PDE6_DROPS
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 03-AUG-2022, entry version 86.
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; 7237.FBpp0300350; -.
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; 1.10.1300.10; -; 1.
DR Gene3D; 3.30.450.40; -; 2.
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 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 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
