLD

Computationally mapped potential isoform sequences

There are 4 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
A0A384D7I3A0A384D7I3_URSMAPDE1B527
A0A384D774A0A384D774_URSMAPDE1B519
A0A384D812A0A384D812_URSMAPDE1B516
A0A384D824A0A384D824_URSMAPDE1B479

Keywords

Sequence databases

Genome annotation databases

Similar Proteins

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