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Q9W4T0 (PDE4D_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 97. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
cAMP-specific 3',5'-cyclic phosphodiesterase, isoform M

EC=3.1.4.53
Alternative name(s):
Learning/memory process protein
Protein dunce
Gene names
Name:dnc
ORF Names:CG32498
OrganismDrosophila melanogaster (Fruit fly) [Reference proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length903 AA.
Sequence statusComplete.
Protein existenceInferred from homology

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.

Vital for female fertility. Required for learning/memory By similarity. UniProtKB P12252

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 diversityAlternative splicing
   LigandcAMP
Metal-binding
   Molecular functionHydrolase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processaxon extension

Inferred from mutant phenotype PubMed 14960616. Source: FlyBase

behavioral response to ethanol

Non-traceable author statement PubMed 11715043. Source: FlyBase

cAMP catabolic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

cAMP-mediated signaling

Non-traceable author statement PubMed 11092827PubMed 11462211PubMed 11741030PubMed 14515157. Source: FlyBase

conditioned taste aversion

Inferred from mutant phenotype PubMed 19158309. Source: FlyBase

courtship behavior

Traceable author statement PubMed 11092827PubMed 11715043PubMed 12486700. Source: FlyBase

lateral inhibition

Inferred from mutant phenotype PubMed 19363474. Source: FlyBase

locomotor rhythm

Non-traceable author statement PubMed 11715043. Source: FlyBase

nonassociative learning

Traceable author statement PubMed 14504657. Source: FlyBase

olfactory learning

Traceable author statement PubMed 11462211PubMed 11715043. Source: FlyBase

oogenesis

Traceable author statement PubMed 3089870. Source: FlyBase

short-term memory

Inferred from mutant phenotype PubMed 19158309. Source: FlyBase

synaptic transmission

Inferred from mutant phenotype PubMed 12040051PubMed 14507965. Source: FlyBase

thermosensory behavior

Inferred from mutant phenotype PubMed 18594510. Source: FlyBase

   Molecular_function3',5'-cyclic-nucleotide phosphodiesterase activity

Inferred from electronic annotation. Source: InterPro

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 M Ref.1 (identifier: Q9W4T0-1)

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 F Ref.1 (identifier: Q8IRU4-1)

The sequence of this isoform can be found in the external entry Q8IRU4.
Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.
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 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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 903903cAMP-specific 3',5'-cyclic phosphodiesterase, isoform M
PRO_0000198819

Regions

Nucleotide binding565 – 5695cAMP By similarity

Sites

Active site5651Proton donor By similarity
Metal binding5691Divalent metal cation 1 By similarity
Metal binding6051Divalent metal cation 1 By similarity
Metal binding6061Divalent metal cation 1 By similarity
Metal binding6061Divalent metal cation 2 By similarity
Metal binding7231Divalent metal cation 1 By similarity
Binding site6061cAMP By similarity
Binding site7231cAMP By similarity
Binding site7741cAMP By similarity
Site7261Binds AMP, but not cAMP By similarity

Sequences

Sequence LengthMass (Da)Tools
Isoform M [UniParc].

Last modified July 5, 2004. Version 2.
Checksum: 6CAC55960750C9F6

FASTA90397,968
        10         20         30         40         50         60 
MPPPRRRRTA VAASAAAAAA ATTTTTTTTA TRAATTTPVT TAPTPTAITT TYRSRNLLKA 

        70         80         90        100        110        120 
TAKVKKKKKW KQISFVDDQQ RLKQAATSAE RKRSTSSAPP ALESNVPPRL GRFLRQKSSE 

       130        140        150        160        170        180 
TNSAATSAAA AAVQTEAETG RRKSSAASII AAAAGAAGLH NNNSSSCAAT ASEEQNSSGT 

       190        200        210        220        230        240 
LTGSSGNTST STWCGSINFL VYMVCSFCCC CYNFRNSPFD VENGQGARSP LEGGSPSAGL 

       250        260        270        280        290        300 
VLQNLPQRRE SFLYRSDSDF EMSPKSMSRN SSIASERFKE QEASILVDRS HGEDLIVTPF 

       310        320        330        340        350        360 
AQILASLRSV RNNLLSLTNV PASNKSRRPN QSSSASRSGN PPGAPLSQGE EAYTRLATDT 

       370        380        390        400        410        420 
IEELDWCLDQ LETIQTHRSV SDMASLKFKR MLNKELSHFS ESSRSGNQIS EYICSTFLDK 

       430        440        450        460        470        480 
QQEFDLPSLR VEDNPELVAA NAAAGQQSAG QYARSRSPRG PPMSQISGVK RPLSHTNSFT 

       490        500        510        520        530        540 
GERLPTFGVE TPRENELGTL LGELDTWGIQ IFSIGEFSVN RPLTCVAYTI FQSRELLTSL 

       550        560        570        580        590        600 
MIPPKTFLNF MSTLEDHYVK DNPFHNSLHA ADVTQSTNVL LNTPALEGVF TPLEVGGALF 

       610        620        630        640        650        660 
AACIHDVDHP GLTNQFLVNS SSELALMYND ESVLENHHLA VAFKLLQNQG CDIFCNMQKK 

       670        680        690        700        710        720 
QRQTLRKMVI DIVLSTDMSK HMSLLADLKT MVETKKVAGS GVLLLDNYTD RIQVLENLVH 

       730        740        750        760        770        780 
CADLSNPTKP LPLYKRWVAL LMEEFFLQGD KERESGMDIS PMCDRHNATI EKSQVGFIDY 

       790        800        810        820        830        840 
IVHPLWETWA DLVHPDAQDI LDTLEENRDY YQSMIPPSPP PSGVDENPQE DRIRFQVTLE 

       850        860        870        880        890        900 
ESDQENLAEL EEGDESGGES TTTGTTGTTA ASALSGAGGG GGGGGGMAPR TGGCQNQPQH 


GGM 

« Hide

Isoform F [UniParc].

See Q8IRU4.

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 N [UniParc].

See Q9W4S9.

References

« Hide '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. expand/collapse author list , 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] [Europe PMC] [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. expand/collapse author list , 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] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION, ALTERNATIVE SPLICING.
Strain: Berkeley.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE014298 Genomic DNA. Translation: AAF45862.2.
RefSeqNP_001259202.1. NM_001272273.1.
NP_726854.2. NM_166966.3.
UniGeneDm.4817.

3D structure databases

ProteinModelPortalQ9W4T0.
SMRQ9W4T0. Positions 385-817.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid57834. 7 interactions.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID31309.
KEGGdme:Dmel_CG32498.
UCSCCG32498-RA. d. melanogaster. [Q9W4T0-1]

Organism-specific databases

CTD31309.
FlyBaseFBgn0000479. dnc.

Phylogenomic databases

InParanoidQ9W4T0.
KOK01120.

Enzyme and pathway databases

UniPathwayUPA00762; UER00747.

Gene expression databases

BgeeQ9W4T0.

Family and domain databases

Gene3D1.10.1300.10. 1 hit.
InterProIPR003607. HD/PDEase_dom.
IPR023088. PDEase.
IPR002073. PDEase_catalytic_dom.
IPR023174. PDEase_CS.
IPR006311. TAT_signal.
[Graphical view]
PfamPF00233. PDEase_I. 1 hit.
[Graphical view]
PRINTSPR00387. PDIESTERASE1.
SMARTSM00471. HDc. 1 hit.
[Graphical view]
PROSITEPS00126. PDEASE_I. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSdnc. drosophila.
NextBio772953.

Entry information

Entry namePDE4D_DROME
AccessionPrimary (citable) accession number: Q9W4T0
Entry history
Integrated into UniProtKB/Swiss-Prot: August 16, 2005
Last sequence update: July 5, 2004
Last modified: March 19, 2014
This is version 97 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

Drosophila

Drosophila: entries, gene names and cross-references to FlyBase