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B4K9L4 (PDE6_DROMO) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 24. 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:GI10668
OrganismDrosophila mojavensis (Fruit fly) [Complete proteome]
Taxonomic identifier7230 [NCBI]
Taxonomic lineageEukaryotaMetazoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophila

Protein attributes

Sequence length1116 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 – 11131113cGMP-specific 3',5'-cyclic phosphodiesterase UniProtKB Q9VFI9
PRO_0000363690
Propeptide1114 – 11163Removed in mature form By similarity UniProtKB Q9VFI9
PRO_0000363691

Regions

Domain241 – 393153GAF 1
Domain425 – 611187GAF 2
Compositional bias44 – 7431Thr-rich

Sites

Active site7171Proton donor By similarity
Metal binding7211Divalent metal cation 1 By similarity
Metal binding7571Divalent metal cation 1 By similarity
Metal binding7581Divalent metal cation 1 By similarity
Metal binding7581Divalent metal cation 2 By similarity
Metal binding8681Divalent metal cation 1 By similarity

Amino acid modifications

Modified residue11131Cysteine methyl ester By similarity UniProtKB Q9VFI9
Lipidation11131S-farnesyl cysteine By similarity UniProtKB Q9VFI9

Sequences

Sequence LengthMass (Da)Tools
B4K9L4 [UniParc].

Last modified September 23, 2008. Version 1.
Checksum: 53186D5E1651993E

FASTA1,116124,330
        10         20         30         40         50         60 
MTDVSATTGR AGDRVSSTSS EVAVETTSQA LTNGAAKEPL AAVTAEATAT ATVTATTTAT 

        70         80         90        100        110        120 
VTATTTAATA TMATAVISKQ AKSECHSQSN NNQHVETAPS KQSSDSEASA PTTVSIPSAN 

       130        140        150        160        170        180 
AKINSSSSGK TTATQQDVDE VARLFEEKPE AFEKWLTERA PPEALSRLHE FIESRKPHKR 

       190        200        210        220        230        240 
PSVTSDLFQQ WMASPTVQQK SPRKLSNSSV HALPESRRHL MELDEGELFM ELIRDVANEL 

       250        260        270        280        290        300 
DIDVLCHKIL VNVGLLTHAD RGSLFLAKGT PNNRYLVAKL FDVTQTTALK DAVTRARAEE 

       310        320        330        340        350        360 
IIIPFGIGIA GMVAQTKQMI NIKEAYKDAR FNCEIDLKTG YTTNAILCMP ICNYEGDIIG 

       370        380        390        400        410        420 
VAQIINKTNG CMEFDEHDVE IFRRYLTFCG IGIQNAQLFE MSVQEYRRNQ ILLNLARSIF 

       430        440        450        460        470        480 
EEQNNLECLV TKIMTEAREL LKCERCSVFL VDLDCCEESH LEKIIEKPHQ LQQQRTPRAI 

       490        500        510        520        530        540 
MSGDSFEEKQ NMRNRFTVLF ELGGENHAAN VSRPSINDLS HSTLAQIAQF VATTGQTVNI 

       550        560        570        580        590        600 
CDVQDWVREH NQIRAESEID STQAILCMPI VNAQKTVIGV AQLINKASGL PFTESDASIF 

       610        620        630        640        650        660 
EAFAIFCGLG IHNTQMYENA CKLMAKQKVA LECLSYHATA SQDQTEKLAQ DVIAEAEAYN 

       670        680        690        700        710        720 
LYSFTFTDFD LVDDDTCRAV LRMFMQCNLV SQFHIPYDVL CRWVLSVRKN YRPVKYHNWR 

       730        740        750        760        770        780 
HALNVAQTMF AMLKTGKMER FMTDLEILGL LVACLCHDLD HRGTNNAFQT KTESPLAILY 

       790        800        810        820        830        840 
TTSTMEHHHF DQCVMILNSE GNNIFQALSP EDYRSVMKTV ESAILSTDLA MYFKKRNAFL 

       850        860        870        880        890        900 
ELVENGEFDW QGEEKKDLLC GMMMTACDVS AIAKPWEVQH RVAKLVADEF FDQGDLEKLQ 

       910        920        930        940        950        960 
LNTQPVAMMD RERKDELPKM QVGFIDVICL PLYRVLCDTF PWITPLYEGT LENRRNWQDL 

       970        980        990       1000       1010       1020 
AEKVEMGLTW IDHDTIDKPV EEFAGCADEE IKDIEFTVTT LNCNQHGGSA GGGEDTHTPE 

      1030       1040       1050       1060       1070       1080 
HQRSSSRLSI KKTGALGKVV RSKLSKTLYN SMDGSKPKTS LKLLESHVSE DMDDKSPTSP 

      1090       1100       1110 
SQPHSGSVGR MSASSSTSSA GTVDKSKKRS KLCALL 

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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 15081-1352.22.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CH933806 Genomic DNA. Translation: EDW16674.1.
RefSeqXP_002001213.1. XM_002001177.1.

3D structure databases

ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0161393; FBpp0159885; FBgn0133432.
GeneID6575197.
KEGGdmo:Dmoj_GI10668.

Organism-specific databases

FlyBaseFBgn0133432. Dmoj\GI10668.

Phylogenomic databases

GeneTreeEMGT00050000002162.
InParanoidB4K9L4.
OrthoDBEOG41RN8T.
PhylomeDBB4K9L4.

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_DROMO
AccessionPrimary (citable) accession number: B4K9L4
Entry history
Integrated into UniProtKB/Swiss-Prot: February 10, 2009
Last sequence update: September 23, 2008
Last modified: January 25, 2012
This is version 24 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