PDE6_DROSI
ID PDE6_DROSI Reviewed; 1143 AA.
AC B4QZU1;
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=GD20415;
OS Drosophila simulans (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7240;
RN [1] {ECO:0000312|EMBL:EDX12939.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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; CM000364; EDX12939.1; -; Genomic_DNA.
DR RefSeq; XP_016034708.1; XM_016176727.1.
DR AlphaFoldDB; B4QZU1; -.
DR SMR; B4QZU1; -.
DR STRING; 7240.B4QZU1; -.
DR EnsemblMetazoa; FBtr0220325; FBpp0218817; FBgn0191887.
DR GeneID; 6728084; -.
DR HOGENOM; CLU_006980_0_2_1; -.
DR OMA; ATIRMFK; -.
DR PhylomeDB; B4QZU1; -.
DR ChiTaRS; Pde6; fly.
DR Proteomes; UP000000304; Chromosome 3r.
DR Bgee; FBgn0191887; Expressed in adult organism and 2 other tissues.
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..1140
FT /note="cGMP-specific 3',5'-cyclic phosphodiesterase"
FT /id="PRO_0000363698"
FT PROPEP 1141..1143
FT /note="Removed in mature form"
FT /evidence="ECO:0000250|UniProtKB:Q9VFI9"
FT /id="PRO_0000363699"
FT DOMAIN 272..424
FT /note="GAF 1"
FT /evidence="ECO:0000255"
FT DOMAIN 456..637
FT /note="GAF 2"
FT /evidence="ECO:0000255"
FT DOMAIN 667..990
FT /note="PDEase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01192"
FT REGION 1..167
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1031..1060
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1090..1143
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..60
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 98..114
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 125..167
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1099..1130
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 743
FT /note="Proton donor"
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 783
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 784
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 784
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 894
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT MOD_RES 1140
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000250|UniProtKB:Q9VFI9"
FT LIPID 1140
FT /note="S-farnesyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:Q9VFI9"
SQ SEQUENCE 1143 AA; 126868 MW; 33060D06C24BA337 CRC64;
MHGPVSRSSS SSNMTDVSSP AGGAASPVEM TTSSSSAATT SASSSKPLTN GANKTTISTV
AGGVAPGAVP GPGSGAIPAS SSSGNQVKLE HHHRQSNNNR PAATNRSSET KLRSPAGESD
GASRLMTPAG SSSSPSQSPS QTQASIQTQT SQQDRLAKAS TTASQQDVDE VARLFEEKPE
AFEKWLTERA PPEALSRLQE FIENRKPHKR PSVTSDLFQQ WMAASPTVQQ KSPRSLSNSS
ASSLPECRRH LMDLDEGELF MELIRDVANE LDIDVLCHKI LVNVGLLTHA DRGSLFLAKG
TPTNKYLVAK LFDVTQKTAL KDAVTRASAE EIIIPFGIGI AGMVAQTKQM INIKEAYKDA
RFNCEIDLKT GYKTNAILCM PICNYEGDII GVAQIINKTN GCMEFDEHDV EIFRRYLTFC
GIGIQNAQLF EMSVQEYRRN QILLNLARSI FEEQNNLECL VTKIMTEARE LLKCERCSVF
LVDLDCCEAS HLEKIIEKPN QQATRAIKSA DSFEEKKMRN RFTVLFELGG EYQAANVSRP
SVSELSSSTL AQIAQFVATT GQTVNICDVI EWVRDHNQIR AEDEIDSTQA ILCMPIMNAQ
KKVIGVAQLI NKANGVPFTD SDASIFEAFA IFCGLGIHNT QMYENACKLM AKQKVALECL
SYHATASQDQ TEKLTQDVIA EAESYNLYSF TFTDFELVDD DTCRAVLRMF MQCNLVSQFQ
IPYDVLCRWV LSVRKNYRPV KYHNWRHALN VAQTMFAMLK TGKMERFMTD LEILGLLVAC
LCHDLDHRGT NNAFQTKTES PLAILYTTST MEHHHFDQCV MILNSEGNNI FQALSPEDYR
SVMKTVESAI LSTDLAMYFK KRNAFLELVE NGEFDWQGEE KKDLLCGMMM TACDVSAIAK
PWEVQHKVAK LVADEFFDQG DLEKLQLNTQ PVAMMDRERK DELPKMQVGF IDVICLPLYR
VLCDTFPWIT PLYEGTLENR RNWQDLAEKV EMGLTWIDHD TIDKPVEEFA ACADEEIKDI
EFTVTTLNCN QQSQHGSEDS HTPEHQRSGS RLSMKKTGAL GKAVRSKLSK TLYNSMDGSK
PKTSLKLLES HVSEDMDDKS PTSPSQPQAS GSMGRMSASS STSSTGGQMV DKSKKRSKLC
ALL
