ID PDE6_DROGR Reviewed; 1078 AA. AC B4JXX2; DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot. DT 23-SEP-2008, sequence version 1. DT 24-JAN-2024, entry version 75. 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=GH14135; OS Drosophila grimshawi (Hawaiian fruit fly) (Idiomyia grimshawi). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea; OC Drosophilidae; Drosophila; Hawaiian Drosophila. OX NCBI_TaxID=7222; RN [1] {ECO:0000312|EMBL:EDV90534.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Tucson 15287-2541.00 {ECO:0000312|EMBL:EDV90534.1}; 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; CH916377; EDV90534.1; -; Genomic_DNA. DR RefSeq; XP_001995876.1; XM_001995840.1. DR AlphaFoldDB; B4JXX2; -. DR SMR; B4JXX2; -. DR STRING; 7222.B4JXX2; -. DR EnsemblMetazoa; FBtr0467024; FBpp0417204; FBgn0121611. DR eggNOG; KOG3689; Eukaryota. DR HOGENOM; CLU_006980_0_2_1; -. DR InParanoid; B4JXX2; -. DR OMA; ATIRMFK; -. DR PhylomeDB; B4JXX2; -. DR ChiTaRS; Pde6; fly. DR Proteomes; UP000001070; 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..1075 FT /note="cGMP-specific 3',5'-cyclic phosphodiesterase" FT /id="PRO_0000363688" FT PROPEP 1076..1078 FT /note="Removed in mature form" FT /evidence="ECO:0000250|UniProtKB:Q9VFI9" FT /id="PRO_0000363689" FT DOMAIN 196..348 FT /note="GAF 1" FT /evidence="ECO:0000255" FT DOMAIN 380..564 FT /note="GAF 2" FT /evidence="ECO:0000255" FT DOMAIN 594..917 FT /note="PDEase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01192" FT REGION 24..168 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 958..994 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1011..1078 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 61..123 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 129..168 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 958..974 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1037..1065 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 670 FT /note="Proton donor" FT /evidence="ECO:0000250" FT BINDING 674 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /ligand_label="1" FT /evidence="ECO:0000250" FT BINDING 710 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /ligand_label="1" FT /evidence="ECO:0000250" FT BINDING 711 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /ligand_label="1" FT /evidence="ECO:0000250" FT BINDING 711 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 821 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /ligand_label="1" FT /evidence="ECO:0000250" FT MOD_RES 1075 FT /note="Cysteine methyl ester" FT /evidence="ECO:0000250|UniProtKB:Q9VFI9" FT LIPID 1075 FT /note="S-farnesyl cysteine" FT /evidence="ECO:0000250|UniProtKB:Q9VFI9" SQ SEQUENCE 1078 AA; 120555 MW; 4193E7C8A5FB672E CRC64; MRIQTMILGC AFLAICIIGS SNAACDEPDK CTPEECEDPA NAAEESCAEN PDDNPSNPDD DPSNPDDNPS NPDDNPSNPD DNPSNPDDNP SNPDDNPSNP DDNPSNPDDN PSNPDDNPTN PDDNPNNPSN PSNPSGGVEA TTAANNGGSG SNAQKSPRRL SNSSVQALPE GRRHLMDLDE GDLFMELIRD VANELDIDVL CHKILVNVGL LTHADRGSLF LAKGTPNNKY LVAKLFDVTQ KTALKDAVTR ARAEEIIIPF GIGIAGMVAQ TKEMINIKEA YQDVRFNCEI DQKTGYKTNA ILCMPICNYE GDIIGVAQII NKTNGCMEFD EHDVEIFRRY LTFCGIGIQN AQLFEMSVQE YRRNQILLNL ARSIFEEQNN LECLVTKIMT EARELLKCER CSVFLVDLDC CEESHLEKII EKPHQQEQRT MRAIKGGDSF EEQQKMRNRF TVLFELGGEY QAANVSRPSI NELSHSTLAQ IAQFVSTTGQ TVNICDVHEW VRDHNQIRDS EIDSTHAILC MPIVNAQKTV IGVAQLINKA NGLPFSESDV SIFEAFAIFC GLGIHNTQMY ENACKLMAKQ KVALECLSYH ATASQDQTEK LTQDPIAEAE SYNLYSFTFT DFDLVDDDTC RAVLRMFMQC NLVSQFHIPY DVLCRWVLSV RKNYRPVKYH NWRHALNVAQ TMFAMLKTGK MERFMTDLEI LGLLVACLCH DLDHRGTNNA FQTKTESPLA ILYTTSTMEH HHFDQCVMIL NSEGNNIFQA LSPEDYRCVM KTVESAILST DLAMYFKKRN AFLELVENGE FDWQGEEKKD LLCGMMMTAC DVSAIAKPWE VQHRVAKLVA DEFFDQGDLE KLQLNTQPVA MMDRERKDEL PKMQVGFIDV ICLPLYRVLC DTFPWITPLY EGTLENRRNW QDLAEKVEMG LTWIDHDTID KPVEEFAGCA DEEIKDIEFT VTTLNCNQQS QSQSQSQSQS QHGGDDIHTP EHQRSSGSRL SIKKTGALGK VVRSKLSKTL YNSMDGSKPK TSLKLLESHV SEDMDDKSPT SPSQPHSGSV GRMSASSSTS SAGTVDKTKK RSKLCALL //