U3E7R5 · U3E7R5_CALJA

Function

Catalytic activity

Cofactor

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.

Type
IDPosition(s)Description
Active site228Proton donor
Binding site228-232AMP (UniProtKB | ChEBI)
Binding site232Zn2+ 1 (UniProtKB | ChEBI)
Binding site268Zn2+ 1 (UniProtKB | ChEBI)
Binding site269AMP (UniProtKB | ChEBI)
Binding site269Zn2+ 2 (UniProtKB | ChEBI)
Binding site269Zn2+ 1 (UniProtKB | ChEBI)
Binding site376AMP (UniProtKB | ChEBI)
Binding site376Zn2+ 1 (UniProtKB | ChEBI)
Binding site427AMP (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentneuronal cell body
Molecular Functioncalmodulin-activated 3',5'-cyclic-GMP phosphodiesterase activity
Molecular Functionmetal ion binding
Biological Processsignal transduction

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Phosphodiesterase
  • EC number

Gene names

    • Name
      PDE1C

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Platyrrhini > Cebidae > Callitrichinae > Callithrix > Callithrix

Accessions

  • Primary accession
    U3E7R5

Subcellular Location

Family & Domains

Features

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

Type
IDPosition(s)Description
Coiled coil34-64
Domain151-528PDEase
Compositional bias456-495Polar residues
Region456-497Disordered
Compositional bias523-570Basic and acidic residues
Region523-634Disordered
Compositional bias583-597Basic and acidic residues
Compositional bias609-634Basic and acidic residues

Sequence similarities

Belongs to the cyclic nucleotide phosphodiesterase family. PDE1 subfamily.

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    634
  • Mass (Da)
    72,317
  • Last updated
    2013-11-13 v1
  • Checksum
    6D9405B7F4FD63C9
MESPTKEIEEFESNSLKYLQPEQIEKIWLRLRGLRKYKKTSQRLRSLVKQLERGEASVVDLKKNLEYAATVLESVYIDETRRLLDTEDELSDIQSDAVPSEVRDWLASTFTRQMGMMLRRSEEKPRFKSIVHAVQAGIFVERMYRRTSNMVGLSYPPAVIEALKDVDKWSFDVFSLNEASGDHALKFIFYELLTRYDLISRFKIPISALVSFVEALEVGYSKHKNPYHNLMHAADVTQTVHYLLYKTGVANWLTELEIFAIIFSAAIHDYEHTGTTNNFHIQTRSDPAILYNDRSVLENHHLSAAYRLLQDDEEMNILINLSKDDWREFRTLVIEMVMATDMSCHFQQIKAMKTALQQPEAIEKPKALSLMLHTADISHPAKAWDLHHRWTMSLLEEFFRQGDREAELGLPFSPLCDRKSTMVAQSQVGFIDFIVEPTFTVLTDMTEKIVSPLIDETSQTGGAGQRRSSLNSISSSDAKRSGVKSSGSEGSAPINNSVIPIDYKSFKATWTEVVHINRERWRAKVPKEEKAKKEAEEKARLAAEEQQKEMEAKRQAEEGTSGKAEKEMSGEARNQVSGTRAHKSDNPHGKDSKAERSSGEQQQNGDLKDSKNQTDKKDHANIGNDSKKTDDSEE

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias456-495Polar residues
Compositional bias523-570Basic and acidic residues
Compositional bias583-597Basic and acidic residues
Compositional bias609-634Basic and acidic residues

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
GAMS01004442
EMBL· GenBank· DDBJ
JAB18694.1
EMBL· GenBank· DDBJ
mRNA
GAMR01004229
EMBL· GenBank· DDBJ
JAB29703.1
EMBL· GenBank· DDBJ
mRNA
GAMQ01003617
EMBL· GenBank· DDBJ
JAB38234.1
EMBL· GenBank· DDBJ
mRNA
GAMP01007550
EMBL· GenBank· DDBJ
JAB45205.1
EMBL· GenBank· DDBJ
mRNA

Similar Proteins

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