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Q01061 (PDE1B_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 86. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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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
Alternative name(s):
63 kDa Cam-PDE
Gene names
Name:PDE1B
Synonyms:PDE1B1
OrganismBos taurus (Bovine) [Reference proteome]
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

Protein attributes

Sequence length534 AA.
Sequence statusComplete.
Protein existenceEvidence at protein 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+. Regulated by phosphorylation by CaM-dependent protein kinase II.

Subunit structure

Homodimer.

Subcellular location

Cytoplasm.

Tissue specificity

Expressed in central nervous system regions. Most abundant in basal ganglia. Also found in kidney papilla and adrenal medulla.

Sequence similarities

Belongs to the cyclic nucleotide phosphodiesterase family. PDE1 subfamily.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 534534Calcium/calmodulin-dependent 3',5'-cyclic nucleotide phosphodiesterase 1B
PRO_0000198787

Regions

Region27 – 4721Calmodulin-binding Potential
Region195 – 494300Catalytic By similarity

Sites

Active site2211Proton donor By similarity
Metal binding2251Divalent metal cation 1 By similarity
Metal binding2611Divalent metal cation 1 By similarity
Metal binding2621Divalent metal cation 1 By similarity
Metal binding2621Divalent metal cation 2 By similarity
Metal binding3681Divalent metal cation 1 By similarity

Amino acid modifications

Modified residue4641Phosphoserine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q01061 [UniParc].

Last modified June 1, 1994. Version 1.
Checksum: C86C3F48E0AE9B69

FASTA53461,006
        10         20         30         40         50         60 
MELSPRSPPE MLESDCPSPL ELKSAPSKKM WIKLRSLLRY MVKQLENGEV NIEELKKNLE 

        70         80         90        100        110        120 
YTASLLEAVY IDETRQILDT EDELQELRSD AVPSEVRDWL ASTFTQQTRA KGPSEEKPKF 

       130        140        150        160        170        180 
RSIVHAVQAG IFVERMFRRT YTSVGPTYST AVLNCLKNVD LWCFDVFSLN RAADDHALRT 

       190        200        210        220        230        240 
IVFELLTRHN LISRFKIPTV FLMTFLDALE TGYGKYKNPY HNQIHAADVT QTVHCFLLRT 

       250        260        270        280        290        300 
GMVHCLSEIE VLAIIFAAAI HDYEHTGTTN SFHIQTKSEC AILYNDRSVL ENHHISSVFR 

       310        320        330        340        350        360 
MMQDDEMNIF INLTKDEFVE LRALVIEMVL ATDMSCHFQQ VKSMKTALQQ LERIDKSKAL 

       370        380        390        400        410        420 
SLLLHAADIS HPTKQWSVHS RWTKALMEEF FRQGDKEAEL GLPFSPLCDR TSTLVAQSQI 

       430        440        450        460        470        480 
GFIDFIVEPT FSVLTDVAEK SVQPTGDDDS KSKNQPSFQW RQPSLDVEVG DPNPDVVSFR 

       490        500        510        520        530 
STWTKYIQEN KQKWKERAAS GITNQMSIDE LSPCEEEAPA SPAEDEHNQN GNLD

« Hide

References

[1]"Molecular cloning of cDNA encoding a '63'-kDa calmodulin-stimulated phosphodiesterase from bovine brain."
Bentley J.K., Kadlecek A., Sherbert C.H., Seger D., Sonnenburg W.K., Charbonneau H., Novack J.P., Beavo J.A.
J. Biol. Chem. 267:18676-18682(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Brain.
[2]"Sequence comparison of the 63-, 61-, and 59-kDa calmodulin-dependent cyclic nucleotide phosphodiesterases."
Novack J.P., Charbonneau H., Bentley J.K., Walsh K.A., Beavo J.A.
Biochemistry 30:7940-7947(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: PARTIAL PROTEIN SEQUENCE.
Tissue: Brain.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		M94867 mRNA. Translation: AAA74558.1.
IPIIPI00838132.
PIRA44162.
RefSeqNP_776840.1. NM_174415.2.
UniGeneBt.3910.

3D structure databases

ProteinModelPortalQ01061.
SMRQ01061. Positions 144-500.
ModBaseSearch...

Protein-protein interaction databases

STRING9913.ENSBTAP00000005680.

Proteomic databases

PRIDEQ01061.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSBTAT00000003552; ENSBTAP00000003552; ENSBTAG00000004337.
GeneID281970.
KEGGbta:281970.

Organism-specific databases

CTD5153.

Phylogenomic databases

eggNOGNOG139098.
GeneTreeENSGT00660000095451.
HOGENOMHOG000231888.
HOVERGENHBG056120.
KOK13755.

Gene expression databases

ArrayExpressQ01061.

Family and domain databases

Gene3D1.10.1300.10. 2 hits.
InterProIPR003607. HD/PDEase_dom.
IPR023088. PDEase.
IPR002073. PDEase_catalytic_dom.
IPR023174. PDEase_CS.
IPR013706. PDEase_N.
[Graphical view]
PfamPF00233. PDEase_I. 1 hit.
PF08499. PDEase_I_N. 1 hit.
[Graphical view]
PRINTSPR00387. PDIESTERASE1.
SMARTSM00471. HDc. 1 hit.
[Graphical view]
PROSITEPS00126. PDEASE_I. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

BindingDBQ01061.
ChEMBLCHEMBL2650.
NextBio20805841.

Entry information

Entry namePDE1B_BOVIN
AccessionPrimary (citable) accession number: Q01061
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: April 3, 2013
This is version 86 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

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