Reviewed, UniProtKB/Swiss-Prot Q9NP56 (PDE7B_HUMAN)

Names and origin

Protein names

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

Gene names

Name:

PDE7B

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	450 AA.
Sequence status	Complete.
Protein existence	Evidence at protein 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. Also expressed in heart, liver, skeletal muscle and pancreas.
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
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	signal transduction Ref.1 Traceable author statement. Source: ProtInc synaptic transmission Ref.1 Traceable author statement. Source: ProtInc
Molecular function	3',5'-cyclic-AMP phosphodiesterase activity Traceable author statement. Source: ProtInc
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 450

450

cAMP-specific 3',5'-cyclic phosphodiesterase 7B

PRO_0000198836

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

Amino acid modifications

Modified residue

45

1

Phosphoserine Ref.6

Modified residue

74

1

Phosphoserine

Secondary structure

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450

Helix Strand Turn

Details...

Helix

105 – 108

4

Helix

109 – 111

3

Helix

119 – 125

7

Turn

126 – 128

3

Helix

130 – 141

12

Helix

144 – 147

4

Helix

152 – 164

13

Beta strand

170 – 174

5

Helix

175 – 189

15

Helix

192 – 194

3

Turn

195 – 197

3

Helix

200 – 212

13

Turn

213 – 216

4

Helix

222 – 227

6

Helix

231 – 235

5

Turn

236 – 238

3

Helix

241 – 252

12

Helix

253 – 256

4

Helix

265 – 280

16

Helix

284 – 286

3

Helix

287 – 299

13

Helix

308 – 323

16

Helix

326 – 328

3

Helix

331 – 354

24

Turn

365 – 367

3

Helix

370 – 380

11

Helix

382 – 393

12

Beta strand

396 – 398

3

Helix

401 – 412

12

Turn

426 – 428

3

Helix

429 – 432

4

Sequences

	Sequence		Length	Mass (Da)
	Q9NP56-1 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: EC142BF3E28D0028	FASTA	450	51,835
	10 20 30 40 50 60 MSCLMVERCG EILFENPDQN AKCVCMLGDI RLRGQTGVRA ERRGSYPFID FRLLNSTTYS 70 80 90 100 110 120 GEIGTKKKVK RLLSFQRYFH ASRLLRGIIP QAPLHLLDED YLGQARHMLS KVGMWDFDIF 130 140 150 160 170 180 LFDRLTNGNS LVTLLCHLFN THGLIHHFKL DMVTLHRFLV MVQEDYHSQN 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 KDLRLEDAQD RHFMLQIALK CADICNPCRI WEMSKQWSER VCEEFYRQGE LEQKFELEIS 370 380 390 400 410 420 PLCNQQKDSI PSIQIGFMSY IVEPLFREWA HFTGNSTLSE NMLGHLAHNK AQWKSLLPRQ 430 440 450 HRSRGSSGSG PDHDHAGQGT ESEEQEGDSP

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Identification of human PDE7B, a cAMP-specific phosphodiesterase." Sasaki T., Kotera J., Yuasa K., Omori K. Biochem. Biophys. Res. Commun. 271:575-583(2000) [PubMed: 10814504] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Brain.
[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: 10872825] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Fetal brain.
[3]	"The DNA sequence and analysis of human chromosome 6." Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D. , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S. Nature 425:805-811(2003) [PubMed: 14574404] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain.
[6]	"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis." Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III J. Proteome Res. 7:1346-1351(2008) [PubMed: 18220336] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-45, MASS SPECTROMETRY.
[7]	"Large-scale proteomics analysis of the human kinome." Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H. Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed: 19369195] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-74, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AB038040 mRNA. Translation: BAA96537.1.
AJ251860 mRNA. Translation: CAB92441.1.
AL360178, AL133319, AL138828 Genomic DNA. Translation: CAH73075.1.
AL133319, AL138828, AL360178 Genomic DNA. Translation: CAH73332.1.
AL138828, AL133319, AL360178 Genomic DNA. Translation: CAI95287.1.
CH471051 Genomic DNA. Translation: EAW47957.1.
BC075082 mRNA. Translation: AAH75082.1.
BC075083 mRNA. Translation: AAH75083.1.

IPI

IPI00014552.

PIR

JC7266.

RefSeq

NP_061818.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1LXW	model	-	A	104-433	[»]

SMR

Q9NP56. Positions 100-416.

ModBase

Search...

Protein-protein interaction databases

STRING

Q9NP56.

PTM databases

PhosphoSite

Q9NP56.

Proteomic databases

PRIDE

Q9NP56.

Genome annotation databases

Ensembl

ENST00000308191; ENSP00000310661; ENSG00000171408; Homo sapiens. [Genome view]

GeneID

27115.

KEGG

hsa:27115.

UCSC

uc003qgp.1. human.

Organism-specific databases

CTD

27115.

GeneCards

GC06P136214.

H-InvDB

HIX0032752.

HGNC

HGNC:8792. PDE7B.

HPA

HPA023967.

MIM

604645. gene.

PharmGKB

PA33140.

GenAtlas

Search...

Phylogenomic databases

HOVERGEN

Q9NP56.

OrthoDB

EOG9T1M6J.

PhylomeDB

Q9NP56.

Enzyme and pathway databases

BRENDA

3.1.4.17. 247.

Reactome

REACT_14797. Signaling by GPCR.

Gene expression databases

ArrayExpress

Q9NP56.

Bgee

Q9NP56.

CleanEx

HS_PDE7B.

Genevestigator

Q9NP56.

GermOnline

ENSG00000171408. Homo sapiens.

Family and domain databases

InterPro

IPR003607. Metal-dep_PHydrolase_HD_dom.
IPR002073. PDEase.
[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 Resources

DrugBank

DB00651. Dyphylline.
DB00920. Ketotifen.

NextBio

49800.

SOURCE

Search...

Entry information

Entry name

PDE7B_HUMAN

Accession

Primary (citable) accession number: Q9NP56
Secondary accession number(s): Q5W154

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 27, 2001
Last sequence update:	October 1, 2000
Last modified:	February 9, 2010
This is version 83 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.