ID   PDE6_DROAN              Reviewed;        1158 AA.
AC   B3LVW5;
DT   10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT   02-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=GF17478;
OS   Drosophila ananassae (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7217;
RN   [1] {ECO:0000312|EMBL:EDV41498.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tucson 14024-0371.13 {ECO:0000312|EMBL:EDV41498.1};
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; CH902617; EDV41498.1; -; Genomic_DNA.
DR   RefSeq; XP_001952915.2; XM_001952880.2.
DR   AlphaFoldDB; B3LVW5; -.
DR   SMR; B3LVW5; -.
DR   STRING; 7217.B3LVW5; -.
DR   GeneID; 6500262; -.
DR   KEGG; dan:6500262; -.
DR   eggNOG; KOG3689; Eukaryota.
DR   HOGENOM; CLU_006980_0_2_1; -.
DR   InParanoid; B3LVW5; -.
DR   OMA; ATIRMFK; -.
DR   OrthoDB; 5479253at2759; -.
DR   PhylomeDB; B3LVW5; -.
DR   ChiTaRS; Pde6; fly.
DR   Proteomes; UP000007801; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0016020; C:membrane; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; 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..1155
FT                   /note="cGMP-specific 3',5'-cyclic phosphodiesterase"
FT                   /id="PRO_0000363684"
FT   PROPEP          1156..1158
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000250|UniProtKB:Q9VFI9"
FT                   /id="PRO_0000363685"
FT   DOMAIN          242..394
FT                   /note="GAF 1"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          426..640
FT                   /note="GAF 2"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          670..993
FT                   /note="PDEase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01192"
FT   REGION          1..137
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          195..216
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1034..1065
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1097..1158
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..48
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        68..91
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        103..137
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1104..1142
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        746
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         750
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         786
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         787
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         787
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         897
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         1155
FT                   /note="Cysteine methyl ester"
FT                   /evidence="ECO:0000250|UniProtKB:Q9VFI9"
FT   LIPID           1155
FT                   /note="S-farnesyl cysteine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9VFI9"
SQ   SEQUENCE   1158 AA;  127966 MW;  977DCAE9614F1792 CRC64;
     MTDVSAPTGG ATSPVDITAS PGSTALPPVA TTSAAASASS SQAKPLTNGA KKAATAAAAA
     GAEEGGASAS NQVKQEQRRQ SNNNRPAASG TPEAKQATPA GNPDPGAGST SKSSSIHTQT
     SQQERAGRPT SSASQHDVDE VARLFEEKPE AFEKWLTERA PPEALGRLQE FIESRKPLKR
     PSVTSDLFQQ WMAASPTVQQ KSPRSLSNSS ASSIPESRRH LMDLDEGELF MELIRDVANE
     LDIDVLCHKI LVNVGLLTHA DRGSLFLAKG APNNKYLVAK LFDVTQKTAL KDAVTRASTE
     EIIIPFGIGI AGMVAQTKQM INIKEAYKDA RFNCEIDLKT GYKTNAILCM PICNYEGDII
     GVAQIINKTN GCMEFDEHDV EIFRRYLTFC GIGIQNAQLF EMSVQEYRRN QILLNLARSI
     FEEQNNLECL VTKIMTEARE LLKCERCSVF LVDLDCCEAG CGRVGGAMRR FGVRSKQVSA
     IVEHVGGRRG NTSHLEKIIE KPNQPATRAI KSADSFEEKK MRNRFTVLFE LGGEYQAANV
     SRPSTSELST STLAQIAQFV ATTGQTVNIC DVHEWVREHN QIRAESEIDS TQAILCMPIV
     NAKKTVIGVA QLINKANGVP FTESDASIFE AFAIFCGLGI HNTQMYENAC KLMAKQKVAL
     ECLSYHATAS QDQTEKLTQD AIADADTYNL YSFTFTDFEL VDDDTCRAVL RMFMQCNLVS
     QFQIPYDVLC RWVLSVRKNY RPVKYHNWRH ALNVAQTMFA MLKTGKMERF MTDLEILGLL
     VACLCHDLDH RGTNNAFQTK TESPLAILYT TSTMEHHHFD QCVMILNSEG NNIFQALSPE
     DYRSVMKTVE SAILSTDLAM YFKKRNAFLE LVENGEFDWQ GEEKKDLLCG MMMTACDVSA
     IAKPWEVQHK VAKLVADEFF DQGDLEKLQL NTQPVAMMDR ERKDELPKMQ VGFIDVICLP
     LYRVLCDTFP WITPLYEGTL ENRRNWQDLA EKVEMGLTWI DHDTIDKPVE EFAACADEEI
     KDIEFTVTTL NCNQSQQSQH GSEDSHTPEH QRSGSRLSMK KTGALGKAVR SKLSKTLYNS
     MDGSKPKTSL KLLESHVSED MDDKSPTSPS QPQAAGSMGR MSASSSTSSA GGQGQCQVAA
     PGQAQDKSKK RSKLCALL
//