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Q64395 (PDE1B_CRIGR) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 59. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

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) (Cricetulus barabensis griseus)
Taxonomic identifier10029 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaCricetidaeCricetinaeCricetulus

Protein attributes

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

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.

Ontologies

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

Sequences

Sequence LengthMass (Da)Tools
Q64395 [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

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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Cross-references

Sequence databases

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

3D structure databases

ProteinModelPortalQ64395.
SMRQ64395. Positions 1-199.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

HOVERGENHBG056120.

Family and domain databases

Gene3D1.10.1300.10. 1 hit.
InterProIPR003607. HD/PDEase_dom.
IPR023088. PDEase.
IPR002073. PDEase_catalytic_dom.
IPR023174. PDEase_CS.
[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...

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: April 16, 2014
This is version 59 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families