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B4HEM4 (PDE6_DROSE) 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:GM25848
OrganismDrosophila sechellia (Fruit fly) [Complete proteome]
Taxonomic identifier7238 [NCBI]
Taxonomic lineageEukaryotaMetazoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length1205 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 – 12021202cGMP-specific 3',5'-cyclic phosphodiesterase UniProtKB Q9VFI9
PRO_0000363696
Propeptide1203 – 12053Removed in mature form By similarity UniProtKB Q9VFI9
PRO_0000363697

Regions

Domain259 – 411153GAF 1
Domain443 – 624182GAF 2

Sites

Active site7301Proton donor By similarity
Metal binding7341Divalent metal cation 1 By similarity
Metal binding7701Divalent metal cation 1 By similarity
Metal binding7711Divalent metal cation 1 By similarity
Metal binding7711Divalent metal cation 2 By similarity
Metal binding9561Divalent metal cation 1 By similarity

Amino acid modifications

Modified residue12021Cysteine methyl ester By similarity UniProtKB Q9VFI9
Lipidation12021S-farnesyl cysteine By similarity UniProtKB Q9VFI9

Sequences

Sequence LengthMass (Da)Tools
B4HEM4 [UniParc].

Last modified September 23, 2008. Version 1.
Checksum: A2D9562B2022719C

FASTA1,205133,207
        10         20         30         40         50         60 
MTDVSSPAGG AASPVEMTTS SSPAATTSAS SSKPLTNGAN KTTISTTAGG VAPGDVPGTG 

        70         80         90        100        110        120 
SGAIPASSSS GNQVKLEHHH RQSNNNRPAA TNRSSETKLR SPAGESDGAS RLMTPAGSSS 

       130        140        150        160        170        180 
SPSQSPSQTQ ASIQTQTSQQ DRLTKASTTA SQQDVDEVAR LFEEKPEAFE KWLTERAPPE 

       190        200        210        220        230        240 
ALSRLQEFIE NRKPHKRPSV TSDLFQQWMA ASPTVQQKSP RSLSNSSASS LPECRRHLMD 

       250        260        270        280        290        300 
LDEGELFMEL IRDVANELDI DVLCHKILVN VGLLTHADRG SLFLAKGTPT NKYLVAKLFD 

       310        320        330        340        350        360 
VTQKTALKDA VARASAEEII IPFGIGIAGM VAQTKQMINI KEAYKDARFN CEIDLKTGYK 

       370        380        390        400        410        420 
TNAILCMPIC NYEGDIIGVA QIINKTNGCM EFDEHDVEIF RRYLTFCGIG IQNAQLFEMS 

       430        440        450        460        470        480 
VQEYRRNQIL LNLARSIFEE QNNLECLVTK IMTEARELLK CERCSVFLVD LDCCEASHLE 

       490        500        510        520        530        540 
KIIEKPNQPA TRAIKSADSF EEKKMRNRFT VLFELGGEYQ AANVSRPSVS ELSSSTLAQI 

       550        560        570        580        590        600 
AQFVATTGQT VNICDVIEWV RDHNQIRAED EIDSTQAILC MPIMNAQKKV IGVAQLINKA 

       610        620        630        640        650        660 
NGVPFTDSDA SIFEAFAIFC GLGIHNTQMY ENACKLMAKQ KVALECLSYH ATASQDQTEK 

       670        680        690        700        710        720 
LTQDVIAEAE SYNLYSFTFT DFELVDDDTC RAVLRMFMQC NLVSQFQIPY DVLCRWVLSV 

       730        740        750        760        770        780 
RKNYRPVKYH NWRHALNVAQ TMFAMLKTGK MERFMTDLEI LGLLVACLCH DLDHRGTNNA 

       790        800        810        820        830        840 
FQTKTESPLA ILYTTSTMEH HHFDQCVMIL NSEGNNIFQT GFAGLGAGTF GSGRGTGGGS 

       850        860        870        880        890        900 
NSNFPGDRVL QIARRTIFFF VPELDAEDDV VDSVVDSVVE LSVVVLVLDS VLVAALSPED 

       910        920        930        940        950        960 
YRSVMKTVES AILSTDLAMY FKKRNAFLEL VENGEFDWQG EEKKDLLCGM MMTACDVSAI 

       970        980        990       1000       1010       1020 
AKPWEVQHKV AKLVADEFFD QGDLEKLQLN TQPVAMMDRE RKDELPKMQV GFIDVICLPL 

      1030       1040       1050       1060       1070       1080 
YRVLCDTFPW ITPLYEGTLE NRRNWQDLAE KVEMGLTWID HDTIDKPVEE FAACADEEIK 

      1090       1100       1110       1120       1130       1140 
DIEFTVTTLN CNQQSQHGSE DSHTPEHQRS GSRLSMKKTG ALGKAVRSKL SKTLYNSMDG 

      1150       1160       1170       1180       1190       1200 
SKPKTSLKLL ESHVSEDMDD KSPTSPSQPQ ASGSMGRMSA SSSTSSAGGQ MVDKSKKRSK 


LCALL 

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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: Rob3c / Tucson 14021-0248.25.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CH480815 Genomic DNA. Translation: EDW42181.1.
RefSeqXP_002031195.1. XM_002031159.1.

3D structure databases

ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0208833; FBpp0207325; FBgn0180704.
GeneID6606390.
KEGGdse:Dsec_GM25848.

Organism-specific databases

FlyBaseFBgn0180704. Dsec\GM25848.

Phylogenomic databases

GeneTreeEMGT00050000002162.
OrthoDBEOG41RN8T.
PhylomeDBB4HEM4.

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. 2 hits.
KOK13763.
PfamPF01590. GAF. 2 hits.
PF00233. PDEase_I. 2 hits.
[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_DROSE
AccessionPrimary (citable) accession number: B4HEM4
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