PDE6_DROVI
ID PDE6_DROVI Reviewed; 893 AA.
AC B4LVU6;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 77.
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=GJ23019;
OS Drosophila virilis (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila.
OX NCBI_TaxID=7244;
RN [1] {ECO:0000312|EMBL:EDW67551.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tucson 15010-1051.87 {ECO:0000312|EMBL:EDW67551.1};
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; CH940650; EDW67551.1; -; Genomic_DNA.
DR RefSeq; XP_002054031.2; XM_002053995.2.
DR AlphaFoldDB; B4LVU6; -.
DR SMR; B4LVU6; -.
DR STRING; 7244.FBpp0237436; -.
DR EnsemblMetazoa; FBtr0238944; FBpp0237436; FBgn0210121.
DR eggNOG; KOG3689; Eukaryota.
DR HOGENOM; CLU_006980_0_2_1; -.
DR InParanoid; B4LVU6; -.
DR OMA; ATIRMFK; -.
DR OrthoDB; 904682at2759; -.
DR PhylomeDB; B4LVU6; -.
DR ChiTaRS; Pde6; fly.
DR Proteomes; UP000008792; 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..890
FT /note="cGMP-specific 3',5'-cyclic phosphodiesterase"
FT /id="PRO_0000363700"
FT PROPEP 891..893
FT /note="Removed in mature form"
FT /evidence="ECO:0000250|UniProtKB:Q9VFI9"
FT /id="PRO_0000363701"
FT DOMAIN 21..173
FT /note="GAF 1"
FT /evidence="ECO:0000255"
FT DOMAIN 205..390
FT /note="GAF 2"
FT /evidence="ECO:0000255"
FT DOMAIN 420..743
FT /note="PDEase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01192"
FT REGION 784..807
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 844..893
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 852..880
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 496
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 500
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 536
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 537
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 537
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 647
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT MOD_RES 890
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000250|UniProtKB:Q9VFI9"
FT LIPID 890
FT /note="S-farnesyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:Q9VFI9"
SQ SEQUENCE 893 AA; 100943 MW; 2CD8AD4CCE687DDE CRC64;
MELDEGELFM ELIRDVANEL DIDVLCHKIL VNVGLLTHAD RGSLFLAKGT PNNKYLVAKL
FDVTQKTALK DAVTRARAEE IIIPFGIGIA GMVAQTKEMI NIKEAYMDAR FNCEIDLKTG
YKTNAILCMP ICNYEGDIIG VAQIINKTNG CMEFDEHDVE IFRRYLTFCG IGIQNAQLFE
MSVQEYRRNQ ILLNLARSIF EEQNNLECLV TKIMTEAREL LKCERCSVFL VDLDCCEESH
LEKIIEKPHQ LEQRATRAIK GGDSFEEKQK MRNRFTVLFE LGGESQAANV SRPSINDLSH
STLAQIAQFV ATTGQTVNIC DVHDWVREHN QIRAEGEIDS THAILCMPIV NAQKTVIGVA
QLINKASGLP FTESDASIFE AFAIFCGLGI HNTQMYENAC KLMAKQKVAL ECLSYHATAG
QDQTEKLIQD PIAEAETYNL YSFTFTDFDL VDDDTCRAVL RMFMQCNLVS QFHIPYDVLC
RWVLSVRKNY RPVKYHNWRH ALNVAQTMFA MLKTGKMERF MTDLEILGLL VACLCHDLDH
RGTNNAFQTK TESPLAILYT TSTMEHHHFD QCVMILNSEG NNIFQALSPE DYRSVMKTVE
SAILSTDLAM YFKKRNAFLE LVENGEFDWQ GEEKKDLLCG MMMTACDVSA IAKPWEVQHR
VAKLVADEFF DQGDLEKLQL NTQPVAMMDR ERKDELPKMQ VGFIDVICLP LYRVLCDTFP
WITPLYEGTL ENRRNWQDLA EKVEMGLTWI DHDTIDKPVE EFAGCADEEI KDIEFTVTTL
NCNQQSQHGG DDSHTPEHQR SGSRLSIKKT GALGKVVRSK LSKTLYNSMD GSKPKTSLKL
LESHVSEDMD DKSPTSPSQP HLGSVGRMSA SSSTSSAGTV DKSKKRSKLC ALL
