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cGMP-dependent 3',5'-cyclic phosphodiesterase (EC 3.1.4.17) (Cyclic GMP-stimulated phosphodiesterase) (CGS-PDE) (cGSPDE)

 PDE2A_HUMAN             Reviewed;         941 AA.
O00408; B2R646; B3KRV5; E9PGI1; F6W5Z0; Q5J791; Q5J792; Q5J793;
Q6ZMR1;
15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
01-JUL-1997, sequence version 1.
27-SEP-2017, entry version 155.
RecName: Full=cGMP-dependent 3',5'-cyclic phosphodiesterase;
EC=3.1.4.17;
AltName: Full=Cyclic GMP-stimulated phosphodiesterase;
Short=CGS-PDE;
Short=cGSPDE;
Name=PDE2A;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM PDE2A3).
TISSUE=Fetal brain, and Hippocampus;
PubMed=9210593; DOI=10.1016/S0378-1119(97)00046-2;
Rosman G.J., Martins T.J., Sonnenburg W.K., Beavo J.A., Ferguson K.,
Loughney K.;
"Isolation and characterization of human cDNAs encoding a cGMP-
stimulated 3',5'-cyclic nucleotide phosphodiesterase.";
Gene 191:89-95(1997).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM PDE2A4), NUCLEOTIDE SEQUENCE
[MRNA] OF 1-27 (ISOFORM PDE2A1), AND NUCLEOTIDE SEQUENCE [MRNA] OF
1-55 (ISOFORM PDE2A2).
Bugaj-Gaweda B., De Vivo M., Wang D.;
"Human PDE2A1, PDE2A2 and PDE2A4.";
Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS PDE2A3; 5 AND 6).
TISSUE=Adrenal gland, Brain, and Tongue;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16554811; DOI=10.1038/nature04632;
Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F.,
Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E.,
FitzGerald M.G., Jaffe D.B., LaButti K., Nicol R., Park H.-S.,
Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W.,
Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S.,
Sakaki Y.;
"Human chromosome 11 DNA sequence and analysis including novel gene
identification.";
Nature 440:497-500(2006).
[5]
MYRISTOYLATION AT GLY-2, PALMITOYLATION AT CYS-5 AND CYS-11, AND
SUBCELLULAR LOCATION (ISOFORMS PDE2A1 AND PDE2A3).
PubMed=19632989; DOI=10.1074/jbc.M109.017194;
Russwurm C., Zoidl G., Koesling D., Russwurm M.;
"Dual acylation of PDE2A splice variant 3: targeting to synaptic
membranes.";
J. Biol. Chem. 284:25782-25790(2009).
[6]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
Mann M., Daub H.;
"Large-scale proteomics analysis of the human kinome.";
Mol. Cell. Proteomics 8:1751-1764(2009).
[7]
MYRISTOYLATION AT GLY-2.
PubMed=20213681; DOI=10.1002/pmic.200900783;
Suzuki T., Moriya K., Nagatoshi K., Ota Y., Ezure T., Ando E.,
Tsunasawa S., Utsumi T.;
"Strategy for comprehensive identification of human N-myristoylated
proteins using an insect cell-free protein synthesis system.";
Proteomics 10:1780-1793(2010).
[8]
FUNCTION (ISOFORM PDE2A2), AND SUBCELLULAR LOCATION (ISOFORM PDE2A2).
PubMed=21724846; DOI=10.1074/jbc.M111.266379;
Acin-Perez R., Russwurm M., Gunnewig K., Gertz M., Zoidl G., Ramos L.,
Buck J., Levin L.R., Rassow J., Manfredi G., Steegborn C.;
"A phosphodiesterase 2A isoform localized to mitochondria regulates
respiration.";
J. Biol. Chem. 286:30423-30432(2011).
[9]
FUNCTION.
PubMed=24705027; DOI=10.1016/j.cellsig.2014.03.031;
Hiramoto K., Murata T., Shimizu K., Morita H., Inui M.,
Manganiello V.C., Tagawa T., Arai N.;
"Role of phosphodiesterase 2 in growth and invasion of human malignant
melanoma cells.";
Cell. Signal. 26:1807-1817(2014).
[10]
SUBCELLULAR LOCATION.
PubMed=28463107; DOI=10.7554/eLife.21374;
Monterisi S., Lobo M.J., Livie C., Castle J.C., Weinberger M.,
Baillie G., Surdo N.C., Musheshe N., Stangherlin A., Gottlieb E.,
Maizels R., Bortolozzi M., Micaroni M., Zaccolo M.;
"PDE2A2 regulates mitochondria morphology and apoptotic cell death via
local modulation of cAMP/PKA signalling.";
Elife 6:0-0(2017).
[11]
X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 578-919 IN COMPLEX WITH
METAL IONS AND PHOSPHATE, AND FUNCTION.
PubMed=15938621; DOI=10.1021/bi047313h;
Iffland A., Kohls D., Low S., Luan J., Zhang Y., Kothe M., Cao Q.,
Kamath A.V., Ding Y.H., Ellenberger T.;
"Structural determinants for inhibitor specificity and selectivity in
PDE2A using the wheat germ in vitro translation system.";
Biochemistry 44:8312-8325(2005).
[12]
X-RAY CRYSTALLOGRAPHY (1.58 ANGSTROMS) OF 215-919 IN COMPLEX WITH
METAL IONS AND THE INHIBITOR IBMX, SUBUNIT, AND FUNCTION.
PubMed=19828435; DOI=10.1073/pnas.0907635106;
Pandit J., Forman M.D., Fennell K.F., Dillman K.S., Menniti F.S.;
"Mechanism for the allosteric regulation of phosphodiesterase 2A
deduced from the X-ray structure of a near full-length construct.";
Proc. Natl. Acad. Sci. U.S.A. 106:18225-18230(2009).
[13]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 578-919 IN COMPLEX WITH
INHIBITOR.
PubMed=23899287; DOI=10.1021/ja404449g;
Zhu J., Yang Q., Dai D., Huang Q.;
"X-ray crystal structure of phosphodiesterase 2 in complex with a
highly selective, nanomolar inhibitor reveals a binding-induced pocket
important for selectivity.";
J. Am. Chem. Soc. 135:11708-11711(2013).
-!- FUNCTION: Cyclic nucleotide phosphodiesterase with a dual-
specificity for the second messengers cAMP and cGMP, which are key
regulators of many important physiological processes. Plays an
important role in growth and invasion of malignant melanoma cells
(e.g. pseudomyxoma peritonei (PMP) cell line) (PubMed:24705027).
{ECO:0000269|PubMed:24705027}.
-!- FUNCTION: Isoform PDE2A2: Regulates mitochondrial cAMP levels and
respiration. Involved in the regulation of mitochondria
morphology/dynamics and apoptotic cell death via local modulation
of cAMP/PKA signaling in the mitochondrion, including the
monitoring of local cAMP levels at the outer mitochondrial
membrane and of PKA-dependent phosphorylation of DNM1L.
{ECO:0000250|UniProtKB:Q01062}.
-!- CATALYTIC ACTIVITY: Nucleoside 3',5'-cyclic phosphate + H(2)O =
nucleoside 5'-phosphate.
-!- COFACTOR:
Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
Evidence={ECO:0000250};
Note=Binds 2 divalent metal cations per subunit. Site 1 may
preferentially bind zinc ions, while site 2 has a preference for
magnesium and/or manganese ions. {ECO:0000250};
-!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:15938621,
ECO:0000269|PubMed:19828435, ECO:0000269|PubMed:23899287}.
-!- INTERACTION:
O00170:AIP; NbExp=6; IntAct=EBI-1785967, EBI-704197;
-!- SUBCELLULAR LOCATION: Isoform PDE2A3: Cell membrane
{ECO:0000269|PubMed:19632989}; Lipid-anchor
{ECO:0000269|PubMed:19632989}.
-!- SUBCELLULAR LOCATION: Isoform PDE2A2: Mitochondrion matrix
{ECO:0000269|PubMed:21724846}. Mitochondrion inner membrane
{ECO:0000269|PubMed:28463107}. Mitochondrion outer membrane
{ECO:0000269|PubMed:28463107}.
-!- SUBCELLULAR LOCATION: Isoform PDE2A1: Cytoplasm
{ECO:0000269|PubMed:19632989}.
-!- SUBCELLULAR LOCATION: Isoform 5: Mitochondrion {ECO:0000305}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=6;
Comment=Additional isoforms seem to exist. Experimental
confirmation may be lacking for some isoforms.;
Name=PDE2A3;
IsoId=O00408-1; Sequence=Displayed;
Name=PDE2A1;
IsoId=O00408-2; Sequence=VSP_055315;
Note=Soluble form.;
Name=PDE2A2;
IsoId=O00408-3; Sequence=VSP_055316;
Note=Contains a transit peptide at positions 1-17.;
Name=PDE2A4;
IsoId=O00408-4; Sequence=VSP_055317;
Name=5;
IsoId=O00408-5; Sequence=VSP_055316, VSP_055318;
Note=No experimental confirmation available.;
Name=6;
IsoId=O00408-6; Sequence=VSP_055315, VSP_055319, VSP_055320;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Expressed in brain and to a lesser extent in
heart, placenta, lung, skeletal muscle, kidney and pancreas.
-!- DOMAIN: GAF 1 functions as a dimerization domain, whereas GAF 2
binds cGMP, which causes activation of the catalytic activity of
the enzyme. {ECO:0000250}.
-!- MISCELLANEOUS: cGMP binds at an allosteric activator site.
{ECO:0000250}.
-!- SIMILARITY: Belongs to the cyclic nucleotide phosphodiesterase
family. PDE2 subfamily. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAS75515.1; Type=Frameshift; Positions=48; Evidence={ECO:0000305};
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EMBL; U67733; AAC51320.1; -; mRNA.
EMBL; AY495087; AAS75513.1; -; mRNA.
EMBL; AY495088; AAS75514.1; -; mRNA.
EMBL; AY495089; AAS75515.1; ALT_FRAME; mRNA.
EMBL; AK092278; BAG52517.1; -; mRNA.
EMBL; AK131525; BAD18664.1; -; mRNA.
EMBL; AK312434; BAG35343.1; -; mRNA.
EMBL; AP003065; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AP005019; -; NOT_ANNOTATED_CDS; Genomic_DNA.
CCDS; CCDS44670.1; -. [O00408-3]
CCDS; CCDS53678.1; -. [O00408-4]
CCDS; CCDS73345.1; -. [O00408-2]
CCDS; CCDS8216.1; -. [O00408-1]
RefSeq; NP_001137311.1; NM_001143839.3. [O00408-3]
RefSeq; NP_001139681.1; NM_001146209.2. [O00408-4]
RefSeq; NP_001230713.1; NM_001243784.1. [O00408-2]
RefSeq; NP_002590.1; NM_002599.4. [O00408-1]
UniGene; Hs.503163; -.
PDB; 1Z1L; X-ray; 1.70 A; A=578-919.
PDB; 3IBJ; X-ray; 3.02 A; A/B=215-900.
PDB; 3ITM; X-ray; 2.49 A; A/B/C/D=579-919.
PDB; 3ITU; X-ray; 1.58 A; A/B/C/D=579-919.
PDB; 4C1I; X-ray; 2.40 A; A/B/C/D=578-921.
PDB; 4D08; X-ray; 1.90 A; A/B/C/D=578-921.
PDB; 4D09; X-ray; 2.50 A; A/B/C/D=578-921.
PDB; 4HTX; X-ray; 1.90 A; A/B/C/D=578-919.
PDB; 4HTZ; X-ray; 2.00 A; A/B/C/D=578-919.
PDB; 4JIB; X-ray; 1.72 A; A/B/C/D=579-919.
PDB; 5TZ3; X-ray; 1.72 A; A/B/C/D=579-919.
PDB; 5TZA; X-ray; 1.70 A; A/B/C/D=579-919.
PDB; 5TZC; X-ray; 2.36 A; A/B/C/D=579-919.
PDB; 5TZH; X-ray; 1.60 A; A/B/C/D=579-919.
PDB; 5TZW; X-ray; 1.59 A; A/B/C/D=579-919.
PDB; 5TZX; X-ray; 1.90 A; A/B/C/D=579-919.
PDB; 5TZZ; X-ray; 1.60 A; A/B/C/D=579-919.
PDB; 5U00; X-ray; 1.41 A; A/B/C/D=579-919.
PDBsum; 1Z1L; -.
PDBsum; 3IBJ; -.
PDBsum; 3ITM; -.
PDBsum; 3ITU; -.
PDBsum; 4C1I; -.
PDBsum; 4D08; -.
PDBsum; 4D09; -.
PDBsum; 4HTX; -.
PDBsum; 4HTZ; -.
PDBsum; 4JIB; -.
PDBsum; 5TZ3; -.
PDBsum; 5TZA; -.
PDBsum; 5TZC; -.
PDBsum; 5TZH; -.
PDBsum; 5TZW; -.
PDBsum; 5TZX; -.
PDBsum; 5TZZ; -.
PDBsum; 5U00; -.
ProteinModelPortal; O00408; -.
SMR; O00408; -.
BioGrid; 111164; 3.
DIP; DIP-40269N; -.
ELM; O00408; -.
IntAct; O00408; 3.
STRING; 9606.ENSP00000334910; -.
BindingDB; O00408; -.
ChEMBL; CHEMBL2652; -.
DrugBank; DB07954; 3-isobutyl-1-methyl-7H-xanthine.
DrugBank; DB00201; Caffeine.
DrugBank; DB02315; Cyclic Guanosine Monophosphate.
DrugBank; DB05142; ND7001.
DrugBank; DB08811; Tofisopam.
GuidetoPHARMACOLOGY; 1297; -.
iPTMnet; O00408; -.
PhosphoSitePlus; O00408; -.
BioMuta; PDE2A; -.
MaxQB; O00408; -.
PaxDb; O00408; -.
PeptideAtlas; O00408; -.
PRIDE; O00408; -.
Ensembl; ENST00000334456; ENSP00000334910; ENSG00000186642. [O00408-1]
Ensembl; ENST00000376450; ENSP00000365633; ENSG00000186642. [O00408-5]
Ensembl; ENST00000444035; ENSP00000411657; ENSG00000186642. [O00408-2]
Ensembl; ENST00000540345; ENSP00000446399; ENSG00000186642. [O00408-4]
Ensembl; ENST00000544570; ENSP00000442256; ENSG00000186642. [O00408-3]
GeneID; 5138; -.
KEGG; hsa:5138; -.
UCSC; uc001osn.4; human. [O00408-1]
CTD; 5138; -.
DisGeNET; 5138; -.
EuPathDB; HostDB:ENSG00000186642.15; -.
GeneCards; PDE2A; -.
HGNC; HGNC:8777; PDE2A.
HPA; CAB009752; -.
HPA; HPA031192; -.
MIM; 602658; gene.
neXtProt; NX_O00408; -.
OpenTargets; ENSG00000186642; -.
PharmGKB; PA33125; -.
eggNOG; KOG3689; Eukaryota.
eggNOG; ENOG410XRI7; LUCA.
GeneTree; ENSGT00760000119066; -.
HOGENOM; HOG000007068; -.
HOVERGEN; HBG053540; -.
KO; K18283; -.
OMA; NREQWTK; -.
OrthoDB; EOG091G0L2F; -.
PhylomeDB; O00408; -.
TreeFam; TF316499; -.
BRENDA; 3.1.4.17; 2681.
Reactome; R-HSA-418457; cGMP effects.
Reactome; R-HSA-418555; G alpha (s) signalling events.
ChiTaRS; PDE2A; human.
EvolutionaryTrace; O00408; -.
GeneWiki; PDE2A; -.
GenomeRNAi; 5138; -.
PRO; PR:O00408; -.
Proteomes; UP000005640; Chromosome 11.
Bgee; ENSG00000186642; -.
CleanEx; HS_PDE2A; -.
ExpressionAtlas; O00408; baseline and differential.
Genevisible; O00408; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
GO; GO:0005743; C:mitochondrial inner membrane; IDA:UniProtKB.
GO; GO:0005759; C:mitochondrial matrix; ISS:UniProtKB.
GO; GO:0005741; C:mitochondrial outer membrane; IDA:UniProtKB.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0042734; C:presynaptic membrane; ISS:UniProtKB.
GO; GO:0004115; F:3',5'-cyclic-AMP phosphodiesterase activity; TAS:Reactome.
GO; GO:0047555; F:3',5'-cyclic-GMP phosphodiesterase activity; TAS:Reactome.
GO; GO:0005262; F:calcium channel activity; TAS:UniProtKB.
GO; GO:0030552; F:cAMP binding; IMP:UniProtKB.
GO; GO:0030553; F:cGMP binding; IDA:UniProtKB.
GO; GO:0004118; F:cGMP-stimulated cyclic-nucleotide phosphodiesterase activity; IDA:UniProtKB.
GO; GO:0004112; F:cyclic-nucleotide phosphodiesterase activity; IDA:UniProtKB.
GO; GO:0008144; F:drug binding; IDA:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB.
GO; GO:0030911; F:TPR domain binding; IPI:UniProtKB.
GO; GO:0006198; P:cAMP catabolic process; IDA:UniProtKB.
GO; GO:0019933; P:cAMP-mediated signaling; IMP:UniProtKB.
GO; GO:0071321; P:cellular response to cGMP; IDA:UniProtKB.
GO; GO:0035690; P:cellular response to drug; IMP:UniProtKB.
GO; GO:0097011; P:cellular response to granulocyte macrophage colony-stimulating factor stimulus; IDA:UniProtKB.
GO; GO:0036006; P:cellular response to macrophage colony-stimulating factor stimulus; IDA:UniProtKB.
GO; GO:0071260; P:cellular response to mechanical stimulus; ISS:UniProtKB.
GO; GO:0071560; P:cellular response to transforming growth factor beta stimulus; IEP:UniProtKB.
GO; GO:0046069; P:cGMP catabolic process; IDA:UniProtKB.
GO; GO:0019934; P:cGMP-mediated signaling; IMP:UniProtKB.
GO; GO:0061028; P:establishment of endothelial barrier; ISS:UniProtKB.
GO; GO:0008152; P:metabolic process; IDA:UniProtKB.
GO; GO:0030224; P:monocyte differentiation; IEP:UniProtKB.
GO; GO:0030818; P:negative regulation of cAMP biosynthetic process; ISS:UniProtKB.
GO; GO:0033159; P:negative regulation of protein import into nucleus, translocation; IDA:UniProtKB.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IDA:UniProtKB.
GO; GO:0043116; P:negative regulation of vascular permeability; IMP:UniProtKB.
GO; GO:0050729; P:positive regulation of inflammatory response; ISS:UniProtKB.
GO; GO:0043117; P:positive regulation of vascular permeability; IMP:UniProtKB.
GO; GO:0006626; P:protein targeting to mitochondrion; ISS:UniProtKB.
CDD; cd00077; HDc; 1.
Gene3D; 1.10.1300.10; -; 1.
Gene3D; 3.30.450.40; -; 2.
InterPro; IPR003018; GAF.
InterPro; IPR029016; GAF_dom-like.
InterPro; IPR003607; HD/PDEase_dom.
InterPro; IPR023088; PDEase.
InterPro; IPR002073; PDEase_catalytic_dom.
InterPro; IPR023174; PDEase_CS.
Pfam; PF01590; GAF; 1.
Pfam; PF13185; GAF_2; 1.
Pfam; PF00233; PDEase_I; 1.
PRINTS; PR00387; PDIESTERASE1.
SMART; SM00065; GAF; 2.
SMART; SM00471; HDc; 1.
SUPFAM; SSF55781; SSF55781; 3.
PROSITE; PS00126; PDEASE_I; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; cAMP; Cell membrane; cGMP;
cGMP-binding; Complete proteome; Cytoplasm; Hydrolase; Lipoprotein;
Membrane; Metal-binding; Mitochondrion; Mitochondrion inner membrane;
Mitochondrion outer membrane; Myristate; Nucleotide-binding;
Palmitate; Polymorphism; Reference proteome; Repeat.
INIT_MET 1 1 Removed.
CHAIN 2 941 cGMP-dependent 3',5'-cyclic
phosphodiesterase.
/FTId=PRO_0000198796.
DOMAIN 241 377 GAF 1. {ECO:0000255}.
DOMAIN 409 548 GAF 2. {ECO:0000255}.
REGION 633 891 Catalytic. {ECO:0000250}.
REGION 656 660 Substrate binding.
ACT_SITE 656 656 Proton donor. {ECO:0000250}.
METAL 660 660 Divalent metal cation 1.
{ECO:0000244|PDB:1Z1L,
ECO:0000244|PDB:3IBJ,
ECO:0000244|PDB:3ITM,
ECO:0000244|PDB:3ITU,
ECO:0000244|PDB:4C1I,
ECO:0000244|PDB:4D08,
ECO:0000244|PDB:4D09,
ECO:0000244|PDB:4HTX,
ECO:0000244|PDB:4HTZ,
ECO:0000244|PDB:4JIB,
ECO:0000244|PDB:5TZ3,
ECO:0000244|PDB:5TZA,
ECO:0000244|PDB:5TZC,
ECO:0000244|PDB:5TZH,
ECO:0000244|PDB:5TZW,
ECO:0000244|PDB:5TZX,
ECO:0000244|PDB:5TZZ,
ECO:0000244|PDB:5U00,
ECO:0000269|PubMed:15938621,
ECO:0000269|PubMed:19828435,
ECO:0000269|PubMed:23899287}.
METAL 696 696 Divalent metal cation 1.
{ECO:0000244|PDB:1Z1L,
ECO:0000244|PDB:3ITM,
ECO:0000244|PDB:3ITU,
ECO:0000244|PDB:4C1I,
ECO:0000244|PDB:4D08,
ECO:0000244|PDB:4D09,
ECO:0000244|PDB:4HTX,
ECO:0000244|PDB:4HTZ,
ECO:0000244|PDB:4JIB,
ECO:0000244|PDB:5TZ3,
ECO:0000244|PDB:5TZA,
ECO:0000244|PDB:5TZC,
ECO:0000244|PDB:5TZH,
ECO:0000244|PDB:5TZW,
ECO:0000244|PDB:5TZX,
ECO:0000244|PDB:5TZZ,
ECO:0000244|PDB:5U00,
ECO:0000269|PubMed:15938621,
ECO:0000269|PubMed:19828435,
ECO:0000269|PubMed:23899287}.
METAL 697 697 Divalent metal cation 1.
{ECO:0000244|PDB:1Z1L,
ECO:0000244|PDB:3IBJ,
ECO:0000244|PDB:3ITM,
ECO:0000244|PDB:3ITU,
ECO:0000244|PDB:4C1I,
ECO:0000244|PDB:4D08,
ECO:0000244|PDB:4D09,
ECO:0000244|PDB:4HTX,
ECO:0000244|PDB:4HTZ,
ECO:0000244|PDB:4JIB,
ECO:0000244|PDB:5TZ3,
ECO:0000244|PDB:5TZA,
ECO:0000244|PDB:5TZC,
ECO:0000244|PDB:5TZH,
ECO:0000244|PDB:5TZW,
ECO:0000244|PDB:5TZX,
ECO:0000244|PDB:5TZZ,
ECO:0000244|PDB:5U00,
ECO:0000269|PubMed:15938621,
ECO:0000269|PubMed:19828435,
ECO:0000269|PubMed:23899287}.
METAL 697 697 Divalent metal cation 2.
{ECO:0000244|PDB:1Z1L,
ECO:0000244|PDB:3IBJ,
ECO:0000244|PDB:3ITM,
ECO:0000244|PDB:3ITU,
ECO:0000244|PDB:4C1I,
ECO:0000244|PDB:4D08,
ECO:0000244|PDB:4D09,
ECO:0000244|PDB:4HTX,
ECO:0000244|PDB:4HTZ,
ECO:0000244|PDB:4JIB,
ECO:0000244|PDB:5TZ3,
ECO:0000244|PDB:5TZA,
ECO:0000244|PDB:5TZC,
ECO:0000244|PDB:5TZH,
ECO:0000244|PDB:5TZW,
ECO:0000244|PDB:5TZX,
ECO:0000244|PDB:5TZZ,
ECO:0000244|PDB:5U00,
ECO:0000269|PubMed:15938621,
ECO:0000269|PubMed:19828435,
ECO:0000269|PubMed:23899287}.
METAL 808 808 Divalent metal cation 1.
{ECO:0000244|PDB:1Z1L,
ECO:0000244|PDB:3IBJ,
ECO:0000244|PDB:3ITM,
ECO:0000244|PDB:3ITU,
ECO:0000244|PDB:4C1I,
ECO:0000244|PDB:4D08,
ECO:0000244|PDB:4D09,
ECO:0000244|PDB:4HTX,
ECO:0000244|PDB:4HTZ,
ECO:0000244|PDB:4JIB,
ECO:0000244|PDB:5TZ3,
ECO:0000244|PDB:5TZA,
ECO:0000244|PDB:5TZC,
ECO:0000244|PDB:5TZH,
ECO:0000244|PDB:5TZW,
ECO:0000244|PDB:5TZX,
ECO:0000244|PDB:5TZZ,
ECO:0000244|PDB:5U00,
ECO:0000269|PubMed:15938621,
ECO:0000269|PubMed:19828435,
ECO:0000269|PubMed:23899287}.
BINDING 431 431 cGMP. {ECO:0000250|UniProtKB:Q922S4}.
BINDING 446 446 cGMP. {ECO:0000250|UniProtKB:Q922S4}.
BINDING 499 499 cGMP. {ECO:0000250|UniProtKB:Q922S4}.
BINDING 697 697 Substrate.
BINDING 808 808 Substrate.
LIPID 2 2 N-myristoyl glycine.
{ECO:0000269|PubMed:19632989,
ECO:0000269|PubMed:20213681}.
LIPID 5 5 S-palmitoyl cysteine.
{ECO:0000305|PubMed:19632989}.
LIPID 11 11 S-palmitoyl cysteine.
{ECO:0000305|PubMed:19632989}.
VAR_SEQ 1 48 MGQACGHSILCRSQQYPAARPAEPRGQQVFLKPDEPPPPPQ
PCADSLQ -> MRRQPAASLDPLAKEPGPPGSRDDRLE
(in isoform PDE2A1 and isoform 6).
{ECO:0000303|PubMed:14702039,
ECO:0000303|Ref.2}.
/FTId=VSP_055315.
VAR_SEQ 1 24 MGQACGHSILCRSQQYPAARPAEP -> MVLVLHHILIAVV
QFLR (in isoform PDE2A2 and isoform 5).
{ECO:0000303|PubMed:14702039,
ECO:0000303|Ref.2}.
/FTId=VSP_055316.
VAR_SEQ 1 24 MGQACGHSILCRSQQYPAARPAEP -> MKKQRIQEGKSLA
HR (in isoform PDE2A4).
{ECO:0000303|Ref.2}.
/FTId=VSP_055317.
VAR_SEQ 109 357 Missing (in isoform 5).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_055318.
VAR_SEQ 750 807 SRKDYQRMLDLMRDIILATDLAHHLRIFKDLQKMAEVGYDR
NNKQHHRLLLCLLMTSC -> PLRTTTILMVGLGPGGYRGP
RKKLPEGQLSALQRGALGRSRMGLMGRRDPRTGRQAQV
(in isoform 6).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_055319.
VAR_SEQ 808 941 Missing (in isoform 6).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_055320.
VARIANT 224 224 T -> I (in dbSNP:rs341047).
/FTId=VAR_024170.
CONFLICT 38 38 P -> L (in Ref. 2; AAS75513).
{ECO:0000305}.
CONFLICT 99 99 H -> R (in Ref. 3; BAG35343).
{ECO:0000305}.
CONFLICT 213 213 T -> A (in Ref. 2; AAS75513).
{ECO:0000305}.
CONFLICT 664 664 V -> A (in Ref. 2; AAS75513).
{ECO:0000305}.
HELIX 226 236 {ECO:0000244|PDB:3IBJ}.
HELIX 242 256 {ECO:0000244|PDB:3IBJ}.
STRAND 262 267 {ECO:0000244|PDB:3IBJ}.
STRAND 271 279 {ECO:0000244|PDB:3IBJ}.
STRAND 282 291 {ECO:0000244|PDB:3IBJ}.
STRAND 294 296 {ECO:0000244|PDB:3IBJ}.
HELIX 297 302 {ECO:0000244|PDB:3IBJ}.
HELIX 308 310 {ECO:0000244|PDB:3IBJ}.
HELIX 313 323 {ECO:0000244|PDB:3IBJ}.
STRAND 330 336 {ECO:0000244|PDB:3IBJ}.
STRAND 338 340 {ECO:0000244|PDB:3IBJ}.
STRAND 342 355 {ECO:0000244|PDB:3IBJ}.
HELIX 362 403 {ECO:0000244|PDB:3IBJ}.
TURN 410 412 {ECO:0000244|PDB:3IBJ}.
HELIX 413 425 {ECO:0000244|PDB:3IBJ}.
STRAND 427 435 {ECO:0000244|PDB:3IBJ}.
STRAND 437 443 {ECO:0000244|PDB:3IBJ}.
STRAND 446 448 {ECO:0000244|PDB:3IBJ}.
STRAND 456 460 {ECO:0000244|PDB:3IBJ}.
HELIX 464 472 {ECO:0000244|PDB:3IBJ}.
STRAND 476 479 {ECO:0000244|PDB:3IBJ}.
STRAND 502 506 {ECO:0000244|PDB:3IBJ}.
STRAND 510 512 {ECO:0000244|PDB:3IBJ}.
STRAND 516 528 {ECO:0000244|PDB:3IBJ}.
TURN 531 534 {ECO:0000244|PDB:3IBJ}.
HELIX 535 570 {ECO:0000244|PDB:3IBJ}.
TURN 571 573 {ECO:0000244|PDB:3IBJ}.
HELIX 579 587 {ECO:0000244|PDB:5U00}.
HELIX 593 596 {ECO:0000244|PDB:5U00}.
TURN 598 601 {ECO:0000244|PDB:5U00}.
HELIX 607 609 {ECO:0000244|PDB:5U00}.
HELIX 612 614 {ECO:0000244|PDB:5U00}.
HELIX 615 625 {ECO:0000244|PDB:5U00}.
HELIX 628 631 {ECO:0000244|PDB:5U00}.
HELIX 636 648 {ECO:0000244|PDB:5U00}.
STRAND 654 657 {ECO:0000244|PDB:5U00}.
HELIX 658 675 {ECO:0000244|PDB:5U00}.
HELIX 677 679 {ECO:0000244|PDB:5U00}.
HELIX 683 695 {ECO:0000244|PDB:5U00}.
TURN 696 699 {ECO:0000244|PDB:5U00}.
HELIX 705 710 {ECO:0000244|PDB:5U00}.
HELIX 714 719 {ECO:0000244|PDB:5U00}.
TURN 720 722 {ECO:0000244|PDB:5U00}.
HELIX 725 738 {ECO:0000244|PDB:5U00}.
TURN 741 743 {ECO:0000244|PDB:3IBJ}.
TURN 745 748 {ECO:0000244|PDB:5U00}.
HELIX 751 766 {ECO:0000244|PDB:5U00}.
HELIX 770 786 {ECO:0000244|PDB:5U00}.
HELIX 793 808 {ECO:0000244|PDB:5U00}.
HELIX 810 813 {ECO:0000244|PDB:5U00}.
HELIX 816 839 {ECO:0000244|PDB:5U00}.
HELIX 846 848 {ECO:0000244|PDB:5U00}.
TURN 850 852 {ECO:0000244|PDB:5U00}.
HELIX 855 865 {ECO:0000244|PDB:5U00}.
HELIX 867 877 {ECO:0000244|PDB:5U00}.
HELIX 879 881 {ECO:0000244|PDB:5U00}.
HELIX 882 898 {ECO:0000244|PDB:5U00}.
HELIX 899 902 {ECO:0000244|PDB:5U00}.
STRAND 904 906 {ECO:0000244|PDB:1Z1L}.
HELIX 914 916 {ECO:0000244|PDB:5TZW}.
SEQUENCE 941 AA; 105717 MW; 9797609B487FD64E CRC64;
MGQACGHSIL CRSQQYPAAR PAEPRGQQVF LKPDEPPPPP QPCADSLQDA LLSLGSVIDI
SGLQRAVKEA LSAVLPRVET VYTYLLDGES QLVCEDPPHE LPQEGKVREA IISQKRLGCN
GLGFSDLPGK PLARLVAPLA PDTQVLVMPL ADKEAGAVAA VILVHCGQLS DNEEWSLQAV
EKHTLVALRR VQVLQQRGPR EAPRAVQNPP EGTAEDQKGG AAYTDRDRKI LQLCGELYDL
DASSLQLKVL QYLQQETRAS RCCLLLVSED NLQLSCKVIG DKVLGEEVSF PLTGCLGQVV
EDKKSIQLKD LTSEDVQQLQ SMLGCELQAM LCVPVISRAT DQVVALACAF NKLEGDLFTD
EDEHVIQHCF HYTSTVLTST LAFQKEQKLK CECQALLQVA KNLFTHLDDV SVLLQEIITE
ARNLSNAEIC SVFLLDQNEL VAKVFDGGVV DDESYEIRIP ADQGIAGHVA TTGQILNIPD
AYAHPLFYRG VDDSTGFRTR NILCFPIKNE NQEVIGVAEL VNKINGPWFS KFDEDLATAF
SIYCGISIAH SLLYKKVNEA QYRSHLANEM MMYHMKVSDD EYTKLLHDGI QPVAAIDSNF
ASFTYTPRSL PEDDTSMAIL SMLQDMNFIN NYKIDCPTLA RFCLMVKKGY RDPPYHNWMH
AFSVSHFCYL LYKNLELTNY LEDIEIFALF ISCMCHDLDH RGTNNSFQVA SKSVLAALYS
SEGSVMERHH FAQAIAILNT HGCNIFDHFS RKDYQRMLDL MRDIILATDL AHHLRIFKDL
QKMAEVGYDR NNKQHHRLLL CLLMTSCDLS DQTKGWKTTR KIAELIYKEF FSQGDLEKAM
GNRPMEMMDR EKAYIPELQI SFMEHIAMPI YKLLQDLFPK AAELYERVAS NREHWTKVSH
KFTIRGLPSN NSLDFLDEEY EVPDLDGTRA PINGCCSLDA E


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