PDE6_DROAN
ID PDE6_DROAN Reviewed; 1158 AA.
AC B3LVW5;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 73.
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=GF17478;
OS Drosophila ananassae (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7217;
RN [1] {ECO:0000312|EMBL:EDV41498.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tucson 14024-0371.13 {ECO:0000312|EMBL:EDV41498.1};
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; CH902617; EDV41498.1; -; Genomic_DNA.
DR RefSeq; XP_001952915.2; XM_001952880.2.
DR AlphaFoldDB; B3LVW5; -.
DR SMR; B3LVW5; -.
DR STRING; 7217.FBpp0120670; -.
DR GeneID; 6500262; -.
DR KEGG; dan:6500262; -.
DR eggNOG; KOG3689; Eukaryota.
DR HOGENOM; CLU_006980_0_2_1; -.
DR InParanoid; B3LVW5; -.
DR OMA; ATIRMFK; -.
DR PhylomeDB; B3LVW5; -.
DR ChiTaRS; Pde6; fly.
DR Proteomes; UP000007801; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0016020; C:membrane; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; 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..1155
FT /note="cGMP-specific 3',5'-cyclic phosphodiesterase"
FT /id="PRO_0000363684"
FT PROPEP 1156..1158
FT /note="Removed in mature form"
FT /evidence="ECO:0000250|UniProtKB:Q9VFI9"
FT /id="PRO_0000363685"
FT DOMAIN 242..394
FT /note="GAF 1"
FT /evidence="ECO:0000255"
FT DOMAIN 426..640
FT /note="GAF 2"
FT /evidence="ECO:0000255"
FT DOMAIN 670..993
FT /note="PDEase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01192"
FT REGION 1..137
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 195..216
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1034..1065
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1097..1158
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..48
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 68..91
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 103..137
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1104..1142
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 746
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 750
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 786
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 787
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 787
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 897
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT MOD_RES 1155
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000250|UniProtKB:Q9VFI9"
FT LIPID 1155
FT /note="S-farnesyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:Q9VFI9"
SQ SEQUENCE 1158 AA; 127966 MW; 977DCAE9614F1792 CRC64;
MTDVSAPTGG ATSPVDITAS PGSTALPPVA TTSAAASASS SQAKPLTNGA KKAATAAAAA
GAEEGGASAS NQVKQEQRRQ SNNNRPAASG TPEAKQATPA GNPDPGAGST SKSSSIHTQT
SQQERAGRPT SSASQHDVDE VARLFEEKPE AFEKWLTERA PPEALGRLQE FIESRKPLKR
PSVTSDLFQQ WMAASPTVQQ KSPRSLSNSS ASSIPESRRH LMDLDEGELF MELIRDVANE
LDIDVLCHKI LVNVGLLTHA DRGSLFLAKG APNNKYLVAK LFDVTQKTAL KDAVTRASTE
EIIIPFGIGI AGMVAQTKQM INIKEAYKDA RFNCEIDLKT GYKTNAILCM PICNYEGDII
GVAQIINKTN GCMEFDEHDV EIFRRYLTFC GIGIQNAQLF EMSVQEYRRN QILLNLARSI
FEEQNNLECL VTKIMTEARE LLKCERCSVF LVDLDCCEAG CGRVGGAMRR FGVRSKQVSA
IVEHVGGRRG NTSHLEKIIE KPNQPATRAI KSADSFEEKK MRNRFTVLFE LGGEYQAANV
SRPSTSELST STLAQIAQFV ATTGQTVNIC DVHEWVREHN QIRAESEIDS TQAILCMPIV
NAKKTVIGVA QLINKANGVP FTESDASIFE AFAIFCGLGI HNTQMYENAC KLMAKQKVAL
ECLSYHATAS QDQTEKLTQD AIADADTYNL YSFTFTDFEL VDDDTCRAVL RMFMQCNLVS
QFQIPYDVLC RWVLSVRKNY RPVKYHNWRH ALNVAQTMFA MLKTGKMERF MTDLEILGLL
VACLCHDLDH RGTNNAFQTK TESPLAILYT TSTMEHHHFD QCVMILNSEG NNIFQALSPE
DYRSVMKTVE SAILSTDLAM YFKKRNAFLE LVENGEFDWQ GEEKKDLLCG MMMTACDVSA
IAKPWEVQHK VAKLVADEFF DQGDLEKLQL NTQPVAMMDR ERKDELPKMQ VGFIDVICLP
LYRVLCDTFP WITPLYEGTL ENRRNWQDLA EKVEMGLTWI DHDTIDKPVE EFAACADEEI
KDIEFTVTTL NCNQSQQSQH GSEDSHTPEH QRSGSRLSMK KTGALGKAVR SKLSKTLYNS
MDGSKPKTSL KLLESHVSED MDDKSPTSPS QPQAAGSMGR MSASSSTSSA GGQGQCQVAA
PGQAQDKSKK RSKLCALL
