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Q01066

- PDE1B_RAT

UniProt

Q01066 - PDE1B_RAT

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Protein
Calcium/calmodulin-dependent 3',5'-cyclic nucleotide phosphodiesterase 1B
Gene
Pde1b, Pde1b1
Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at transcript leveli

Functioni

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 activityi

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

Cofactori

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 regulationi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei222 – 2221Proton donor By similarity
Metal bindingi226 – 2261Divalent metal cation 1 By similarity
Metal bindingi262 – 2621Divalent metal cation 1 By similarity
Metal bindingi263 – 2631Divalent metal cation 1 By similarity
Metal bindingi263 – 2631Divalent metal cation 2 By similarity
Metal bindingi369 – 3691Divalent metal cation 1 By similarity

GO - Molecular functioni

  1. 3',5'-cyclic-AMP phosphodiesterase activity Source: RGD
  2. calcium- and calmodulin-regulated 3',5'-cyclic-GMP phosphodiesterase activity Source: RGD
  3. cyclic-nucleotide phosphodiesterase activity Source: RGD
  4. metal ion binding Source: UniProtKB-KW
Complete GO annotation...

GO - Biological processi

  1. cAMP catabolic process Source: RGD
  2. cGMP catabolic process Source: RGD
  3. cellular response to granulocyte macrophage colony-stimulating factor stimulus Source: Ensembl
  4. cellular response to macrophage colony-stimulating factor stimulus Source: Ensembl
  5. locomotory behavior Source: Ensembl
  6. monocyte differentiation Source: Ensembl
  7. regulation of dopamine metabolic process Source: Ensembl
  8. regulation of neurotransmitter levels Source: Ensembl
  9. response to amphetamine Source: Ensembl
  10. serotonin metabolic process Source: Ensembl
  11. signal transduction Source: Ensembl
  12. visual learning Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

Calmodulin-binding, cAMP, cGMP, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Calcium/calmodulin-dependent 3',5'-cyclic nucleotide phosphodiesterase 1B (EC:3.1.4.17)
Short name:
Cam-PDE 1B
Alternative name(s):
63 kDa Cam-PDE
Gene namesi
Name:Pde1b
Synonyms:Pde1b1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Chromosome 7

Organism-specific databases

RGDi3278. Pde1b.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
  2. neuronal cell body Source: RGD
  3. nucleus Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 535535Calcium/calmodulin-dependent 3',5'-cyclic nucleotide phosphodiesterase 1B
PRO_0000198791Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei465 – 4651Phosphoserine By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ01066.
PRIDEiQ01066.

Expressioni

Gene expression databases

ArrayExpressiQ01066.
GenevestigatoriQ01066.

Interactioni

Subunit structurei

Homodimer.

Structurei

3D structure databases

ProteinModelPortaliQ01066.
SMRiQ01066. Positions 145-501.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni27 – 4721Calmodulin-binding Reviewed prediction
Add
BLAST
Regioni196 – 495300Catalytic By similarity
Add
BLAST

Sequence similaritiesi

Phylogenomic databases

eggNOGiNOG139098.
GeneTreeiENSGT00660000095451.
HOGENOMiHOG000231888.
HOVERGENiHBG056120.
InParanoidiQ01066.
KOiK13755.
OMAiSTAVHNC.
OrthoDBiEOG7X9G6J.
PhylomeDBiQ01066.
TreeFamiTF314638.

Family and domain databases

Gene3Di1.10.1300.10. 2 hits.
InterProiIPR003607. HD/PDEase_dom.
IPR023088. PDEase.
IPR002073. PDEase_catalytic_dom.
IPR023174. PDEase_CS.
IPR013706. PDEase_N.
[Graphical view]
PfamiPF00233. PDEase_I. 1 hit.
PF08499. PDEase_I_N. 1 hit.
[Graphical view]
PRINTSiPR00387. PDIESTERASE1.
SMARTiSM00471. HDc. 1 hit.
[Graphical view]
PROSITEiPS00126. PDEASE_I. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q01066-1 [UniParc]FASTAAdd to Basket

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MELSPRSPPE MLESDCPSPL ELKSAPSKKM WIKLRSLLRY MVKQLENGEV    50
NIEELKKNLE YTASLLEAVY IDETRQILDT EDELRELRSD AVPSEVRDWL 100
ASTFTQQTRA KGRRAEEKPK FRSIVHAVQA GIFVERMFRR TYTAVGPTYS 150
TAVHNCLKNL DVWCFDVFSL NRAADDHALR TIVFELLTRH SLISRFKIPT 200
VFLMSFLEAL ETGYGKYKNP YHNQIHAADV TQTVHCFLLR TGMVHCLSEI 250
EVLAIIFAAA IHDYEHTGTT NSFHIQTKSE CAILYNDRSV LENHHISSVF 300
RMMQDDEMNI FINLTKDEFV ELRALVIEMV LATDMSCHFQ QVKTMKTALQ 350
QLERIDKSKA LSLLLHAADI SHPTKQWSVH SRWTKALMEE FFRQGDKEAE 400
LGLPFSPLCD RTSTLVAQSQ IGFIDFIVEP TFSVLTDVAE KSVQPLTDDD 450
SKSKSQPSFQ WRQPSLDVDV GDPNPDVVSF RSTWTKYIQE NKQKWKERAA 500
SGITNQMSID ELSPCEEEAP SSPAEDEHNQ NGNLD 535
Length:535
Mass (Da):61,260
Last modified:April 1, 1993 - v1
Checksum:iF98FFFE61F848F89
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M94537 mRNA. Translation: AAA16530.1.
AF327906 mRNA. Translation: AAK15740.1.
PIRiA44161.
RefSeqiNP_073201.1. NM_022710.1.
UniGeneiRn.53489.

Genome annotation databases

EnsembliENSRNOT00000055272; ENSRNOP00000052147; ENSRNOG00000036828.
GeneIDi29691.
KEGGirno:29691.
UCSCiRGD:3278. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M94537 mRNA. Translation: AAA16530.1 .
AF327906 mRNA. Translation: AAK15740.1 .
PIRi A44161.
RefSeqi NP_073201.1. NM_022710.1.
UniGenei Rn.53489.

3D structure databases

ProteinModelPortali Q01066.
SMRi Q01066. Positions 145-501.
ModBasei Search...

Chemistry

BindingDBi Q01066.
ChEMBLi CHEMBL2111322.

Proteomic databases

PaxDbi Q01066.
PRIDEi Q01066.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSRNOT00000055272 ; ENSRNOP00000052147 ; ENSRNOG00000036828 .
GeneIDi 29691.
KEGGi rno:29691.
UCSCi RGD:3278. rat.

Organism-specific databases

CTDi 5153.
RGDi 3278. Pde1b.

Phylogenomic databases

eggNOGi NOG139098.
GeneTreei ENSGT00660000095451.
HOGENOMi HOG000231888.
HOVERGENi HBG056120.
InParanoidi Q01066.
KOi K13755.
OMAi STAVHNC.
OrthoDBi EOG7X9G6J.
PhylomeDBi Q01066.
TreeFami TF314638.

Miscellaneous databases

NextBioi 610076.
PROi Q01066.

Gene expression databases

ArrayExpressi Q01066.
Genevestigatori Q01066.

Family and domain databases

Gene3Di 1.10.1300.10. 2 hits.
InterProi IPR003607. HD/PDEase_dom.
IPR023088. PDEase.
IPR002073. PDEase_catalytic_dom.
IPR023174. PDEase_CS.
IPR013706. PDEase_N.
[Graphical view ]
Pfami PF00233. PDEase_I. 1 hit.
PF08499. PDEase_I_N. 1 hit.
[Graphical view ]
PRINTSi PR00387. PDIESTERASE1.
SMARTi SM00471. HDc. 1 hit.
[Graphical view ]
PROSITEi PS00126. PDEASE_I. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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.

Entry informationi

Entry nameiPDE1B_RAT
AccessioniPrimary (citable) accession number: Q01066
Secondary accession number(s): Q548L3
Entry historyi
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 statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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