PDE6_DROMO
ID PDE6_DROMO Reviewed; 1116 AA.
AC B4K9L4;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 72.
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=GI10668;
OS Drosophila mojavensis (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila.
OX NCBI_TaxID=7230;
RN [1] {ECO:0000312|EMBL:EDW16674.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tucson 15081-1352.22 {ECO:0000312|EMBL:EDW16674.1};
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; CH933806; EDW16674.1; -; Genomic_DNA.
DR RefSeq; XP_002001213.2; XM_002001177.2.
DR AlphaFoldDB; B4K9L4; -.
DR SMR; B4K9L4; -.
DR STRING; 7230.FBpp0159885; -.
DR EnsemblMetazoa; FBtr0429027; FBpp0386515; FBgn0133432.
DR KEGG; dmo:Dmoj_GI10668; -.
DR eggNOG; KOG3689; Eukaryota.
DR HOGENOM; CLU_006980_0_2_1; -.
DR InParanoid; B4K9L4; -.
DR OMA; ATIRMFK; -.
DR OrthoDB; 904682at2759; -.
DR PhylomeDB; B4K9L4; -.
DR ChiTaRS; Pde6; fly.
DR Proteomes; UP000009192; 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..1113
FT /note="cGMP-specific 3',5'-cyclic phosphodiesterase"
FT /id="PRO_0000363690"
FT PROPEP 1114..1116
FT /note="Removed in mature form"
FT /evidence="ECO:0000250|UniProtKB:Q9VFI9"
FT /id="PRO_0000363691"
FT DOMAIN 241..393
FT /note="GAF 1"
FT /evidence="ECO:0000255"
FT DOMAIN 425..611
FT /note="GAF 2"
FT /evidence="ECO:0000255"
FT DOMAIN 641..964
FT /note="PDEase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01192"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 82..136
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1005..1031
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1067..1116
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..34
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1075..1103
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 717
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 721
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 757
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 758
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 758
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 868
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT MOD_RES 1113
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000250|UniProtKB:Q9VFI9"
FT LIPID 1113
FT /note="S-farnesyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:Q9VFI9"
SQ SEQUENCE 1116 AA; 124330 MW; 53186D5E1651993E CRC64;
MTDVSATTGR AGDRVSSTSS EVAVETTSQA LTNGAAKEPL AAVTAEATAT ATVTATTTAT
VTATTTAATA TMATAVISKQ AKSECHSQSN NNQHVETAPS KQSSDSEASA PTTVSIPSAN
AKINSSSSGK TTATQQDVDE VARLFEEKPE AFEKWLTERA PPEALSRLHE FIESRKPHKR
PSVTSDLFQQ WMASPTVQQK SPRKLSNSSV HALPESRRHL MELDEGELFM ELIRDVANEL
DIDVLCHKIL VNVGLLTHAD RGSLFLAKGT PNNRYLVAKL FDVTQTTALK DAVTRARAEE
IIIPFGIGIA GMVAQTKQMI NIKEAYKDAR FNCEIDLKTG YTTNAILCMP ICNYEGDIIG
VAQIINKTNG CMEFDEHDVE IFRRYLTFCG IGIQNAQLFE MSVQEYRRNQ ILLNLARSIF
EEQNNLECLV TKIMTEAREL LKCERCSVFL VDLDCCEESH LEKIIEKPHQ LQQQRTPRAI
MSGDSFEEKQ NMRNRFTVLF ELGGENHAAN VSRPSINDLS HSTLAQIAQF VATTGQTVNI
CDVQDWVREH NQIRAESEID STQAILCMPI VNAQKTVIGV AQLINKASGL PFTESDASIF
EAFAIFCGLG IHNTQMYENA CKLMAKQKVA LECLSYHATA SQDQTEKLAQ DVIAEAEAYN
LYSFTFTDFD LVDDDTCRAV LRMFMQCNLV SQFHIPYDVL CRWVLSVRKN YRPVKYHNWR
HALNVAQTMF AMLKTGKMER FMTDLEILGL LVACLCHDLD HRGTNNAFQT KTESPLAILY
TTSTMEHHHF DQCVMILNSE GNNIFQALSP EDYRSVMKTV ESAILSTDLA MYFKKRNAFL
ELVENGEFDW QGEEKKDLLC GMMMTACDVS AIAKPWEVQH RVAKLVADEF FDQGDLEKLQ
LNTQPVAMMD RERKDELPKM QVGFIDVICL PLYRVLCDTF PWITPLYEGT LENRRNWQDL
AEKVEMGLTW IDHDTIDKPV EEFAGCADEE IKDIEFTVTT LNCNQHGGSA GGGEDTHTPE
HQRSSSRLSI KKTGALGKVV RSKLSKTLYN SMDGSKPKTS LKLLESHVSE DMDDKSPTSP
SQPHSGSVGR MSASSSTSSA GTVDKSKKRS KLCALL
