PDE6_DROGR
ID PDE6_DROGR Reviewed; 1078 AA.
AC B4JXX2;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-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=GH14135;
OS Drosophila grimshawi (Hawaiian fruit fly) (Idiomyia grimshawi).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Hawaiian Drosophila.
OX NCBI_TaxID=7222;
RN [1] {ECO:0000312|EMBL:EDV90534.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tucson 15287-2541.00 {ECO:0000312|EMBL:EDV90534.1};
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; CH916377; EDV90534.1; -; Genomic_DNA.
DR RefSeq; XP_001995876.1; XM_001995840.1.
DR AlphaFoldDB; B4JXX2; -.
DR SMR; B4JXX2; -.
DR STRING; 7222.FBpp0148041; -.
DR EnsemblMetazoa; FBtr0467024; FBpp0417204; FBgn0121611.
DR eggNOG; KOG3689; Eukaryota.
DR HOGENOM; CLU_006980_0_2_1; -.
DR InParanoid; B4JXX2; -.
DR OMA; ATIRMFK; -.
DR OrthoDB; 904682at2759; -.
DR PhylomeDB; B4JXX2; -.
DR ChiTaRS; Pde6; fly.
DR Proteomes; UP000001070; 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..1075
FT /note="cGMP-specific 3',5'-cyclic phosphodiesterase"
FT /id="PRO_0000363688"
FT PROPEP 1076..1078
FT /note="Removed in mature form"
FT /evidence="ECO:0000250|UniProtKB:Q9VFI9"
FT /id="PRO_0000363689"
FT DOMAIN 196..348
FT /note="GAF 1"
FT /evidence="ECO:0000255"
FT DOMAIN 380..564
FT /note="GAF 2"
FT /evidence="ECO:0000255"
FT DOMAIN 594..917
FT /note="PDEase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01192"
FT REGION 24..168
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 958..994
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1011..1078
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 61..123
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 129..168
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 958..974
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1037..1065
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 670
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 674
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 710
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
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 711
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 821
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT MOD_RES 1075
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000250|UniProtKB:Q9VFI9"
FT LIPID 1075
FT /note="S-farnesyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:Q9VFI9"
SQ SEQUENCE 1078 AA; 120555 MW; 4193E7C8A5FB672E CRC64;
MRIQTMILGC AFLAICIIGS SNAACDEPDK CTPEECEDPA NAAEESCAEN PDDNPSNPDD
DPSNPDDNPS NPDDNPSNPD DNPSNPDDNP SNPDDNPSNP DDNPSNPDDN PSNPDDNPTN
PDDNPNNPSN PSNPSGGVEA TTAANNGGSG SNAQKSPRRL SNSSVQALPE GRRHLMDLDE
GDLFMELIRD VANELDIDVL CHKILVNVGL LTHADRGSLF LAKGTPNNKY LVAKLFDVTQ
KTALKDAVTR ARAEEIIIPF GIGIAGMVAQ TKEMINIKEA YQDVRFNCEI DQKTGYKTNA
ILCMPICNYE GDIIGVAQII NKTNGCMEFD EHDVEIFRRY LTFCGIGIQN AQLFEMSVQE
YRRNQILLNL ARSIFEEQNN LECLVTKIMT EARELLKCER CSVFLVDLDC CEESHLEKII
EKPHQQEQRT MRAIKGGDSF EEQQKMRNRF TVLFELGGEY QAANVSRPSI NELSHSTLAQ
IAQFVSTTGQ TVNICDVHEW VRDHNQIRDS EIDSTHAILC MPIVNAQKTV IGVAQLINKA
NGLPFSESDV SIFEAFAIFC GLGIHNTQMY ENACKLMAKQ KVALECLSYH ATASQDQTEK
LTQDPIAEAE SYNLYSFTFT DFDLVDDDTC RAVLRMFMQC NLVSQFHIPY DVLCRWVLSV
RKNYRPVKYH NWRHALNVAQ TMFAMLKTGK MERFMTDLEI LGLLVACLCH DLDHRGTNNA
FQTKTESPLA ILYTTSTMEH HHFDQCVMIL NSEGNNIFQA LSPEDYRCVM KTVESAILST
DLAMYFKKRN AFLELVENGE FDWQGEEKKD LLCGMMMTAC DVSAIAKPWE VQHRVAKLVA
DEFFDQGDLE KLQLNTQPVA MMDRERKDEL PKMQVGFIDV ICLPLYRVLC DTFPWITPLY
EGTLENRRNW QDLAEKVEMG LTWIDHDTID KPVEEFAGCA DEEIKDIEFT VTTLNCNQQS
QSQSQSQSQS QHGGDDIHTP EHQRSSGSRL SIKKTGALGK VVRSKLSKTL YNSMDGSKPK
TSLKLLESHV SEDMDDKSPT SPSQPHSGSV GRMSASSSTS SAGTVDKTKK RSKLCALL
