Reviewed, UniProtKB/Swiss-Prot Q01066 (PDE1B_RAT)

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

Rattus norvegicus (Rat)

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	535 AA.
Sequence status	Complete.
Protein existence	Evidence 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 component	Cytoplasm
Ligand	Calmodulin-binding Metal-binding cAMP cGMP
Molecular function	Hydrolase
PTM	Phosphoprotein
Gene Ontology (GO)
Biological process	cAMP catabolic process Inferred from direct assay. Source: RGD cGMP catabolic process Inferred from direct assay. Source: RGD
Cellular component	cell soma Inferred from direct assay. Source: RGD cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	3',5'-cyclic-AMP phosphodiesterase activity Inferred from direct assay. Source: RGD calcium- and calmodulin-regulated 3',5'-cyclic-GMP phosphodiesterase activity Inferred from direct assay. Source: RGD calmodulin 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_0000198791
Regions
	Region	27 – 47	21	Calmodulin-binding Potential
	Region	196 – 495	300	Catalytic By similarity
Sites
	Active site	222	1	Proton donor By similarity
	Metal binding	226	1	Divalent metal cation 1 By similarity
	Metal binding	262	1	Divalent metal cation 1 By similarity
	Metal binding	263	1	Divalent metal cation 1 By similarity
	Metal binding	263	1	Divalent metal cation 2 By similarity
	Metal binding	369	1	Divalent metal cation 1 By similarity
Amino acid modifications
	Modified residue	465	1	Phosphoserine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q01066-1 [UniParc]. Last modified April 1, 1993. Version 1. Checksum: F98FFFE61F848F89	FASTA	535	61,260
	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

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: 1326532] [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.
IPI	IPI00199077.
PIR	A44161.
RefSeq	NP_073201.1.
UniGene	Rn.53489
3D structure databases
SMR	Q01066. Positions 145-501.
ModBase	Search...
Protein-protein interaction databases
STRING	Q01066.
Genome annotation databases
Ensembl	ENSRNOT00000055272; ENSRNOP00000052147; ENSRNOG00000036828; Rattus norvegicus. [Genome view]
GeneID	29691.
KEGG	rno:29691.
UCSC	NM_022710. rat.
Organism-specific databases
CTD	29691.
RGD	3278. Pde1b.
Phylogenomic databases
eggNOG	maNOG10177.
HOVERGEN	Q01066.
InParanoid	Q01066.
OMA	DVDVGDP.
OrthoDB	EOG9S4S20.
Enzyme and pathway databases
BRENDA	3.1.4.17. 248.
Gene expression databases
ArrayExpress	Q01066.
Genevestigator	Q01066.
GermOnline	ENSRNOG00000036828. Rattus norvegicus.
Family and domain databases
InterPro	IPR003607. Metal-dep_PHydrolase_HD_dom. IPR002073. PDEase. 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 Resources
NextBio	610076.

Entry information

Entry name

PDE1B_RAT

Accession

Primary (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:	January 19, 2010
This is version 75 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)