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P14099

- PDE2A_BOVIN

UniProt

P14099 - PDE2A_BOVIN

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Protein

cGMP-dependent 3',5'-cyclic phosphodiesterase

Gene
PDE2A
Organism
Bos taurus (Bovine)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Cyclic nucleotide phosphodiesterase with a dual-specificity for the second messengers cAMP and cGMP, which are key regulators of many important physiological processes By similarity.

Catalytic activityi

Nucleoside 3',5'-cyclic phosphate + H2O = nucleoside 5'-phosphate.

Cofactori

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 By similarity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei411 – 4111cGMP By similarity
Binding sitei426 – 4261cGMP By similarity
Binding sitei479 – 4791cGMP By similarity
Active sitei636 – 6361Proton donor By similarity
Metal bindingi640 – 6401Divalent metal cation 1 By similarity
Metal bindingi676 – 6761Divalent metal cation 1 By similarity
Metal bindingi677 – 6771Divalent metal cation 1 By similarity
Metal bindingi677 – 6771Divalent metal cation 2 By similarity
Binding sitei677 – 6771Substrate By similarity
Metal bindingi788 – 7881Divalent metal cation 1 By similarity
Binding sitei788 – 7881Substrate By similarity

GO - Molecular functioni

  1. cGMP binding Source: UniProtKB
  2. cGMP-stimulated cyclic-nucleotide phosphodiesterase activity Source: UniProtKB
  3. cyclic-nucleotide phosphodiesterase activity Source: UniProtKB
  4. drug binding Source: UniProtKB
  5. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. cAMP catabolic process Source: UniProtKB
  2. cAMP-mediated signaling Source: UniProtKB
  3. cellular response to cGMP Source: UniProtKB
  4. cellular response to drug Source: UniProtKB
  5. cellular response to granulocyte macrophage colony-stimulating factor stimulus Source: UniProtKB
  6. cellular response to macrophage colony-stimulating factor stimulus Source: UniProtKB
  7. cellular response to mechanical stimulus Source: UniProtKB
  8. cGMP catabolic process Source: UniProtKB
  9. cGMP-mediated signaling Source: UniProtKB
  10. establishment of endothelial barrier Source: UniProtKB
  11. GMP catabolic process Source: AgBase
  12. metabolic process Source: GOC
  13. negative regulation of cAMP biosynthetic process Source: UniProtKB
  14. negative regulation of protein import into nucleus, translocation Source: UniProtKB
  15. negative regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  16. negative regulation of vascular permeability Source: UniProtKB
  17. positive regulation of inflammatory response Source: UniProtKB
  18. positive regulation of vascular permeability Source: UniProtKB
  19. protein targeting to mitochondrion Source: UniProtKB
  20. regulation of cAMP metabolic process Source: AgBase
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

cAMP, cGMP, cGMP-binding, Metal-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
cGMP-dependent 3',5'-cyclic phosphodiesterase (EC:3.1.4.17)
Alternative name(s):
Cyclic GMP-stimulated phosphodiesterase
Short name:
CGS-PDE
Short name:
cGSPDE
Gene namesi
Name:PDE2A
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
ProteomesiUP000009136: Unplaced

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. cytosol Source: UniProtKB
  3. endoplasmic reticulum Source: UniProtKB
  4. Golgi apparatus Source: UniProtKB
  5. mitochondrial matrix Source: UniProtKB
  6. nucleus Source: UniProtKB
  7. perinuclear region of cytoplasm Source: UniProtKB
  8. plasma membrane Source: UniProtKB
  9. presynaptic membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 921921cGMP-dependent 3',5'-cyclic phosphodiesterasePRO_0000198795Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

PRIDEiP14099.

Interactioni

Subunit structurei

Homodimer.

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000042623.

Structurei

3D structure databases

ProteinModelPortaliP14099.
SMRiP14099. Positions 202-542, 558-895.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini220 – 357138GAF 1Add
BLAST
Domaini389 – 528140GAF 2Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni613 – 871259CatalyticAdd
BLAST
Regioni636 – 6405Substrate binding By similarity

Domaini

GAF 1 functions as a dimerization domain, whereas GAF 2 binds cGMP, which causes activation of the catalytic activity of the enzyme By similarity.

Sequence similaritiesi

Contains 2 GAF domains.

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiNOG270709.
HOGENOMiHOG000007068.
HOVERGENiHBG053540.
KOiK18283.

Family and domain databases

Gene3Di1.10.1300.10. 1 hit.
3.30.450.40. 2 hits.
InterProiIPR003018. GAF.
IPR029016. GAF_dom_like.
IPR003607. HD/PDEase_dom.
IPR023088. PDEase.
IPR002073. PDEase_catalytic_dom.
IPR023174. PDEase_CS.
[Graphical view]
PfamiPF01590. GAF. 2 hits.
PF00233. PDEase_I. 1 hit.
[Graphical view]
PRINTSiPR00387. PDIESTERASE1.
SMARTiSM00065. GAF. 2 hits.
SM00471. HDc. 1 hit.
[Graphical view]
SUPFAMiSSF55781. SSF55781. 3 hits.
PROSITEiPS00126. PDEASE_I. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Note: Additional isoforms seem to exist.

Isoform PDE2A1 (identifier: P14099-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

MRRQPAASRD LFAQEPVPPG SGDGALQDAL LSLGSVIDVA GLQQAVKEAL    50
SAVLPKVETV YTYLLDGESR LVCEEPPHEL PQEGKVREAV ISRKRLGCNG 100
LGPSDLPGKP LARLVAPLAP DTQVLVIPLV DKEAGAVAAV ILVHCGQLSD 150
NEEWSLQAVE KHTLVALKRV QALQQRESSV APEATQNPPE EAAGDQKGGV 200
AYTNQDRKIL QLCGELYDLD ASSLQLKVLQ YLQQETQASR CCLLLVSEDN 250
LQLSCKVIGD KVLEEEISFP LTTGRLGQVV EDKKSIQLKD LTSEDMQQLQ 300
SMLGCEVQAM LCVPVISRAT DQVVALACAF NKLGGDLFTD QDEHVIQHCF 350
HYTSTVLTST LAFQKEQKLK CECQALLQVA KNLFTHLDDV SVLLQEIITE 400
ARNLSNAEIC SVFLLDQNEL VAKVFDGGVV EDESYEIRIP ADQGIAGHVA 450
TTGQILNIPD AYAHPLFYRG VDDSTGFRTR NILCFPIKNE NQEVIGVAEL 500
VNKINGPWFS KFDEDLATAF SIYCGISIAH SLLYKKVNEA QYRSHLANEM 550
MMYHMKVSDD EYTKLLHDGI QPVAAIDSNF ASFTYTPRSL PEDDTSMAIL 600
SMLQDMNFIN NYKIDCPTLA RFCLMVKKGY RDPPYHNWMH AFSVSHFCYL 650
LYKNLELTNY LEDMEIFALF ISCMCHDLDH RGTNNSFQVA SKSVLAALYS 700
SEGSVMERHH FAQAIAILNT HGCNIFDHFS RKDYQRMLDL MRDIILATDL 750
AHHLRIFKDL QKMAEVGYDR TNKQHHSLLL CLLMTSCDLS DQTKGWKTTR 800
KIAELIYKEF FSQGDLEKAM GNRPMEMMDR EKAYIPELQI SFMEHIAMPI 850
YKLLQDLFPK AAELYERVAS NREHWTKVSH KFTIRGLPSN NSLDFLDEEY 900
EVPDLDGARA PINGCCSLDA E 921
Length:921
Mass (Da):103,228
Last modified:December 1, 1992 - v2
Checksum:iE29F4C9875E83640
GO
Isoform PDE2A2 (identifier: P14099-3)

Sequence is not available
Length:
Mass (Da):
Isoform PDE2A3 (identifier: P14099-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-25: MRRQPAASRDLFAQEPVPPGSGDGA → MGQACGHSILCRSQQYPAARPAEPRGQQVFLKPDEPPPPPQPCADS

Show »
Length:942
Mass (Da):105,575
Checksum:iC2EC7D62C1C3F993
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 2525MRRQP…SGDGA → MGQACGHSILCRSQQYPAAR PAEPRGQQVFLKPDEPPPPP QPCADS in isoform PDE2A3. VSP_004555Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti204 – 2041N → D in AAA87353. 1 Publication
Sequence conflicti633 – 6331P → L AA sequence 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M73512 mRNA. Translation: AAA74559.1.
L49503 mRNA. Translation: AAA87353.1.
PIRiA40981.
RefSeqiNP_001137318.1. NM_001143846.1.
NP_001243202.1. NM_001256273.1. [P14099-1]
UniGeneiBt.4716.

Genome annotation databases

GeneIDi281971.
KEGGibta:281971.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M73512 mRNA. Translation: AAA74559.1 .
L49503 mRNA. Translation: AAA87353.1 .
PIRi A40981.
RefSeqi NP_001137318.1. NM_001143846.1.
NP_001243202.1. NM_001256273.1. [P14099-1 ]
UniGenei Bt.4716.

3D structure databases

ProteinModelPortali P14099.
SMRi P14099. Positions 202-542, 558-895.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 9913.ENSBTAP00000042623.

Chemistry

BindingDBi P14099.
ChEMBLi CHEMBL3477.

Proteomic databases

PRIDEi P14099.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 281971.
KEGGi bta:281971.

Organism-specific databases

CTDi 5138.

Phylogenomic databases

eggNOGi NOG270709.
HOGENOMi HOG000007068.
HOVERGENi HBG053540.
KOi K18283.

Miscellaneous databases

NextBioi 20805842.

Family and domain databases

Gene3Di 1.10.1300.10. 1 hit.
3.30.450.40. 2 hits.
InterProi IPR003018. GAF.
IPR029016. GAF_dom_like.
IPR003607. HD/PDEase_dom.
IPR023088. PDEase.
IPR002073. PDEase_catalytic_dom.
IPR023174. PDEase_CS.
[Graphical view ]
Pfami PF01590. GAF. 2 hits.
PF00233. PDEase_I. 1 hit.
[Graphical view ]
PRINTSi PR00387. PDIESTERASE1.
SMARTi SM00065. GAF. 2 hits.
SM00471. HDc. 1 hit.
[Graphical view ]
SUPFAMi SSF55781. SSF55781. 3 hits.
PROSITEi PS00126. PDEASE_I. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Molecular cloning of a cyclic GMP-stimulated cyclic nucleotide phosphodiesterase cDNA. Identification and distribution of isozyme variants."
    Sonnenburg W.K., Mullaney P.J., Beavo J.A.
    J. Biol. Chem. 266:17655-17661(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM PDE2A1).
  2. Juilfs D.M., Sonnenburg W.K., Seraji S., Beavo J.A.
    Submitted (FEB-1996) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM PDE2A3).
    Tissue: Brain.
  3. "Amino acid sequence of the cyclic GMP stimulated cyclic nucleotide phosphodiesterase from bovine heart."
    le Trong H., Beier N., Sonnenburg W.K., Stroop S.D., Walsh K.A., Beavo J.A., Charbonneau H.
    Biochemistry 29:10280-10288(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 592-921.
    Tissue: Heart.
  4. "Identification of a conserved domain among cyclic nucleotide phosphodiesterases from diverse species."
    Charbonneau H., Beier N., Walsh K.A., Beavo J.A.
    Proc. Natl. Acad. Sci. U.S.A. 83:9308-9312(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 613-694 AND 808-868.
    Tissue: Heart.

Entry informationi

Entry nameiPDE2A_BOVIN
AccessioniPrimary (citable) accession number: P14099
Secondary accession number(s): Q28064
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: December 1, 1992
Last modified: September 3, 2014
This is version 106 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

cGMP binds at an allosteric activator site By similarity.

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi