PDE6_DROER
ID PDE6_DROER Reviewed; 1131 AA.
AC B3P3K2;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 70.
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=GG21262;
OS Drosophila erecta (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7220;
RN [1] {ECO:0000312|EMBL:EDV48890.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tucson 14021-0224.01 {ECO:0000312|EMBL:EDV48890.1};
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; CH954181; EDV48890.1; -; Genomic_DNA.
DR RefSeq; XP_001979932.2; XM_001979896.2.
DR AlphaFoldDB; B3P3K2; -.
DR SMR; B3P3K2; -.
DR STRING; 7220.FBpp0139808; -.
DR GeneID; 6552139; -.
DR KEGG; der:6552139; -.
DR eggNOG; KOG3689; Eukaryota.
DR HOGENOM; CLU_006980_0_2_1; -.
DR OMA; ATIRMFK; -.
DR PhylomeDB; B3P3K2; -.
DR ChiTaRS; Pde6; fly.
DR Proteomes; UP000008711; 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; Repeat.
FT CHAIN 1..1128
FT /note="cGMP-specific 3',5'-cyclic phosphodiesterase"
FT /id="PRO_0000363686"
FT PROPEP 1129..1131
FT /note="Removed in mature form"
FT /evidence="ECO:0000250|UniProtKB:Q9VFI9"
FT /id="PRO_0000363687"
FT DOMAIN 255..412
FT /note="GAF 1"
FT /evidence="ECO:0000255"
FT DOMAIN 444..625
FT /note="GAF 2"
FT /evidence="ECO:0000255"
FT DOMAIN 655..978
FT /note="PDEase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01192"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 42..150
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1019..1048
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1078..1131
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 77..93
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 104..150
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1087..1118
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 731
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 735
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 772
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 772
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 882
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT MOD_RES 1128
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000250|UniProtKB:Q9VFI9"
FT LIPID 1128
FT /note="S-farnesyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:Q9VFI9"
SQ SEQUENCE 1131 AA; 125578 MW; D63B518C430CAE35 CRC64;
MTDVSSPAGG AASPVEMATS SSSAATTLTN GANKTAISTA AGVAPGAVPG PGSAAIPASS
SSGNQVKLEH HHRQSNNNRP AATNRSSETK LRSPAGESDG ASRLMTPAGS SSTPSQSPSP
SQSPSQASIQ TQTSQQDRLA KASTTASQQD VDEVARLFEE KPEAFEKWLT ERAPPEALSR
LQEFIENRKP HKRPSVTSDL FQQWMAASPT VQQKSPRSLS NSSASSIPEC RRHLMDLDEG
ELFMELIRDV ANELDIDVLC HKILVNVGLL THADRGSLFL AKGTPTNKYL VAKLFDVTQK
TALKDAVTRA SAEEIIIPFG IGIAGMVAQT KQMINIKEAY KDARFNCEID LKTGYKTNAI
LCMPICNYEG DIIGVAQIIN KTNGGCFKGC MEFDEHDVEI FRRYLTFCGI GIQNAQLFEM
SVQEYRRNQI LLNLARSIFE EQNNLECLVT KIMTEARELL KCERCSVFLV DLDCCEASHL
EKIIEKPNQP ATRAIKSADS FEEKKMRNRF TVLFELGGEY QAANVSRPSV SELSSSTLAQ
IAQFVATTGQ TVNICDVIEW VRDHNQIRAE DEIDSTQAIL CMPIMNAQKK VIGVAQLINK
ANGVPFTDSD ASIFEAFAIF CGLGIHNTQM YENACKLMAK QKVALECLSY HATASQDQTE
KLTQDVIAEA ESYNLYSFTF TDFELVDDDT CRAVLRMFMQ CNLVSQFQIP YDVLCRWVLS
VRKNYRPVKY HNWRHALNVA QTMFAMLKTG KMERFMTDLE ILGLLVACLC HDLDHRGTNN
AFQTKTESPL AILYTTSTME HHHFDQCVMI LNSEGNNIFQ ALSPEDYRSV MKTVESAILS
TDLAMYFKKR NAFLELVENG EFDWQGEEKK DLLCGMMMTA CDVSAIAKPW EVQHKVAKLV
ADEFFDQGDL EKLQLNTQPV AMMDRERKDE LPKMQVGFID VICLPLYRVL CDTFPWITPL
YEGTLENRRN WQDLAEKVEM GLTWIDHDTI DKPVEEFAAC ADEEIKDIEF TVTTLNCNQQ
SQHGSEDSHT PEHQRSGSRL SMKKTGALGK AVRSKLSKTL YNSMDGSKPK TSLKLLESHV
SEDMDDKSPT SPSQPQASGS MGRMSASSST SSAGGQMVDK SKKRSKLCAL L
