ID   PDE11_FUGRU             Reviewed;         903 AA.
AC   Q1KKS3;
DT   25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2006, sequence version 1.
DT   16-JUN-2009, entry version 16.
DE   RecName: Full=Dual 3',5'-cyclic-AMP and -GMP phosphodiesterase 11A;
DE            EC=3.1.4.17;
DE            EC=3.1.4.35;
DE   AltName: Full=cAMP and cGMP phosphodiesterase 11A;
GN   Name=pde11a;
OS   Fugu rubripes (Japanese pufferfish) (Takifugu rubripes).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei;
OC   Acanthomorpha; Acanthopterygii; Percomorpha; Tetraodontiformes;
OC   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
RT   conserved 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'-
CC       GMP, respectively (By similarity).
CC   -!- CATALYTIC ACTIVITY: Guanosine 3',5'-cyclic phosphate + H(2)O =
CC       guanosine 5'-phosphate.
CC   -!- CATALYTIC ACTIVITY: Adenosine 3',5'-cyclic phosphate + H(2)O =
CC       adenosine 5'-phosphate.
CC   -!- COFACTOR: Divalent cations (By similarity).
CC   -!- ENZYME REGULATION: Inhibited by 3-isobutyl-1-methylxanthine
CC       (IBMX), zaprinast and dipyridamole. cGMP acts as an allosteric
CC       activator (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol (By similarity).
CC   -!- DOMAIN: The tandem GAF domains bind cGMP, and regulate enzyme
CC       activity. The binding of cGMP leading to stimulate the enzyme
CC       activity (By similarity).
CC   -!- SIMILARITY: Belongs to the cyclic nucleotide phosphodiesterase
CC       family.
CC   -!- SIMILARITY: Contains 2 GAF domains.
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DR   EMBL; DQ481668; ABF22471.1; -; Genomic_DNA.
DR   HOVERGEN; Q1KKS3; -.
DR   BRENDA; 3.1.4.17; 281122.
DR   BRENDA; 3.1.4.35; 281122.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR   GO; GO:0047555; F:3',5'-cyclic-GMP phosphodiesterase activity; IEA:EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   InterPro; IPR003018; GAF.
DR   InterPro; IPR003607; Met-dep_phosphohydro_HD.
DR   InterPro; IPR002073; PDEase.
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.
PE   3: Inferred from homology;
KW   Allosteric enzyme; cAMP; cGMP; Cytoplasm; Hydrolase; Metal-binding;
KW   Repeat.
FT   CHAIN         1    903       Dual 3',5'-cyclic-AMP and -GMP
FT                                phosphodiesterase 11A.
FT                                /FTId=PRO_0000247043.
FT   DOMAIN      175    324       GAF 1.
FT   DOMAIN      356    512       GAF 2.
FT   REGION      594    859       Catalytic (By similarity).
FT   METAL       622    622       Divalent metal cation 1 (By similarity).
FT   METAL       658    658       Divalent metal cation 1 (By similarity).
FT   METAL       659    659       Divalent metal cation 1 (By similarity).
FT   METAL       659    659       Divalent metal cation 2 (By similarity).
FT   METAL       662    662       Divalent metal cation 2 (By similarity).
FT   METAL       688    688       Divalent metal cation 2 (By similarity).
FT   METAL       770    770       Divalent metal cation 1 (By similarity).
FT   BINDING     823    823       cAMP or cGMP (By similarity).
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
//