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cAMP-specific 3',5'-cyclic phosphodiesterase 4D (EC 3.1.4.53) (DPDE3)

 PDE4D_RAT               Reviewed;         803 AA.
P14270; A1E347; A1EC59; F1M1H7; O35470; Q6TRI0; Q8CG04; Q8CG06;
01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
04-JAN-2005, sequence version 4.
27-SEP-2017, entry version 151.
RecName: Full=cAMP-specific 3',5'-cyclic phosphodiesterase 4D;
EC=3.1.4.53;
AltName: Full=DPDE3;
Name=Pde4d;
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] (ISOFORM 31), AND INDUCTION.
TISSUE=Testis;
PubMed=2554303; DOI=10.1073/pnas.86.21.8197;
Swinnen J.V., Joseph D.R., Conti M.;
"The mRNA encoding a high-affinity cAMP phosphodiesterase is regulated
by hormones and cAMP.";
Proc. Natl. Acad. Sci. U.S.A. 86:8197-8201(1989).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 31; 32 AND 33).
PubMed=8034568;
Sette C., Vicini E., Conti M.;
"The ratPDE3/IVd phosphodiesterase gene codes for multiple proteins
differentially activated by cAMP-dependent protein kinase.";
J. Biol. Chem. 269:18271-18274(1994).
[3]
SEQUENCE REVISION TO 6.
Conti M.;
Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 31 AND 32).
STRAIN=Wistar;
PubMed=8276818;
Monaco L., Vicini E., Conti M.;
"Structure of two rat genes coding for closely related rolipram-
sensitive cAMP phosphodiesterases. Multiple mRNA variants originate
from alternative splicing and multiple start sites.";
J. Biol. Chem. 269:347-357(1994).
[5]
ERRATUM.
Monaco L., Vicini E., Conti M.;
J. Biol. Chem. 269:20806-20806(1994).
[6]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4).
STRAIN=Sprague-Dawley; TISSUE=Brain;
Jin S.-L.C., Kuo W.-P., Conti M.;
"Characterization of a cAMP-specific phosphodiesterase variant
(PDE4D4) expressed in the rat brain.";
Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 6 AND 7).
STRAIN=Sprague-Dawley;
PubMed=12834813; DOI=10.1016/S0898-6568(03)00042-1;
Wang D., Deng C., Bugaj-Gaweda B., Kwan M., Gunwaldsen C., Leonard C.,
Xin X., Hu Y., Unterbeck A., De Vivo M.;
"Cloning and characterization of novel PDE4D isoforms PDE4D6 and
PDE4D7.";
Cell. Signal. 15:883-891(2003).
[8]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 5 AND 8), BIOPHYSICOCHEMICAL
PROPERTIES, ENZYME REGULATION, AND TISSUE SPECIFICITY.
STRAIN=Sprague-Dawley;
PubMed=17261351; DOI=10.1016/j.bbagen.2006.12.006;
Levallet G., Levallet J., Bonnamy P.J.;
"Alterations in proteoglycan synthesis selectively impair FSH-induced
particulate cAMP-phosphodiesterase 4 (PDE4) activation in immature rat
Sertoli cells.";
Biochim. Biophys. Acta 1770:638-648(2007).
[9]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 9).
Gaweda B., De Vivo M., Wang D.;
"Novel PDE4D isoform, PDE4D9.";
Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases.
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Brown Norway;
PubMed=15057822; DOI=10.1038/nature02426;
Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T.,
Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A.,
Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M.,
Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K.,
Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S.,
Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J.,
Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y.,
Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A.,
Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J.,
D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R.,
Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A.,
Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E.,
Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E.,
Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D.,
Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M.,
Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O.,
Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O.,
Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H.,
Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S.,
Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J.,
Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E.,
Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F.,
Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K.,
Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S.,
Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M.,
Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M.,
Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A.,
Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S.,
Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G.,
Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H.,
Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R.,
Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M.,
Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H.,
Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S.,
Collins F.S.;
"Genome sequence of the Brown Norway rat yields insights into
mammalian evolution.";
Nature 428:493-521(2004).
[11]
NUCLEOTIDE SEQUENCE OF 224-672.
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).
[12]
NUCLEOTIDE SEQUENCE [MRNA] OF 226-803 (ISOFORM 33), AND NUCLEOTIDE
SEQUENCE [MRNA] OF 253-803 (ISOFORM 31).
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).
[13]
PHOSPHORYLATION, AND SUBCELLULAR LOCATION.
PubMed=10187850; DOI=10.1074/jbc.274.15.10557;
Liu H., Maurice D.H.;
"Phosphorylation-mediated activation and translocation of the cyclic
AMP-specific phosphodiesterase PDE4D3 by cyclic AMP-dependent protein
kinase and mitogen-activated protein kinases. A potential mechanism
allowing for the coordinated regulation of PDE4D activity and
targeting.";
J. Biol. Chem. 274:10557-10565(1999).
[14]
INTERACTION WITH PDE4DIP.
PubMed=11134006; DOI=10.1074/jbc.M006546200;
Verde I., Pahlke G., Salanova M., Zhang G., Wang S., Coletti D.,
Onuffer J., Jin S.-L.C., Conti M.;
"Myomegalin is a novel protein of the Golgi/centrosome that interacts
with a cyclic nucleotide phosphodiesterase.";
J. Biol. Chem. 276:11189-11198(2001).
[15]
SUBCELLULAR LOCATION, AND INTERACTION WITH THE CENTROSOME (ISOFORM
33).
PubMed=11285255; DOI=10.1074/jbc.C000911200;
Tasken K.A., Collas P., Kemmner W.A., Witczak O., Conti M., Tasken K.;
"Phosphodiesterase 4D and protein kinase a type II constitute a
signaling unit in the centrosomal area.";
J. Biol. Chem. 276:21999-22002(2001).
[16]
ALTERNATIVE SPLICING (ISOFORMS 4; 5; 6; 7; 8; 9; 31; 32 AND 33).
PubMed=15717866; DOI=10.1042/BJ20050030;
Richter W., Jin S.L., Conti M.;
"Splice variants of the cyclic nucleotide phosphodiesterase PDE4D are
differentially expressed and regulated in rat tissue.";
Biochem. J. 388:803-811(2005).
[17]
INTERACTION WITH SHANK2, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=17244609; DOI=10.1074/jbc.M610857200;
Lee J.H., Richter W., Namkung W., Kim K.H., Kim E., Conti M.,
Lee M.G.;
"Dynamic regulation of cystic fibrosis transmembrane conductance
regulator by competitive interactions of molecular adaptors.";
J. Biol. Chem. 282:10414-10422(2007).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-137, PHOSPHORYLATION
[LARGE SCALE ANALYSIS] AT SER-52 AND SER-56 (ISOFORM 5), 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).
-!- FUNCTION: Hydrolyzes the second messenger cAMP, which is a key
regulator of many important physiological processes.
-!- 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: Activated by phosphatidic acid (By similarity).
Inhibited by rolipram. {ECO:0000250, ECO:0000269|PubMed:17261351}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
Vmax=18 pmol/min/mg enzyme for cAMP (in the absence of follicle-
stimulating hormone (FSH)) {ECO:0000269|PubMed:17261351};
Vmax=5 pmol/min/mg enzyme for cAMP (in the presence of follicle-
stimulating hormone (FSH)) {ECO:0000269|PubMed:17261351};
-!- PATHWAY: Purine metabolism; 3',5'-cyclic AMP degradation; AMP from
3',5'-cyclic AMP: step 1/1.
-!- SUBUNIT: Homodimer for the long isoforms. Isoforms with truncated
N-termini are monomeric. Binds ARRB2. Isoform 33 is part of a
ternary complex containing PRKAR2A, PRKAR2B and AKAP9. Identified
in a complex composed of RYR1, PDE4D, PKA, FKBP1A and protein
phosphatase 1 (PP1) (By similarity). Interacts with PDE4DIP.
Isoform 5 interacts (via N-terminal region) with SHANK2 (via
proline-rich region); the interaction is increased in a PKA-
dependent manner. Isoform 33, isoform 4, isoform 7, isoform 8 and
isoform 9 but not isoform 32 and isoform 6 interact with SHANK2.
Isoform 31 interacts weakly with SHANK2. {ECO:0000250,
ECO:0000269|PubMed:11134006, ECO:0000269|PubMed:17244609}.
-!- INTERACTION:
P08588:ADRB1 (xeno); NbExp=2; IntAct=EBI-8333209, EBI-991009;
Q9QX74:Shank2; NbExp=4; IntAct=EBI-9032440, EBI-397902;
-!- SUBCELLULAR LOCATION: Apical cell membrane. Cytoplasm. Membrane.
Cytoplasm, cytoskeleton. Cytoplasm, cytoskeleton, microtubule
organizing center, centrosome. Note=Found in the soluble fraction,
associated with membranes, and associated with the cytoskeleton
and the centrosome. Colocalized with SHANK2 to the apical membrane
of colonic crypt cells.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=9;
Name=4; Synonyms=PDE4D4;
IsoId=P14270-5; Sequence=Displayed;
Name=33; Synonyms=PDE4D3, PDE3.3;
IsoId=P14270-1; Sequence=VSP_012398, VSP_012399;
Name=31; Synonyms=PDE3.1;
IsoId=P14270-2; Sequence=VSP_004581;
Name=32; Synonyms=PDE3.2;
IsoId=P14270-3; Sequence=VSP_004582;
Name=5; Synonyms=PDE4D5;
IsoId=P14270-8; Sequence=VSP_053485;
Note=Contains a phosphoserine at position 52. Contains a
phosphoserine at position 56. {ECO:0000244|PubMed:22673903};
Name=6; Synonyms=PDE4D6;
IsoId=P14270-7; Sequence=VSP_012404, VSP_012405;
Name=7; Synonyms=PDE4D7;
IsoId=P14270-4; Sequence=VSP_012400, VSP_012401;
Name=8; Synonyms=PDE4D8;
IsoId=P14270-9; Sequence=VSP_053486;
Name=9; Synonyms=PDE4D9;
IsoId=P14270-6; Sequence=VSP_012402, VSP_012403;
-!- TISSUE SPECIFICITY: Expressed in epithelial cells. Isoform 33,
isoform 4, isoform 5 and isoform 9 are expressed in brain. Isoform
33, isoform 5, isoform 8 and isoform 9 are expressed in heart (at
protein level). Isoform 4 and isoform 6 are strongly expressed in
cortex and cerebellum. Isoform 7 is strongly expressed in cortex
and testis; weakly expressed in kidney, lung, spleen and
cerebellum. Isoform 8 is strongly expressed in lung, heart and
liver. Isoform 31, isoform 32, isoform 33, isoform 5 and isoform 9
are widely distributed. {ECO:0000269|PubMed:17244609,
ECO:0000269|PubMed:17261351}.
-!- INDUCTION: Up-regulated by cAMP and follicle-stimulating hormone.
{ECO:0000269|PubMed:2554303}.
-!- PTM: Isoform 1 and isoform 9 are rapidly activated by PKA through
phosphorylation. Long isoforms that share a conserved PKA
phosphorylation site in the N-terminus are also activated.
{ECO:0000269|PubMed:10187850}.
-!- PTM: Sumoylation of long isoforms by PIAS4 augments their
activation by PKA phosphorylation and represses their inhibition
by ERK phosphorylation. {ECO:0000250}.
-!- SIMILARITY: Belongs to the cyclic nucleotide phosphodiesterase
family. PDE4 subfamily. {ECO:0000305}.
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EMBL; U09455; AAA20401.1; -; mRNA.
EMBL; U09457; AAB81869.1; -; mRNA.
EMBL; U09456; AAA20393.1; -; mRNA.
EMBL; U01280; AAA18925.1; -; Unassigned_DNA.
EMBL; U01278; AAA18925.1; JOINED; Unassigned_DNA.
EMBL; U01282; AAA18925.1; JOINED; Unassigned_DNA.
EMBL; U01283; AAA18925.1; JOINED; Unassigned_DNA.
EMBL; U01284; AAA18925.1; JOINED; Unassigned_DNA.
EMBL; U01285; AAA18925.1; JOINED; Unassigned_DNA.
EMBL; U01286; AAA18925.1; JOINED; Unassigned_DNA.
EMBL; U01287; AAA18925.1; JOINED; Unassigned_DNA.
EMBL; U01279; AAA18925.1; JOINED; Unassigned_DNA.
EMBL; U01280; AAA18924.1; -; Unassigned_DNA.
EMBL; U01278; AAA18924.1; JOINED; Unassigned_DNA.
EMBL; U01282; AAA18924.1; JOINED; Unassigned_DNA.
EMBL; U01283; AAA18924.1; JOINED; Unassigned_DNA.
EMBL; U01284; AAA18924.1; JOINED; Unassigned_DNA.
EMBL; U01285; AAA18924.1; JOINED; Unassigned_DNA.
EMBL; U01286; AAA18924.1; JOINED; Unassigned_DNA.
EMBL; U01287; AAA18924.1; JOINED; Unassigned_DNA.
EMBL; U01279; AAA18924.1; JOINED; Unassigned_DNA.
EMBL; AF031373; AAB95266.1; -; mRNA.
EMBL; AF536974; AAN10116.1; -; mRNA.
EMBL; EF102484; ABK97408.1; -; mRNA.
EMBL; EF121818; ABL14108.1; -; mRNA.
EMBL; AF536979; AAN10121.1; -; mRNA.
EMBL; AY388961; AAQ90405.1; -; mRNA.
EMBL; AABR06012736; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AABR06012737; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AABR06012738; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AABR06012739; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AABR06012740; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AABR06012741; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AABR06012742; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AABR06012743; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AABR06012744; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AABR06012745; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AABR06012746; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AABR06012747; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AABR06012748; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AABR06012749; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AABR06012750; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AABR06012751; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AABR06012752; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AABR06012753; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AABR06012754; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AABR06012755; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AABR06012756; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AABR06012757; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AABR06012758; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AABR06012759; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AABR06012760; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; L27059; AAA56857.1; -; mRNA.
EMBL; L27060; AAC26969.1; -; mRNA.
PIR; B53109; B53109.
PIR; I61259; I61259.
RefSeq; NP_001106799.1; NM_001113328.1.
RefSeq; NP_001106800.1; NM_001113329.1. [P14270-4]
RefSeq; NP_001106803.1; NM_001113332.1. [P14270-8]
RefSeq; NP_001106805.1; NM_001113334.1. [P14270-9]
RefSeq; NP_058728.1; NM_017032.1. [P14270-1]
RefSeq; XP_008758943.1; XM_008760721.1. [P14270-6]
RefSeq; XP_008758944.1; XM_008760722.2. [P14270-7]
RefSeq; XP_008758945.1; XM_008760723.1. [P14270-3]
UniGene; Rn.160519; -.
UniGene; Rn.163460; -.
UniGene; Rn.169992; -.
UniGene; Rn.95959; -.
ProteinModelPortal; P14270; -.
SMR; P14270; -.
BioGrid; 246765; 4.
IntAct; P14270; 2.
STRING; 10116.ENSRNOP00000067171; -.
ChEMBL; CHEMBL2712; -.
iPTMnet; P14270; -.
PhosphoSitePlus; P14270; -.
PaxDb; P14270; -.
PRIDE; P14270; -.
Ensembl; ENSRNOT00000066384; ENSRNOP00000063446; ENSRNOG00000042536. [P14270-9]
Ensembl; ENSRNOT00000067546; ENSRNOP00000062384; ENSRNOG00000042536. [P14270-7]
GeneID; 24627; -.
KEGG; rno:24627; -.
CTD; 5144; -.
RGD; 3281; Pde4d.
eggNOG; KOG3689; Eukaryota.
eggNOG; ENOG410XRI7; LUCA.
GeneTree; ENSGT00760000118889; -.
HOVERGEN; HBG108239; -.
InParanoid; P14270; -.
KO; K13293; -.
OrthoDB; EOG091G06CD; -.
PhylomeDB; P14270; -.
BRENDA; 3.1.4.53; 5301.
Reactome; R-RNO-180024; DARPP-32 events.
Reactome; R-RNO-418555; G alpha (s) signalling events.
UniPathway; UPA00762; UER00747.
PRO; PR:P14270; -.
Proteomes; UP000002494; Chromosome 2.
Bgee; ENSRNOG00000042536; -.
ExpressionAtlas; P14270; baseline.
Genevisible; P14270; RN.
GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0005813; C:centrosome; IDA:RGD.
GO; GO:0005794; C:Golgi apparatus; IDA:RGD.
GO; GO:0030016; C:myofibril; IDA:RGD.
GO; GO:0004115; F:3',5'-cyclic-AMP phosphodiesterase activity; IDA:RGD.
GO; GO:0031698; F:beta-2 adrenergic receptor binding; IPI:BHF-UCL.
GO; GO:0030552; F:cAMP binding; IMP:RGD.
GO; GO:0004112; F:cyclic-nucleotide phosphodiesterase activity; IDA:RGD.
GO; GO:0019899; F:enzyme binding; IPI:BHF-UCL.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0019904; F:protein domain specific binding; IPI:RGD.
GO; GO:0017124; F:SH3 domain binding; IPI:RGD.
GO; GO:0071875; P:adrenergic receptor signaling pathway; IMP:BHF-UCL.
GO; GO:0086024; P:adrenergic receptor signaling pathway involved in positive regulation of heart rate; IC:BHF-UCL.
GO; GO:0006198; P:cAMP catabolic process; IDA:UniProtKB.
GO; GO:0043623; P:cellular protein complex assembly; IDA:RGD.
GO; GO:0061028; P:establishment of endothelial barrier; IDA:UniProtKB.
GO; GO:0030324; P:lung development; IEP:RGD.
GO; GO:0007613; P:memory; IMP:RGD.
GO; GO:0014911; P:positive regulation of smooth muscle cell migration; IMP:RGD.
GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; IMP:RGD.
GO; GO:0086004; P:regulation of cardiac muscle cell contraction; IMP:BHF-UCL.
GO; GO:0008277; P:regulation of G-protein coupled receptor protein signaling pathway; IDA:RGD.
GO; GO:0010738; P:regulation of protein kinase A signaling; IMP:RGD.
GO; GO:0010469; P:regulation of receptor activity; IMP:BHF-UCL.
CDD; cd00077; HDc; 1.
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.
PROSITE; PS00126; PDEASE_I; 1.
1: Evidence at protein level;
Alternative splicing; cAMP; Cell membrane; Complete proteome;
Cytoplasm; Cytoskeleton; Hydrolase; Isopeptide bond; Membrane;
Metal-binding; Phosphoprotein; Reference proteome; Ubl conjugation.
CHAIN 1 803 cAMP-specific 3',5'-cyclic
phosphodiesterase 4D.
/FTId=PRO_0000198816.
NP_BIND 457 461 cAMP. {ECO:0000250}.
ACT_SITE 457 457 Proton donor. {ECO:0000250}.
METAL 461 461 Divalent metal cation 1. {ECO:0000250}.
METAL 497 497 Divalent metal cation 1. {ECO:0000250}.
METAL 498 498 Divalent metal cation 1. {ECO:0000250}.
METAL 498 498 Divalent metal cation 2. {ECO:0000250}.
METAL 615 615 Divalent metal cation 1. {ECO:0000250}.
BINDING 498 498 cAMP. {ECO:0000250}.
SITE 618 618 Binds AMP, but not cAMP. {ECO:0000250}.
MOD_RES 137 137 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 294 294 Phosphoserine.
{ECO:0000250|UniProtKB:Q08499}.
MOD_RES 296 296 Phosphoserine.
{ECO:0000250|UniProtKB:Q08499}.
MOD_RES 343 343 Phosphoserine.
{ECO:0000250|UniProtKB:Q08499}.
MOD_RES 370 370 Phosphoserine.
{ECO:0000250|UniProtKB:Q08499}.
CROSSLNK 382 382 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO).
{ECO:0000250}.
VAR_SEQ 1 297 Missing (in isoform 32).
{ECO:0000303|PubMed:8034568}.
/FTId=VSP_004582.
VAR_SEQ 1 286 Missing (in isoform 6).
{ECO:0000303|PubMed:12834813}.
/FTId=VSP_012404.
VAR_SEQ 1 264 MEAEGSSVPARAGSHEGSDSSGGAALKAPKHLWRHEQHHQY
PLRQPQFRLLHPHHHLPPPPPPSPQPQLQPPPPPPLPPPPP
PPGATRGRYASSGASRVRHRGYSDTERYLYCRAMDRTSYAV
ETGHRPGLKKSRMSWPSSFQGLRRFDVDNGTSAGRSPLDPM
TSPGSGLILQANFVHSQRRESFLYRSDSDYDLSPKSMSRNS
SIASDIHGDDLIVTPFAQVLASLRTVRNNFAALTNLQDRAP
SKRSPMCNQPSINKATIT -> MKEQPSCAGTGHPSMAGYG
RMAPFELAGGPVKRLRTESPFPCLFA (in isoform
31). {ECO:0000303|PubMed:2554303,
ECO:0000303|PubMed:7958996,
ECO:0000303|PubMed:8034568}.
/FTId=VSP_004581.
VAR_SEQ 1 147 MEAEGSSVPARAGSHEGSDSSGGAALKAPKHLWRHEQHHQY
PLRQPQFRLLHPHHHLPPPPPPSPQPQLQPPPPPPLPPPPP
PPGATRGRYASSGASRVRHRGYSDTERYLYCRAMDRTSYAV
ETGHRPGLKKSRMSWPSSFQGLRR -> MAQQTTSPDTLTV
PEVDNPHVPNPWLNEDLVKSLRENLLQHEKSKTARKSVSPK
LSPVISPRNSPRLLRRMLLSSNIPKQRRFTVAHTC (in
isoform 5).
{ECO:0000303|PubMed:17261351}.
/FTId=VSP_053485.
VAR_SEQ 1 147 MEAEGSSVPARAGSHEGSDSSGGAALKAPKHLWRHEQHHQY
PLRQPQFRLLHPHHHLPPPPPPSPQPQLQPPPPPPLPPPPP
PPGATRGRYASSGASRVRHRGYSDTERYLYCRAMDRTSYAV
ETGHRPGLKKSRMSWPSSFQGLRR -> MAFVWDPLGVTVP
GPSPRTRTRLRFSKSYS (in isoform 8).
{ECO:0000303|PubMed:17261351}.
/FTId=VSP_053486.
VAR_SEQ 1 131 Missing (in isoform 33).
{ECO:0000303|PubMed:7958996,
ECO:0000303|PubMed:8034568}.
/FTId=VSP_012398.
VAR_SEQ 1 125 Missing (in isoform 9).
{ECO:0000303|Ref.9}.
/FTId=VSP_012402.
VAR_SEQ 1 56 Missing (in isoform 7).
{ECO:0000303|PubMed:12834813}.
/FTId=VSP_012400.
VAR_SEQ 57 147 LPPPPPPSPQPQLQPPPPPPLPPPPPPPGATRGRYASSGAS
RVRHRGYSDTERYLYCRAMDRTSYAVETGHRPGLKKSRMSW
PSSFQGLRR -> MERNTCDVLSRSKSASEETLHSCNDEED
PFRGMEPYLVRRLSSRSIQLPPLAFRQLEQTDLRSESENIP
RPTSLPLKILPLIAVTSADSTG (in isoform 7).
{ECO:0000303|PubMed:12834813}.
/FTId=VSP_012401.
VAR_SEQ 126 147 GHRPGLKKSRMSWPSSFQGLRR -> MSIIMKPRSRSTSSL
RTTEAVC (in isoform 9).
{ECO:0000303|Ref.9}.
/FTId=VSP_012403.
VAR_SEQ 132 147 KKSRMSWPSSFQGLRR -> MMHVNTFPFRRHSWIC (in
isoform 33). {ECO:0000303|PubMed:7958996,
ECO:0000303|PubMed:8034568}.
/FTId=VSP_012399.
VAR_SEQ 287 301 ETLQTRHSVSEMASN -> MPEANYLLSVSWGYI (in
isoform 6).
{ECO:0000303|PubMed:12834813}.
/FTId=VSP_012405.
CONFLICT 226 226 A -> N (in Ref. 12; AAA56857).
{ECO:0000305}.
CONFLICT 357 357 S -> P (in Ref. 9; AAQ90405).
{ECO:0000305}.
CONFLICT 480 486 Missing (in Ref. 4; AAA18924/AAA18925).
{ECO:0000305}.
CONFLICT 641 641 G -> E (in Ref. 12; AAC26969).
{ECO:0000305}.
CONFLICT 757 757 C -> Y (in Ref. 12; AAA56857).
{ECO:0000305}.
SEQUENCE 803 AA; 90552 MW; 13E28B257556496D CRC64;
MEAEGSSVPA RAGSHEGSDS SGGAALKAPK HLWRHEQHHQ YPLRQPQFRL LHPHHHLPPP
PPPSPQPQLQ PPPPPPLPPP PPPPGATRGR YASSGASRVR HRGYSDTERY LYCRAMDRTS
YAVETGHRPG LKKSRMSWPS SFQGLRRFDV DNGTSAGRSP LDPMTSPGSG LILQANFVHS
QRRESFLYRS DSDYDLSPKS MSRNSSIASD IHGDDLIVTP FAQVLASLRT VRNNFAALTN
LQDRAPSKRS PMCNQPSINK ATITEEAYQK LASETLEELD WCLDQLETLQ TRHSVSEMAS
NKFKRMLNRE LTHLSEMSRS GNQVSEYISN TFLDKQHEVE IPSPTQKEKE KKKRPMSQIS
GVKKLMHSSS LTNSCIPRFG VKTEQEDVLA KELEDVNKWG LHVFRIAELS GNRPLTVIMH
TIFQERDLLK TFKIPVDTLI TYLMTLEDHY HADVAYHNNI HAADVVQSTH VLLSTPALEA
VFTDLEILAA IFASAIHDVD HPGVSNQFLI NTNSELALMY NDSSVLENHH LAVGFKLLQE
ENCDIFQNLT KKQRQSLRKM AIDIVLATDM SKHMNLLADL KTMVETKKVT SSGVLLLDNY
SDRIQVLQNM VHCADLSNPT KPLQLYRQWT DRIMEEFFRQ GDRERERGME ISPMCDKHNA
SVEKSQVGFI DYIVHPLWET WADLVHPDAQ DILDTLEDNR EWYQSTIPQS PSPAPDDQED
GRQGQTEKFQ FELTLEEDGE SDTEKDSGSQ VEEDTSCSDS KTLCTQDSES TEIPLDEQVE
EEAVAEEESQ PQTGVADDCC PDT


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