PDE11_TAKRU
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 03-AUG-2022, entry version 70.
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}.
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DR EMBL; DQ481668; ABF22471.1; -; Genomic_DNA.
DR AlphaFoldDB; Q1KKS3; -.
DR SMR; Q1KKS3; -.
DR STRING; 31033.ENSTRUP00000044767; -.
DR PRIDE; Q1KKS3; -.
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; 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 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
