PDE6_DROPE
ID PDE6_DROPE Reviewed; 1276 AA.
AC B4G4E5;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 71.
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=GL24177;
OS Drosophila persimilis (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7234;
RN [1] {ECO:0000312|EMBL:EDW24493.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MSH-3 / Tucson 14011-0111.49;
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; CH479179; EDW24493.1; -; Genomic_DNA.
DR RefSeq; XP_002013507.1; XM_002013471.1.
DR AlphaFoldDB; B4G4E5; -.
DR SMR; B4G4E5; -.
DR STRING; 7234.FBpp0188284; -.
DR EnsemblMetazoa; FBtr0189792; FBpp0188284; FBgn0161767.
DR eggNOG; KOG3689; Eukaryota.
DR HOGENOM; CLU_006980_0_2_1; -.
DR OMA; ATIRMFK; -.
DR PhylomeDB; B4G4E5; -.
DR ChiTaRS; Pde6; fly.
DR Proteomes; UP000008744; 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; 1.10.1300.10; -; 2.
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; 2.
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..1273
FT /note="cGMP-specific 3',5'-cyclic phosphodiesterase"
FT /id="PRO_0000363692"
FT PROPEP 1274..1276
FT /note="Removed in mature form"
FT /evidence="ECO:0000250|UniProtKB:Q9VFI9"
FT /id="PRO_0000363693"
FT DOMAIN 290..442
FT /note="GAF 1"
FT /evidence="ECO:0000255"
FT DOMAIN 474..658
FT /note="GAF 2"
FT /evidence="ECO:0000255"
FT DOMAIN 688..1119
FT /note="PDEase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01192"
FT REGION 1..76
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 91..185
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 241..260
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1162..1193
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1205..1276
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 7..28
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 37..73
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 108..122
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 146..185
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1232..1263
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 764
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 768
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 804
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 805
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 805
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 1023
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT MOD_RES 1273
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000250|UniProtKB:Q9VFI9"
FT LIPID 1273
FT /note="S-farnesyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:Q9VFI9"
SQ SEQUENCE 1276 AA; 141612 MW; F1DCC81A89C5B141 CRC64;
MHELGTRQRP LSSSSSSSSS SNMTDVSAAA GGATAPAETA ATSSSASKPL TNGANKTSTA
MAAPTTTPTT AATAAGAAEA GAIASVAGIS NQVKLEHHHR QSNNNRPVAP YPPVPAAKPK
PTPTPTAESK FKSTSREVDV ALRPTPARSS TISPGVSIHT QTIQQESSSA KPGMSSSSSS
AQQDVDEVAR LFEEKPEAFE KWLTERAPPE ALSRLQEFIE SRKPLKRPSV TSDLFQQWMS
ASPTVQQKSP RSLSNSSASS TLPECRRHLM DLDEGELFME LIRDVANELD IDVLCHKILV
NVGLLTHADR GSLFLAKGTP HNKYLVAKLF DVTQKTALKD AVTRASAEEI IIPFGIGIAG
MVAQTKQMIN IKEAYKDARF NCEIDLKTGY KTNAILCMPI CNYEGDIIGV AQIINKTNGC
MEFDEHDVEI FRRYLTFCGI GIQNAQLFEM SVQEYRRNQI LLNLARSIFE EQNNLECLVT
KIMTEARELL NCERCSVFLV DLDCCEASHL EKIIEKPNQP EQRPTRAIMP GDSFDEKKMR
NRFTVLFELG GEYQAASVSR PSKTELSTST LAQIAQFVAT TGQTVNICDV HEWVRDHNQI
RAESEIDSTQ AILCMPIVNA QKIVIGVAQL INKANGVPFT ESDASIFEAF AIFCGLGIHN
TQMYENACKL MAKQKVALEC LSYHATASQD QTEKLTQDAI AEAESYNLYS FTFTDFELVD
DDTCRAVLRM FLQCNLVSQF QIPYDVLCRW VLSVRKNYRP VKYHNWRHAL NVAQTMFAML
KTGKMERFMT DLEILGLLVA CLCHDLDHRG TNNAFQTKTE SPLAILYTTS TMEHHHFDQC
VMILNSEGNN IFQPRTTRTF LLLARRFLRF DLLPFRAFTR ALRPLVRPLL ELDVLELPDP
SRIFLLTVYL RLVTRTIFLP PPEDEEEEDE VEDSVVLVVA SVVVVVAVAA SVVLKAELDV
EALSPEDYRS VMKTVESAIL STDLAMYFKK RNAFLELVEN GEFDWQGEEK KDLLCGMMMT
ACDVSAIAKP WEVQHKVAKL VADEFFDQGD LEKLQLNTQP VAMMDRERKD ELPKMQVGFI
DVICLPLYRV LCDTFPWITP LYEGTLENRR NWQDLAEKVE MGLTWIDHDT IDKPVEEFAG
CADEEIKDIE FTVTTLNCNQ QAQHGAGAGG DDSHTPEHQR SGSRLSMKKT GALGKAVRSK
LSKTLYNSMD GSKPKTSLKL LESHVSEDMD DKSPTSPSQP PHAGGSVGRM SASSSTSSAG
TVVDKSKKRS KLCSLL
