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PDE7_DICDI
ID   PDE7_DICDI              Reviewed;         425 AA.
AC   Q54HY0;
DT   10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   25-MAY-2022, entry version 82.
DE   RecName: Full=cAMP/cGMP-dependent 3',5'-cAMP/cGMP phosphodiesterase 7;
DE            EC=3.1.4.35 {ECO:0000269|PubMed:17040207};
DE            EC=3.1.4.53 {ECO:0000269|PubMed:17040207};
DE   AltName: Full=Phosphodiesterase 7;
DE            Short=ddPDE7 {ECO:0000303|PubMed:17040207};
DE   Flags: Precursor;
GN   Name=pde7; ORFNames=DDB_G0289145;
OS   Dictyostelium discoideum (Slime mold).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=15875012; DOI=10.1038/nature03481;
RA   Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA   Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA   Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA   Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA   Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA   Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA   Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA   Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA   Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA   Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA   Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA   Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA   Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA   Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA   Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA   Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA   Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT   "The genome of the social amoeba Dictyostelium discoideum.";
RL   Nature 435:43-57(2005).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY
RP   REGULATION, AND SUBCELLULAR LOCATION.
RX   PubMed=17040207; DOI=10.1042/bj20061153;
RA   Bader S., Kortholt A., Van Haastert P.J.M.;
RT   "Seven Dictyostelium discoideum phosphodiesterases degrade three pools of
RT   cAMP and cGMP.";
RL   Biochem. J. 402:153-161(2007).
RN   [3]
RP   INDUCTION [LARGE SCALE ANALYSIS].
RX   PubMed=18559084; DOI=10.1186/1471-2164-9-291;
RA   Sillo A., Bloomfield G., Balest A., Balbo A., Pergolizzi B., Peracino B.,
RA   Skelton J., Ivens A., Bozzaro S.;
RT   "Genome-wide transcriptional changes induced by phagocytosis or growth on
RT   bacteria in Dictyostelium.";
RL   BMC Genomics 9:291-291(2008).
CC   -!- FUNCTION: Phosphodiesterase with dual cAMP/cGMP specificity. However,
CC       displays a preference for cAMP over cGMP. Seems to regulate cAMP/cGMP
CC       concentration especially during cell aggregation.
CC       {ECO:0000269|PubMed:17040207}.
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:17040207};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25278;
CC         Evidence={ECO:0000269|PubMed:17040207};
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:17040207};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16958;
CC         Evidence={ECO:0000269|PubMed:17040207};
CC   -!- ACTIVITY REGULATION: Inhibited by dithiotreitol (DTT).
CC       {ECO:0000269|PubMed:17040207}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=12.5 uM for cAMP {ECO:0000269|PubMed:17040207};
CC         KM=36 uM for cGMP {ECO:0000269|PubMed:17040207};
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space
CC       {ECO:0000269|PubMed:17040207}. Cell surface
CC       {ECO:0000269|PubMed:17040207}.
CC   -!- INDUCTION: Down-regulated by growth on bacteria.
CC       {ECO:0000269|PubMed:18559084}.
CC   -!- SIMILARITY: Belongs to the cyclic nucleotide phosphodiesterase class-II
CC       family. {ECO:0000305}.
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DR   EMBL; AAFI02000130; EAL62880.1; -; Genomic_DNA.
DR   RefSeq; XP_636383.1; XM_631291.1.
DR   AlphaFoldDB; Q54HY0; -.
DR   SMR; Q54HY0; -.
DR   STRING; 44689.DDB0238626; -.
DR   PaxDb; Q54HY0; -.
DR   EnsemblProtists; EAL62880; EAL62880; DDB_G0289145.
DR   GeneID; 8626984; -.
DR   KEGG; ddi:DDB_G0289145; -.
DR   dictyBase; DDB_G0289145; pde7.
DR   HOGENOM; CLU_606124_0_0_1; -.
DR   InParanoid; Q54HY0; -.
DR   OMA; ATWFIKN; -.
DR   PhylomeDB; Q54HY0; -.
DR   SABIO-RK; Q54HY0; -.
DR   PRO; PR:Q54HY0; -.
DR   Proteomes; UP000002195; Chromosome 5.
DR   GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
DR   GO; GO:0005576; C:extracellular region; IDA:dictyBase.
DR   GO; GO:0005615; C:extracellular space; IEA:UniProtKB-SubCell.
DR   GO; GO:0004115; F:3',5'-cyclic-AMP phosphodiesterase activity; IGI:dictyBase.
DR   GO; GO:0047555; F:3',5'-cyclic-GMP phosphodiesterase activity; IGI:dictyBase.
DR   GO; GO:0030552; F:cAMP binding; IEA:UniProtKB-KW.
DR   GO; GO:0030553; F:cGMP binding; IEA:UniProtKB-KW.
DR   GO; GO:0006198; P:cAMP catabolic process; IGI:dictyBase.
DR   GO; GO:0046069; P:cGMP catabolic process; IGI:dictyBase.
DR   GO; GO:1902660; P:negative regulation of glucose mediated signaling pathway; IBA:GO_Central.
DR   CDD; cd07735; class_II_PDE_MBL-fold; 1.
DR   Gene3D; 3.60.15.10; -; 1.
DR   InterPro; IPR024225; cAMP-PdiesteraseII_CS.
DR   InterPro; IPR000396; Pdiesterase2.
DR   InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
DR   PANTHER; PTHR28283; PTHR28283; 2.
DR   Pfam; PF02112; PDEase_II; 1.
DR   PIRSF; PIRSF000962; Cyc_nuc_PDEase; 1.
DR   PRINTS; PR00388; PDIESTERASE2.
DR   SUPFAM; SSF56281; SSF56281; 1.
DR   PROSITE; PS00607; PDEASE_II; 1.
PE   1: Evidence at protein level;
KW   cAMP; cAMP-binding; cGMP; cGMP-binding; Hydrolase; Nucleotide-binding;
KW   Reference proteome; Secreted; Signal.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000255"
FT   CHAIN           18..425
FT                   /note="cAMP/cGMP-dependent 3',5'-cAMP/cGMP
FT                   phosphodiesterase 7"
FT                   /id="PRO_0000363968"
SQ   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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