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Reviewed, UniProtKB/Swiss-Prot B3LVW5 (PDE6_DROAN)

Last modified February 9, 2010. Version 15. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    cGMP-specific 3',5'-cyclic phosphodiesterase
    EC=3.1.4.35
Gene names
Name: Pde6
ORF Names: GF17478
OrganismDrosophila ananassae (Fruit fly)
Taxonomic identifier7217 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Ephydroidea › Drosophilidae › Drosophila › Sophophora

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Protein attributes

Sequence length1158 AA.
Sequence statusComplete.
Protein existenceInferred from homology.

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General annotation (Comments)

Function

Has a role regulating cGMP transport in Malpighian tubule principal cells By similarity. UniProtKB Q9VFI9

Catalytic activity

Guanosine 3',5'-cyclic phosphate + H2O = guanosine 5'-phosphate. UniProtKB Q9VFI9

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 By similarity. UniProtKB Q9VFI9

Subcellular location

Cell membrane; Lipid-anchor; Cytoplasmic side By similarity UniProtKB Q9VFI9.

Sequence similarities

Belongs to the cyclic nucleotide phosphodiesterase family.

Contains 2 GAF domains.

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Ontologies

Keywords
   Cellular componentCell membrane
Membrane
   DomainRepeat
   LigandMetal-binding
cGMP
   Molecular functionHydrolase
   PTMLipoprotein
Methylation
Prenylation
Gene Ontology (GO)
   Biological processcGMP metabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

signal transduction

Inferred from electronic annotation. Source: InterPro

   Cellular componentanchored to membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

plasma membrane

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular function3',5'-cyclic-GMP phosphodiesterase activity

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 11551155cGMP-specific 3',5'-cyclic phosphodiesterase UniProtKB Q9VFI9
PRO_0000363684
Propeptide1156 – 11583Removed in mature form By similarity UniProtKB Q9VFI9
PRO_0000363685

Regions

Domain242 – 394153GAF 1
Domain426 – 640215GAF 2
Compositional bias30 – 6940Ala-rich

Sites

Active site7461Proton donor By similarity
Metal binding7501Divalent metal cation 1 By similarity
Metal binding7861Divalent metal cation 1 By similarity
Metal binding7871Divalent metal cation 1 By similarity
Metal binding7871Divalent metal cation 2 By similarity
Metal binding8971Divalent metal cation 1 By similarity

Amino acid modifications

Modified residue11551Cysteine methyl ester By similarity UniProtKB Q9VFI9
Lipidation11551S-farnesyl cysteine By similarity UniProtKB Q9VFI9

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Sequences

Sequence LengthMass (Da)Tools
B3LVW5-1 [UniParc].

Last modified September 2, 2008. Version 1.
Checksum: 977DCAE9614F1792

FASTA1,158127,966
        10         20         30         40         50         60 
MTDVSAPTGG ATSPVDITAS PGSTALPPVA TTSAAASASS SQAKPLTNGA KKAATAAAAA 

        70         80         90        100        110        120 
GAEEGGASAS NQVKQEQRRQ SNNNRPAASG TPEAKQATPA GNPDPGAGST SKSSSIHTQT 

       130        140        150        160        170        180 
SQQERAGRPT SSASQHDVDE VARLFEEKPE AFEKWLTERA PPEALGRLQE FIESRKPLKR 

       190        200        210        220        230        240 
PSVTSDLFQQ WMAASPTVQQ KSPRSLSNSS ASSIPESRRH LMDLDEGELF MELIRDVANE 

       250        260        270        280        290        300 
LDIDVLCHKI LVNVGLLTHA DRGSLFLAKG APNNKYLVAK LFDVTQKTAL KDAVTRASTE 

       310        320        330        340        350        360 
EIIIPFGIGI AGMVAQTKQM INIKEAYKDA RFNCEIDLKT GYKTNAILCM PICNYEGDII 

       370        380        390        400        410        420 
GVAQIINKTN GCMEFDEHDV EIFRRYLTFC GIGIQNAQLF EMSVQEYRRN QILLNLARSI 

       430        440        450        460        470        480 
FEEQNNLECL VTKIMTEARE LLKCERCSVF LVDLDCCEAG CGRVGGAMRR FGVRSKQVSA 

       490        500        510        520        530        540 
IVEHVGGRRG NTSHLEKIIE KPNQPATRAI KSADSFEEKK MRNRFTVLFE LGGEYQAANV 

       550        560        570        580        590        600 
SRPSTSELST STLAQIAQFV ATTGQTVNIC DVHEWVREHN QIRAESEIDS TQAILCMPIV 

       610        620        630        640        650        660 
NAKKTVIGVA QLINKANGVP FTESDASIFE AFAIFCGLGI HNTQMYENAC KLMAKQKVAL 

       670        680        690        700        710        720 
ECLSYHATAS QDQTEKLTQD AIADADTYNL YSFTFTDFEL VDDDTCRAVL RMFMQCNLVS 

       730        740        750        760        770        780 
QFQIPYDVLC RWVLSVRKNY RPVKYHNWRH ALNVAQTMFA MLKTGKMERF MTDLEILGLL 

       790        800        810        820        830        840 
VACLCHDLDH RGTNNAFQTK TESPLAILYT TSTMEHHHFD QCVMILNSEG NNIFQALSPE 

       850        860        870        880        890        900 
DYRSVMKTVE SAILSTDLAM YFKKRNAFLE LVENGEFDWQ GEEKKDLLCG MMMTACDVSA 

       910        920        930        940        950        960 
IAKPWEVQHK VAKLVADEFF DQGDLEKLQL NTQPVAMMDR ERKDELPKMQ VGFIDVICLP 

       970        980        990       1000       1010       1020 
LYRVLCDTFP WITPLYEGTL ENRRNWQDLA EKVEMGLTWI DHDTIDKPVE EFAACADEEI 

      1030       1040       1050       1060       1070       1080 
KDIEFTVTTL NCNQSQQSQH GSEDSHTPEH QRSGSRLSMK KTGALGKAVR SKLSKTLYNS 

      1090       1100       1110       1120       1130       1140 
MDGSKPKTSL KLLESHVSED MDDKSPTSPS QPQAAGSMGR MSASSSTSSA GGQGQCQVAA 

      1150 
PGQAQDKSKK RSKLCALL

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References

[1]"Evolution of genes and genomes on the Drosophila phylogeny."
Drosophila 12 genomes consortium
Nature 450:203-218(2007) [PubMed: 17994087] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Tucson 14024-0371.13.

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CH902617 Genomic DNA. Translation: EDV41498.1.
RefSeqXP_001952915.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID6500262.
KEGGdan:Dana_GF17478.

Organism-specific databases

FlyBaseFBgn0094496. Dana\GF17478.

Phylogenomic databases

InParanoidB3LVW5.
OrthoDBEOG9MCX5S.

Family and domain databases

InterProIPR003018. GAF.
IPR003607. Metal-dep_PHydrolase_HD_dom.
IPR002073. PDEase.
[Graphical view]
PfamPF01590. GAF. 2 hits.
PF00233. PDEase_I. 1 hit.
[Graphical view]
PRINTSPR00387. PDIESTERASE1.
SMARTSM00065. GAF. 2 hits.
SM00471. HDc. 1 hit.
[Graphical view]
PROSITEPS00126. PDEASE_I. 1 hit.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry namePDE6_DROAN
AccessionPrimary (citable) accession number: B3LVW5
Entry history
Integrated into UniProtKB/Swiss-Prot: February 10, 2009
Last sequence update: September 2, 2008
Last modified: February 9, 2010
This is version 15 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectDrosophila annotation project

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Relevant documents

Drosophila

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

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents