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Q01066 (PDE1B_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 105. 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
Alternative name(s):
63 kDa Cam-PDE
Gene names
Name:Pde1b
Synonyms:Pde1b1
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length535 AA.
Sequence statusComplete.
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.

Sequence similarities

Belongs to the cyclic nucleotide phosphodiesterase family. PDE1 subfamily.

Ontologies

Keywords
   Cellular componentCytoplasm
   LigandCalmodulin-binding
cAMP
cGMP
Metal-binding
   Molecular functionHydrolase
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcAMP catabolic process

Inferred from direct assay PubMed 15305867PubMed 16881052. Source: RGD

cGMP catabolic process

Inferred from direct assay PubMed 15305867PubMed 16881052. Source: RGD

cellular response to granulocyte macrophage colony-stimulating factor stimulus

Inferred from electronic annotation. Source: Ensembl

cellular response to macrophage colony-stimulating factor stimulus

Inferred from electronic annotation. Source: Ensembl

locomotory behavior

Inferred from electronic annotation. Source: Ensembl

monocyte differentiation

Inferred from electronic annotation. Source: Ensembl

regulation of dopamine metabolic process

Inferred from electronic annotation. Source: Ensembl

regulation of neurotransmitter levels

Inferred from electronic annotation. Source: Ensembl

response to amphetamine

Inferred from electronic annotation. Source: Ensembl

serotonin metabolic process

Inferred from electronic annotation. Source: Ensembl

signal transduction

Inferred from electronic annotation. Source: Ensembl

visual learning

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

neuronal cell body

Inferred from direct assay PubMed 15305867. Source: RGD

nucleus

Inferred from electronic annotation. Source: Ensembl

   Molecular_function3',5'-cyclic-AMP phosphodiesterase activity

Inferred from direct assay PubMed 15305867PubMed 16881052. Source: RGD

calcium- and calmodulin-regulated 3',5'-cyclic-GMP phosphodiesterase activity

Inferred from direct assay PubMed 15305867PubMed 16881052. Source: RGD

cyclic-nucleotide phosphodiesterase activity

Inferred from direct assay Ref.1. Source: RGD

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 535535Calcium/calmodulin-dependent 3',5'-cyclic nucleotide phosphodiesterase 1B
PRO_0000198791

Regions

Region27 – 4721Calmodulin-binding Potential
Region196 – 495300Catalytic By similarity

Sites

Active site2221Proton donor By similarity
Metal binding2261Divalent metal cation 1 By similarity
Metal binding2621Divalent metal cation 1 By similarity
Metal binding2631Divalent metal cation 1 By similarity
Metal binding2631Divalent metal cation 2 By similarity
Metal binding3691Divalent metal cation 1 By similarity

Amino acid modifications

Modified residue4651Phosphoserine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q01066 [UniParc].

Last modified April 1, 1993. Version 1.
Checksum: F98FFFE61F848F89

FASTA53561,260
        10         20         30         40         50         60 
MELSPRSPPE MLESDCPSPL ELKSAPSKKM WIKLRSLLRY MVKQLENGEV NIEELKKNLE 

        70         80         90        100        110        120 
YTASLLEAVY IDETRQILDT EDELRELRSD AVPSEVRDWL ASTFTQQTRA KGRRAEEKPK 

       130        140        150        160        170        180 
FRSIVHAVQA GIFVERMFRR TYTAVGPTYS TAVHNCLKNL DVWCFDVFSL NRAADDHALR 

       190        200        210        220        230        240 
TIVFELLTRH SLISRFKIPT VFLMSFLEAL ETGYGKYKNP YHNQIHAADV TQTVHCFLLR 

       250        260        270        280        290        300 
TGMVHCLSEI EVLAIIFAAA IHDYEHTGTT NSFHIQTKSE CAILYNDRSV LENHHISSVF 

       310        320        330        340        350        360 
RMMQDDEMNI FINLTKDEFV ELRALVIEMV LATDMSCHFQ QVKTMKTALQ QLERIDKSKA 

       370        380        390        400        410        420 
LSLLLHAADI SHPTKQWSVH SRWTKALMEE FFRQGDKEAE LGLPFSPLCD RTSTLVAQSQ 

       430        440        450        460        470        480 
IGFIDFIVEP TFSVLTDVAE KSVQPLTDDD SKSKSQPSFQ WRQPSLDVDV GDPNPDVVSF 

       490        500        510        520        530 
RSTWTKYIQE NKQKWKERAA SGITNQMSID ELSPCEEEAP SSPAEDEHNQ NGNLD 

« Hide

References

[1]"A polymerase chain reaction strategy to identify and clone cyclic nucleotide phosphodiesterase cDNAs. Molecular cloning of the cDNA encoding the 63-kDa calmodulin-dependent phosphodiesterase."
Repaske D.R., Swinnen J.V., Jin S.-L.C., van Wyk J.J., Conti M.
J. Biol. Chem. 267:18683-18688(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Phosphodiesterase 1B (PDE1B) in rat brain."
Prime G.R., Sutor B.
Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Wistar.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M94537 mRNA. Translation: AAA16530.1.
AF327906 mRNA. Translation: AAK15740.1.
PIRA44161.
RefSeqNP_073201.1. NM_022710.1.
UniGeneRn.53489.

3D structure databases

ProteinModelPortalQ01066.
SMRQ01066. Positions 145-501.
ModBaseSearch...
MobiDBSearch...

Chemistry

BindingDBQ01066.
ChEMBLCHEMBL2111322.

Proteomic databases

PaxDbQ01066.
PRIDEQ01066.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000055272; ENSRNOP00000052147; ENSRNOG00000036828.
GeneID29691.
KEGGrno:29691.
UCSCRGD:3278. rat.

Organism-specific databases

CTD5153.
RGD3278. Pde1b.

Phylogenomic databases

eggNOGNOG139098.
GeneTreeENSGT00660000095451.
HOGENOMHOG000231888.
HOVERGENHBG056120.
InParanoidQ01066.
KOK13755.
OMASTAVHNC.
OrthoDBEOG7X9G6J.
PhylomeDBQ01066.
TreeFamTF314638.

Gene expression databases

ArrayExpressQ01066.
GenevestigatorQ01066.

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

NextBio610076.
PROQ01066.

Entry information

Entry namePDE1B_RAT
AccessionPrimary (citable) accession number: Q01066
Secondary accession number(s): Q548L3
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: April 1, 1993
Last modified: April 16, 2014
This is version 105 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