ID PDE6_DROSI Reviewed; 1143 AA. AC B4QZU1; DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot. DT 23-SEP-2008, sequence version 1. DT 24-JAN-2024, entry version 73. DE RecName: Full=cGMP-specific 3',5'-cyclic phosphodiesterase {ECO:0000250|UniProtKB:Q9VFI9}; DE EC=3.1.4.35; DE Flags: Precursor; GN Name=Pde6 {ECO:0000250|UniProtKB:Q9VFI9}; ORFNames=GD20415; OS Drosophila simulans (Fruit fly). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea; OC Drosophilidae; Drosophila; Sophophora. OX NCBI_TaxID=7240; RN [1] {ECO:0000312|EMBL:EDX12939.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=17994087; DOI=10.1038/nature06341; RG Drosophila 12 genomes consortium; RT "Evolution of genes and genomes on the Drosophila phylogeny."; RL Nature 450:203-218(2007). CC -!- FUNCTION: Has a role regulating cGMP transport in Malpighian tubule CC principal cells. {ECO:0000250|UniProtKB:Q9VFI9}. CC -!- CATALYTIC ACTIVITY: CC Reaction=3',5'-cyclic GMP + H2O = GMP + H(+); Xref=Rhea:RHEA:16957, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57746, CC ChEBI:CHEBI:58115; EC=3.1.4.35; CC Evidence={ECO:0000250|UniProtKB:Q9VFI9}; CC -!- COFACTOR: CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240; CC Evidence={ECO:0000250}; CC Note=Binds 2 divalent metal cations per subunit. Site 1 may CC preferentially bind zinc ions, while site 2 has a preference for CC magnesium and/or manganese ions. {ECO:0000250}; CC -!- SUBUNIT: Interacts with PrBP. {ECO:0000250|UniProtKB:Q9VFI9}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9VFI9}; CC Lipid-anchor {ECO:0000250|UniProtKB:Q9VFI9}; Cytoplasmic side CC {ECO:0000250|UniProtKB:Q9VFI9}. CC -!- SIMILARITY: Belongs to the cyclic nucleotide phosphodiesterase family. CC {ECO:0000255}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CM000364; EDX12939.1; -; Genomic_DNA. DR RefSeq; XP_016034708.1; XM_016176727.1. DR AlphaFoldDB; B4QZU1; -. DR SMR; B4QZU1; -. DR STRING; 7240.B4QZU1; -. DR EnsemblMetazoa; FBtr0220325; FBpp0218817; FBgn0191887. DR GeneID; 6728084; -. DR HOGENOM; CLU_006980_0_2_1; -. DR OMA; ATIRMFK; -. DR OrthoDB; 5479253at2759; -. DR PhylomeDB; B4QZU1; -. DR ChiTaRS; Pde6; fly. DR Proteomes; UP000000304; Chromosome 3r. DR Bgee; FBgn0191887; Expressed in adult organism and 2 other cell types or tissues. DR GO; GO:0016020; C:membrane; ISS:UniProtKB. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0047555; F:3',5'-cyclic-GMP phosphodiesterase activity; ISS:UniProtKB. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0046068; P:cGMP metabolic process; ISS:UniProtKB. DR GO; GO:0007165; P:signal transduction; IEA:InterPro. DR CDD; cd00077; HDc; 1. DR Gene3D; 3.30.450.40; -; 2. DR Gene3D; 1.10.1300.10; 3'5'-cyclic nucleotide phosphodiesterase, catalytic domain; 1. DR InterPro; IPR003018; GAF. DR InterPro; IPR029016; GAF-like_dom_sf. DR InterPro; IPR003607; HD/PDEase_dom. DR InterPro; IPR023088; PDEase. DR InterPro; IPR002073; PDEase_catalytic_dom. DR InterPro; IPR036971; PDEase_catalytic_dom_sf. DR InterPro; IPR023174; PDEase_CS. DR PANTHER; PTHR11347; CYCLIC NUCLEOTIDE PHOSPHODIESTERASE; 1. DR PANTHER; PTHR11347:SF216; PHOSPHODIESTERASE; 1. DR Pfam; PF01590; GAF; 2. DR Pfam; PF00233; PDEase_I; 1. DR PRINTS; PR00387; PDIESTERASE1. DR SMART; SM00065; GAF; 2. DR SMART; SM00471; HDc; 1. DR SUPFAM; SSF55781; GAF domain-like; 2. DR SUPFAM; SSF109604; HD-domain/PDEase-like; 1. DR PROSITE; PS00126; PDEASE_I_1; 1. DR PROSITE; PS51845; PDEASE_I_2; 1. PE 3: Inferred from homology; KW Cell membrane; cGMP; Hydrolase; Lipoprotein; Membrane; Metal-binding; KW Methylation; Prenylation; Reference proteome; Repeat. FT CHAIN 1..1140 FT /note="cGMP-specific 3',5'-cyclic phosphodiesterase" FT /id="PRO_0000363698" FT PROPEP 1141..1143 FT /note="Removed in mature form" FT /evidence="ECO:0000250|UniProtKB:Q9VFI9" FT /id="PRO_0000363699" FT DOMAIN 272..424 FT /note="GAF 1" FT /evidence="ECO:0000255" FT DOMAIN 456..637 FT /note="GAF 2" FT /evidence="ECO:0000255" FT DOMAIN 667..990 FT /note="PDEase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01192" FT REGION 1..167 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1031..1060 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1090..1143 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1..60 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 98..114 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 125..167 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1099..1130 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 743 FT /note="Proton donor" FT /evidence="ECO:0000250" FT BINDING 747 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /ligand_label="1" FT /evidence="ECO:0000250" FT BINDING 783 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /ligand_label="1" FT /evidence="ECO:0000250" FT BINDING 784 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /ligand_label="1" FT /evidence="ECO:0000250" FT BINDING 784 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 894 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /ligand_label="1" FT /evidence="ECO:0000250" FT MOD_RES 1140 FT /note="Cysteine methyl ester" FT /evidence="ECO:0000250|UniProtKB:Q9VFI9" FT LIPID 1140 FT /note="S-farnesyl cysteine" FT /evidence="ECO:0000250|UniProtKB:Q9VFI9" SQ SEQUENCE 1143 AA; 126868 MW; 33060D06C24BA337 CRC64; MHGPVSRSSS SSNMTDVSSP AGGAASPVEM TTSSSSAATT SASSSKPLTN GANKTTISTV AGGVAPGAVP GPGSGAIPAS SSSGNQVKLE HHHRQSNNNR PAATNRSSET KLRSPAGESD GASRLMTPAG SSSSPSQSPS QTQASIQTQT SQQDRLAKAS TTASQQDVDE VARLFEEKPE AFEKWLTERA PPEALSRLQE FIENRKPHKR PSVTSDLFQQ WMAASPTVQQ KSPRSLSNSS ASSLPECRRH LMDLDEGELF MELIRDVANE LDIDVLCHKI LVNVGLLTHA DRGSLFLAKG TPTNKYLVAK LFDVTQKTAL KDAVTRASAE EIIIPFGIGI AGMVAQTKQM INIKEAYKDA RFNCEIDLKT GYKTNAILCM PICNYEGDII GVAQIINKTN GCMEFDEHDV EIFRRYLTFC GIGIQNAQLF EMSVQEYRRN QILLNLARSI FEEQNNLECL VTKIMTEARE LLKCERCSVF LVDLDCCEAS HLEKIIEKPN QQATRAIKSA DSFEEKKMRN RFTVLFELGG EYQAANVSRP SVSELSSSTL AQIAQFVATT GQTVNICDVI EWVRDHNQIR AEDEIDSTQA ILCMPIMNAQ KKVIGVAQLI NKANGVPFTD SDASIFEAFA IFCGLGIHNT QMYENACKLM AKQKVALECL SYHATASQDQ TEKLTQDVIA EAESYNLYSF TFTDFELVDD DTCRAVLRMF MQCNLVSQFQ IPYDVLCRWV LSVRKNYRPV KYHNWRHALN VAQTMFAMLK TGKMERFMTD LEILGLLVAC LCHDLDHRGT NNAFQTKTES PLAILYTTST MEHHHFDQCV MILNSEGNNI FQALSPEDYR SVMKTVESAI LSTDLAMYFK KRNAFLELVE NGEFDWQGEE KKDLLCGMMM TACDVSAIAK PWEVQHKVAK LVADEFFDQG DLEKLQLNTQ PVAMMDRERK DELPKMQVGF IDVICLPLYR VLCDTFPWIT PLYEGTLENR RNWQDLAEKV EMGLTWIDHD TIDKPVEEFA ACADEEIKDI EFTVTTLNCN QQSQHGSEDS HTPEHQRSGS RLSMKKTGAL GKAVRSKLSK TLYNSMDGSK PKTSLKLLES HVSEDMDDKS PTSPSQPQAS GSMGRMSASS STSSTGGQMV DKSKKRSKLC ALL //