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cAMP-specific 3',5'-cyclic phosphodiesterase 4A (EC 3.1.4.53) (DPDE2)

 PDE4A_RAT               Reviewed;         844 AA.
P54748; P14645; Q9EQR7;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
01-OCT-1996, sequence version 1.
10-MAY-2017, entry version 131.
RecName: Full=cAMP-specific 3',5'-cyclic phosphodiesterase 4A;
EC=3.1.4.53;
AltName: Full=DPDE2;
Name=Pde4a;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3; 4 AND 5).
PubMed=2542942; DOI=10.1073/pnas.86.10.3604;
Davis R.L., Takayasu H., Eberwine M., Myres J.;
"Cloning and characterization of mammalian homologs of the Drosophila
dunce+ gene.";
Proc. Natl. Acad. Sci. U.S.A. 86:3604-3608(1989).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 3; 4 AND 5).
TISSUE=Brain;
PubMed=7958996; DOI=10.1016/0378-1119(94)90155-4;
Bolger G.B., Rodgers L., Riggs M.;
"Differential CNS expression of alternative mRNA isoforms of the
mammalian genes encoding cAMP-specific phosphodiesterases.";
Gene 149:237-244(1994).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
STRAIN=Sprague-Dawley; TISSUE=Testis;
PubMed=8557632; DOI=10.1074/jbc.271.2.1065;
Bolger G.B., McPhee I., Houslay M.D.;
"Alternative splicing of cAMP-specific phosphodiesterase mRNA
transcripts. Characterization of a novel tissue-specific isoform,
RNPDE4A8.";
J. Biol. Chem. 271:1065-1071(1996).
[4]
NUCLEOTIDE SEQUENCE [MRNA] OF 319-677 (ISOFORMS 3/4).
TISSUE=Testis;
PubMed=2546153; DOI=10.1073/pnas.86.14.5325;
Swinnen J.V., Joseph D.R., Conti M.;
"Molecular cloning of rat homologues of the Drosophila melanogaster
dunce cAMP phosphodiesterase: evidence for a family of genes.";
Proc. Natl. Acad. Sci. U.S.A. 86:5325-5329(1989).
[5]
PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 6).
PubMed=11306681;
Rena G., Begg F., Ross A., MacKenzie C., McPhee I., Campbell L.,
Huston E., Sullivan M., Houslay M.D.;
"Molecular cloning, genomic positioning, promoter identification, and
characterization of the novel cyclic AMP-specific phosphodiesterase
PDE4A10.";
Mol. Pharmacol. 59:996-1011(2001).
[6]
PHOSPHORYLATION AT SER-147, AND MUTAGENESIS OF SER-147 AND SER-161.
PubMed=21323643; DOI=10.1042/BJ20101184;
MacKenzie K.F., Wallace D.A., Hill E.V., Anthony D.F., Henderson D.J.,
Houslay D.M., Arthur J.S., Baillie G.S., Houslay M.D.;
"Phosphorylation of cAMP-specific PDE4A5 (phosphodiesterase-4A5) by
MK2 (MAPKAPK2) attenuates its activation through protein kinase A
phosphorylation.";
Biochem. J. 435:755-769(2011).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-147; SER-152; SER-672
AND SER-674, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
[8]
STRUCTURE BY NMR OF 1-26 OF ISOFORM 3.
PubMed=8663181; DOI=10.1074/jbc.271.28.16703;
Smith K.J., Scotland G., Beattie J., Trayer I.P., Houslay M.D.;
"Determination of the structure of the N-terminal splice region of the
cyclic AMP-specific phosphodiesterase RD1 (RNPDE4A1) by 1H NMR and
identification of the membrane association domain using chimeric
constructs.";
J. Biol. Chem. 271:16703-16711(1996).
-!- FUNCTION: Hydrolyzes the second messenger cAMP, which is a key
regulator of many important physiological processes.
{ECO:0000250}.
-!- CATALYTIC ACTIVITY: Adenosine 3',5'-cyclic phosphate + H(2)O =
adenosine 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};
-!- ENZYME REGULATION: Inhibited by rolipram.
-!- PATHWAY: Purine metabolism; 3',5'-cyclic AMP degradation; AMP from
3',5'-cyclic AMP: step 1/1.
-!- SUBUNIT: Interacts with LYN and ARRB2. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=6;
Name=1;
IsoId=P54748-1; Sequence=Displayed;
Name=2; Synonyms=PDE4A8;
IsoId=P54748-2; Sequence=VSP_004565;
Name=3;
IsoId=P54748-3; Sequence=VSP_004566, VSP_004567;
Name=4; Synonyms=Medium;
IsoId=P54748-4; Sequence=VSP_004568;
Name=5; Synonyms=Short;
IsoId=P54748-5; Sequence=VSP_004569, VSP_004570;
Name=6; Synonyms=PDE4A10;
IsoId=P54748-6; Sequence=VSP_038187;
Note=Incomplete sequence.;
-!- TISSUE SPECIFICITY: Isoform 2 is testis specific.
-!- PTM: Proteolytically cleaved by caspase-3. {ECO:0000250}.
-!- PTM: Phosphorylation by MAPKAPK2 its activation through PKA
phosphorylation. {ECO:0000269|PubMed:21323643}.
-!- SIMILARITY: Belongs to the cyclic nucleotide phosphodiesterase
family. PDE4 subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; L27057; AAC27098.1; -; mRNA.
EMBL; L36467; AAB00357.1; -; mRNA.
EMBL; L27062; AAA56859.1; -; mRNA.
EMBL; M25348; AAA41848.1; -; mRNA.
EMBL; M28411; AAA41823.1; -; mRNA.
EMBL; M26715; AAC37699.1; -; mRNA.
EMBL; M26716; AAA41101.1; -; mRNA.
EMBL; M26717; AAA41102.1; -; mRNA.
EMBL; AF110461; AAF14352.2; -; mRNA.
PIR; I53865; I53865.
PIR; I67946; I67946.
RefSeq; NP_037233.3; NM_013101.3. [P54748-1]
UniGene; Rn.91357; -.
PDB; 1LOI; NMR; -; A=1-25.
PDBsum; 1LOI; -.
ProteinModelPortal; P54748; -.
SMR; P54748; -.
BioGrid; 247667; 4.
STRING; 10116.ENSRNOP00000057815; -.
ChEMBL; CHEMBL2094267; -.
iPTMnet; P54748; -.
PhosphoSitePlus; P54748; -.
PaxDb; P54748; -.
PRIDE; P54748; -.
GeneID; 25638; -.
KEGG; rno:25638; -.
UCSC; RGD:3279; rat. [P54748-1]
CTD; 5141; -.
RGD; 3279; Pde4a.
eggNOG; KOG3689; Eukaryota.
eggNOG; ENOG410XRI7; LUCA.
HOGENOM; HOG000236297; -.
HOVERGEN; HBG108239; -.
InParanoid; P54748; -.
KO; K13293; -.
PhylomeDB; P54748; -.
BRENDA; 3.1.4.53; 5301.
UniPathway; UPA00762; UER00747.
EvolutionaryTrace; P54748; -.
PMAP-CutDB; P54748; -.
PRO; PR:P54748; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0005737; C:cytoplasm; IDA:RGD.
GO; GO:0005829; C:cytosol; IDA:RGD.
GO; GO:0005634; C:nucleus; IDA:RGD.
GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:RGD.
GO; GO:0004115; F:3',5'-cyclic-AMP phosphodiesterase activity; IDA:RGD.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0006198; P:cAMP catabolic process; IDA:UniProtKB.
GO; GO:0042493; P:response to drug; IEP:RGD.
GO; GO:0007165; P:signal transduction; IEA:InterPro.
Gene3D; 1.10.1300.10; -; 1.
InterPro; IPR003607; HD/PDEase_dom.
InterPro; IPR023088; PDEase.
InterPro; IPR002073; PDEase_catalytic_dom.
InterPro; IPR023174; PDEase_CS.
Pfam; PF00233; PDEase_I; 1.
PRINTS; PR00387; PDIESTERASE1.
SMART; SM00471; HDc; 1.
PROSITE; PS00126; PDEASE_I; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; cAMP; Complete proteome;
Cytoplasm; Hydrolase; Isopeptide bond; Metal-binding; Phosphoprotein;
Reference proteome; Ubl conjugation.
CHAIN 1 844 cAMP-specific 3',5'-cyclic
phosphodiesterase 4A.
/FTId=PRO_0000198808.
NP_BIND 419 423 cAMP. {ECO:0000250}.
REGION 317 710 Catalytic. {ECO:0000250}.
ACT_SITE 419 419 Proton donor. {ECO:0000250}.
METAL 423 423 Divalent metal cation 1. {ECO:0000250}.
METAL 459 459 Divalent metal cation 1. {ECO:0000250}.
METAL 460 460 Divalent metal cation 1. {ECO:0000250}.
METAL 460 460 Divalent metal cation 2. {ECO:0000250}.
METAL 577 577 Divalent metal cation 1. {ECO:0000250}.
BINDING 460 460 cAMP. {ECO:0000250}.
BINDING 577 577 cAMP. {ECO:0000250}.
BINDING 628 628 cAMP. {ECO:0000250}.
SITE 69 70 Cleavage; by caspase-3. {ECO:0000250}.
SITE 580 580 Binds AMP, but not cAMP. {ECO:0000250}.
MOD_RES 13 13 Phosphoserine.
{ECO:0000250|UniProtKB:P27815}.
MOD_RES 147 147 Phosphoserine; by MAPKAPK2.
{ECO:0000244|PubMed:22673903,
ECO:0000269|PubMed:21323643}.
MOD_RES 152 152 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 160 160 Phosphoserine.
{ECO:0000250|UniProtKB:P27815}.
MOD_RES 204 204 Phosphoserine.
{ECO:0000250|UniProtKB:P27815}.
MOD_RES 333 333 Phosphoserine.
{ECO:0000250|UniProtKB:P27815}.
MOD_RES 672 672 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 674 674 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
CROSSLNK 344 344 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO).
{ECO:0000250}.
VAR_SEQ 1 318 Missing (in isoform 5).
{ECO:0000303|PubMed:2542942,
ECO:0000303|PubMed:7958996}.
/FTId=VSP_004569.
VAR_SEQ 1 259 Missing (in isoform 4).
{ECO:0000303|PubMed:2542942,
ECO:0000303|PubMed:7958996}.
/FTId=VSP_004568.
VAR_SEQ 1 234 Missing (in isoform 3).
{ECO:0000303|PubMed:2542942,
ECO:0000303|PubMed:7958996}.
/FTId=VSP_004566.
VAR_SEQ 1 102 MEPPAAPSERSLSLSLPGPREGQATLKPPPQHLWRQPRTPI
RIQQRGYPDSAERSETERSPHRPIERADAVDTGDRPGLRTT
RMSWPSSFHGTGTGGGSSRR -> MPSRKRLTLPRIFIVRK
NGNS (in isoform 2).
{ECO:0000303|PubMed:8557632}.
/FTId=VSP_004565.
VAR_SEQ 1 102 MEPPAAPSERSLSLSLPGPREGQATLKPPPQHLWRQPRTPI
RIQQRGYPDSAERSETERSPHRPIERADAVDTGDRPGLRTT
RMSWPSSFHGTGTGGGSSRR -> ALPLGPESLTHFSFSEE
DTLRHPPGRCVS (in isoform 6).
{ECO:0000305}.
/FTId=VSP_038187.
VAR_SEQ 235 256 WCLEQLETMQTYRSVSEMASHK -> MPLVDFFCETCSKPW
LVGWWDQ (in isoform 3).
{ECO:0000303|PubMed:2542942,
ECO:0000303|PubMed:7958996}.
/FTId=VSP_004567.
VAR_SEQ 354 386 Missing (in isoform 5).
{ECO:0000303|PubMed:2542942,
ECO:0000303|PubMed:7958996}.
/FTId=VSP_004570.
MUTAGEN 147 147 S->A: Abolishes phosphorylation by
MAPKAPK2. {ECO:0000269|PubMed:21323643}.
MUTAGEN 161 161 S->A: Does not affect phosphorylation by
MAPKAPK2. {ECO:0000269|PubMed:21323643}.
CONFLICT 130 130 A -> R (in Ref. 5; AAF14352).
{ECO:0000305}.
CONFLICT 465 466 GV -> AL (in Ref. 4; AAA41848/AAA41823).
{ECO:0000305}.
CONFLICT 603 604 GD -> AH (in Ref. 4; AAA41848/AAA41823).
{ECO:0000305}.
CONFLICT 833 833 A -> T (in Ref. 1; AAC37699/AAA41101/
AAA41102 and 5; AAF14352). {ECO:0000305}.
HELIX 3 9 {ECO:0000244|PDB:1LOI}.
HELIX 16 19 {ECO:0000244|PDB:1LOI}.
HELIX 20 23 {ECO:0000244|PDB:1LOI}.
SEQUENCE 844 AA; 93439 MW; 1A5F5101E4DBF1B6 CRC64;
MEPPAAPSER SLSLSLPGPR EGQATLKPPP QHLWRQPRTP IRIQQRGYPD SAERSETERS
PHRPIERADA VDTGDRPGLR TTRMSWPSSF HGTGTGGGSS RRLEAENGPT PSPGRSPLDS
QASPGLVLHA GATTSQRRES FLYRSDSDYD MSPKAVSRSS SVASEAHAED LIVTPFAQVL
ASLRSVRSNF SLLTNVPIPS NKRSPLGGPP SVCKATLSEE TCQQLARETL EELDWCLEQL
ETMQTYRSVS EMASHKFKRM LNRELTHLSE MSRSGNQVSE YISNTFLDKQ NEVEIPSPTP
RQRAFQQPPP SVLRQSQPMS QITGLKKLVH TGSLNTNVPR FGVKTDQEDL LAQELENLSK
WGLNIFCVSE YAGGRSLSCI MYTIFQERDL LKKFHIPVDT MMMYMLTLED HYHADVAYHN
SLHAADVLQS THVLLATPAL DAVFTDLEIL AALFAAAIHD VDHPGVSNQF LINTNSELAL
MYNDESVLEN HHLAVGFKLL QEENCDIFQN LSKRQRQSLR KMVIDMVLAT DMSKHMTLLA
DLKTMVETKK VTSSGVLLLD NYSDRIQVLR NMVHCADLSN PTKPLELYRQ WTDRIMAEFF
QQGDRERERG MEISPMCDKH TASVEKSQVG FIDYIVHPLW ETWADLVHPD AQDILDTLED
NRDWYHSAIR QSPSPPLEEE PGGLGHPSLP DKFQFELTLE EEEEEDSLEV PGLPTTEETF
LAAEDARAQA VDWSKVKGPS TTVVEVAERL KQETASAYGA PQESMEAVGC SFSPGTPILP
DVRTLSSSEE APGLLGLPST AAEVEAPRDH LAATRACSAC SGTSGDNSAI ISAPGRWGSG
GDPA


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