Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-9606-01068
Entry Name
UniProt Accession
Theoretical PI
5.21
Molecular Weight
105716.9
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
cGMP-dependent 3',5'-cyclic phosphodiesterase
Protein Synonyms/Alias
3.1.4.17; Cyclic GMP-stimulated phosphodiesterase; CGS-PDE; cGSPDE;
Gene Name
PDE2A
Gene Synonyms/Alias
Created Date
15-JUL-1998
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
2
Canonical
******MGQACGHSI
[1][2]
N-Myristoylation
5
Canonical
***MGQACGHSILCR
[1]
S-Palmitoylation
11
Canonical
ACGHSILCRSQQYPA
[1]
S-Palmitoylation
Organism
Homo sapiens (Human)
NCBI Taxa ID
9606
Reference
[1] Russwurm C, Zoidl G, Koesling D, Russwurm M. Dual acylation of PDE2A splicevariant 3: targeting to synaptic membranes. J Biol Chem. 2009 Sep18;284(38):25782-90. doi: 10.1074/jbc.M109.017194. Epub 2009 Jul 24.[PMID:19632989]
[2] Suzuki T, Moriya K, Nagatoshi K, Ota Y, Ezure T, Ando E, Tsunasawa S, UtsumiT. Strategy for comprehensive identification of human N-myristoylated proteinsusing an insect cell-free protein synthesis system. Proteomics. 2010May;10(9):1780-93. doi: 10.1002/pmic.200900783.[PMID:20213681]
Functional Description
Cyclic nucleotide phosphodiesterase with a dual- specificity for the second messengers cAMP and cGMP, which are key regulators of many important physiological processes.
Sequence Annotation
Domain: 241 377 GAF 1.
Domain: 409 548 GAF 2.
Region: 633 891 Catalytic.
Region: 656 660 Substrate binding.
Active site: 656 656 Proton donor.
Metal binding site: 660 660 Divalent metal cation 1.
Metal binding site: 696 696 Divalent metal cation 1.
Metal binding site: 697 697 Divalent metal cation 1.
Metal binding site: 697 697 Divalent metal cation 2.
Metal binding site: 808 808 Divalent metal cation 1.
Binding site: 431 431 cGMP.
Binding site: 446 446 cGMP.
Binding site: 499 499 cGMP.
Binding site: 697 697 Substrate.
Binding site: 808 808 Substrate.
Protein Length
941 AA.
Protein Sequence
(Canonical)
MGQACGHSIL CRSQQYPAAR PAEPRGQQVF LKPDEPPPPP QPCADSLQDA LLSLGSVIDI  60
SGLQRAVKEA LSAVLPRVET VYTYLLDGES QLVCEDPPHE LPQEGKVREA IISQKRLGCN  120
GLGFSDLPGK PLARLVAPLA PDTQVLVMPL ADKEAGAVAA VILVHCGQLS DNEEWSLQAV  180
EKHTLVALRR VQVLQQRGPR EAPRAVQNPP EGTAEDQKGG AAYTDRDRKI LQLCGELYDL  240
DASSLQLKVL QYLQQETRAS RCCLLLVSED NLQLSCKVIG DKVLGEEVSF PLTGCLGQVV  300
EDKKSIQLKD LTSEDVQQLQ SMLGCELQAM LCVPVISRAT DQVVALACAF NKLEGDLFTD  360
EDEHVIQHCF HYTSTVLTST LAFQKEQKLK CECQALLQVA KNLFTHLDDV SVLLQEIITE  420
ARNLSNAEIC SVFLLDQNEL VAKVFDGGVV DDESYEIRIP ADQGIAGHVA TTGQILNIPD  480
AYAHPLFYRG VDDSTGFRTR NILCFPIKNE NQEVIGVAEL VNKINGPWFS KFDEDLATAF  540
SIYCGISIAH SLLYKKVNEA QYRSHLANEM MMYHMKVSDD EYTKLLHDGI QPVAAIDSNF  600
ASFTYTPRSL PEDDTSMAIL SMLQDMNFIN NYKIDCPTLA RFCLMVKKGY RDPPYHNWMH  660
AFSVSHFCYL LYKNLELTNY LEDIEIFALF ISCMCHDLDH RGTNNSFQVA SKSVLAALYS  720
SEGSVMERHH FAQAIAILNT HGCNIFDHFS RKDYQRMLDL MRDIILATDL AHHLRIFKDL  780
QKMAEVGYDR NNKQHHRLLL CLLMTSCDLS DQTKGWKTTR KIAELIYKEF FSQGDLEKAM  840
GNRPMEMMDR EKAYIPELQI SFMEHIAMPI YKLLQDLFPK AAELYERVAS NREHWTKVSH  900
KFTIRGLPSN NSLDFLDEEY EVPDLDGTRA PINGCCSLDA E                      941
MGQACGHSIL CRSQQYPAAR PAEPRGQQVF LKPDEPPPPP QPCADSLQDA LLSLGSVIDI  60
SGLQRAVKEA LSAVLPRVET VYTYLLDGES QLVCEDPPHE LPQEGKVREA IISQKRLGCN  120
GLGFSDLPGK PLARLVAPLA PDTQVLVMPL ADKEAGAVAA VILVHCGQLS DNEEWSLQAV  180
EKHTLVALRR VQVLQQRGPR EAPRAVQNPP EGTAEDQKGG AAYTDRDRKI LQLCGELYDL  240
DASSLQLKVL QYLQQETRAS RCCLLLVSED NLQLSCKVIG DKVLGEEVSF PLTGCLGQVV  300
EDKKSIQLKD LTSEDVQQLQ SMLGCELQAM LCVPVISRAT DQVVALACAF NKLEGDLFTD  360
EDEHVIQHCF HYTSTVLTST LAFQKEQKLK CECQALLQVA KNLFTHLDDV SVLLQEIITE  420
ARNLSNAEIC SVFLLDQNEL VAKVFDGGVV DDESYEIRIP ADQGIAGHVA TTGQILNIPD  480
AYAHPLFYRG VDDSTGFRTR NILCFPIKNE NQEVIGVAEL VNKINGPWFS KFDEDLATAF  540
SIYCGISIAH SLLYKKVNEA QYRSHLANEM MMYHMKVSDD EYTKLLHDGI QPVAAIDSNF  600
ASFTYTPRSL PEDDTSMAIL SMLQDMNFIN NYKIDCPTLA RFCLMVKKGY RDPPYHNWMH  660
AFSVSHFCYL LYKNLELTNY LEDIEIFALF ISCMCHDLDH RGTNNSFQVA SKSVLAALYS  720
SEGSVMERHH FAQAIAILNT HGCNIFDHFS RKDYQRMLDL MRDIILATDL AHHLRIFKDL  780
QKMAEVGYDR NNKQHHRLLL CLLMTSCDLS DQTKGWKTTR KIAELIYKEF FSQGDLEKAM  840
GNRPMEMMDR EKAYIPELQI SFMEHIAMPI YKLLQDLFPK AAELYERVAS NREHWTKVSH  900
KFTIRGLPSN NSLDFLDEEY EVPDLDGTRA PINGCCSLDA E                      941
FASTA
(Canonical)
>LipidDB-9606-01068|O00408
MGQACGHSILCRSQQYPAARPAEPRGQQVFLKPDEPPPPPQPCADSLQDALLSLGSVIDI
SGLQRAVKEALSAVLPRVETVYTYLLDGESQLVCEDPPHELPQEGKVREAIISQKRLGCN
GLGFSDLPGKPLARLVAPLAPDTQVLVMPLADKEAGAVAAVILVHCGQLSDNEEWSLQAV
EKHTLVALRRVQVLQQRGPREAPRAVQNPPEGTAEDQKGGAAYTDRDRKILQLCGELYDL
DASSLQLKVLQYLQQETRASRCCLLLVSEDNLQLSCKVIGDKVLGEEVSFPLTGCLGQVV
EDKKSIQLKDLTSEDVQQLQSMLGCELQAMLCVPVISRATDQVVALACAFNKLEGDLFTD
EDEHVIQHCFHYTSTVLTSTLAFQKEQKLKCECQALLQVAKNLFTHLDDVSVLLQEIITE
ARNLSNAEICSVFLLDQNELVAKVFDGGVVDDESYEIRIPADQGIAGHVATTGQILNIPD
AYAHPLFYRGVDDSTGFRTRNILCFPIKNENQEVIGVAELVNKINGPWFSKFDEDLATAF
SIYCGISIAHSLLYKKVNEAQYRSHLANEMMMYHMKVSDDEYTKLLHDGIQPVAAIDSNF
ASFTYTPRSLPEDDTSMAILSMLQDMNFINNYKIDCPTLARFCLMVKKGYRDPPYHNWMH
AFSVSHFCYLLYKNLELTNYLEDIEIFALFISCMCHDLDHRGTNNSFQVASKSVLAALYS
SEGSVMERHHFAQAIAILNTHGCNIFDHFSRKDYQRMLDLMRDIILATDLAHHLRIFKDL
QKMAEVGYDRNNKQHHRLLLCLLMTSCDLSDQTKGWKTTRKIAELIYKEFFSQGDLEKAM
GNRPMEMMDREKAYIPELQISFMEHIAMPIYKLLQDLFPKAAELYERVASNREHWTKVSH
KFTIRGLPSNNSLDFLDEEYEVPDLDGTRAPINGCCSLDAE
MGQACGHSILCRSQQYPAARPAEPRGQQVFLKPDEPPPPPQPCADSLQDALLSLGSVIDI
SGLQRAVKEALSAVLPRVETVYTYLLDGESQLVCEDPPHELPQEGKVREAIISQKRLGCN
GLGFSDLPGKPLARLVAPLAPDTQVLVMPLADKEAGAVAAVILVHCGQLSDNEEWSLQAV
EKHTLVALRRVQVLQQRGPREAPRAVQNPPEGTAEDQKGGAAYTDRDRKILQLCGELYDL
DASSLQLKVLQYLQQETRASRCCLLLVSEDNLQLSCKVIGDKVLGEEVSFPLTGCLGQVV
EDKKSIQLKDLTSEDVQQLQSMLGCELQAMLCVPVISRATDQVVALACAFNKLEGDLFTD
EDEHVIQHCFHYTSTVLTSTLAFQKEQKLKCECQALLQVAKNLFTHLDDVSVLLQEIITE
ARNLSNAEICSVFLLDQNELVAKVFDGGVVDDESYEIRIPADQGIAGHVATTGQILNIPD
AYAHPLFYRGVDDSTGFRTRNILCFPIKNENQEVIGVAELVNKINGPWFSKFDEDLATAF
SIYCGISIAHSLLYKKVNEAQYRSHLANEMMMYHMKVSDDEYTKLLHDGIQPVAAIDSNF
ASFTYTPRSLPEDDTSMAILSMLQDMNFINNYKIDCPTLARFCLMVKKGYRDPPYHNWMH
AFSVSHFCYLLYKNLELTNYLEDIEIFALFISCMCHDLDHRGTNNSFQVASKSVLAALYS
SEGSVMERHHFAQAIAILNTHGCNIFDHFSRKDYQRMLDLMRDIILATDLAHHLRIFKDL
QKMAEVGYDRNNKQHHRLLLCLLMTSCDLSDQTKGWKTTRKIAELIYKEFFSQGDLEKAM
GNRPMEMMDREKAYIPELQISFMEHIAMPIYKLLQDLFPKAAELYERVASNREHWTKVSH
KFTIRGLPSNNSLDFLDEEYEVPDLDGTRAPINGCCSLDAE
Gene Ontology
GO:0030424; C:axon; IEA:Ensembl
GO:0005737; C:cytoplasm; IDA:UniProtKB
GO:0005829; C:cytosol; IDA:UniProtKB
GO:0030425; C:dendrite; IEA:Ensembl
GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB
GO:0005794; C:Golgi apparatus; ISS:UniProtKB
GO:0005759; C:mitochondrial matrix; ISS:UniProtKB
GO:0005634; C:nucleus; IDA:UniProtKB
GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB
GO:0005886; C:plasma membrane; IDA:UniProtKB
GO:0042734; C:presynaptic membrane; ISS:UniProtKB
GO:0005262; F:calcium channel activity; TAS:UniProtKB
GO:0030552; F:cAMP binding; IMP:UniProtKB
GO:0030553; F:cGMP binding; IDA:UniProtKB
GO:0004118; F:cGMP-stimulated cyclic-nucleotide phosphodiesterase activity; IDA:UniProtKB
GO:0004112; F:cyclic-nucleotide phosphodiesterase activity; IDA:UniProtKB
GO:0008144; F:drug binding; IDA:UniProtKB
GO:0046872; F:metal ion binding; IEA:UniProtKB-KW
GO:0042803; F:protein homodimerization activity; IPI:UniProtKB
GO:0030911; F:TPR domain binding; IPI:UniProtKB
GO:0007596; P:blood coagulation; TAS:Reactome
GO:0070588; P:calcium ion transmembrane transport; TAS:GOC
GO:0006198; P:cAMP catabolic process; IDA:UniProtKB
GO:0019933; P:cAMP-mediated signaling; IMP:UniProtKB
GO:0071321; P:cellular response to cGMP; IDA:UniProtKB
GO:0035690; P:cellular response to drug; IEP:UniProtKB
GO:0097011; P:cellular response to granulocyte macrophage colony-stimulating factor stimulus; IDA:UniProtKB
GO:0036006; P:cellular response to macrophage colony-stimulating factor stimulus; IDA:UniProtKB
GO:0071260; P:cellular response to mechanical stimulus; ISS:UniProtKB
GO:0071560; P:cellular response to transforming growth factor beta stimulus; IEP:UniProtKB
GO:0046069; P:cGMP catabolic process; IDA:UniProtKB
GO:0019934; P:cGMP-mediated signaling; IMP:UniProtKB
GO:0061028; P:establishment of endothelial barrier; ISS:UniProtKB
GO:0008152; P:metabolic process; IDA:UniProtKB
GO:0030224; P:monocyte differentiation; IEP:UniProtKB
GO:0030818; P:negative regulation of cAMP biosynthetic process; ISS:UniProtKB
GO:0033159; P:negative regulation of protein import into nucleus, translocation; IDA:UniProtKB
GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IDA:UniProtKB
GO:0043116; P:negative regulation of vascular permeability; IMP:UniProtKB
GO:0050729; P:positive regulation of inflammatory response; ISS:UniProtKB
GO:0043117; P:positive regulation of vascular permeability; IMP:UniProtKB
GO:0006626; P:protein targeting to mitochondrion; ISS:UniProtKB
Interpro
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
Pfam; PF01590; GAF;
Pfam; PF00233; PDEase_I;
SMART
SMART; SM00065; GAF;
SMART; SM00471; HDc;
PROSITE
PROSITE; PS00126; PDEASE_I;
PRINTS
PRINTS; PR00387; PDIESTERASE1;