Calcium/calmodulin-dependent 3',5'-cyclic nucleotide phosphodiesterase 1B

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Q01065 (PDE1B_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 105. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended 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

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	535 AA.
Sequence status	Complete.
Protein existence	Evidence 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⁺.
Subunit structure	Homodimer By similarity.
Subcellular location	Cytoplasm.
Sequence similarities	Belongs to the cyclic nucleotide phosphodiesterase family. PDE1 subfamily.

Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	Calmodulin-binding Metal-binding cAMP cGMP
Molecular function	Hydrolase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cAMP catabolic process Inferred from electronic annotation. Source: Compara cGMP catabolic process Inferred from electronic annotation. Source: Compara cellular response to granulocyte macrophage colony-stimulating factor stimulus Inferred from electronic annotation. Source: Compara cellular response to macrophage colony-stimulating factor stimulus Inferred from electronic annotation. Source: Compara locomotory behavior Inferred from mutant phenotype PubMed 12077213 PubMed 17559891. Source: MGI monocyte differentiation Inferred from electronic annotation. Source: Compara regulation of dopamine metabolic process Inferred from mutant phenotype PubMed 17559891. Source: MGI regulation of neurotransmitter levels Inferred from mutant phenotype PubMed 17559891. Source: MGI response to amphetamine Inferred from mutant phenotype PubMed 17010100 PubMed 17559891. Source: MGI serotonin metabolic process Inferred from mutant phenotype PubMed 17559891. Source: MGI signal transduction Inferred from mutant phenotype PubMed 12077213. Source: MGI visual learning Inferred from mutant phenotype PubMed 12077213. Source: MGI
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell neuronal cell body Inferred from electronic annotation. Source: Compara nucleus Inferred from electronic annotation. Source: Compara
Molecular_function	3',5'-cyclic-AMP phosphodiesterase activity Inferred from electronic annotation. Source: Compara calcium- and calmodulin-regulated 3',5'-cyclic-GMP phosphodiesterase activity Inferred from sequence orthology PubMed 7568196. Source: MGI calmodulin-dependent cyclic-nucleotide phosphodiesterase activity Inferred from sequence orthology PubMed 7568196. Source: MGI metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 535

535

Calcium/calmodulin-dependent 3',5'-cyclic nucleotide phosphodiesterase 1B

PRO_0000198790

Regions

Region

27 – 47

Calmodulin-binding Potential

Region

196 – 495

300

Catalytic By similarity

Sites

Active site

222

Proton donor By similarity

Metal binding

226

Divalent metal cation 1 By similarity

Metal binding

262

Divalent metal cation 1 By similarity

Metal binding

263

Divalent metal cation 1 By similarity

Metal binding

263

Divalent metal cation 2 By similarity

Metal binding

369

Divalent metal cation 1 By similarity

Amino acid modifications

Modified residue

465

Phosphoserine Ref.4

Experimental info

Sequence conflict

L → M Ref.2

Sequence conflict

224

Q → R in AAA37367. Ref.3

Sequences

Sequence

Length

Mass (Da)

Tools

Q01065 [UniParc].

Last modified October 1, 1996. Version 2.
Checksum: F87A585537C8D1CD
Show »

FASTA

535

61,226

        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 TYTSVGPTYS TAVHNCLKNL DLWCFDVFSL 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 FINLTKDEFA ELRALVIEMV LATDMSCHFQ QVKTMKTALQ QLERIDKSKA 

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

       430        440        450        460        470        480 
IGFIDFIVEP TFSVLTDVAE KSVQPLADDD SKPKSQPSFQ WRQPSLDVDV GDPNPDVVSF 

       490        500        510        520        530 
RATWTKYIQE NKQKWKERAA SGITNQMSID ELSPCEEEAP SSPAEDEHNQ NGNLD

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular cloning of DNA encoding a calmodulin-dependent phosphodiesterase enriched in striatum." Polli J.W., Kincaid R.L. Proc. Natl. Acad. Sci. U.S.A. 89:11079-11083(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Genomic structure and chromosome location of the murine PDE1B phosphodiesterase gene." Reed T.M., Browning J.E., Blough R.I., Vorhees C.V., Repaske D.R. Mamm. Genome 9:571-576(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 38-535. Strain: 129/SvJ.
[3]	"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] OF 221-336.
[4]	"Phosphoproteomic analysis of the developing mouse brain." Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P. Mol. Cell. Proteomics 3:1093-1101(2004) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-465, MASS SPECTROMETRY. Tissue: Embryonic brain.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	L01695 mRNA. Translation: AAA39902.1. AH007066 Genomic DNA. Translation: AAC96022.1. M94538 mRNA. Translation: AAA37367.1.
IPI	IPI00118900.
PIR	A46378.
RefSeq	NP_032826.1. NM_008800.1.
UniGene	Mm.390792.
3D structure databases
ProteinModelPortal	Q01065.
SMR	Q01065. Positions 145-501.
ModBase	Search...
PTM databases
PhosphoSite	Q01065.
Proteomic databases
PaxDb	Q01065.
PRIDE	Q01065.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000023132; ENSMUSP00000023132; ENSMUSG00000022489.
GeneID	18574.
KEGG	mmu:18574.
UCSC	uc007xyh.1. mouse.
Organism-specific databases
CTD	5153.
MGI	MGI:97523. Pde1b.
Phylogenomic databases
eggNOG	NOG139098.
GeneTree	ENSGT00660000095451.
HOGENOM	HOG000231888.
HOVERGEN	HBG056120.
InParanoid	Q01065.
KO	K13755.
OMA	STAVHNC.
OrthoDB	EOG4FXR79.
Gene expression databases
ArrayExpress	Q01065.
Bgee	Q01065.
CleanEx	MM_PDE1B.
Genevestigator	Q01065.
GermOnline	ENSMUSG00000022489. Mus musculus.
Family and domain databases
Gene3D	1.10.1300.10. 2 hits.
InterPro	IPR003607. HD/PDEase_dom. IPR023088. PDEase. IPR002073. PDEase_catalytic_dom. IPR023174. PDEase_CS. IPR013706. PDEase_N. [Graphical view]
Pfam	PF00233. PDEase_I. 1 hit. PF08499. PDEase_I_N. 1 hit. [Graphical view]
PRINTS	PR00387. PDIESTERASE1.
SMART	SM00471. HDc. 1 hit. [Graphical view]
PROSITE	PS00126. PDEASE_I. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	294424.
SOURCE	Search...

Entry information

Entry name

PDE1B_MOUSE

Accession

Primary (citable) accession number: Q01065
Secondary accession number(s): O35384

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1993
Last sequence update:	October 1, 1996
Last modified:	May 1, 2013
This is version 105 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents