ID   PDE6_DROVI              Reviewed;         893 AA.
AC   B4LVU6;
DT   10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   24-JAN-2024, entry version 79.
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=GJ23019;
OS   Drosophila virilis (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila.
OX   NCBI_TaxID=7244;
RN   [1] {ECO:0000312|EMBL:EDW67551.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tucson 15010-1051.87 {ECO:0000312|EMBL:EDW67551.1};
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}.
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DR   EMBL; CH940650; EDW67551.1; -; Genomic_DNA.
DR   RefSeq; XP_002054031.2; XM_002053995.2.
DR   AlphaFoldDB; B4LVU6; -.
DR   SMR; B4LVU6; -.
DR   STRING; 7244.B4LVU6; -.
DR   EnsemblMetazoa; FBtr0238944; FBpp0237436; FBgn0210121.
DR   eggNOG; KOG3689; Eukaryota.
DR   HOGENOM; CLU_006980_0_2_1; -.
DR   InParanoid; B4LVU6; -.
DR   OMA; ATIRMFK; -.
DR   PhylomeDB; B4LVU6; -.
DR   ChiTaRS; Pde6; fly.
DR   Proteomes; UP000008792; 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..890
FT                   /note="cGMP-specific 3',5'-cyclic phosphodiesterase"
FT                   /id="PRO_0000363700"
FT   PROPEP          891..893
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000250|UniProtKB:Q9VFI9"
FT                   /id="PRO_0000363701"
FT   DOMAIN          21..173
FT                   /note="GAF 1"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          205..390
FT                   /note="GAF 2"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          420..743
FT                   /note="PDEase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01192"
FT   REGION          784..807
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          844..893
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        852..880
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        496
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         500
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         536
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         537
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         537
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         647
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         890
FT                   /note="Cysteine methyl ester"
FT                   /evidence="ECO:0000250|UniProtKB:Q9VFI9"
FT   LIPID           890
FT                   /note="S-farnesyl cysteine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9VFI9"
SQ   SEQUENCE   893 AA;  100943 MW;  2CD8AD4CCE687DDE CRC64;
     MELDEGELFM ELIRDVANEL DIDVLCHKIL VNVGLLTHAD RGSLFLAKGT PNNKYLVAKL
     FDVTQKTALK DAVTRARAEE IIIPFGIGIA GMVAQTKEMI NIKEAYMDAR FNCEIDLKTG
     YKTNAILCMP ICNYEGDIIG VAQIINKTNG CMEFDEHDVE IFRRYLTFCG IGIQNAQLFE
     MSVQEYRRNQ ILLNLARSIF EEQNNLECLV TKIMTEAREL LKCERCSVFL VDLDCCEESH
     LEKIIEKPHQ LEQRATRAIK GGDSFEEKQK MRNRFTVLFE LGGESQAANV SRPSINDLSH
     STLAQIAQFV ATTGQTVNIC DVHDWVREHN QIRAEGEIDS THAILCMPIV NAQKTVIGVA
     QLINKASGLP FTESDASIFE AFAIFCGLGI HNTQMYENAC KLMAKQKVAL ECLSYHATAG
     QDQTEKLIQD PIAEAETYNL YSFTFTDFDL VDDDTCRAVL RMFMQCNLVS QFHIPYDVLC
     RWVLSVRKNY RPVKYHNWRH ALNVAQTMFA MLKTGKMERF MTDLEILGLL VACLCHDLDH
     RGTNNAFQTK TESPLAILYT TSTMEHHHFD QCVMILNSEG NNIFQALSPE DYRSVMKTVE
     SAILSTDLAM YFKKRNAFLE LVENGEFDWQ GEEKKDLLCG MMMTACDVSA IAKPWEVQHR
     VAKLVADEFF DQGDLEKLQL NTQPVAMMDR ERKDELPKMQ VGFIDVICLP LYRVLCDTFP
     WITPLYEGTL ENRRNWQDLA EKVEMGLTWI DHDTIDKPVE EFAGCADEEI KDIEFTVTTL
     NCNQQSQHGG DDSHTPEHQR SGSRLSIKKT GALGKVVRSK LSKTLYNSMD GSKPKTSLKL
     LESHVSEDMD DKSPTSPSQP HLGSVGRMSA SSSTSSAGTV DKSKKRSKLC ALL
//