ID PDE6_DROWI Reviewed; 1127 AA. AC B4NAL6; DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot. DT 23-SEP-2008, sequence version 1. DT 24-JAN-2024, entry version 81. 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=GK11355; OS Drosophila willistoni (Fruit fly). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea; OC Drosophilidae; Drosophila; Sophophora. OX NCBI_TaxID=7260; RN [1] {ECO:0000312|EMBL:EDW80830.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Tucson 14030-0811.24 {ECO:0000312|EMBL:EDW80830.1}; 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; CH964232; EDW80830.1; -; Genomic_DNA. DR RefSeq; XP_002069844.2; XM_002069808.2. DR AlphaFoldDB; B4NAL6; -. DR SMR; B4NAL6; -. DR STRING; 7260.B4NAL6; -. DR EnsemblMetazoa; FBtr0242006; FBpp0240498; FBgn0213366. DR KEGG; dwi:6647390; -. DR eggNOG; KOG3689; Eukaryota. DR HOGENOM; CLU_006980_0_2_1; -. DR OMA; ATIRMFK; -. DR OrthoDB; 5479253at2759; -. DR PhylomeDB; B4NAL6; -. DR ChiTaRS; Pde6; fly. DR Proteomes; UP000007798; Unassembled WGS sequence. 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..1124 FT /note="cGMP-specific 3',5'-cyclic phosphodiesterase" FT /id="PRO_0000363702" FT PROPEP 1125..1127 FT /note="Removed in mature form" FT /evidence="ECO:0000250|UniProtKB:Q9VFI9" FT /id="PRO_0000363703" FT DOMAIN 255..407 FT /note="GAF 1" FT /evidence="ECO:0000255" FT DOMAIN 439..624 FT /note="GAF 2" FT /evidence="ECO:0000255" FT DOMAIN 654..977 FT /note="PDEase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01192" FT REGION 1..147 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 206..225 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1018..1045 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1078..1127 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 16..100 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 110..147 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1085..1114 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 730 FT /note="Proton donor" FT /evidence="ECO:0000250" FT BINDING 734 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /ligand_label="1" FT /evidence="ECO:0000250" FT BINDING 770 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /ligand_label="1" FT /evidence="ECO:0000250" FT BINDING 771 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /ligand_label="1" FT /evidence="ECO:0000250" FT BINDING 771 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 881 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /ligand_label="1" FT /evidence="ECO:0000250" FT MOD_RES 1124 FT /note="Cysteine methyl ester" FT /evidence="ECO:0000250|UniProtKB:Q9VFI9" FT LIPID 1124 FT /note="S-farnesyl cysteine" FT /evidence="ECO:0000250|UniProtKB:Q9VFI9" SQ SEQUENCE 1127 AA; 125223 MW; 32473E517D9B55C5 CRC64; MTDVSAAAGG ATAEPPTATM SPTSVEPLTN GAKKSAMATT TETQTAAAAA AATTTPAATT TVTVTAAATT EASTSNQVKL ARVENVLGST STSSPANETK PKSLPDGGNA SVAPASSSSN SISTQTLIQS QSQPHAKTNK STTVASQQDV DEVARLFEEK PEAFEKWLTE RAPPEALSRL HEFIESRKPP KRPSVTSDLF QQWMASSPTV QQKSPGRSLS NSSASSLPEC RRHLMDLDEG ELFMELIRDV ANELDIDVLC HKILVNVGLL THADRGSLFL AKGTANNKYL VAKLFDVTQK TALKDAVTRA STEEIIIPFG IGIAGMVAQT KQMINIKEAY KDARFNCEID LKTGYKTNAI LCMPICNYEG DIIGVAQIIN KTNGCMEFDE HDVEIFRRYL TFCGIGIQNA QLFEMSVQEY RRNQILLNLA RSIFEEQNNL ECLVTKIMTE ARELLKCERC SVFLVDLDCC EASHLEKIIE KPNQLEQRPS RAIKSADSFE EKKLRNRFTV LFELGGEYQA ANVSRPSISE LSHSTLAQIA QFVATTGQTV NICDVNEWVR EHNHQIRTES EIDSTQAILC MPIVNAQKTV IGVAQLINKA NGVPFTESDA SIFEAFAIFC GLGIHNTQMY ENACKLMAKQ KVALECLSYH ATANQDQTEK LTQDVVAEAE SYNLYSFTFT DFDLVDDDTC RAVLRMFMQC NLVSQFQIPY DVLCRWVLSV RKNYRPVKYH NWRHALNVAQ TMFAMLKTGK MERFMTDLEI LGLLVACLCH DLDHRGTNNA FQTKTESPLA ILYTTSTMEH HHFDQCVMIL NSEGNNIFQA LSPEDYRSVM KTVESAILST DLAMYFKKRN AFLELVENGE FDWQGEEKKD LLCGMMMTAC DVSAIAKPWE VQHRVAKLVA DEFFDQGDLE KLQLNTQPVA MMDRERKDEL PKMQVGFIDV ICLPLYRVLC DTFPWITPLY EGTLENRRNW QDLAEKVEMG LTWIDHDTID KPVEEFAGCA DEDIKDIEFT VQTLNCNQQS QETDAHTTPE HHRSGSRLSM KKTGALGKAV RSKLSKTLYN SMDGSKPKTS LKLLESHVSE DMDDKSPTSP SQPHGGSVGR MSASSSTSSA GTVVDKTKKR SKLCALL //