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cAMP/cGMP-dependent 3',5'-cAMP/cGMP phosphodiesterase 7 (EC 3.1.4.35) (EC 3.1.4.53) (Phosphodiesterase 7) (ddPDE7)

 PDE7_DICDI              Reviewed;         425 AA.
Q54HY0;
10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
24-MAY-2005, sequence version 1.
28-MAR-2018, entry version 67.
RecName: Full=cAMP/cGMP-dependent 3',5'-cAMP/cGMP phosphodiesterase 7;
EC=3.1.4.35;
EC=3.1.4.53;
AltName: Full=Phosphodiesterase 7;
Short=ddPDE7;
Flags: Precursor;
Name=pde7; ORFNames=DDB_G0289145;
Dictyostelium discoideum (Slime mold).
Eukaryota; Amoebozoa; Mycetozoa; Dictyostelids; Dictyosteliales;
Dictyosteliaceae; Dictyostelium.
NCBI_TaxID=44689;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=AX4;
PubMed=15875012; DOI=10.1038/nature03481;
Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A.,
Sucgang R., Berriman M., Song J., Olsen R., Szafranski K., Xu Q.,
Tunggal B., Kummerfeld S., Madera M., Konfortov B.A., Rivero F.,
Bankier A.T., Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P.,
Pilcher K., Chen G., Saunders D., Sodergren E.J., Davis P.,
Kerhornou A., Nie X., Hall N., Anjard C., Hemphill L., Bason N.,
Farbrother P., Desany B., Just E., Morio T., Rost R., Churcher C.M.,
Cooper J., Haydock S., van Driessche N., Cronin A., Goodhead I.,
Muzny D.M., Mourier T., Pain A., Lu M., Harper D., Lindsay R.,
Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
Knights A., Loulseged H., Mungall K.L., Oliver K., Price C.,
Quail M.A., Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D.,
Sanders M., Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S.,
Tivey A., Sugano S., White B., Walker D., Woodward J.R., Winckler T.,
Tanaka Y., Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A.,
Cox E.C., Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M.,
Kay R.R., Williams J.G., Dear P.H., Noegel A.A., Barrell B.G.,
Kuspa A.;
"The genome of the social amoeba Dictyostelium discoideum.";
Nature 435:43-57(2005).
[2]
BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, AND SUBCELLULAR
LOCATION.
PubMed=17040207; DOI=10.1042/BJ20061153;
Bader S., Kortholt A., Van Haastert P.J.M.;
"Seven Dictyostelium discoideum phosphodiesterases degrade three pools
of cAMP and cGMP.";
Biochem. J. 402:153-161(2007).
[3]
INDUCTION [LARGE SCALE ANALYSIS].
PubMed=18559084; DOI=10.1186/1471-2164-9-291;
Sillo A., Bloomfield G., Balest A., Balbo A., Pergolizzi B.,
Peracino B., Skelton J., Ivens A., Bozzaro S.;
"Genome-wide transcriptional changes induced by phagocytosis or growth
on bacteria in Dictyostelium.";
BMC Genomics 9:291-291(2008).
-!- FUNCTION: Phosphodiesterase with dual cAMP/cGMP specificity.
However, displays a preference for cAMP over cGMP. Seems to
regulate cAMP/cGMP concentration especially during cell
aggregation.
-!- CATALYTIC ACTIVITY: Adenosine 3',5'-cyclic phosphate + H(2)O =
adenosine 5'-phosphate.
-!- CATALYTIC ACTIVITY: Guanosine 3',5'-cyclic phosphate + H(2)O =
guanosine 5'-phosphate.
-!- ENZYME REGULATION: Inhibited by dithiotreitol (DTT).
{ECO:0000269|PubMed:17040207}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=12.5 uM for cAMP {ECO:0000269|PubMed:17040207};
KM=36 uM for cGMP {ECO:0000269|PubMed:17040207};
-!- SUBCELLULAR LOCATION: Secreted, extracellular space
{ECO:0000269|PubMed:17040207}. Cell surface
{ECO:0000269|PubMed:17040207}.
-!- INDUCTION: Down-regulated by growth on bacteria.
{ECO:0000269|PubMed:18559084}.
-!- SIMILARITY: Belongs to the cAMP phosphodiesterase class-II family.
{ECO:0000305}.
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EMBL; AAFI02000130; EAL62880.1; -; Genomic_DNA.
RefSeq; XP_636383.1; XM_631291.1.
STRING; 44689.DDB0238626; -.
PaxDb; Q54HY0; -.
EnsemblProtists; EAL62880; EAL62880; DDB_G0289145.
GeneID; 8626984; -.
KEGG; ddi:DDB_G0289145; -.
dictyBase; DDB_G0289145; pde7.
eggNOG; COG5212; LUCA.
InParanoid; Q54HY0; -.
OMA; ATWFIKN; -.
PhylomeDB; Q54HY0; -.
SABIO-RK; Q54HY0; -.
PRO; PR:Q54HY0; -.
Proteomes; UP000002195; Chromosome 5.
Proteomes; UP000002195; Unassembled WGS sequence.
GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
GO; GO:0005576; C:extracellular region; IDA:dictyBase.
GO; GO:0005615; C:extracellular space; IEA:UniProtKB-SubCell.
GO; GO:0004115; F:3',5'-cyclic-AMP phosphodiesterase activity; IGI:dictyBase.
GO; GO:0047555; F:3',5'-cyclic-GMP phosphodiesterase activity; IGI:dictyBase.
GO; GO:0030552; F:cAMP binding; IEA:UniProtKB-KW.
GO; GO:0030553; F:cGMP binding; IEA:UniProtKB-KW.
GO; GO:0006198; P:cAMP catabolic process; IGI:dictyBase.
GO; GO:0046069; P:cGMP catabolic process; IGI:dictyBase.
GO; GO:0030818; P:negative regulation of cAMP biosynthetic process; IBA:GO_Central.
GO; GO:2000480; P:negative regulation of cAMP-dependent protein kinase activity; IBA:GO_Central.
GO; GO:1902660; P:negative regulation of glucose mediated signaling pathway; IBA:GO_Central.
GO; GO:0043949; P:regulation of cAMP-mediated signaling; IBA:GO_Central.
CDD; cd07735; class_II_PDE_MBL-fold; 1.
InterPro; IPR024225; cAMP-PdiesteraseII_CS.
InterPro; IPR000396; Pdiesterase2.
InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
PANTHER; PTHR28283; PTHR28283; 1.
Pfam; PF02112; PDEase_II; 1.
PIRSF; PIRSF000962; Cyc_nuc_PDEase; 1.
PRINTS; PR00388; PDIESTERASE2.
SUPFAM; SSF56281; SSF56281; 2.
PROSITE; PS00607; PDEASE_II; 1.
1: Evidence at protein level;
cAMP; cAMP-binding; cGMP; cGMP-binding; Complete proteome; Hydrolase;
Nucleotide-binding; Reference proteome; Secreted; Signal.
SIGNAL 1 17 {ECO:0000255}.
CHAIN 18 425 cAMP/cGMP-dependent 3',5'-cAMP/cGMP
phosphodiesterase 7.
/FTId=PRO_0000363968.
SEQUENCE 425 AA; 48505 MW; ADE7F8A5D17D3713 CRC64;
MKYLILILIF FIEINNGSRL INSGNLFSEL KDYYIPENLN YYSGGYSEQH CKDSSYITIP
LGVTGGLDEG SLSSFLLTKK GSSLFIGLDA GTVWQGVRRL TMLQDFNSVF NITYPPWATL
PEQRATWFIK NHIQGYLIGH SHLDHVGGLI VESAEDQLSP KKNELEVSQP EIYRGCIEMI
HKMGYVSDFP NITSIPDQKK PIIGINETLY SMATDLFNGF VWPSLPNYGR YSYYYLGNGN
QYSFKDLTPY ANKYVTKVQN DFPFNHLVKS FEICHDSLTS TAFILTDSQS GEQIVFFSDT
GISTTKCDWE FKILQVWRNI KIDKLKAVYI ESSFTNEVAD NVLFGHLRPK DIMKLMDSLL
ENSIQTSPPK TNLKHVKLII EHIKPQVGMN QYYLTSQRMV YQQLQEINNH GVKVIIPNQG
VPICL


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