PDE6_DROYA
ID PDE6_DROYA Reviewed; 1149 AA.
AC B4PSS5;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 69.
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=GE26445;
OS Drosophila yakuba (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7245;
RN [1] {ECO:0000312|EMBL:EDW97571.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tai18E2 / Tucson 14021-0261.01 {ECO:0000312|EMBL:EDW97571.1};
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; CM000160; EDW97571.1; -; Genomic_DNA.
DR RefSeq; XP_002097859.1; XM_002097823.2.
DR AlphaFoldDB; B4PSS5; -.
DR SMR; B4PSS5; -.
DR STRING; 7245.FBpp0271455; -.
DR EnsemblMetazoa; FBtr0272963; FBpp0271455; FBgn0243466.
DR GeneID; 6537301; -.
DR KEGG; dya:Dyak_GE26445; -.
DR eggNOG; KOG3689; Eukaryota.
DR HOGENOM; CLU_006980_0_2_1; -.
DR OMA; ATIRMFK; -.
DR OrthoDB; 904682at2759; -.
DR PhylomeDB; B4PSS5; -.
DR ChiTaRS; Pde6; fly.
DR Proteomes; UP000002282; Chromosome 3R.
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; Repeat.
FT CHAIN 1..1146
FT /note="cGMP-specific 3',5'-cyclic phosphodiesterase"
FT /id="PRO_0000363704"
FT PROPEP 1147..1149
FT /note="Removed in mature form"
FT /evidence="ECO:0000250|UniProtKB:Q9VFI9"
FT /id="PRO_0000363705"
FT DOMAIN 278..430
FT /note="GAF 1"
FT /evidence="ECO:0000255"
FT DOMAIN 462..643
FT /note="GAF 2"
FT /evidence="ECO:0000255"
FT DOMAIN 673..996
FT /note="PDEase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01192"
FT REGION 1..175
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1037..1066
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1096..1149
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..20
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 28..62
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 80..115
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 126..174
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1105..1136
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 749
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 753
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 789
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 790
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 790
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 900
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT MOD_RES 1146
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000250|UniProtKB:Q9VFI9"
FT LIPID 1146
FT /note="S-farnesyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:Q9VFI9"
SQ SEQUENCE 1149 AA; 127347 MW; 96E9219B5B84983C CRC64;
MHGTVSRSSS SSNMTDVSSP AGGAASPVEI ATSSSTAATT SASASSSKPL TNGANKTAIS
TAAGVTPGAA PGPGCAAIPA SGSSGNQVKL EHHYRQSNNN RPAGSNRSSE TKLRSPAGES
DGASRLMTPA GSSSSPSQSP SQSQSQSQAS IQTQTSQQDR LVKAPSTTAS QQDVDEVARL
FEEKPEAFEK WLTERAPPEA LSRLQEFIEN RKPHKRPSVT SDLFQQWMAA SPTVQQKSPR
SLSNSSASSL PECRRHLMDL DEGELFMELI RDVANELDID VLCHKILVNV GLLTHADRGS
LFLAKGTPTN KYLVAKLFDV TQKTALKDAV TRASAEEIII PFGIGIAGMV AQTKQMINIK
EAYKDARFNC EIDLKTGYKT NAILCMPICN YEGDIIGVAQ IINKTNGCME FDEHDVEIFR
RYLTFCGIGI QNAQLFEMSV QEYRRNQILL NLARSIFEEQ NNLECLVTKI MTEARELLKC
ERCSVFLVDL DCCEASHLEK IIEKPNQPAT RAIKSADSFE EKKMRNRFTV LFELGGEYQA
ANVSRPSVSE LSSSTLAQIA QFVATTGQTV NICDVIEWVR DHNQIRAEDE IDSTQAILCM
PIMNAQKKVI GVAQLINKAN GVPFTESDAS IFEAFAIFCG LGIHNTQMYE NACKLMAKQK
VALECLSYHA TASQDQTEKL TQDAIAEAES YNLYSFTFTD FELVDDDTCR AVLRMFMQCN
LVSQFQIPYD VLCRWVLSVR KNYRPVKYHN WRHALNVAQT MFAMLKTGKM ERFMTDLEIL
GLLVACLCHD LDHRGTNNAF QTKTESPLAI LYTTSTMEHH HFDQCVMILN SEGNNIFQAL
SPEDYRSVMK TVESAILSTD LAMYFKKRNA FLELVENGEF DWQGEEKKDL LCGMMMTACD
VSAIAKPWEV QHKVAKLVAD EFFDQGDLEK LQLNTQPVAM MDRERKDELP KMQVGFIDVI
CLPLYRVLCD TFPWITPLYE GTLENRRNWQ DLAEKVEMGL TWIDHDTIDK PVEEFAACAD
EEIKDIEFTV TTLNCNQQSQ HGSEDSHTPE HQRSGSRLSM KKTGALGKAV RSKLSKTLYN
SMDGSKPKTS LKLLESHVSE DMDDKSPTSP SQPQASGSMG RMSASSSTSS AGGQMVDKSK
KRSKLCALL
