Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q9VJ79

- PDE11_DROME

UniProt

Q9VJ79 - PDE11_DROME

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Dual 3',5'-cyclic-AMP and -GMP phosphodiesterase 11

Gene

Pde11

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Plays a role in signal transduction by regulating the intracellular concentration of cyclic nucleotides cAMP and cGMP. Catalyzes the hydrolysis of both cAMP and cGMP to 5'-AMP and 5'-GMP, respectively.1 Publication

Catalytic activityi

Guanosine 3',5'-cyclic phosphate + H2O = guanosine 5'-phosphate.
Adenosine 3',5'-cyclic phosphate + H2O = adenosine 5'-phosphate.

Cofactori

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).By similarity

Kineticsi

  1. KM=18.5 µM for cAMP KM=6 µM for cGMP1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei860 – 8601Proton donorBy similarity
Metal bindingi864 – 8641Divalent metal cation 1By similarity
Metal bindingi900 – 9001Divalent metal cation 1By similarity
Metal bindingi901 – 9011Divalent metal cation 1By similarity
Metal bindingi901 – 9011Divalent metal cation 2By similarity
Metal bindingi904 – 9041Divalent metal cation 2By similarity
Metal bindingi929 – 9291Divalent metal cation 2By similarity
Metal bindingi1011 – 10111Divalent metal cation 1By similarity
Binding sitei1064 – 10641cAMP or cGMPBy similarity

GO - Molecular functioni

  1. 3',5'-cyclic-AMP phosphodiesterase activity Source: UniProtKB
  2. 3',5'-cyclic-GMP phosphodiesterase activity Source: UniProtKB
  3. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. cAMP metabolic process Source: UniProtKB
  2. cGMP metabolic process Source: UniProtKB
  3. lateral inhibition Source: FlyBase
  4. signal transduction Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

cAMP, cGMP, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Dual 3',5'-cyclic-AMP and -GMP phosphodiesterase 11 (EC:3.1.4.17, EC:3.1.4.35)
Alternative name(s):
cAMP and cGMP phosphodiesterase 11
Gene namesi
Name:Pde11
ORF Names:CG34341
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
ProteomesiUP000000803: Chromosome 2L

Organism-specific databases

FlyBaseiFBgn0085370. Pde11.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 14511451Dual 3',5'-cyclic-AMP and -GMP phosphodiesterase 11PRO_0000247044Add
BLAST

Proteomic databases

PaxDbiQ9VJ79.

Expressioni

Tissue specificityi

In adults, it is enriched in Malpighian tubules.1 Publication

Gene expression databases

BgeeiQ9VJ79.
ExpressionAtlasiQ9VJ79. differential.

Interactioni

Protein-protein interaction databases

BioGridi61102. 6 interactions.
MINTiMINT-1027877.

Structurei

3D structure databases

ProteinModelPortaliQ9VJ79.
SMRiQ9VJ79. Positions 402-1137.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini419 – 572154GAF 1Add
BLAST
Domaini604 – 754151GAF 2Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni836 – 1100265CatalyticBy similarityAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi1121 – 11244Poly-Gln
Compositional biasi1328 – 1436109His-richAdd
BLAST

Sequence similaritiesi

Contains 2 GAF domains.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiNOG270709.
GeneTreeiENSGT00760000119066.
InParanoidiQ9VJ79.
KOiK13298.
OMAiCEIDSLT.
OrthoDBiEOG7RRF69.
PhylomeDBiQ9VJ79.

Family and domain databases

Gene3Di1.10.1300.10. 1 hit.
3.30.450.40. 2 hits.
InterProiIPR003018. GAF.
IPR029016. GAF_dom_like.
IPR003607. HD/PDEase_dom.
IPR023088. PDEase.
IPR002073. PDEase_catalytic_dom.
IPR023174. PDEase_CS.
[Graphical view]
PfamiPF01590. GAF. 2 hits.
PF00233. PDEase_I. 1 hit.
[Graphical view]
PRINTSiPR00387. PDIESTERASE1.
SMARTiSM00065. GAF. 2 hits.
SM00471. HDc. 1 hit.
[Graphical view]
SUPFAMiSSF55781. SSF55781. 2 hits.
PROSITEiPS00126. PDEASE_I. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform B (identifier: Q9VJ79-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MGQAASMCRF RGCRYKNKNK SSKQQQQQQQ QQQQQQQQHQ QQQQQTPSHS
60 70 80 90 100
PQIQHHSEII PATTGLHLRS IEEPATTPLQ FQPTGRMNTE QGGTGYGGYG
110 120 130 140 150
SSEHSLLIAT RHAGVPLPLA QHQPLPAHYQ PLNHSGAAPP SSSNGSSSSG
160 170 180 190 200
GGVQTSATPQ QQQQYQVQQP YQYQYQHHYH HQANSPQHHR PYDPEHARME
210 220 230 240 250
AWLDENQEFV QDYFIRKATR QTVDAWLVSH ATSAGNDVVS STSPTHANGQ
260 270 280 290 300
TSSSRGGSGA TTPVRKISAH EFERGGLLKP IVNTIDGTPT FLSIGPPMDN
310 320 330 340 350
GSVGGSCSNL QNVGGVVAGQ YQYNHQQHHH NHAHLHHSQH SHYQAGGAVG
360 370 380 390 400
SSSLGSTGGA SGAGGAPSLG GSGGAGNGHQ YPYYHCHQRP QRLSRNELKQ
410 420 430 440 450
LDEKELIFEL VKDICNELEV RTLCHKILQN VSILLNADRG SLFLVQGRCN
460 470 480 490 500
GPDGLKKCLV SKLFDVCPRS TVEEMEQQDE VRVAWGTGIA GHVAESGEPV
510 520 530 540 550
NIPDAYQDER FNCEIDSLTG YRTKALLCMP IKDSSGDVIG VAQVINKMNG
560 570 580 590 600
ECFSEIDEKV FSSYLQFCGI GLRNAQLYEK SQLEIKRNQV LLDLARMIFE
610 620 630 640 650
EQSTIEHMVF RILTHMQSLI QCQRVQILLV HEADKGSFSR VFDFEANDLS
660 670 680 690 700
EEEATSRTSP YESRFPINIG ITGHVATTGE TVNVPNAYED DRFDASVDEN
710 720 730 740 750
SCFKHRSILC MAIKNSLGQI IGVIQLINKF NELDFTKNDE NFVEAFAIFC
760 770 780 790 800
GMGIHNTHMY EKAIVAMAKQ SVTLEVLSYH ASATMDEAHR LRRLRVPSAV
810 820 830 840 850
HFRLHDFKFD DIHFEDDDTL KACLRMFLDL DFVERFHIDY EVLCRWLLSV
860 870 880 890 900
KKNYRNVTYH NWRHAFNVAQ MMFAILTTTQ WWKIFGEIEC LALIIGCLCH
910 920 930 940 950
DLDHRGTNNS FQIKASSPLA QLYSTSTMEH HHFDQCLMIL NSPGNQILAN
960 970 980 990 1000
LSSDDYCRVI RVLEDAILST DLAVYFKKRG PFLESVSQPT SYWVAEEPRA
1010 1020 1030 1040 1050
LLRAMSMTVC DLSAITKPWE IEKRVADLVS SEFFEQGDME KQELNITPID
1060 1070 1080 1090 1100
IMNREKEDEL PMMQVNFIDS ICLPIYEAFA TLSDKLEPLV EGVRDNRGHW
1110 1120 1130 1140 1150
IDLADVVKTK TSQDQEPEEE QQQQNVISNG DCKAMSDDDV AASEAEVAVD
1160 1170 1180 1190 1200
SPSEKASVNG SNVANNSSNT NKKIAVASHP TSTQPSDDDN DVDADADDVD
1210 1220 1230 1240 1250
EQAAEENGHD AEVDEASCRS NSTCSSSTAS SCLSTPPPTG EDDSTPVSPL
1260 1270 1280 1290 1300
KTLQAKLVAA NLNALQRQTS NQAQTQKQRC KSCDHSRSGL QVRKTSSLRG
1310 1320 1330 1340 1350
AQELDLDSKT RNGTHAALCK STPVINNHSH HHNHSHSHNH NHHHHHHHHS
1360 1370 1380 1390 1400
HHNHSQHGIG IGSASIGGSG LISLTTPLLA MDSDRIPKIV GKIGNLDGLP
1410 1420 1430 1440 1450
FANGIGGPQN GHGLPFGSYQ HHHHHQHHHH LLARRHSETN SNGATAMAVE

K

Note: No experimental confirmation available.

Length:1,451
Mass (Da):160,930
Last modified:January 15, 2008 - v4
Checksum:iDFEC01058FB600A9
GO
Isoform C (identifier: Q9VJ79-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-44: Missing.
     45-64: QTPSHSPQIQHHSEIIPATT → MASSPNNAAPPVLWRARRKI

Note: No experimental confirmation available.

Show »
Length:1,407
Mass (Da):155,622
Checksum:iDC01CA40E8325C1E
GO
Isoform D (identifier: Q9VJ79-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MKVTQSEENT...GLTFALLAGP

Note: No experimental confirmation available.

Show »
Length:1,539
Mass (Da):170,998
Checksum:iE1EBAD64C5391214
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti38 – 381Q → QQQ in AAM52774. (PubMed:12537569)Curated
Sequence conflicti1192 – 11921V → A in AAM52774. (PubMed:12537569)Curated
Sequence conflicti1196 – 11961A → V in AAM52774. (PubMed:12537569)Curated
Sequence conflicti1232 – 12321C → R in AAM52774. (PubMed:12537569)Curated
Sequence conflicti1342 – 13421H → HNH in AAM52774. (PubMed:12537569)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 4444Missing in isoform C. CuratedVSP_030328Add
BLAST
Alternative sequencei1 – 11M → MKVTQSEENTRNTSDRSKSV QTNRKFDNFNWLLSCGLLAA VKSTKLIPQLPRQQQPKKYN LRYAAELLKFDKIQFIKTEG LTFALLAGP in isoform D. 1 PublicationVSP_019906
Alternative sequencei45 – 6420QTPSH…IPATT → MASSPNNAAPPVLWRARRKI in isoform C. CuratedVSP_030329Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE014134 Genomic DNA. Translation: AAF53675.3.
AE014134 Genomic DNA. Translation: AAF53676.2.
AY122262 mRNA. Translation: AAM52774.1.
RefSeqiNP_001097177.1. NM_001103707.2. [Q9VJ79-3]
NP_609885.2. NM_136041.2. [Q9VJ79-1]
UniGeneiDm.13948.

Genome annotation databases

EnsemblMetazoaiFBtr0112544; FBpp0111456; FBgn0085370. [Q9VJ79-1]
GeneIDi35107.
KEGGidme:Dmel_CG34341.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE014134 Genomic DNA. Translation: AAF53675.3 .
AE014134 Genomic DNA. Translation: AAF53676.2 .
AY122262 mRNA. Translation: AAM52774.1 .
RefSeqi NP_001097177.1. NM_001103707.2. [Q9VJ79-3 ]
NP_609885.2. NM_136041.2. [Q9VJ79-1 ]
UniGenei Dm.13948.

3D structure databases

ProteinModelPortali Q9VJ79.
SMRi Q9VJ79. Positions 402-1137.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 61102. 6 interactions.
MINTi MINT-1027877.

Proteomic databases

PaxDbi Q9VJ79.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblMetazoai FBtr0112544 ; FBpp0111456 ; FBgn0085370 . [Q9VJ79-1 ]
GeneIDi 35107.
KEGGi dme:Dmel_CG34341.

Organism-specific databases

CTDi 35107.
FlyBasei FBgn0085370. Pde11.

Phylogenomic databases

eggNOGi NOG270709.
GeneTreei ENSGT00760000119066.
InParanoidi Q9VJ79.
KOi K13298.
OMAi CEIDSLT.
OrthoDBi EOG7RRF69.
PhylomeDBi Q9VJ79.

Miscellaneous databases

GenomeRNAii 35107.
NextBioi 791899.

Gene expression databases

Bgeei Q9VJ79.
ExpressionAtlasi Q9VJ79. differential.

Family and domain databases

Gene3Di 1.10.1300.10. 1 hit.
3.30.450.40. 2 hits.
InterProi IPR003018. GAF.
IPR029016. GAF_dom_like.
IPR003607. HD/PDEase_dom.
IPR023088. PDEase.
IPR002073. PDEase_catalytic_dom.
IPR023174. PDEase_CS.
[Graphical view ]
Pfami PF01590. GAF. 2 hits.
PF00233. PDEase_I. 1 hit.
[Graphical view ]
PRINTSi PR00387. PDIESTERASE1.
SMARTi SM00065. GAF. 2 hits.
SM00471. HDc. 1 hit.
[Graphical view ]
SUPFAMi SSF55781. SSF55781. 2 hits.
PROSITEi PS00126. PDEASE_I. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Berkeley.
  2. Cited for: GENOME REANNOTATION, ALTERNATIVE SPLICING.
    Strain: Berkeley.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM D).
    Strain: Berkeley.
    Tissue: Embryo.
  4. "Cyclic nucleotide phosphodiesterases in Drosophila melanogaster."
    Day J.P., Dow J.A.T., Houslay M.D., Davies S.A.
    Biochem. J. 388:333-342(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY.

Entry informationi

Entry nameiPDE11_DROME
AccessioniPrimary (citable) accession number: Q9VJ79
Secondary accession number(s): Q8MQW0, Q9VJ78
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 25, 2006
Last sequence update: January 15, 2008
Last modified: October 29, 2014
This is version 91 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3