Q8IRU4 (PDE4E_DROME) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
cAMP-specific 3',5'-cyclic phosphodiesterase, isoform F
EC=3.1.4.17

Alternative name(s):
Learning/memory process protein
Protein dunce

Gene names

Name:	dnc
ORF Names:	CG32498

Organism

Drosophila melanogaster (Fruit fly)

Taxonomic identifier

7227 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Ephydroidea › Drosophilidae › Drosophila › Sophophora

Protein attributes

Sequence length	662 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 By similarity. Vital for female fertility. Required for learning/memory By similarity.
Catalytic activity	Adenosine 3',5'-cyclic phosphate + H2O = adenosine 5'-phosphate. UniProtKB P12252
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.
Pathway	Purine metabolism; 3',5'-cyclic AMP degradation; AMP from 3',5'-cyclic AMP: step 1/1.
Subunit structure	Monomer By similarity. UniProtKB P12252
Sequence similarities	Belongs to the cyclic nucleotide phosphodiesterase family. PDE4 subfamily. UniProtKB P12252

Ontologies

Keywords
Coding sequence diversity	Alternative splicing
Ligand	Metal-binding cAMP
Molecular function	Hydrolase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	axon extension Inferred from mutant phenotype. Source: FlyBase behavioral response to ethanol Non-traceable author statement. Source: FlyBase cAMP-mediated signaling Non-traceable author statement. Source: FlyBase conditioned taste aversion Inferred from mutant phenotype. Source: FlyBase courtship behavior Traceable author statement. Source: FlyBase locomotor rhythm Non-traceable author statement. Source: FlyBase nonassociative learning Traceable author statement. Source: FlyBase olfactory learning Traceable author statement. Source: FlyBase oogenesis Traceable author statement. Source: FlyBase short-term memory Inferred from mutant phenotype. Source: FlyBase synaptic transmission Inferred from mutant phenotype. Source: FlyBase
Molecular function	3',5'-cyclic-nucleotide phosphodiesterase activity Inferred from electronic annotation. Source: EC metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Alternative products

This entry describes 11 isoforms produced by alternative splicing. [Align] [Select]

Isoform F Ref.1 (identifier: Q8IRU4-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Note: No experimental confirmation available.

Isoform G Ref.1 (identifier: Q9W4S9-2)

The sequence of this isoform can be found in the external entry Q9W4S9.
Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.

Note: No experimental confirmation available.

Isoform I UniProtKB P12252 (identifier: Q9W4T4-1)

Also known as: B; O;

The sequence of this isoform can be found in the external entry Q9W4T4.
Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.

Isoform II UniProtKB P12252 (identifier: P12252-1)

Also known as: I; J;

The sequence of this isoform can be found in the external entry P12252.
Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.

Isoform III (identifier: P12252-7)

Also known as: E;

The sequence of this isoform can be found in the external entry P12252.
Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.

Note: Produced by alternative initiation at Met-429 of isoform II.

Isoform IV UniProtKB P12252 (identifier: P12252-3)

Also known as: A;

The sequence of this isoform can be found in the external entry P12252.
Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.

Isoform V UniProtKB P12252 (identifier: P12252-4)

Also known as: C;

The sequence of this isoform can be found in the external entry P12252.
Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.

Isoform VI UniProtKB P12252 (identifier: P12252-5)

Also known as: D;

The sequence of this isoform can be found in the external entry P12252.
Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.

Isoform VII UniProtKB P12252 (identifier: P12252-6)

Also known as: L;

The sequence of this isoform can be found in the external entry P12252.
Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.

Isoform M Ref.1 (identifier: Q9W4T0-1)

The sequence of this isoform can be found in the external entry Q9W4T0.
Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.

Note: No experimental confirmation available.

Isoform N Ref.1 (identifier: Q9W4S9-1)

The sequence of this isoform can be found in the external entry Q9W4S9.
Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 662	662	cAMP-specific 3',5'-cyclic phosphodiesterase, isoform F		PRO_0000198820
Regions
	Nucleotide binding	324 – 328	5	cAMP By similarity
Sites
	Active site	324	1	Proton donor By similarity
	Metal binding	328	1	Divalent metal cation 1 By similarity
	Metal binding	364	1	Divalent metal cation 1 By similarity
	Metal binding	365	1	Divalent metal cation 1 By similarity
	Metal binding	365	1	Divalent metal cation 2 By similarity
	Metal binding	482	1	Divalent metal cation 1 By similarity
	Binding site	365	1	cAMP By similarity
	Binding site	482	1	cAMP By similarity
	Binding site	533	1	cAMP By similarity
	Site	485	1	Binds AMP, but not cAMP By similarity

Sequences

	Sequence		Length	Mass (Da)
	Isoform F [UniParc]. Last modified March 1, 2003. Version 1. Checksum: D195C7DAFCBD3CC3	FASTA	662	72,954
	10 20 30 40 50 60 MLNKNSASSQ SLPRVHSFFN MIPSIMQDDL ALTILNDRDN MFSIKSQRSH GEDLIVTPFA 70 80 90 100 110 120 QILASLRSVR NNLLSLTNVP ASNKSRRPNQ SSSASRSGNP PGAPLSQGEE AYTRLATDTI 130 140 150 160 170 180 EELDWCLDQL ETIQTHRSVS DMASLKFKRM LNKELSHFSE SSRSGNQISE YICSTFLDKQ 190 200 210 220 230 240 QEFDLPSLRV EDNPELVAAN AAAGQQSAGQ YARSRSPRGP PMSQISGVKR PLSHTNSFTG 250 260 270 280 290 300 ERLPTFGVET PRENELGTLL GELDTWGIQI FSIGEFSVNR PLTCVAYTIF QSRELLTSLM 310 320 330 340 350 360 IPPKTFLNFM STLEDHYVKD NPFHNSLHAA DVTQSTNVLL NTPALEGVFT PLEVGGALFA 370 380 390 400 410 420 ACIHDVDHPG LTNQFLVNSS SELALMYNDE SVLENHHLAV AFKLLQNQGC DIFCNMQKKQ 430 440 450 460 470 480 RQTLRKMVID IVLSTDMSKH MSLLADLKTM VETKKVAGSG VLLLDNYTDR IQVLENLVHC 490 500 510 520 530 540 ADLSNPTKPL PLYKRWVALL MEEFFLQGDK ERESGMDISP MCDRHNATIE KSQVGFIDYI 550 560 570 580 590 600 VHPLWETWAD LVHPDAQDIL DTLEENRDYY QSMIPPSPPP SGVDENPQED RIRFQVTLEE 610 620 630 640 650 660 SDQENLAELE EGDESGGEST TTGTTGTTAA SALSGAGGGG GGGGGMAPRT GGCQNQPQHG GM
	Isoform G [UniParc]. See Q9W4S9.		–	–
	Isoform I (B) (O) [UniParc]. See Q9W4T4.		–	–
	Isoform II (I) (J) [UniParc]. See P12252.		–	–
	Isoform III (E) [UniParc]. See P12252.		–	–
	Isoform IV (A) [UniParc]. See P12252.		–	–
	Isoform V (C) [UniParc]. See P12252.		–	–
	Isoform VI (D) [UniParc]. See P12252.		–	–
	Isoform VII (L) [UniParc]. See P12252.		–	–
	Isoform M [UniParc]. See Q9W4T0.		–	–
	Isoform N [UniParc]. See Q9W4S9.		–	–

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The genome sequence of Drosophila melanogaster." Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D. , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C. Science 287:2185-2195(2000) [PubMed: 10731132] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Berkeley.
[2]	"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review." Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E. Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed: 12537572] [Abstract] Cited for: GENOME REANNOTATION, ALTERNATIVE SPLICING. Strain: Berkeley.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE014298 Genomic DNA. Translation: AAN09606.1.
RefSeq	NP_525061.2. NM_080322.3.
UniGene	Dm.4817.
3D structure databases
ProteinModelPortal	Q8IRU4.
SMR	Q8IRU4. Positions 144-178, 253-574.
ModBase	Search...
Protein-protein interaction databases
STRING	Q8IRU4.
Proteomic databases
PRIDE	Q8IRU4.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblMetazoa	FBtr0070521; FBpp0070497; FBgn0000479.
GeneID	31309.
KEGG	dme:Dmel_CG32498.
UCSC	CG32498-RA. d. melanogaster.
Organism-specific databases
CTD	31309.
FlyBase	FBgn0000479. dnc.
Phylogenomic databases
GeneTree	EMGT00050000002162.
InParanoid	Q8IRU4.
Gene expression databases
ArrayExpress	Q8IRU4.
Bgee	Q8IRU4.
GermOnline	CG32498. Drosophila melanogaster.
Family and domain databases
InterPro	IPR003607. Metal-dep_PHydrolase_HD_dom. IPR023088. PDEase. IPR002073. PDEase_catalytic_dom. IPR023174. PDEase_CS. [Graphical view]
Gene3D	G3DSA:1.10.1300.10. PDEase_catalytic_dom. 1 hit.
KO	K01120.
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	772953.

Entry information

Entry name

PDE4E_DROME

Accession

Primary (citable) accession number: Q8IRU4

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 16, 2005
Last sequence update:	March 1, 2003
Last modified:	January 25, 2012
This is version 71 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Drosophila annotation project