ID   PDE6_DROPS              Reviewed;        1110 AA.
AC   Q298P4;
DT   10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2012, sequence version 3.
DT   24-JAN-2024, entry version 88.
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=GA20950;
OS   Drosophila pseudoobscura pseudoobscura (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=46245;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MV2-25 / Tucson 14011-0121.94;
RX   PubMed=15632085; DOI=10.1101/gr.3059305;
RA   Richards S., Liu Y., Bettencourt B.R., Hradecky P., Letovsky S.,
RA   Nielsen R., Thornton K., Hubisz M.J., Chen R., Meisel R.P., Couronne O.,
RA   Hua S., Smith M.A., Zhang P., Liu J., Bussemaker H.J., van Batenburg M.F.,
RA   Howells S.L., Scherer S.E., Sodergren E., Matthews B.B., Crosby M.A.,
RA   Schroeder A.J., Ortiz-Barrientos D., Rives C.M., Metzker M.L., Muzny D.M.,
RA   Scott G., Steffen D., Wheeler D.A., Worley K.C., Havlak P., Durbin K.J.,
RA   Egan A., Gill R., Hume J., Morgan M.B., Miner G., Hamilton C., Huang Y.,
RA   Waldron L., Verduzco D., Clerc-Blankenburg K.P., Dubchak I., Noor M.A.F.,
RA   Anderson W., White K.P., Clark A.G., Schaeffer S.W., Gelbart W.M.,
RA   Weinstock G.M., Gibbs R.A.;
RT   "Comparative genome sequencing of Drosophila pseudoobscura: chromosomal,
RT   gene, and cis-element evolution.";
RL   Genome Res. 15:1-18(2005).
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; CM000070; EAL27911.3; -; Genomic_DNA.
DR   AlphaFoldDB; Q298P4; -.
DR   SMR; Q298P4; -.
DR   STRING; 46245.Q298P4; -.
DR   eggNOG; KOG3689; Eukaryota.
DR   HOGENOM; CLU_006980_0_2_1; -.
DR   InParanoid; Q298P4; -.
DR   OMA; ATIRMFK; -.
DR   ChiTaRS; Pde6; fly.
DR   Proteomes; UP000001819; Genome assembly.
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..1107
FT                   /note="cGMP-specific 3',5'-cyclic phosphodiesterase"
FT                   /id="PRO_0000363694"
FT   PROPEP          1108..1110
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000363695"
FT   DOMAIN          233..385
FT                   /note="GAF 1"
FT   DOMAIN          417..601
FT                   /note="GAF 2"
FT   DOMAIN          631..954
FT                   /note="PDEase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01192"
FT   REGION          1..55
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          67..128
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          184..203
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          997..1028
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1040..1110
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        15..52
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        87..101
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        104..128
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1067..1097
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        707
FT                   /note="Proton donor"
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         747
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         748
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         748
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         858
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         1107
FT                   /note="Cysteine methyl ester"
FT                   /evidence="ECO:0000250"
FT   LIPID           1107
FT                   /note="S-farnesyl cysteine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   1110 AA;  123338 MW;  4FB8DECD51B085A6 CRC64;
     MTDVSAAAGG ATAPAETAAT SSSASKPLTN GANKTSTAMA APTATPTTAA TASGAAEAGA
     ITSVAGISNQ VKLEHHHHRQ SNNNRPVAPY PPVPAAKPKP TPTPESKFKS TSREPGMSSS
     SSSAQQDVDE VARLFEEKPE AFEKWLTERA PPEALSRLQE FIESRKPLKR PSVTSDLFQQ
     WMSASPTVQQ KSPRSLSNSS ASSTLPECRR HLMDLDEGEL FMELIRDVAN ELDIDVLCHK
     ILVNVGLLTH ADRGSLFLAK GTPHNKYLVA KLFDVTQKTA LKDAVTRASA EEIIIPFGIG
     IAGMVAQTKQ MINIKEAYKD ARFNCEIDLK TGYKTNAILC MPICNYEGDI IGVAQIINKT
     NGCMEFDEHD VEIFRRYLTF CGIGIQNAQL FEMSVQEYRR NQILLNLARS IFEEQNNLEC
     LVTKIMTEAR ELLNCERCSV FLVDLDCCEA SHLEKIIEKP NQPEQRPTRA IMPGDSFDEK
     KMRNRFTVLF ELGGEYQAAS VSRPSKTELS TSTLAQIAQF VATTGQTVNI CDVHEWVRDH
     NQIRAESEID STQAILCMPI VNAQKVVIGV AQLINKANGV PFTESDASIF EAFAIFCGLG
     IHNTQMYENA CKLMAKQKVA LECLSYHATA SQDQTEKLTQ DAIAEAESYN LYSFTFTDFE
     LVDDDTCRAV LRMFLQCNLV SQFQIPYDVL CRWVLSVRKN YRPVKYHNWR HALNVAQTMF
     AMLKTGKMER FMTDLEILGL LVACLCHDLD HRGTNNAFQT KTESPLAILY TTSTMEHHHF
     DQCVMILNSE GNNIFQALSP EDYRSVMKTV ESAILSTDLA MYFKKRNAFL ELVENGEFDW
     QGEEKKDLLC GMMMTACDVS AIAKPWEVQH KVAKLVADEF FDQGDLEKLQ LNTQPVAMMD
     RERKDELPKM QVGFIDVICL PLYRVLCDTF PWITPLYEGT LENRRNWQDL AEKVEMGLTW
     IDHDTIDKPV EEFAGCADEE IKDIEFTVTT LNCNQQAQHG AGAGGDDSHT PEHQRSGSRL
     SMKKTGALGK AVRSKLSKTL YNSMDGSKPK TSLKLLESHV SEDMDDKSPT SPSQPHAGGS
     VGRMSASSST SSAGTVVDKS KKRSKLCSLL
//