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cAMP-specific 3',5'-cyclic phosphodiesterase 4B (EC 3.1.4.53) (DPDE4)

 PDE4B_RAT               Reviewed;         736 AA.
P14646; Q5RKL0; Q8VD81; Q8VD82;
01-APR-1990, integrated into UniProtKB/Swiss-Prot.
10-JUL-2007, sequence version 4.
25-OCT-2017, entry version 140.
RecName: Full=cAMP-specific 3',5'-cyclic phosphodiesterase 4B;
EC=3.1.4.53;
AltName: Full=DPDE4;
Name=Pde4b;
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 2), AND INDUCTION.
TISSUE=Sertoli cell;
PubMed=1655746;
Swinnen J.V., Tsikalas K.E., Conti M.;
"Properties and hormonal regulation of two structurally related cAMP
phosphodiesterases from the rat Sertoli cell.";
J. Biol. Chem. 266:18370-18377(1991).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
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=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).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
TISSUE=Olfactory bulb;
PubMed=9371714; DOI=10.1042/bj3280549;
Huston E., Lumb S., Russell A., Catterall C., Ross A.H., Steele M.R.,
Bolger G.B., Perry M.J., Owens R.J., Houslay M.D.;
"Molecular cloning and transient expression in COS7 cells of a novel
human PDE4B cAMP-specific phosphodiesterase, HSPDE4B3.";
Biochem. J. 328:549-558(1997).
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 4), BIOPHYSICOCHEMICAL
PROPERTIES, PHOSPHORYLATION AT SER-56 (ISOFORM 4), AND TISSUE
SPECIFICITY.
STRAIN=Sprague-Dawley; TISSUE=Brain cortex;
PubMed=12441002; DOI=10.1042/BJ20021082;
Shepherd M., McSorley T., Olsen A.E., Johnston L.A., Thomson N.C.,
Baillie G.S., Houslay M.D., Bolger G.B.;
"Molecular cloning and subcellular distribution of the novel PDE4B4
cAMP-specific phosphodiesterase isoform.";
Biochem. J. 370:429-438(2003).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
TISSUE=Heart;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
NUCLEOTIDE SEQUENCE [MRNA] OF 175-736.
TISSUE=Brain;
PubMed=2542941; DOI=10.1073/pnas.86.10.3599;
Colicelli J., Birchmeier C., Michaeli T., O'Neill K., Riggs M.,
Wigler M.;
"Isolation and characterization of a mammalian gene encoding a high-
affinity cAMP phosphodiesterase.";
Proc. Natl. Acad. Sci. U.S.A. 86:3599-3603(1989).
[8]
NUCLEOTIDE SEQUENCE [MRNA] OF 304-663.
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).
[9]
TISSUE SPECIFICITY, AND INDUCTION.
PubMed=19103603; DOI=10.1074/jbc.M808394200;
Bailey M.J., Coon S.L., Carter D.A., Humphries A., Kim J.S., Shi Q.,
Gaildrat P., Morin F., Ganguly S., Hogenesch J.B., Weller J.L.,
Rath M.F., Moller M., Baler R., Sugden D., Rangel Z.G., Munson P.J.,
Klein D.C.;
"Night/day changes in pineal expression of >600 genes: central role of
adrenergic/cAMP signaling.";
J. Biol. Chem. 284:7606-7622(2009).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-290; SER-659 AND
SER-661, 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.
{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: Expression is under the control of follicle-
stimulating hormone and cAMP. Inhibited by rolipram.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=5.4 uM for cAMP (isoform 4) {ECO:0000269|PubMed:12441002};
Note=Vmax values for isoforms 2, 3 and 4 relative to isoform 1
are 3.8, 1.6 and 2.1.;
-!- PATHWAY: Purine metabolism; 3',5'-cyclic AMP degradation; AMP from
3',5'-cyclic AMP: step 1/1.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=5;
Name=1; Synonyms=PDE4B1;
IsoId=P14646-3; Sequence=Displayed;
Name=2; Synonyms=PDE4B2;
IsoId=P14646-2; Sequence=VSP_026678, VSP_004573;
Name=3; Synonyms=PDE4B3;
IsoId=P14646-1; Sequence=VSP_026679;
Name=4; Synonyms=PDE4B4;
IsoId=P14646-4; Sequence=VSP_026680;
Note=Contains a phosphoserine at position 56. Activated by
phosphorylation at Ser-56. Mutagenesis of Ser-56 abolishes
activation. {ECO:0000269|PubMed:12441002};
Name=5;
IsoId=P14646-5; Sequence=VSP_026679, VSP_026681;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Widely expressed. Isoform 3 expressed in
brain, heart, lung and liver. Isoform 4 expressed in liver and
brain. {ECO:0000269|PubMed:12441002, ECO:0000269|PubMed:19103603}.
-!- INDUCTION: In Sertoli cells, induced by FSH. In the pineal gland,
exhibits night/day variations with a 7-fold increased expression
at night. Up-regulation is due to a large degree to the release of
norepinephrine from nerve terminals in the pineal gland and cAMP
signaling pathway. {ECO:0000269|PubMed:1655746,
ECO:0000269|PubMed:19103603}.
-!- SIMILARITY: Belongs to the cyclic nucleotide phosphodiesterase
family. PDE4 subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; L27058; AAA74478.1; -; mRNA.
EMBL; U01291; AAA18926.1; -; Unassigned_DNA.
EMBL; U01289; AAA18926.1; JOINED; Unassigned_DNA.
EMBL; U01293; AAA18926.1; JOINED; Unassigned_DNA.
EMBL; U01294; AAA18926.1; JOINED; Unassigned_DNA.
EMBL; U01295; AAA18926.1; JOINED; Unassigned_DNA.
EMBL; U01296; AAA18926.1; JOINED; Unassigned_DNA.
EMBL; U01297; AAA18926.1; JOINED; Unassigned_DNA.
EMBL; U01298; AAA18926.1; JOINED; Unassigned_DNA.
EMBL; U01290; AAA18926.1; JOINED; Unassigned_DNA.
EMBL; U95748; AAB96560.1; -; mRNA.
EMBL; AF202732; AAL31763.1; -; mRNA.
EMBL; AF202733; AAL31764.1; -; mRNA.
EMBL; BC085704; AAH85704.1; -; mRNA.
EMBL; J04563; AAA66039.1; -; mRNA.
EMBL; M25350; AAA41846.1; -; mRNA.
EMBL; M28413; AAA41824.1; -; mRNA.
PIR; A40949; A40949.
PIR; I59143; I59143.
RefSeq; NP_058727.2; NM_017031.2. [P14646-1]
UniGene; Rn.37733; -.
ProteinModelPortal; P14646; -.
SMR; P14646; -.
BioGrid; 246764; 1.
STRING; 10116.ENSRNOP00000007738; -.
BindingDB; P14646; -.
ChEMBL; CHEMBL3382; -.
iPTMnet; P14646; -.
PhosphoSitePlus; P14646; -.
PaxDb; P14646; -.
PRIDE; P14646; -.
Ensembl; ENSRNOT00000007738; ENSRNOP00000007738; ENSRNOG00000005905. [P14646-2]
GeneID; 24626; -.
KEGG; rno:24626; -.
UCSC; RGD:3280; rat. [P14646-3]
CTD; 5142; -.
RGD; 3280; Pde4b.
eggNOG; KOG3689; Eukaryota.
eggNOG; ENOG410XRI7; LUCA.
GeneTree; ENSGT00760000118889; -.
HOGENOM; HOG000236297; -.
HOVERGEN; HBG108239; -.
InParanoid; P14646; -.
KO; K13293; -.
PhylomeDB; P14646; -.
TreeFam; TF314638; -.
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:P14646; -.
Proteomes; UP000002494; Chromosome 5.
Bgee; ENSRNOG00000005905; -.
ExpressionAtlas; P14646; baseline and differential.
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:0007165; P:signal transduction; IEA:InterPro.
CDD; cd00077; HDc; 1.
Gene3D; 1.10.1300.10; -; 1.
InterPro; IPR003607; HD/PDEase_dom.
InterPro; IPR023088; PDEase.
InterPro; IPR002073; PDEase_catalytic_dom.
InterPro; IPR036971; PDEase_catalytic_dom_sf.
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;
Alternative splicing; cAMP; Complete proteome; Hydrolase;
Metal-binding; Phosphoprotein; Reference proteome.
CHAIN 1 736 cAMP-specific 3',5'-cyclic
phosphodiesterase 4B.
/FTId=PRO_0000198810.
NP_BIND 406 410 cAMP. {ECO:0000250}.
ACT_SITE 406 406 Proton donor. {ECO:0000250}.
METAL 410 410 Divalent metal cation 1. {ECO:0000250}.
METAL 446 446 Divalent metal cation 1. {ECO:0000250}.
METAL 447 447 Divalent metal cation 1. {ECO:0000250}.
METAL 447 447 Divalent metal cation 2. {ECO:0000250}.
METAL 564 564 Divalent metal cation 1. {ECO:0000250}.
BINDING 447 447 cAMP. {ECO:0000250}.
BINDING 564 564 cAMP. {ECO:0000250}.
BINDING 615 615 cAMP. {ECO:0000250}.
SITE 567 567 Binds AMP, but not cAMP. {ECO:0000250}.
MOD_RES 290 290 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 659 659 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 661 661 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
VAR_SEQ 1 172 Missing (in isoform 2).
{ECO:0000303|PubMed:1655746,
ECO:0000303|PubMed:7958996,
ECO:0000303|PubMed:8276818}.
/FTId=VSP_026678.
VAR_SEQ 1 93 MKKSRSVMAVTADDNLKDYFECSLSKSYSSSSYTLGIDLWR
GRRCCSGNLQLPPLSQRQSERARTPEGDGISRPTTLPLTTL
PSIAITTVSQE -> MTAKNSSKELPASESEVCIKTFKEQM
RLELELPKLPGNRPTSPKISPRSSPRNSPCFFRKLLVNKSI
RQRRRFTVAHT (in isoform 3 and isoform 5).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:9371714}.
/FTId=VSP_026679.
VAR_SEQ 1 93 MKKSRSVMAVTADDNLKDYFECSLSKSYSSSSYTLGIDLWR
GRRCCSGNLQLPPLSQRQSERARTPEGDGISRPTTLPLTTL
PSIAITTVSQE -> MLHVNDLPPPRRHSWI (in
isoform 4).
{ECO:0000303|PubMed:12441002}.
/FTId=VSP_026680.
VAR_SEQ 173 211 LASLRIVRNNFTLLTNLHGAPNKRSPAASQAPVTRVSLQ
-> MKEQGGTVSGAGSSRGGGDSAMASLQPLQPNYLSVCLF
A (in isoform 2).
{ECO:0000303|PubMed:1655746,
ECO:0000303|PubMed:7958996,
ECO:0000303|PubMed:8276818}.
/FTId=VSP_004573.
VAR_SEQ 710 736 VIDPENRDSLEETDIDIATEDKSLIDT -> KPCHAANGLA
LPVGGGNAASTQPRCGHV (in isoform 5).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_026681.
CONFLICT 178 178 I -> S (in Ref. 5; AAL31763/AAL31764 and
6; AAH85704). {ECO:0000305}.
CONFLICT 531 531 T -> S (in Ref. 3; AAA18926).
{ECO:0000305}.
SEQUENCE 736 AA; 83375 MW; C48F576EFA8DF498 CRC64;
MKKSRSVMAV TADDNLKDYF ECSLSKSYSS SSYTLGIDLW RGRRCCSGNL QLPPLSQRQS
ERARTPEGDG ISRPTTLPLT TLPSIAITTV SQECFDVENG PSPGRSPLDP QASSSSGLVL
HAAFPGHSQR RESFLYRSDS DYDLSPKAMS RNSSLPSEQH GDDLIVTPFA QVLASLRIVR
NNFTLLTNLH GAPNKRSPAA SQAPVTRVSL QEESYQKLAM ETLEELDWCL DQLETIQTYR
SVSEMASNKF KRMLNRELTH LSEMSRSGNQ VSEYISNTFL DKQNDVEIPS PTQKDREKKK
KQQLMTQISG VKKLMHSSSL NNTSISRFGV NTENEDHLAK ELEDLNKWGL NIFNVAGYSH
NRPLTCIMYA IFQERDLLKT FKISSDTFVT YMMTLEDHYH SDVAYHNSLH AADVAQSTHV
LLSTPALDAV FTDLEILAAI FAAAIHDVDH PGVSNQFLIN TNSELALMYN DESVLENHHL
AVGFKLLQEE HCDIFQNLTK KQRQTLRKMV IDMVLATDMS KHMSLLADLK TMVETKKVTS
SGVLLLDNYT DRIQVLRNMV HCADLSNPTK SLELYRQWTD RIMEEFFQQG DKERERGMEI
SPMCDKHTAS VEKSQVGFID YIVHPLWETW ADLVQPDAQD ILDTLEDNRN WYQSMIPQSP
SPPLDERSRD CQGLMEKFQF ELTLEEEDSE GPEKEGEGPN YFSSTKTLCV IDPENRDSLE
ETDIDIATED KSLIDT


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