PDE11_DROME
ID PDE11_DROME Reviewed; 1451 AA.
AC Q9VJ79; Q8MQW0; Q9VJ78;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 4.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Dual 3',5'-cyclic-AMP and -GMP phosphodiesterase 11;
DE EC=3.1.4.35 {ECO:0000269|PubMed:15673286};
DE EC=3.1.4.53 {ECO:0000269|PubMed:15673286};
DE AltName: Full=cAMP and cGMP phosphodiesterase 11;
DE Short=PDE11 {ECO:0000303|PubMed:15673286};
GN Name=Pde11; ORFNames=CG34341;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [2]
RP GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM D).
RC STRAIN=Berkeley; TISSUE=Embryo;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND TISSUE
RP SPECIFICITY.
RX PubMed=15673286; DOI=10.1042/bj20050057;
RA Day J.P., Dow J.A.T., Houslay M.D., Davies S.A.;
RT "Cyclic nucleotide phosphodiesterases in Drosophila melanogaster.";
RL Biochem. J. 388:333-342(2005).
CC -!- FUNCTION: Plays a role in signal transduction by regulating the
CC intracellular concentration of cyclic nucleotides cAMP and cGMP. Dual-
CC specificity phosphodiesterase that catalyzes the hydrolysis of both
CC cAMP and cGMP to 5'-AMP and 5'-GMP, respectively.
CC {ECO:0000269|PubMed:15673286}.
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:0000269|PubMed:15673286};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16958;
CC Evidence={ECO:0000269|PubMed:15673286};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3',5'-cyclic AMP + H2O = AMP + H(+); Xref=Rhea:RHEA:25277,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:58165,
CC ChEBI:CHEBI:456215; EC=3.1.4.53;
CC Evidence={ECO:0000269|PubMed:15673286};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25278;
CC Evidence={ECO:0000269|PubMed:15673286};
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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=18.5 uM for cAMP {ECO:0000269|PubMed:15673286};
CC KM=6 uM for cGMP {ECO:0000269|PubMed:15673286};
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=B;
CC IsoId=Q9VJ79-1; Sequence=Displayed;
CC Name=C;
CC IsoId=Q9VJ79-3; Sequence=VSP_030328, VSP_030329;
CC Name=D;
CC IsoId=Q9VJ79-2; Sequence=VSP_019906;
CC -!- TISSUE SPECIFICITY: In adults, it is enriched in Malpighian tubules.
CC {ECO:0000269|PubMed:15673286}.
CC -!- SIMILARITY: Belongs to the cyclic nucleotide phosphodiesterase family.
CC {ECO:0000305}.
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DR EMBL; AE014134; AAF53675.3; -; Genomic_DNA.
DR EMBL; AE014134; AAF53676.2; -; Genomic_DNA.
DR EMBL; AY122262; AAM52774.1; -; mRNA.
DR RefSeq; NP_001097177.1; NM_001103707.2. [Q9VJ79-3]
DR RefSeq; NP_001286044.1; NM_001299115.1. [Q9VJ79-1]
DR RefSeq; NP_001286045.1; NM_001299116.1. [Q9VJ79-3]
DR RefSeq; NP_609885.2; NM_136041.2. [Q9VJ79-1]
DR AlphaFoldDB; Q9VJ79; -.
DR SMR; Q9VJ79; -.
DR BioGRID; 61102; 6.
DR STRING; 7227.FBpp0111456; -.
DR PaxDb; Q9VJ79; -.
DR PRIDE; Q9VJ79; -.
DR EnsemblMetazoa; FBtr0112544; FBpp0111456; FBgn0085370. [Q9VJ79-1]
DR EnsemblMetazoa; FBtr0112545; FBpp0111457; FBgn0085370. [Q9VJ79-3]
DR EnsemblMetazoa; FBtr0343830; FBpp0310380; FBgn0085370. [Q9VJ79-1]
DR EnsemblMetazoa; FBtr0343831; FBpp0310381; FBgn0085370. [Q9VJ79-3]
DR GeneID; 35107; -.
DR KEGG; dme:Dmel_CG34341; -.
DR CTD; 35107; -.
DR FlyBase; FBgn0085370; Pde11.
DR VEuPathDB; VectorBase:FBgn0085370; -.
DR eggNOG; KOG3689; Eukaryota.
DR InParanoid; Q9VJ79; -.
DR PhylomeDB; Q9VJ79; -.
DR BioGRID-ORCS; 35107; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 35107; -.
DR PRO; PR:Q9VJ79; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0085370; Expressed in saliva-secreting gland and 34 other tissues.
DR ExpressionAtlas; Q9VJ79; baseline and differential.
DR Genevisible; Q9VJ79; DM.
DR GO; GO:0005829; C:cytosol; HDA:FlyBase.
DR GO; GO:0004115; F:3',5'-cyclic-AMP phosphodiesterase activity; IDA:UniProtKB.
DR GO; GO:0047555; F:3',5'-cyclic-GMP phosphodiesterase activity; IDA:UniProtKB.
DR GO; GO:0004114; F:3',5'-cyclic-nucleotide phosphodiesterase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0046058; P:cAMP metabolic process; IDA:UniProtKB.
DR GO; GO:0046068; P:cGMP metabolic process; IDA:UniProtKB.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
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 1: Evidence at protein level;
KW Alternative splicing; cAMP; cGMP; Hydrolase; Metal-binding;
KW Reference proteome; Repeat.
FT CHAIN 1..1451
FT /note="Dual 3',5'-cyclic-AMP and -GMP phosphodiesterase 11"
FT /id="PRO_0000247044"
FT DOMAIN 419..572
FT /note="GAF 1"
FT DOMAIN 604..754
FT /note="GAF 2"
FT DOMAIN 783..1107
FT /note="PDEase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01192"
FT REGION 1..54
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 75..100
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 125..169
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 235..262
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 327..374
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1109..1171
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1200..1248
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1268..1305
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1325..1364
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 19..54
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 75..98
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 135..169
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 235..261
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 344..359
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1154..1171
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1217..1248
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1289..1303
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1327..1355
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 860
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 864
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01192"
FT BINDING 900
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01192"
FT BINDING 901
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01192"
FT BINDING 901
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01192"
FT BINDING 1011
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01192"
FT VAR_SEQ 1..44
FT /note="Missing (in isoform C)"
FT /evidence="ECO:0000305"
FT /id="VSP_030328"
FT VAR_SEQ 1
FT /note="M -> MKVTQSEENTRNTSDRSKSVQTNRKFDNFNWLLSCGLLAAVKSTKLI
FT PQLPRQQQPKKYNLRYAAELLKFDKIQFIKTEGLTFALLAGP (in isoform D)"
FT /evidence="ECO:0000303|PubMed:12537569"
FT /id="VSP_019906"
FT VAR_SEQ 45..64
FT /note="QTPSHSPQIQHHSEIIPATT -> MASSPNNAAPPVLWRARRKI (in
FT isoform C)"
FT /evidence="ECO:0000305"
FT /id="VSP_030329"
FT CONFLICT 38
FT /note="Q -> QQQ (in Ref. 3; AAM52774)"
FT /evidence="ECO:0000305"
FT CONFLICT 1192
FT /note="V -> A (in Ref. 3; AAM52774)"
FT /evidence="ECO:0000305"
FT CONFLICT 1196
FT /note="A -> V (in Ref. 3; AAM52774)"
FT /evidence="ECO:0000305"
FT CONFLICT 1232
FT /note="C -> R (in Ref. 3; AAM52774)"
FT /evidence="ECO:0000305"
FT CONFLICT 1342
FT /note="H -> HNH (in Ref. 3; AAM52774)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1451 AA; 160930 MW; DFEC01058FB600A9 CRC64;
MGQAASMCRF RGCRYKNKNK SSKQQQQQQQ QQQQQQQQHQ QQQQQTPSHS PQIQHHSEII
PATTGLHLRS IEEPATTPLQ FQPTGRMNTE QGGTGYGGYG SSEHSLLIAT RHAGVPLPLA
QHQPLPAHYQ PLNHSGAAPP SSSNGSSSSG GGVQTSATPQ QQQQYQVQQP YQYQYQHHYH
HQANSPQHHR PYDPEHARME AWLDENQEFV QDYFIRKATR QTVDAWLVSH ATSAGNDVVS
STSPTHANGQ TSSSRGGSGA TTPVRKISAH EFERGGLLKP IVNTIDGTPT FLSIGPPMDN
GSVGGSCSNL QNVGGVVAGQ YQYNHQQHHH NHAHLHHSQH SHYQAGGAVG SSSLGSTGGA
SGAGGAPSLG GSGGAGNGHQ YPYYHCHQRP QRLSRNELKQ LDEKELIFEL VKDICNELEV
RTLCHKILQN VSILLNADRG SLFLVQGRCN GPDGLKKCLV SKLFDVCPRS TVEEMEQQDE
VRVAWGTGIA GHVAESGEPV NIPDAYQDER FNCEIDSLTG YRTKALLCMP IKDSSGDVIG
VAQVINKMNG ECFSEIDEKV FSSYLQFCGI GLRNAQLYEK SQLEIKRNQV LLDLARMIFE
EQSTIEHMVF RILTHMQSLI QCQRVQILLV HEADKGSFSR VFDFEANDLS EEEATSRTSP
YESRFPINIG ITGHVATTGE TVNVPNAYED DRFDASVDEN SCFKHRSILC MAIKNSLGQI
IGVIQLINKF NELDFTKNDE NFVEAFAIFC GMGIHNTHMY EKAIVAMAKQ SVTLEVLSYH
ASATMDEAHR LRRLRVPSAV HFRLHDFKFD DIHFEDDDTL KACLRMFLDL DFVERFHIDY
EVLCRWLLSV KKNYRNVTYH NWRHAFNVAQ MMFAILTTTQ WWKIFGEIEC LALIIGCLCH
DLDHRGTNNS FQIKASSPLA QLYSTSTMEH HHFDQCLMIL NSPGNQILAN LSSDDYCRVI
RVLEDAILST DLAVYFKKRG PFLESVSQPT SYWVAEEPRA LLRAMSMTVC DLSAITKPWE
IEKRVADLVS SEFFEQGDME KQELNITPID IMNREKEDEL PMMQVNFIDS ICLPIYEAFA
TLSDKLEPLV EGVRDNRGHW IDLADVVKTK TSQDQEPEEE QQQQNVISNG DCKAMSDDDV
AASEAEVAVD SPSEKASVNG SNVANNSSNT NKKIAVASHP TSTQPSDDDN DVDADADDVD
EQAAEENGHD AEVDEASCRS NSTCSSSTAS SCLSTPPPTG EDDSTPVSPL KTLQAKLVAA
NLNALQRQTS NQAQTQKQRC KSCDHSRSGL QVRKTSSLRG AQELDLDSKT RNGTHAALCK
STPVINNHSH HHNHSHSHNH NHHHHHHHHS HHNHSQHGIG IGSASIGGSG LISLTTPLLA
MDSDRIPKIV GKIGNLDGLP FANGIGGPQN GHGLPFGSYQ HHHHHQHHHH LLARRHSETN
SNGATAMAVE K
