ID PDE6_DROMO Reviewed; 1116 AA. AC B4K9L4; DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot. DT 23-SEP-2008, sequence version 1. DT 24-JAN-2024, entry version 74. 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=GI10668; OS Drosophila mojavensis (Fruit fly). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea; OC Drosophilidae; Drosophila. OX NCBI_TaxID=7230; RN [1] {ECO:0000312|EMBL:EDW16674.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Tucson 15081-1352.22 {ECO:0000312|EMBL:EDW16674.1}; 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; CH933806; EDW16674.1; -; Genomic_DNA. DR RefSeq; XP_002001213.2; XM_002001177.2. DR AlphaFoldDB; B4K9L4; -. DR SMR; B4K9L4; -. DR EnsemblMetazoa; FBtr0429027; FBpp0386515; FBgn0133432. DR KEGG; dmo:Dmoj_GI10668; -. DR eggNOG; KOG3689; Eukaryota. DR HOGENOM; CLU_006980_0_2_1; -. DR InParanoid; B4K9L4; -. DR OMA; ATIRMFK; -. DR OrthoDB; 5479253at2759; -. DR PhylomeDB; B4K9L4; -. DR ChiTaRS; Pde6; fly. DR Proteomes; UP000009192; 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..1113 FT /note="cGMP-specific 3',5'-cyclic phosphodiesterase" FT /id="PRO_0000363690" FT PROPEP 1114..1116 FT /note="Removed in mature form" FT /evidence="ECO:0000250|UniProtKB:Q9VFI9" FT /id="PRO_0000363691" FT DOMAIN 241..393 FT /note="GAF 1" FT /evidence="ECO:0000255" FT DOMAIN 425..611 FT /note="GAF 2" FT /evidence="ECO:0000255" FT DOMAIN 641..964 FT /note="PDEase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01192" FT REGION 1..36 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 82..136 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1005..1031 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1067..1116 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1..34 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1075..1103 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 717 FT /note="Proton donor" FT /evidence="ECO:0000250" FT BINDING 721 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /ligand_label="1" FT /evidence="ECO:0000250" FT BINDING 757 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /ligand_label="1" FT /evidence="ECO:0000250" FT BINDING 758 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /ligand_label="1" FT /evidence="ECO:0000250" FT BINDING 758 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 868 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /ligand_label="1" FT /evidence="ECO:0000250" FT MOD_RES 1113 FT /note="Cysteine methyl ester" FT /evidence="ECO:0000250|UniProtKB:Q9VFI9" FT LIPID 1113 FT /note="S-farnesyl cysteine" FT /evidence="ECO:0000250|UniProtKB:Q9VFI9" SQ SEQUENCE 1116 AA; 124330 MW; 53186D5E1651993E CRC64; MTDVSATTGR AGDRVSSTSS EVAVETTSQA LTNGAAKEPL AAVTAEATAT ATVTATTTAT VTATTTAATA TMATAVISKQ AKSECHSQSN NNQHVETAPS KQSSDSEASA PTTVSIPSAN AKINSSSSGK TTATQQDVDE VARLFEEKPE AFEKWLTERA PPEALSRLHE FIESRKPHKR PSVTSDLFQQ WMASPTVQQK SPRKLSNSSV HALPESRRHL MELDEGELFM ELIRDVANEL DIDVLCHKIL VNVGLLTHAD RGSLFLAKGT PNNRYLVAKL FDVTQTTALK DAVTRARAEE IIIPFGIGIA GMVAQTKQMI NIKEAYKDAR FNCEIDLKTG YTTNAILCMP ICNYEGDIIG VAQIINKTNG CMEFDEHDVE IFRRYLTFCG IGIQNAQLFE MSVQEYRRNQ ILLNLARSIF EEQNNLECLV TKIMTEAREL LKCERCSVFL VDLDCCEESH LEKIIEKPHQ LQQQRTPRAI MSGDSFEEKQ NMRNRFTVLF ELGGENHAAN VSRPSINDLS HSTLAQIAQF VATTGQTVNI CDVQDWVREH NQIRAESEID STQAILCMPI VNAQKTVIGV AQLINKASGL PFTESDASIF EAFAIFCGLG IHNTQMYENA CKLMAKQKVA LECLSYHATA SQDQTEKLAQ DVIAEAEAYN LYSFTFTDFD LVDDDTCRAV LRMFMQCNLV SQFHIPYDVL CRWVLSVRKN YRPVKYHNWR HALNVAQTMF AMLKTGKMER FMTDLEILGL LVACLCHDLD HRGTNNAFQT KTESPLAILY TTSTMEHHHF DQCVMILNSE GNNIFQALSP EDYRSVMKTV ESAILSTDLA MYFKKRNAFL ELVENGEFDW QGEEKKDLLC GMMMTACDVS AIAKPWEVQH RVAKLVADEF FDQGDLEKLQ LNTQPVAMMD RERKDELPKM QVGFIDVICL PLYRVLCDTF PWITPLYEGT LENRRNWQDL AEKVEMGLTW IDHDTIDKPV EEFAGCADEE IKDIEFTVTT LNCNQHGGSA GGGEDTHTPE HQRSSSRLSI KKTGALGKVV RSKLSKTLYN SMDGSKPKTS LKLLESHVSE DMDDKSPTSP SQPHSGSVGR MSASSSTSSA GTVDKSKKRS KLCALL //