PDE6_DROSE
ID PDE6_DROSE Reviewed; 1205 AA.
AC B4HEM4;
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=GM25848;
OS Drosophila sechellia (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7238;
RN [1] {ECO:0000312|EMBL:EDW42181.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Rob3c / Tucson 14021-0248.25 {ECO:0000312|EMBL:EDW42181.1};
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; CH480815; EDW42181.1; -; Genomic_DNA.
DR RefSeq; XP_002031195.1; XM_002031159.1.
DR AlphaFoldDB; B4HEM4; -.
DR SMR; B4HEM4; -.
DR STRING; 7238.B4HEM4; -.
DR EnsemblMetazoa; FBtr0208833; FBpp0207325; FBgn0180704.
DR HOGENOM; CLU_006980_0_2_1; -.
DR OMA; ATIRMFK; -.
DR PhylomeDB; B4HEM4; -.
DR ChiTaRS; Pde6; fly.
DR Proteomes; UP000001292; 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; 2.
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..1202
FT /note="cGMP-specific 3',5'-cyclic phosphodiesterase"
FT /id="PRO_0000363696"
FT PROPEP 1203..1205
FT /note="Removed in mature form"
FT /evidence="ECO:0000250|UniProtKB:Q9VFI9"
FT /id="PRO_0000363697"
FT DOMAIN 259..411
FT /note="GAF 1"
FT /evidence="ECO:0000255"
FT DOMAIN 443..624
FT /note="GAF 2"
FT /evidence="ECO:0000255"
FT DOMAIN 654..1052
FT /note="PDEase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01192"
FT REGION 1..153
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1093..1122
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1152..1205
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..49
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 85..101
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 112..153
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1161..1192
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 730
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 734
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 770
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 771
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 771
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 956
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT MOD_RES 1202
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000250|UniProtKB:Q9VFI9"
FT LIPID 1202
FT /note="S-farnesyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:Q9VFI9"
SQ SEQUENCE 1205 AA; 133207 MW; A2D9562B2022719C CRC64;
MTDVSSPAGG AASPVEMTTS SSPAATTSAS SSKPLTNGAN KTTISTTAGG VAPGDVPGTG
SGAIPASSSS GNQVKLEHHH RQSNNNRPAA TNRSSETKLR SPAGESDGAS RLMTPAGSSS
SPSQSPSQTQ ASIQTQTSQQ DRLTKASTTA SQQDVDEVAR LFEEKPEAFE KWLTERAPPE
ALSRLQEFIE NRKPHKRPSV TSDLFQQWMA ASPTVQQKSP RSLSNSSASS LPECRRHLMD
LDEGELFMEL IRDVANELDI DVLCHKILVN VGLLTHADRG SLFLAKGTPT NKYLVAKLFD
VTQKTALKDA VARASAEEII IPFGIGIAGM VAQTKQMINI KEAYKDARFN CEIDLKTGYK
TNAILCMPIC NYEGDIIGVA QIINKTNGCM EFDEHDVEIF RRYLTFCGIG IQNAQLFEMS
VQEYRRNQIL LNLARSIFEE QNNLECLVTK IMTEARELLK CERCSVFLVD LDCCEASHLE
KIIEKPNQPA TRAIKSADSF EEKKMRNRFT VLFELGGEYQ AANVSRPSVS ELSSSTLAQI
AQFVATTGQT VNICDVIEWV RDHNQIRAED EIDSTQAILC MPIMNAQKKV IGVAQLINKA
NGVPFTDSDA SIFEAFAIFC GLGIHNTQMY ENACKLMAKQ KVALECLSYH ATASQDQTEK
LTQDVIAEAE SYNLYSFTFT DFELVDDDTC RAVLRMFMQC NLVSQFQIPY DVLCRWVLSV
RKNYRPVKYH NWRHALNVAQ TMFAMLKTGK MERFMTDLEI LGLLVACLCH DLDHRGTNNA
FQTKTESPLA ILYTTSTMEH HHFDQCVMIL NSEGNNIFQT GFAGLGAGTF GSGRGTGGGS
NSNFPGDRVL QIARRTIFFF VPELDAEDDV VDSVVDSVVE LSVVVLVLDS VLVAALSPED
YRSVMKTVES AILSTDLAMY FKKRNAFLEL VENGEFDWQG EEKKDLLCGM MMTACDVSAI
AKPWEVQHKV AKLVADEFFD QGDLEKLQLN TQPVAMMDRE RKDELPKMQV GFIDVICLPL
YRVLCDTFPW ITPLYEGTLE NRRNWQDLAE KVEMGLTWID HDTIDKPVEE FAACADEEIK
DIEFTVTTLN CNQQSQHGSE DSHTPEHQRS GSRLSMKKTG ALGKAVRSKL SKTLYNSMDG
SKPKTSLKLL ESHVSEDMDD KSPTSPSQPQ ASGSMGRMSA SSSTSSAGGQ MVDKSKKRSK
LCALL
