ID   PDE6_DROYA              Reviewed;        1149 AA.
AC   B4PSS5;
DT   10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   02-SEP-2026, 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=GE26445;
OS   Drosophila yakuba (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Altocrustacea; Allotriocarida;
OC   Hexapoda; Insecta; Pterygota; Neoptera; Eumetabola; Endopterygota;
OC   Aparaglossata; Panorpida; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7245;
RN   [1] {ECO:0000312|EMBL:EDW97571.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tai18E2 / Tucson 14021-0261.01 {ECO:0000312|EMBL:EDW97571.1};
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; CM000160; EDW97571.1; -; Genomic_DNA.
DR   AlphaFoldDB; B4PSS5; -.
DR   SMR; B4PSS5; -.
DR   EnsemblMetazoa; XM_002097823.4; XP_002097859.1; LOC6537301.
DR   GeneID; 6537301; -.
DR   KEGG; dya:Dyak_GE26445; -.
DR   eggNOG; KOG3689; Eukaryota.
DR   HOGENOM; CLU_006980_0_2_1; -.
DR   OMA; FHIPYEV; -.
DR   OrthoDB; 74705at2759; -.
DR   PhylomeDB; B4PSS5; -.
DR   Proteomes; UP000002282; Chromosome 3R.
DR   GO; GO:0016020; C:membrane; ISS:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR   GO; GO:0047555; F:3',5'-cyclic-GMP phosphodiesterase activity; ISS:UniProtKB.
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   FunFam; 1.10.1300.10:FF:000003; Phosphodiesterase; 1.
DR   FunFam; 3.30.450.40:FF:000031; Phosphodiesterase; 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   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; PS50813; GAF; 2.
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..1146
FT                   /note="cGMP-specific 3',5'-cyclic phosphodiesterase"
FT                   /id="PRO_0000363704"
FT   PROPEP          1147..1149
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000250|UniProtKB:Q9VFI9"
FT                   /id="PRO_0000363705"
FT   DOMAIN          262..431
FT                   /note="GAF 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01434"
FT   DOMAIN          445..644
FT                   /note="GAF 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01434"
FT   DOMAIN          673..996
FT                   /note="PDEase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01192"
FT   REGION          1..175
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1037..1066
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1096..1149
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..19
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        31..47
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        48..59
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        60..85
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        96..108
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        132..158
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1042..1053
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1096..1106
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1115..1135
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1139..1149
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        749
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         753
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         789
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         790
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         790
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         900
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         1146
FT                   /note="Cysteine methyl ester"
FT                   /evidence="ECO:0000250|UniProtKB:Q9VFI9"
FT   LIPID           1146
FT                   /note="S-farnesyl cysteine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9VFI9"
SQ   SEQUENCE   1149 AA;  127347 MW;  96E9219B5B84983C CRC64;
     MHGTVSRSSS SSNMTDVSSP AGGAASPVEI ATSSSTAATT SASASSSKPL TNGANKTAIS
     TAAGVTPGAA PGPGCAAIPA SGSSGNQVKL EHHYRQSNNN RPAGSNRSSE TKLRSPAGES
     DGASRLMTPA GSSSSPSQSP SQSQSQSQAS IQTQTSQQDR LVKAPSTTAS QQDVDEVARL
     FEEKPEAFEK WLTERAPPEA LSRLQEFIEN RKPHKRPSVT SDLFQQWMAA SPTVQQKSPR
     SLSNSSASSL PECRRHLMDL DEGELFMELI RDVANELDID VLCHKILVNV GLLTHADRGS
     LFLAKGTPTN KYLVAKLFDV TQKTALKDAV TRASAEEIII PFGIGIAGMV AQTKQMINIK
     EAYKDARFNC EIDLKTGYKT NAILCMPICN YEGDIIGVAQ IINKTNGCME FDEHDVEIFR
     RYLTFCGIGI QNAQLFEMSV QEYRRNQILL NLARSIFEEQ NNLECLVTKI MTEARELLKC
     ERCSVFLVDL DCCEASHLEK IIEKPNQPAT RAIKSADSFE EKKMRNRFTV LFELGGEYQA
     ANVSRPSVSE LSSSTLAQIA QFVATTGQTV NICDVIEWVR DHNQIRAEDE IDSTQAILCM
     PIMNAQKKVI GVAQLINKAN GVPFTESDAS IFEAFAIFCG LGIHNTQMYE NACKLMAKQK
     VALECLSYHA TASQDQTEKL TQDAIAEAES YNLYSFTFTD FELVDDDTCR AVLRMFMQCN
     LVSQFQIPYD VLCRWVLSVR KNYRPVKYHN WRHALNVAQT MFAMLKTGKM ERFMTDLEIL
     GLLVACLCHD LDHRGTNNAF QTKTESPLAI LYTTSTMEHH HFDQCVMILN SEGNNIFQAL
     SPEDYRSVMK TVESAILSTD LAMYFKKRNA FLELVENGEF DWQGEEKKDL LCGMMMTACD
     VSAIAKPWEV QHKVAKLVAD EFFDQGDLEK LQLNTQPVAM MDRERKDELP KMQVGFIDVI
     CLPLYRVLCD TFPWITPLYE GTLENRRNWQ DLAEKVEMGL TWIDHDTIDK PVEEFAACAD
     EEIKDIEFTV TTLNCNQQSQ HGSEDSHTPE HQRSGSRLSM KKTGALGKAV RSKLSKTLYN
     SMDGSKPKTS LKLLESHVSE DMDDKSPTSP SQPQASGSMG RMSASSSTSS AGGQMVDKSK
     KRSKLCALL
//