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B4JXX2 (PDE6_DROGR) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 27. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
cGMP-specific 3',5'-cyclic phosphodiesterase

EC=3.1.4.35
Gene names
Name:Pde6
ORF Names:GH14135
OrganismDrosophila grimshawi (Fruit fly) (Idiomyia grimshawi) [Complete proteome]
Taxonomic identifier7222 [NCBI]
Taxonomic lineageEukaryotaMetazoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaHawaiian Drosophila

Protein attributes

Sequence length1078 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

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.

Ontologies

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

Inferred from sequence or structural similarity. Source: UniProtKB

signal transduction

Inferred from electronic annotation. Source: InterPro

   Cellular componentplasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

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

Inferred from sequence or structural similarity. Source: UniProtKB

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 10751075cGMP-specific 3',5'-cyclic phosphodiesterase UniProtKB Q9VFI9
PRO_0000363688
Propeptide1076 – 10783Removed in mature form By similarity UniProtKB Q9VFI9
PRO_0000363689

Regions

Domain196 – 348153GAF 1
Domain380 – 564185GAF 2
Compositional bias50 – 13384Asn-rich

Sites

Active site6701Proton donor By similarity
Metal binding6741Divalent metal cation 1 By similarity
Metal binding7101Divalent metal cation 1 By similarity
Metal binding7111Divalent metal cation 1 By similarity
Metal binding7111Divalent metal cation 2 By similarity
Metal binding8211Divalent metal cation 1 By similarity

Amino acid modifications

Modified residue10751Cysteine methyl ester By similarity UniProtKB Q9VFI9
Lipidation10751S-farnesyl cysteine By similarity UniProtKB Q9VFI9

Sequences

Sequence LengthMass (Da)Tools
B4JXX2 [UniParc].

Last modified September 23, 2008. Version 1.
Checksum: 4193E7C8A5FB672E

FASTA1,078120,555
        10         20         30         40         50         60 
MRIQTMILGC AFLAICIIGS SNAACDEPDK CTPEECEDPA NAAEESCAEN PDDNPSNPDD 

        70         80         90        100        110        120 
DPSNPDDNPS NPDDNPSNPD DNPSNPDDNP SNPDDNPSNP DDNPSNPDDN PSNPDDNPTN 

       130        140        150        160        170        180 
PDDNPNNPSN PSNPSGGVEA TTAANNGGSG SNAQKSPRRL SNSSVQALPE GRRHLMDLDE 

       190        200        210        220        230        240 
GDLFMELIRD VANELDIDVL CHKILVNVGL LTHADRGSLF LAKGTPNNKY LVAKLFDVTQ 

       250        260        270        280        290        300 
KTALKDAVTR ARAEEIIIPF GIGIAGMVAQ TKEMINIKEA YQDVRFNCEI DQKTGYKTNA 

       310        320        330        340        350        360 
ILCMPICNYE GDIIGVAQII NKTNGCMEFD EHDVEIFRRY LTFCGIGIQN AQLFEMSVQE 

       370        380        390        400        410        420 
YRRNQILLNL ARSIFEEQNN LECLVTKIMT EARELLKCER CSVFLVDLDC CEESHLEKII 

       430        440        450        460        470        480 
EKPHQQEQRT MRAIKGGDSF EEQQKMRNRF TVLFELGGEY QAANVSRPSI NELSHSTLAQ 

       490        500        510        520        530        540 
IAQFVSTTGQ TVNICDVHEW VRDHNQIRDS EIDSTHAILC MPIVNAQKTV IGVAQLINKA 

       550        560        570        580        590        600 
NGLPFSESDV SIFEAFAIFC GLGIHNTQMY ENACKLMAKQ KVALECLSYH ATASQDQTEK 

       610        620        630        640        650        660 
LTQDPIAEAE SYNLYSFTFT DFDLVDDDTC RAVLRMFMQC NLVSQFHIPY DVLCRWVLSV 

       670        680        690        700        710        720 
RKNYRPVKYH NWRHALNVAQ TMFAMLKTGK MERFMTDLEI LGLLVACLCH DLDHRGTNNA 

       730        740        750        760        770        780 
FQTKTESPLA ILYTTSTMEH HHFDQCVMIL NSEGNNIFQA LSPEDYRCVM KTVESAILST 

       790        800        810        820        830        840 
DLAMYFKKRN AFLELVENGE FDWQGEEKKD LLCGMMMTAC DVSAIAKPWE VQHRVAKLVA 

       850        860        870        880        890        900 
DEFFDQGDLE KLQLNTQPVA MMDRERKDEL PKMQVGFIDV ICLPLYRVLC DTFPWITPLY 

       910        920        930        940        950        960 
EGTLENRRNW QDLAEKVEMG LTWIDHDTID KPVEEFAGCA DEEIKDIEFT VTTLNCNQQS 

       970        980        990       1000       1010       1020 
QSQSQSQSQS QHGGDDIHTP EHQRSSGSRL SIKKTGALGK VVRSKLSKTL YNSMDGSKPK 

      1030       1040       1050       1060       1070 
TSLKLLESHV SEDMDDKSPT SPSQPHSGSV GRMSASSSTS SAGTVDKTKK 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 15287-2541.00.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CH916377 Genomic DNA. Translation: EDV90534.1.
RefSeqXP_001995876.1. XM_001995840.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGB4JXX2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0149549; FBpp0148041; FBgn0121611.
GeneID6569905.
KEGGdgr:Dgri_GH14135.

Organism-specific databases

FlyBaseFBgn0121611. Dgri\GH14135.

Phylogenomic databases

GeneTreeEMGT00050000002162.
InParanoidB4JXX2.
OMADDNPSNP.
OrthoDBEOG41RN8T.
PhylomeDBB4JXX2.

Family and domain databases

InterProIPR003018. GAF.
IPR003607. Metal-dep_PHydrolase_HD_dom.
IPR023088. PDEase.
IPR002073. PDEase_catalytic_dom.
IPR023174. PDEase_CS.
[Graphical view]
Gene3DG3DSA:1.10.1300.10. PDEase_catalytic_dom. 1 hit.
KOK13763.
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...

Entry information

Entry namePDE6_DROGR
AccessionPrimary (citable) accession number: B4JXX2
Entry history
Integrated into UniProtKB/Swiss-Prot: February 10, 2009
Last sequence update: September 23, 2008
Last modified: January 25, 2012
This is version 27 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Relevant documents

Drosophila

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

SIMILARITY comments

Index of protein domains and families