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Reviewed, UniProtKB/Swiss-Prot Q64395 (PDE1B_CRIGR)

Last modified January 19, 2010. Version 45. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Calcium/calmodulin-dependent 3',5'-cyclic nucleotide phosphodiesterase 1B
      Short name=Cam-PDE 1B
    EC=3.1.4.17
Gene names
Name: PDE1B1
OrganismCricetulus griseus (Chinese hamster)
Taxonomic identifier10029 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Cricetidae › Cricetinae › Cricetulus

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Protein attributes

Sequence length199 AA.
Sequence statusFragment.
Protein existenceEvidence at transcript level.

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General annotation (Comments)

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 By similarity.

Catalytic activity

Nucleoside 3',5'-cyclic phosphate + H2O = nucleoside 5'-phosphate.

Cofactor

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 By similarity.

Enzyme regulation

Type I PDE are activated by the binding of calmodulin in the presence of Ca2+.

Subunit structure

Homodimer.

Subcellular location

Cytoplasm By similarity.

Sequence similarities

Belongs to the cyclic nucleotide phosphodiesterase family. PDE1 subfamily.

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Ontologies

Keywords
   Cellular componentCytoplasm
   LigandMetal-binding
cAMP
cGMP
   Molecular functionHydrolase
Gene Ontology (GO)
   Biological processsignal transduction

Inferred from electronic annotation. Source: InterPro

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular function3',5'-cyclic-nucleotide phosphodiesterase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain‹1 – ›199›199Calcium/calmodulin-dependent 3',5'-cyclic nucleotide phosphodiesterase 1B
PRO_0000198788

Sites

Active site311Proton donor By similarity
Metal binding351Divalent metal cation 1 By similarity
Metal binding711Divalent metal cation 1 By similarity
Metal binding721Divalent metal cation 1 By similarity
Metal binding721Divalent metal cation 2 By similarity
Metal binding1781Divalent metal cation 1 By similarity

Experimental info

Non-terminal residue11
Non-terminal residue1991

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Sequences

Sequence LengthMass (Da)Tools
Q64395-1 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 17AD1392C727BB5F

FASTA19922,904
        10         20         30         40         50         60 
LISRFKIPTV FLMSFLEALE TGYGKYKNPY HNQIHAADVT QTVHCFLLRT GMVHCLSEIE 

        70         80         90        100        110        120 
VLAIIFAAAI HDYEHTGTTN SFHIQTKSEC AILYNDRSVL ENHHISSVFR MMQDDEMNIF 

       130        140        150        160        170        180 
INLTKDEFVE LRALVIEMVL ATDMSCHFQQ VKSMKTALQQ LERIDKSKAL SLLLHAADIS 

       190 
HPTKQWSVHS HWTKALMEE

« Hide

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References

[1]"Receptor-mediated stimulation of lipid signalling pathways in CHO cells elicits the rapid transient induction of the PDE1B isoform of Ca2+/calmodulin-stimulated cAMP phosphodiesterase."
Spence S., Rena G., Sullivan M., Erdogan S., Houslay M.D.
Biochem. J. 321:157-163(1997) [PubMed: 9003415] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ		U40585 mRNA. Translation: AAB50017.1.

3D structure databases

SMRQ64395. Positions 1-199.
ModBaseSearch...

Phylogenomic databases

HOVERGENQ64395.

Enzyme and pathway databases

BRENDA3.1.4.17. 18.

Family and domain databases

InterProIPR003607. Metal-dep_PHydrolase_HD_dom.
IPR002073. PDEase.
[Graphical view]
PfamPF00233. PDEase_I. 1 hit.
[Graphical view]
PRINTSPR00387. PDIESTERASE1.
SMARTSM00471. HDc. 1 hit.
[Graphical view]
PROSITEPS00126. PDEASE_I. 1 hit.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry namePDE1B_CRIGR
AccessionPrimary (citable) accession number: Q64395
Entry history
Integrated into UniProtKB/Swiss-Prot: March 15, 2004
Last sequence update: November 1, 1996
Last modified: January 19, 2010
This is version 45 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents