Q9VFI9 (PDE6_DROME) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
cGMP-specific 3',5'-cyclic phosphodiesterase
EC=3.1.4.35

Alternative name(s):
DmPDE5/6
Short name=DmPDE6

Gene names

Name:	Pde6
ORF Names:	CG8279

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	1118 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Has a role regulating cGMP transport in Malpighian tubule principal cells. Ref.4
Catalytic activity	Guanosine 3',5'-cyclic phosphate + H2O = guanosine 5'-phosphate. Ref.4 Ref.5
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.
Subunit structure	Interacts with PrBP. Ref.5
Subcellular location	Cell membrane; Lipid-anchor; Cytoplasmic side. Note: Expressed on the apical side of the Malpighian tubule principal cell polarised membrane. Loss of prenylation causes protein location to the cytoplasm. Ref.4 Ref.5
Tissue specificity	Expressed in Malpighian tubule principal cells. Ref.4
Disruption phenotype	Flies display increased active transport of cGMP. Overexpression of Pde6 confers inhibition of the active transport and efflux of cGMP by tubules. Ref.4
Sequence similarities	Belongs to the cyclic nucleotide phosphodiesterase family. Contains 2 GAF domains.
Sequence caution	The sequence AAL13699.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Ontologies

Keywords
Cellular component	Cell membrane Membrane
Domain	Repeat
Ligand	Metal-binding cGMP
Molecular function	Hydrolase
PTM	Lipoprotein Methylation Prenylation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	cGMP metabolic process Inferred from direct assay Ref.4Ref.5. Source: UniProtKB negative regulation of nucleobase-containing compound transport Inferred from mutant phenotype Ref.4. Source: FlyBase signal transduction Inferred from electronic annotation. Source: InterPro
Cellular component	apical plasma membrane Inferred from direct assay Ref.4Ref.5. Source: FlyBase
Molecular function	3',5'-cyclic-GMP phosphodiesterase activity Inferred from direct assay Ref.4Ref.5. Source: UniProtKB metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW protein binding Inferred from physical interaction Ref.5. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1115	1115	cGMP-specific 3',5'-cyclic phosphodiesterase		PRO_0000356892
	Propeptide	1116 – 1118	3	Removed in mature form Probable		PRO_0000356893
Regions
	Domain	247 – 399	153	GAF 1
	Domain	431 – 612	182	GAF 2
	Compositional bias	5 – 33	29	Ser-rich
Sites
	Active site	718	1	Proton donor By similarity
	Metal binding	722	1	Divalent metal cation 1 By similarity
	Metal binding	758	1	Divalent metal cation 1 By similarity
	Metal binding	759	1	Divalent metal cation 1 By similarity
	Metal binding	759	1	Divalent metal cation 2 By similarity
	Metal binding	869	1	Divalent metal cation 1 By similarity
Amino acid modifications
	Modified residue	1115	1	Cysteine methyl ester Probable
	Lipidation	1115	1	S-farnesyl cysteine Probable
Experimental info
	Mutagenesis	1115	1	C → S: Impairs prenylation and membrane. Ref.5

Sequences

	Sequence		Length	Mass (Da)
	Q9VFI9 [UniParc]. Last modified October 19, 2011. Version 4. Checksum: 1CFB89721F84DC5A	FASTA	1,118	124,325
	10 20 30 40 50 60 MTDVSSPAGG AASPVEMSTT SSSSAATTSA SSSKPLTNGA NKTAISTAAG GVTPGAVPGP 70 80 90 100 110 120 GSGAIPASSS SGNQVKLEHH HRQSNNNRPA VTNRSSETKL MTPTGSSSSP SQSPSQTQAS 130 140 150 160 170 180 IQTQTSQQDR LAKASTTASQ QDVDEVARLF EEKPEAFEKW LTERAPPEAL SRLQEFIENR 190 200 210 220 230 240 KPHKRPSVTS DLFQQWMAAS PTVQQKSPRS LSNSSASSLP ECRRHLMDLD EGELFMELIR 250 260 270 280 290 300 DVANELDIDV LCHKILVNVG LLTHADRGSL FLAKGTPTNK YLVAKLFDVT QKTALKDAVT 310 320 330 340 350 360 RASAEEIIIP FGIGIAGMVA QTKQMINIKE AYKDARFNCE IDLKTGYKTN AILCMPICNY 370 380 390 400 410 420 EGDIIGVAQI INKTNGCMEF DEHDVEIFRR YLTFCGIGIQ NAQLFEMSVQ EYRRNQILLN 430 440 450 460 470 480 LARSIFEEQN NLECLVTKIM TEARELLKCE RCSVFLVDLD CCEASHLEKI IEKPNQPATR 490 500 510 520 530 540 AIKSADSFEE KKMRNRFTVL FELGGEYQAA NVSRPSVSEL SSSTLAQIAQ FVATTGQTVN 550 560 570 580 590 600 ICDVIEWVRD HNQIRAEDEI DSTQAILCMP IMNAQKKVIG VAQLINKANG VPFTDSDASI 610 620 630 640 650 660 FEAFAIFCGL GIHNTQMYEN ACKLMAKQKV ALECLSYHAT ASQDQTEKLT QDVIAEAESY 670 680 690 700 710 720 NLYSFTFTDF ELVDDDTCRA VLRMFMQCNL VSQFQIPYDV LCRWVLSVRK NYRPVKYHNW 730 740 750 760 770 780 RHALNVAQTM FAMLKTGKME RFMTDLEILG LLVACLCHDL DHRGTNNAFQ TKTESPLAIL 790 800 810 820 830 840 YTTSTMEHHH FDQCVMILNS EGNNIFQALS PEDYRSVMKT VESAILSTDL AMYFKKRNAF 850 860 870 880 890 900 LELVENGEFD WQGEEKKDLL CGMMMTACDV SAIAKPWEVQ HKVAKLVADE FFDQGDLEKL 910 920 930 940 950 960 QLNTQPVAMM DRERKDELPK MQVGFIDVIC LPLYRVLCDT FPWITPLYEG TLENRRNWQD 970 980 990 1000 1010 1020 LAEKVEMGLT WIDHDTIDKP VEEFAACADE EIKDIEFTVT TLNCNQQSQH GSEDSHTPEH 1030 1040 1050 1060 1070 1080 QRSGSRLSMK KTGALGKAVR SKLSKTLYNS MDGSKPKTSL KLLESHVSED MDDKSPTSPS 1090 1100 1110 QPQASGSMGR MSASSSTSSA GGQMVDKSKK RSKLCALL

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. Strain: Berkeley.
[3]	"A Drosophila full-length cDNA resource." Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E. Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed: 12537569] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 84-1118. Strain: Berkeley. Tissue: Head.
[4]	"A novel role for a Drosophila homologue of cGMP-specific phosphodiesterase in the active transport of cGMP." Day J.P., Houslay M.D., Davies S.-A. Biochem. J. 393:481-488(2006) [PubMed: 16232123] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY.
[5]	"Regulation of a Drosophila melanogaster cGMP-specific phosphodiesterase by prenylation and interaction with a prenyl-binding protein." Day J.P., Cleghon V., Houslay M.D., Davies S.-A. Biochem. J. 414:363-374(2008) [PubMed: 18503409] [Abstract] Cited for: CATALYTIC ACTIVITY, INTERACTION WITH PRBP, SUBCELLULAR LOCATION, MUTAGENESIS OF CYS-1115.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE014297 Genomic DNA. Translation: AAF55066.4. AY058470 mRNA. Translation: AAL13699.1. Different initiation.
RefSeq	NP_650369.3. NM_142112.3.
UniGene	Dm.4259.
3D structure databases
HSSP	HSSP built from PDB template 1T9R based on UniProtKB O76074.
ProteinModelPortal	Q9VFI9.
ModBase	Search...
Protein-protein interaction databases
STRING	Q9VFI9.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	41760.
KEGG	dme:Dmel_CG8279.
Organism-specific databases
CTD	41760.
FlyBase	FBgn0038237. Pde6.
Phylogenomic databases
eggNOG	inNOG05101.
GeneTree	EMGT00050000002162.
InParanoid	Q9VFI9.
OMA	DDNPSNP.
OrthoDB	EOG41RN8T.
PhylomeDB	Q9VFI9.
Gene expression databases
ArrayExpress	Q9VFI9.
Bgee	Q9VFI9.
Family and domain databases
InterPro	IPR003018. GAF. 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	K13763.
Pfam	PF01590. GAF. 2 hits. PF00233. PDEase_I. 1 hit. [Graphical view]
PRINTS	PR00387. PDIESTERASE1.
SMART	SM00065. GAF. 2 hits. SM00471. HDc. 1 hit. [Graphical view]
PROSITE	PS00126. PDEASE_I. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	825438.

Entry information

Entry name

PDE6_DROME

Accession

Primary (citable) accession number: Q9VFI9
Secondary accession number(s): Q95TW8

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 16, 2008
Last sequence update:	October 19, 2011
Last modified:	January 25, 2012
This is version 77 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Drosophila annotation project