ID PDE11_TAKRU Reviewed; 903 AA. AC Q1KKS3; DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot. DT 30-MAY-2006, sequence version 1. DT 22-FEB-2023, entry version 72. DE RecName: Full=Dual 3',5'-cyclic-AMP and -GMP phosphodiesterase 11A; DE EC=3.1.4.35 {ECO:0000250|UniProtKB:Q9HCR9}; DE EC=3.1.4.53 {ECO:0000250|UniProtKB:Q9HCR9}; DE AltName: Full=cAMP and cGMP phosphodiesterase 11A; GN Name=pde11a; OS Takifugu rubripes (Japanese pufferfish) (Fugu rubripes). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata; OC Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Takifugu. OX NCBI_TaxID=31033; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=16636282; DOI=10.1073/pnas.0601492103; RA Lee A.P., Koh E.G.L., Tay A., Brenner S., Venkatesh B.; RT "Highly conserved syntenic blocks at the vertebrate Hox loci and conserved RT regulatory elements within and outside Hox gene clusters."; RL Proc. Natl. Acad. Sci. U.S.A. 103:6994-6999(2006). CC -!- FUNCTION: Plays a role in signal transduction by regulating the CC intracellular concentration of cyclic nucleotides cAMP and cGMP. CC Catalyzes the hydrolysis of both cAMP and cGMP to 5'-AMP and 5'-GMP, CC respectively. {ECO:0000250|UniProtKB:Q9HCR9}. 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:Q9HCR9}; 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:0000250|UniProtKB:Q9HCR9}; CC -!- COFACTOR: CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240; CC Evidence={ECO:0000250|UniProtKB:O76083}; 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|UniProtKB:O76083}; CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol CC {ECO:0000250|UniProtKB:Q9HCR9}. CC -!- DOMAIN: The tandem GAF domains bind cGMP, and regulate enzyme activity. CC The binding of cGMP stimulates enzyme activity. CC {ECO:0000250|UniProtKB:Q9HCR9}. CC -!- SIMILARITY: Belongs to the cyclic nucleotide phosphodiesterase family. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; DQ481668; ABF22471.1; -; Genomic_DNA. DR AlphaFoldDB; Q1KKS3; -. DR SMR; Q1KKS3; -. DR STRING; 31033.ENSTRUP00000044767; -. DR eggNOG; KOG3689; Eukaryota. DR HOGENOM; CLU_006980_0_1_1; -. DR InParanoid; Q1KKS3; -. DR Proteomes; UP000005226; Unplaced. DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell. DR GO; GO:0004115; F:3',5'-cyclic-AMP phosphodiesterase activity; IEA:UniProtKB-EC. DR GO; GO:0047555; F:3',5'-cyclic-GMP phosphodiesterase activity; IEA:UniProtKB-EC. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008152; P:metabolic process; IEA:UniProtKB-KW. DR GO; GO:0007165; P:signal transduction; IEA:InterPro. DR CDD; cd00077; HDc; 1. DR Gene3D; 3.30.450.40; -; 2. DR Gene3D; 1.10.1300.10; 3'5'-cyclic nucleotide phosphodiesterase, catalytic domain; 1. 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 PANTHER; PTHR11347; CYCLIC NUCLEOTIDE PHOSPHODIESTERASE; 1. DR PANTHER; PTHR11347:SF139; PHOSPHODIESTERASE; 1. DR Pfam; PF01590; GAF; 2. DR Pfam; PF00233; PDEase_I; 1. DR PRINTS; PR00387; PDIESTERASE1. DR SMART; SM00065; GAF; 2. DR SUPFAM; SSF55781; GAF domain-like; 2. DR SUPFAM; SSF109604; HD-domain/PDEase-like; 1. DR PROSITE; PS00126; PDEASE_I_1; 1. DR PROSITE; PS51845; PDEASE_I_2; 1. PE 3: Inferred from homology; KW Allosteric enzyme; cAMP; cGMP; Cytoplasm; Hydrolase; Metal-binding; KW Reference proteome; Repeat. FT CHAIN 1..903 FT /note="Dual 3',5'-cyclic-AMP and -GMP phosphodiesterase FT 11A" FT /id="PRO_0000247043" FT DOMAIN 175..324 FT /note="GAF 1" FT DOMAIN 356..512 FT /note="GAF 2" FT DOMAIN 542..866 FT /note="PDEase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01192" FT REGION 863..903 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 889..903 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 618 FT /note="Proton donor" FT /evidence="ECO:0000250|UniProtKB:O76083" FT BINDING 378 FT /ligand="3',5'-cyclic GMP" FT /ligand_id="ChEBI:CHEBI:57746" FT /evidence="ECO:0000250|UniProtKB:Q922S4" FT BINDING 622 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 658 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 659 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 659 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 770 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01192" SQ SEQUENCE 903 AA; 102019 MW; 0B12D6E7897E2E26 CRC64; MAVPKMVFSD VESFLDSHPE LFEDYLNRKG SSSMVEKWLK NHQAGKSEAE PKEEKSSVCK DSWASKCDGL QRRASQKELR KTFARSKAIN VNRTYDEHVN SRAQEPLTSM RRRALLRKAS SLPPTTAHIL SALLESRVNI PQYPSTAVDF KYYLKEHNER EFFLELVKDI SNDLDLTSLS YKILVFVCIM VDADRCSLFL VEGTGNKKTL VSKFFDVHAG TTVLPSMNSG EVQVPWGKGI IGYVAEHGET VNIPDAYQDR RFSDEIDKLT GYKTKSLLCM PIQNSDGEII GVAQAINKSS SGELFTEDDE KVLQMYLPFC GIAISNAQLF AASRKEYDRS RALLEVVNDL FEEQTDLEKI VRKIMHRAQT LLKCERCSVQ LLEDIESPVV KFTKSFELLS PKCSADAESS FKDSMEKSSY SDWLINNSIA ELVASTGLPV NISDAYQDPR FDAEADQFSD FHIRSVLCVP IWNSNHQIIG VAQVLNRLDG KPFDDADQRL FEAFVIFCGL GINNTIMYDQ VKKSWAKQSV ALDVLSYHAT CSKTEVDKFK AANIPLVCEL GIDKLSFDDF SLDVDAMITA ALRMFIELGM VQKFKIDYET LCRWLLTVRK NYRMVLYHNW RHAFNVCQCM FAMLTTAGFQ ETLTDVEILA LIVGCVCHDL DHRGTNNAFQ AKTGSALSLL YGTSATLEHH HFNHAVMILQ SEGHNIFCNL SSTEYSDLMQ LLKQSILATD LTLYFENRNS FFELVSIGEY NWNVKTHRDM CRSMMMTACD LGAVTKPWDI SRKVAELVTS EFFEQGDRER SELKLTPSAI FDRNRKDELP GLQLEWIDGI CAPLYETLVK LNPKLQPMVD MINANRVKWE ELDKKRQHDH GASVPASPCS AAEGSETGGV PCCSNNTPPT HVS //