Q9QXQ1 (PDE7B_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
cAMP-specific 3',5'-cyclic phosphodiesterase 7B
EC=3.1.4.17

Gene names

Name:

Pde7b

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	446 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	Hydrolyzes the second messenger cAMP, which is a key regulator of many important physiological processes. May be involved in the control of cAMP-mediated neural activity and cAMP metabolism in the brain.
Catalytic activity	Adenosine 3',5'-cyclic phosphate + H2O = adenosine 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	Inhibited by dipyridamole, IBMX and SCH 51866. Insensitive to zaprinast, rolipram, and milrinone.
Pathway	Purine metabolism; 3',5'-cyclic AMP degradation; AMP from 3',5'-cyclic AMP: step 1/1.
Tissue specificity	Highly expressed in brain.
Domain	Composed of a C-terminal catalytic domain containing two putative divalent metal sites and an N-terminal regulatory domain.
Sequence similarities	Belongs to the cyclic nucleotide phosphodiesterase family. PDE7 subfamily.

Ontologies

Keywords
Ligand	Metal-binding cAMP
Molecular function	Hydrolase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cAMP catabolic process Inferred from electronic annotation. Source: UniProtKB-UniPathway signal transduction Inferred from electronic annotation. Source: InterPro
Molecular_function	3',5'-cyclic-AMP phosphodiesterase activity Inferred from direct assay Ref.2. 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 – 446	446	cAMP-specific 3',5'-cyclic phosphodiesterase 7B		PRO_0000198837
Regions
	Region	172 – 410	239	Catalytic By similarity
Sites
	Active site	173	1	Proton donor By similarity
	Metal binding	177	1	Divalent metal cation 1 By similarity
	Metal binding	213	1	Divalent metal cation 1 By similarity
	Metal binding	214	1	Divalent metal cation 1 By similarity
	Metal binding	214	1	Divalent metal cation 2 By similarity
	Metal binding	323	1	Divalent metal cation 1 By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9QXQ1 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: 7C052664B693A5A8	FASTA	446	51,337
	10 20 30 40 50 60 MSCLMVERCG EVLFESPEQS VKCVCMLGDV RLRGQTGVPA ERRGSYPFID FRLLNNTTHS 70 80 90 100 110 120 GEIGTKKKVK RLLSFQRYFH ASRLLRGIIP QAPLHLLDED YLGQARHMLS KVGTWDFDIF 130 140 150 160 170 180 LFDRLTNGNS LVTLLCHLFN SHGLIHHFKL DMVTLHRFLV MVQEDYHGHN PYHNAVHAAD 190 200 210 220 230 240 VTQAMHCYLK EPKLASFLTP LDIMLGLLAA AAHDVDHPGV NQPFLIKTNH HLANLYQNMS 250 260 270 280 290 300 VLENHHWRST IGMLRESRLL AHLPKEMTQD IEQQLGSLIL ATDINRQNEF LTRLKAHLHN 310 320 330 340 350 360 KDLRLENVQD RHFMLQIALK CADICNPCRI WEMSKQWSER VCEEFYRQGD LEQKFELEIS 370 380 390 400 410 420 PLCNQQKDSI PSIQIGFMTY IVEPLFREWA RFTGNSTLSE NMLSHLAHNK AQWKSLLSNQ 430 440 HRRRGSGQDL AGPAPETLEQ TEGATP

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and characterization of PDE7B, a cAMP-specific phosphodiesterase." Hetman J.M., Soderling S.H., Glavas N.A., Beavo J.A. Proc. Natl. Acad. Sci. U.S.A. 97:472-476(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Cloning and characterisation of the human and mouse PDE7B, a novel cAMP-specific nucleotide phosphodiesterase." Gardner C.E., Robas N.M., Cawkill D., Fidock M.D. Biochem. Biophys. Res. Commun. 272:186-192(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: C57BL/6J.
[3]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF190639 mRNA. Translation: AAF25195.1. AJ251859 mRNA. Translation: CAB92530.1. BC130267 mRNA. Translation: AAI30268.1.
IPI	IPI00135368.
RefSeq	NP_038903.3. NM_013875.5.
UniGene	Mm.425617.
3D structure databases
ProteinModelPortal	Q9QXQ1.
SMR	Q9QXQ1. Positions 100-416.
ModBase	Search...
PTM databases
PhosphoSite	Q9QXQ1.
Proteomic databases
PaxDb	Q9QXQ1.
PRIDE	Q9QXQ1.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000020165; ENSMUSP00000020165; ENSMUSG00000019990.
GeneID	29863.
KEGG	mmu:29863.
UCSC	uc007eoa.2. mouse.
Organism-specific databases
CTD	27115.
MGI	MGI:1352752. Pde7b.
Phylogenomic databases
eggNOG	NOG300643.
GeneTree	ENSGT00690000101749.
HOGENOM	HOG000220881.
HOVERGEN	HBG053543.
InParanoid	A1L3T2.
KO	K01120.
OrthoDB	EOG4JDH6S.
Enzyme and pathway databases
UniPathway	UPA00762; UER00747.
Gene expression databases
ArrayExpress	Q9QXQ1.
Bgee	Q9QXQ1.
CleanEx	MM_PDE7B.
Genevestigator	Q9QXQ1.
GermOnline	ENSMUSG00000019990. Mus musculus.
Family and domain databases
Gene3D	1.10.1300.10. 1 hit.
InterPro	IPR003607. HD/PDEase_dom. IPR023088. PDEase. IPR002073. PDEase_catalytic_dom. IPR023174. PDEase_CS. [Graphical view]
Pfam	PF00233. PDEase_I. 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	307074.
SOURCE	Search...

Entry information

Entry name

PDE7B_MOUSE

Accession

Primary (citable) accession number: Q9QXQ1
Secondary accession number(s): A1L3T2

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 27, 2001
Last sequence update:	May 1, 2000
Last modified:	April 3, 2013
This is version 97 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program