PDE6_DROWI
ID PDE6_DROWI Reviewed; 1127 AA.
AC B4NAL6;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 78.
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=GK11355;
OS Drosophila willistoni (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7260;
RN [1] {ECO:0000312|EMBL:EDW80830.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tucson 14030-0811.24 {ECO:0000312|EMBL:EDW80830.1};
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}.
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DR EMBL; CH964232; EDW80830.1; -; Genomic_DNA.
DR RefSeq; XP_002069844.2; XM_002069808.2.
DR AlphaFoldDB; B4NAL6; -.
DR SMR; B4NAL6; -.
DR STRING; 7260.FBpp0240498; -.
DR EnsemblMetazoa; FBtr0242006; FBpp0240498; FBgn0213366.
DR GeneID; 6647390; -.
DR KEGG; dwi:6647390; -.
DR eggNOG; KOG3689; Eukaryota.
DR HOGENOM; CLU_006980_0_2_1; -.
DR InParanoid; B4NAL6; -.
DR OMA; ATIRMFK; -.
DR OrthoDB; 904682at2759; -.
DR PhylomeDB; B4NAL6; -.
DR ChiTaRS; Pde6; fly.
DR Proteomes; UP000007798; 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; -; 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..1124
FT /note="cGMP-specific 3',5'-cyclic phosphodiesterase"
FT /id="PRO_0000363702"
FT PROPEP 1125..1127
FT /note="Removed in mature form"
FT /evidence="ECO:0000250|UniProtKB:Q9VFI9"
FT /id="PRO_0000363703"
FT DOMAIN 255..407
FT /note="GAF 1"
FT /evidence="ECO:0000255"
FT DOMAIN 439..624
FT /note="GAF 2"
FT /evidence="ECO:0000255"
FT DOMAIN 654..977
FT /note="PDEase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01192"
FT REGION 1..147
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 206..225
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1018..1045
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1078..1127
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 16..100
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 110..147
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1085..1114
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 730
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 734
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 770
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 771
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 771
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 881
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT MOD_RES 1124
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000250|UniProtKB:Q9VFI9"
FT LIPID 1124
FT /note="S-farnesyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:Q9VFI9"
SQ SEQUENCE 1127 AA; 125223 MW; 32473E517D9B55C5 CRC64;
MTDVSAAAGG ATAEPPTATM SPTSVEPLTN GAKKSAMATT TETQTAAAAA AATTTPAATT
TVTVTAAATT EASTSNQVKL ARVENVLGST STSSPANETK PKSLPDGGNA SVAPASSSSN
SISTQTLIQS QSQPHAKTNK STTVASQQDV DEVARLFEEK PEAFEKWLTE RAPPEALSRL
HEFIESRKPP KRPSVTSDLF QQWMASSPTV QQKSPGRSLS NSSASSLPEC RRHLMDLDEG
ELFMELIRDV ANELDIDVLC HKILVNVGLL THADRGSLFL AKGTANNKYL VAKLFDVTQK
TALKDAVTRA STEEIIIPFG IGIAGMVAQT KQMINIKEAY KDARFNCEID LKTGYKTNAI
LCMPICNYEG DIIGVAQIIN KTNGCMEFDE HDVEIFRRYL TFCGIGIQNA QLFEMSVQEY
RRNQILLNLA RSIFEEQNNL ECLVTKIMTE ARELLKCERC SVFLVDLDCC EASHLEKIIE
KPNQLEQRPS RAIKSADSFE EKKLRNRFTV LFELGGEYQA ANVSRPSISE LSHSTLAQIA
QFVATTGQTV NICDVNEWVR EHNHQIRTES EIDSTQAILC MPIVNAQKTV IGVAQLINKA
NGVPFTESDA SIFEAFAIFC GLGIHNTQMY ENACKLMAKQ KVALECLSYH ATANQDQTEK
LTQDVVAEAE SYNLYSFTFT DFDLVDDDTC RAVLRMFMQC NLVSQFQIPY DVLCRWVLSV
RKNYRPVKYH NWRHALNVAQ TMFAMLKTGK MERFMTDLEI LGLLVACLCH DLDHRGTNNA
FQTKTESPLA ILYTTSTMEH HHFDQCVMIL NSEGNNIFQA LSPEDYRSVM KTVESAILST
DLAMYFKKRN AFLELVENGE FDWQGEEKKD LLCGMMMTAC DVSAIAKPWE VQHRVAKLVA
DEFFDQGDLE KLQLNTQPVA MMDRERKDEL PKMQVGFIDV ICLPLYRVLC DTFPWITPLY
EGTLENRRNW QDLAEKVEMG LTWIDHDTID KPVEEFAGCA DEDIKDIEFT VQTLNCNQQS
QETDAHTTPE HHRSGSRLSM KKTGALGKAV RSKLSKTLYN SMDGSKPKTS LKLLESHVSE
DMDDKSPTSP SQPHGGSVGR MSASSSTSSA GTVVDKTKKR SKLCALL
