P14270 (PDE4D_RAT) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
cAMP-specific 3',5'-cyclic phosphodiesterase 4D
EC=3.1.4.17

Alternative name(s):
DPDE3

Gene names

Name:

Pde4d

Organism

Rattus norvegicus (Rat) [Reference proteome]

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	803 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Hydrolyzes the second messenger cAMP, which is a key regulator of many important physiological processes.
Catalytic activity	Adenosine 3',5'-cyclic phosphate + H2O = adenosine 5'-phosphate.
Cofactor	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.
Enzyme regulation	Inhibited by rolipram. Activated by phosphatidic acid By similarity.
Pathway	Purine metabolism; 3',5'-cyclic AMP degradation; AMP from 3',5'-cyclic AMP: step 1/1.
Subunit structure	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. Ref.12 Ref.13
Subcellular location	Cytoplasm. Membrane. Cytoplasm › cytoskeleton. Cytoplasm › cytoskeleton › centrosome. Note: Found in the soluble fraction, associated with membranes, and associated with the cytoskeleton and the centrosome. Ref.11 Ref.13
Induction	Up-regulated by cAMP and follicle-stimulating hormone. Ref.1
Post-translational modification	Isoform 1 is rapidly activated by PKA through phosphorylation. Sumoylation of long isoforms by PIAS4 augments their activation by PKA phosphorylation and represses their inhibition by ERK phosphorylation By similarity.
Sequence similarities	Belongs to the cyclic nucleotide phosphodiesterase family. PDE4 subfamily.

Ontologies

Keywords
Cellular component	Cytoplasm Cytoskeleton Membrane
Coding sequence diversity	Alternative splicing
Ligand	Metal-binding cAMP
Molecular function	Hydrolase
PTM	Isopeptide bond Phosphoprotein Ubl conjugation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cAMP catabolic process Inferred from direct assay PubMed 21724846. Source: UniProtKB cellular protein complex assembly Inferred from direct assay Ref.12. Source: RGD establishment of endothelial barrier Inferred from direct assay PubMed 20139324. Source: UniProtKB memory Inferred from expression pattern PubMed 15302115. Source: RGD regulation of G-protein coupled receptor protein signaling pathway Inferred from direct assay PubMed 12552097. Source: RGD regulation of protein kinase A signaling cascade Inferred from mutant phenotype PubMed 11296225. Source: RGD signal transduction Inferred from electronic annotation. Source: InterPro
Cellular_component	Golgi apparatus Inferred from direct assay Ref.12. Source: RGD centrosome Inferred from direct assay Ref.12. Source: RGD membrane Inferred from electronic annotation. Source: UniProtKB-SubCell myofibril Inferred from direct assay Ref.12. Source: RGD
Molecular_function	3',5'-cyclic-AMP phosphodiesterase activity Inferred from direct assay PubMed 12181425PubMed 18073242. Source: RGD cAMP binding Inferred from mutant phenotype PubMed 11296225. Source: RGD metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Alternative products

This entry describes 7 isoforms produced by alternative splicing. [Align] [Select]

Isoform 4 (identifier: P14270-5)

Also known as: PDE4D4;

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.

Isoform 33 (identifier: P14270-1)

Also known as: PDE4D3; PDE3.3;

The sequence of this isoform differs from the canonical sequence as follows:
     1-131: Missing.
     132-147: KKSRMSWPSSFQGLRR → MMHVNTFPFRRHSWIC

Isoform 31 (identifier: P14270-2)

Also known as: PDE3.1;

The sequence of this isoform differs from the canonical sequence as follows:
     1-264: MEAEGSSVPA...QPSINKATIT → MKEQPSCAGT...TESPFPCLFA

Isoform 32 (identifier: P14270-3)

Also known as: PDE3.2;

The sequence of this isoform differs from the canonical sequence as follows:
     1-297: Missing.

Isoform 7 (identifier: P14270-4)

Also known as: PDE4D7;

The sequence of this isoform differs from the canonical sequence as follows:
     1-56: Missing.
     57-147: LPPPPPPSPQ...WPSSFQGLRR → MERNTCDVLS...IAVTSADSTG

Isoform 9 (identifier: P14270-6)

Also known as: PDE4D9;

The sequence of this isoform differs from the canonical sequence as follows:
     1-125: Missing.
     126-147: GHRPGLKKSRMSWPSSFQGLRR → MSIIMKPRSRSTSSLRTTEAVC

Isoform 6 (identifier: P14270-7)

Also known as: PDE4D6;

The sequence of this isoform differs from the canonical sequence as follows:
     1-286: Missing.
     287-301: ETLQTRHSVSEMASN → MPEANYLLSVSWGYI

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 803	803	cAMP-specific 3',5'-cyclic phosphodiesterase 4D		PRO_0000198816
Regions
	Nucleotide binding	457 – 461	5	cAMP By similarity
Sites
	Active site	457	1	Proton donor By similarity
	Metal binding	461	1	Divalent metal cation 1 By similarity
	Metal binding	497	1	Divalent metal cation 1 By similarity
	Metal binding	498	1	Divalent metal cation 1 By similarity
	Metal binding	498	1	Divalent metal cation 2 By similarity
	Metal binding	615	1	Divalent metal cation 1 By similarity
	Binding site	498	1	cAMP By similarity
	Site	618	1	Binds AMP, but not cAMP By similarity
Amino acid modifications
	Modified residue	185	1	Phosphoserine By similarity
	Modified residue	294	1	Phosphoserine By similarity
	Modified residue	296	1	Phosphoserine By similarity
	Cross-link	382		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity
Natural variations
	Alternative sequence	1 – 297	297	Missing in isoform 32.		VSP_004582
	Alternative sequence	1 – 286	286	Missing in isoform 6.		VSP_012404
	Alternative sequence	1 – 264	264	MEAEG…KATIT → MKEQPSCAGTGHPSMAGYGR MAPFELAGGPVKRLRTESPF PCLFA in isoform 31.		VSP_004581
	Alternative sequence	1 – 131	131	Missing in isoform 33.		VSP_012398
	Alternative sequence	1 – 125	125	Missing in isoform 9.		VSP_012402
	Alternative sequence	1 – 56	56	Missing in isoform 7.		VSP_012400
	Alternative sequence	57 – 147	91	LPPPP…QGLRR → MERNTCDVLSRSKSASEETL HSCNDEEDPFRGMEPYLVRR LSSRSIQLPPLAFRQLEQTD LRSESENIPRPTSLPLKILP LIAVTSADSTG in isoform 7.		VSP_012401
	Alternative sequence	126 – 147	22	GHRPG…QGLRR → MSIIMKPRSRSTSSLRTTEA VC in isoform 9.		VSP_012403
	Alternative sequence	132 – 147	16	KKSRM…QGLRR → MMHVNTFPFRRHSWIC in isoform 33.		VSP_012399
	Alternative sequence	287 – 301	15	ETLQT…EMASN → MPEANYLLSVSWGYI in isoform 6.		VSP_012405
Experimental info
	Sequence conflict	226	1	A → N in AAA56857. Ref.4
	Sequence conflict	357	1	S → P in AAQ90405. Ref.9
	Sequence conflict	480 – 486	7	Missing Ref.5
	Sequence conflict	641	1	G → E in AAC26969. Ref.4
	Sequence conflict	757	1	C → Y in AAA56857. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	Isoform 4 (PDE4D4) [UniParc]. Last modified January 4, 2005. Version 4. Checksum: 13E28B257556496D	FASTA	803	90,552
	10 20 30 40 50 60 MEAEGSSVPA RAGSHEGSDS SGGAALKAPK HLWRHEQHHQ YPLRQPQFRL LHPHHHLPPP 70 80 90 100 110 120 PPPSPQPQLQ PPPPPPLPPP PPPPGATRGR YASSGASRVR HRGYSDTERY LYCRAMDRTS 130 140 150 160 170 180 YAVETGHRPG LKKSRMSWPS SFQGLRRFDV DNGTSAGRSP LDPMTSPGSG LILQANFVHS 190 200 210 220 230 240 QRRESFLYRS DSDYDLSPKS MSRNSSIASD IHGDDLIVTP FAQVLASLRT VRNNFAALTN 250 260 270 280 290 300 LQDRAPSKRS PMCNQPSINK ATITEEAYQK LASETLEELD WCLDQLETLQ TRHSVSEMAS 310 320 330 340 350 360 NKFKRMLNRE LTHLSEMSRS GNQVSEYISN TFLDKQHEVE IPSPTQKEKE KKKRPMSQIS 370 380 390 400 410 420 GVKKLMHSSS LTNSCIPRFG VKTEQEDVLA KELEDVNKWG LHVFRIAELS GNRPLTVIMH 430 440 450 460 470 480 TIFQERDLLK TFKIPVDTLI TYLMTLEDHY HADVAYHNNI HAADVVQSTH VLLSTPALEA 490 500 510 520 530 540 VFTDLEILAA IFASAIHDVD HPGVSNQFLI NTNSELALMY NDSSVLENHH LAVGFKLLQE 550 560 570 580 590 600 ENCDIFQNLT KKQRQSLRKM AIDIVLATDM SKHMNLLADL KTMVETKKVT SSGVLLLDNY 610 620 630 640 650 660 SDRIQVLQNM VHCADLSNPT KPLQLYRQWT DRIMEEFFRQ GDRERERGME ISPMCDKHNA 670 680 690 700 710 720 SVEKSQVGFI DYIVHPLWET WADLVHPDAQ DILDTLEDNR EWYQSTIPQS PSPAPDDQED 730 740 750 760 770 780 GRQGQTEKFQ FELTLEEDGE SDTEKDSGSQ VEEDTSCSDS KTLCTQDSES TEIPLDEQVE 790 800 EEAVAEEESQ PQTGVADDCC PDT
	Isoform 33 (PDE4D3) (PDE3.3) [UniParc]. Checksum: 63CE38FA654A0BDD	FASTA	672	76,263
	10 20 30 40 50 60 MMHVNTFPFR RHSWICFDVD NGTSAGRSPL DPMTSPGSGL ILQANFVHSQ RRESFLYRSD 70 80 90 100 110 120 SDYDLSPKSM SRNSSIASDI HGDDLIVTPF AQVLASLRTV RNNFAALTNL QDRAPSKRSP 130 140 150 160 170 180 MCNQPSINKA TITEEAYQKL ASETLEELDW CLDQLETLQT RHSVSEMASN KFKRMLNREL 190 200 210 220 230 240 THLSEMSRSG NQVSEYISNT FLDKQHEVEI PSPTQKEKEK KKRPMSQISG VKKLMHSSSL 250 260 270 280 290 300 TNSCIPRFGV KTEQEDVLAK ELEDVNKWGL HVFRIAELSG NRPLTVIMHT IFQERDLLKT 310 320 330 340 350 360 FKIPVDTLIT YLMTLEDHYH ADVAYHNNIH AADVVQSTHV LLSTPALEAV FTDLEILAAI 370 380 390 400 410 420 FASAIHDVDH PGVSNQFLIN TNSELALMYN DSSVLENHHL AVGFKLLQEE NCDIFQNLTK 430 440 450 460 470 480 KQRQSLRKMA IDIVLATDMS KHMNLLADLK TMVETKKVTS SGVLLLDNYS DRIQVLQNMV 490 500 510 520 530 540 HCADLSNPTK PLQLYRQWTD RIMEEFFRQG DRERERGMEI SPMCDKHNAS VEKSQVGFID 550 560 570 580 590 600 YIVHPLWETW ADLVHPDAQD ILDTLEDNRE WYQSTIPQSP SPAPDDQEDG RQGQTEKFQF 610 620 630 640 650 660 ELTLEEDGES DTEKDSGSQV EEDTSCSDSK TLCTQDSEST EIPLDEQVEE EAVAEEESQP 670 QTGVADDCCP DT
	Isoform 31 (PDE3.1) [UniParc]. Checksum: 7C0DAEB75774F2F8	FASTA	584	66,243
	10 20 30 40 50 60 MKEQPSCAGT GHPSMAGYGR MAPFELAGGP VKRLRTESPF PCLFAEEAYQ KLASETLEEL 70 80 90 100 110 120 DWCLDQLETL QTRHSVSEMA SNKFKRMLNR ELTHLSEMSR SGNQVSEYIS NTFLDKQHEV 130 140 150 160 170 180 EIPSPTQKEK EKKKRPMSQI SGVKKLMHSS SLTNSCIPRF GVKTEQEDVL AKELEDVNKW 190 200 210 220 230 240 GLHVFRIAEL SGNRPLTVIM HTIFQERDLL KTFKIPVDTL ITYLMTLEDH YHADVAYHNN 250 260 270 280 290 300 IHAADVVQST HVLLSTPALE AVFTDLEILA AIFASAIHDV DHPGVSNQFL INTNSELALM 310 320 330 340 350 360 YNDSSVLENH HLAVGFKLLQ EENCDIFQNL TKKQRQSLRK MAIDIVLATD MSKHMNLLAD 370 380 390 400 410 420 LKTMVETKKV TSSGVLLLDN YSDRIQVLQN MVHCADLSNP TKPLQLYRQW TDRIMEEFFR 430 440 450 460 470 480 QGDRERERGM EISPMCDKHN ASVEKSQVGF IDYIVHPLWE TWADLVHPDA QDILDTLEDN 490 500 510 520 530 540 REWYQSTIPQ SPSPAPDDQE DGRQGQTEKF QFELTLEEDG ESDTEKDSGS QVEEDTSCSD 550 560 570 580 SKTLCTQDSE STEIPLDEQV EEEAVAEEES QPQTGVADDC CPDT
	Isoform 32 (PDE3.2) [UniParc]. Checksum: 7DCA5A564384FC34	FASTA	506	57,601
	10 20 30 40 50 60 MASNKFKRML NRELTHLSEM SRSGNQVSEY ISNTFLDKQH EVEIPSPTQK EKEKKKRPMS 70 80 90 100 110 120 QISGVKKLMH SSSLTNSCIP RFGVKTEQED VLAKELEDVN KWGLHVFRIA ELSGNRPLTV 130 140 150 160 170 180 IMHTIFQERD LLKTFKIPVD TLITYLMTLE DHYHADVAYH NNIHAADVVQ STHVLLSTPA 190 200 210 220 230 240 LEAVFTDLEI LAAIFASAIH DVDHPGVSNQ FLINTNSELA LMYNDSSVLE NHHLAVGFKL 250 260 270 280 290 300 LQEENCDIFQ NLTKKQRQSL RKMAIDIVLA TDMSKHMNLL ADLKTMVETK KVTSSGVLLL 310 320 330 340 350 360 DNYSDRIQVL QNMVHCADLS NPTKPLQLYR QWTDRIMEEF FRQGDRERER GMEISPMCDK 370 380 390 400 410 420 HNASVEKSQV GFIDYIVHPL WETWADLVHP DAQDILDTLE DNREWYQSTI PQSPSPAPDD 430 440 450 460 470 480 QEDGRQGQTE KFQFELTLEE DGESDTEKDS GSQVEEDTSC SDSKTLCTQD SESTEIPLDE 490 500 QVEEEAVAEE ESQPQTGVAD DCCPDT
	Isoform 7 (PDE4D7) [UniParc]. Checksum: D63B9EF50AA3EFC9	FASTA	747	84,430
	10 20 30 40 50 60 MERNTCDVLS RSKSASEETL HSCNDEEDPF RGMEPYLVRR LSSRSIQLPP LAFRQLEQTD 70 80 90 100 110 120 LRSESENIPR PTSLPLKILP LIAVTSADST GFDVDNGTSA GRSPLDPMTS PGSGLILQAN 130 140 150 160 170 180 FVHSQRRESF LYRSDSDYDL SPKSMSRNSS IASDIHGDDL IVTPFAQVLA SLRTVRNNFA 190 200 210 220 230 240 ALTNLQDRAP SKRSPMCNQP SINKATITEE AYQKLASETL EELDWCLDQL ETLQTRHSVS 250 260 270 280 290 300 EMASNKFKRM LNRELTHLSE MSRSGNQVSE YISNTFLDKQ HEVEIPSPTQ KEKEKKKRPM 310 320 330 340 350 360 SQISGVKKLM HSSSLTNSCI PRFGVKTEQE DVLAKELEDV NKWGLHVFRI AELSGNRPLT 370 380 390 400 410 420 VIMHTIFQER DLLKTFKIPV DTLITYLMTL EDHYHADVAY HNNIHAADVV QSTHVLLSTP 430 440 450 460 470 480 ALEAVFTDLE ILAAIFASAI HDVDHPGVSN QFLINTNSEL ALMYNDSSVL ENHHLAVGFK 490 500 510 520 530 540 LLQEENCDIF QNLTKKQRQS LRKMAIDIVL ATDMSKHMNL LADLKTMVET KKVTSSGVLL 550 560 570 580 590 600 LDNYSDRIQV LQNMVHCADL SNPTKPLQLY RQWTDRIMEE FFRQGDRERE RGMEISPMCD 610 620 630 640 650 660 KHNASVEKSQ VGFIDYIVHP LWETWADLVH PDAQDILDTL EDNREWYQST IPQSPSPAPD 670 680 690 700 710 720 DQEDGRQGQT EKFQFELTLE EDGESDTEKD SGSQVEEDTS CSDSKTLCTQ DSESTEIPLD 730 740 EQVEEEAVAE EESQPQTGVA DDCCPDT
	Isoform 9 (PDE4D9) [UniParc]. Checksum: E3069D16ADEBEC6C	FASTA	678	76,656
	10 20 30 40 50 60 MSIIMKPRSR STSSLRTTEA VCFDVDNGTS AGRSPLDPMT SPGSGLILQA NFVHSQRRES 70 80 90 100 110 120 FLYRSDSDYD LSPKSMSRNS SIASDIHGDD LIVTPFAQVL ASLRTVRNNF AALTNLQDRA 130 140 150 160 170 180 PSKRSPMCNQ PSINKATITE EAYQKLASET LEELDWCLDQ LETLQTRHSV SEMASNKFKR 190 200 210 220 230 240 MLNRELTHLS EMSRSGNQVS EYISNTFLDK QHEVEIPSPT QKEKEKKKRP MSQISGVKKL 250 260 270 280 290 300 MHSSSLTNSC IPRFGVKTEQ EDVLAKELED VNKWGLHVFR IAELSGNRPL TVIMHTIFQE 310 320 330 340 350 360 RDLLKTFKIP VDTLITYLMT LEDHYHADVA YHNNIHAADV VQSTHVLLST PALEAVFTDL 370 380 390 400 410 420 EILAAIFASA IHDVDHPGVS NQFLINTNSE LALMYNDSSV LENHHLAVGF KLLQEENCDI 430 440 450 460 470 480 FQNLTKKQRQ SLRKMAIDIV LATDMSKHMN LLADLKTMVE TKKVTSSGVL LLDNYSDRIQ 490 500 510 520 530 540 VLQNMVHCAD LSNPTKPLQL YRQWTDRIME EFFRQGDRER ERGMEISPMC DKHNASVEKS 550 560 570 580 590 600 QVGFIDYIVH PLWETWADLV HPDAQDILDT LEDNREWYQS TIPQSPSPAP DDQEDGRQGQ 610 620 630 640 650 660 TEKFQFELTL EEDGESDTEK DSGSQVEEDT SCSDSKTLCT QDSESTEIPL DEQVEEEAVA 670 EEESQPQTGV ADDCCPDT
	Isoform 6 (PDE4D6) [UniParc]. Checksum: 251BF853D7CE6870	FASTA	517	58,923
	10 20 30 40 50 60 MPEANYLLSV SWGYIKFKRM LNRELTHLSE MSRSGNQVSE YISNTFLDKQ HEVEIPSPTQ 70 80 90 100 110 120 KEKEKKKRPM SQISGVKKLM HSSSLTNSCI PRFGVKTEQE DVLAKELEDV NKWGLHVFRI 130 140 150 160 170 180 AELSGNRPLT VIMHTIFQER DLLKTFKIPV DTLITYLMTL EDHYHADVAY HNNIHAADVV 190 200 210 220 230 240 QSTHVLLSTP ALEAVFTDLE ILAAIFASAI HDVDHPGVSN QFLINTNSEL ALMYNDSSVL 250 260 270 280 290 300 ENHHLAVGFK LLQEENCDIF QNLTKKQRQS LRKMAIDIVL ATDMSKHMNL LADLKTMVET 310 320 330 340 350 360 KKVTSSGVLL LDNYSDRIQV LQNMVHCADL SNPTKPLQLY RQWTDRIMEE FFRQGDRERE 370 380 390 400 410 420 RGMEISPMCD KHNASVEKSQ VGFIDYIVHP LWETWADLVH PDAQDILDTL EDNREWYQST 430 440 450 460 470 480 IPQSPSPAPD DQEDGRQGQT EKFQFELTLE EDGESDTEKD SGSQVEEDTS CSDSKTLCTQ 490 500 510 DSESTEIPLD EQVEEEAVAE EESQPQTGVA DDCCPDT

References

[1]	"The mRNA encoding a high-affinity cAMP phosphodiesterase is regulated by hormones and cAMP." Swinnen J.V., Joseph D.R., Conti M. Proc. Natl. Acad. Sci. U.S.A. 86:8197-8201(1989) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 31), INDUCTION. Tissue: Testis.
[2]	"The ratPDE3/IVd phosphodiesterase gene codes for multiple proteins differentially activated by cAMP-dependent protein kinase." Sette C., Vicini E., Conti M. J. Biol. Chem. 269:18271-18274(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 31; 32 AND 33).
[3]	Conti M. Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases Cited for: SEQUENCE REVISION TO 6.
[4]	"Differential CNS expression of alternative mRNA isoforms of the mammalian genes encoding cAMP-specific phosphodiesterases." Bolger G.B., Rodgers L., Riggs M. Gene 149:237-244(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 226-803 (ISOFORM 33), NUCLEOTIDE SEQUENCE [MRNA] OF 253-803 (ISOFORM 31).
[5]	"Structure of two rat genes coding for closely related rolipram-sensitive cAMP phosphodiesterases. Multiple mRNA variants originate from alternative splicing and multiple start sites." Monaco L., Vicini E., Conti M. J. Biol. Chem. 269:347-357(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE (ISOFORMS 31 AND 32). Strain: Wistar.
[6]	Erratum Monaco L., Vicini E., Conti M. J. Biol. Chem. 269:20806-20806(1994)
[7]	"Characterization of a cAMP-specific phosphodiesterase variant (PDE4D4) expressed in the rat brain." Jin S.-L.C., Kuo W.-P., Conti M. Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE (ISOFORM 4). Strain: Sprague-Dawley. Tissue: Brain.
[8]	"Cloning and characterization of novel PDE4D isoforms PDE4D6 and PDE4D7." Wang D., Deng C., Bugaj-Gaweda B., Kwan M., Gunwaldsen C., Leonard C., Xin X., Hu Y., Unterbeck A., De Vivo M. Cell. Signal. 15:883-891(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 6 AND 7). Strain: Sprague-Dawley.
[9]	"Novel PDE4D isoform, PDE4D9." Gaweda B., De Vivo M., Wang D. Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE (ISOFORM 9).
[10]	"Molecular cloning of rat homologues of the Drosophila melanogaster dunce cAMP phosphodiesterase: evidence for a family of genes." Swinnen J.V., Joseph D.R., Conti M. Proc. Natl. Acad. Sci. U.S.A. 86:5325-5329(1989) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE OF 224-672. Tissue: Testis.
[11]	"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." Liu H., Maurice D.H. J. Biol. Chem. 274:10557-10565(1999) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION, SUBCELLULAR LOCATION.
[12]	"Myomegalin is a novel protein of the Golgi/centrosome that interacts with a cyclic nucleotide phosphodiesterase." Verde I., Pahlke G., Salanova M., Zhang G., Wang S., Coletti D., Onuffer J., Jin S.-L.C., Conti M. J. Biol. Chem. 276:11189-11198(2001) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH PDE4DIP.
[13]	"Phosphodiesterase 4D and protein kinase a type II constitute a signaling unit in the centrosomal area." Tasken K.A., Collas P., Kemmner W.A., Witczak O., Conti M., Tasken K. J. Biol. Chem. 276:21999-22002(2001) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION, INTERACTION WITH THE CENTROSOME (ISOFORM 33).
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U09457 mRNA. Translation: AAB81869.1. U09456 mRNA. Translation: AAA20393.1. L27059 mRNA. Translation: AAA56857.1. L27060 mRNA. Translation: AAC26969.1. U01280 , U01278, U01282, U01283, U01284, U01285, U01286, U01287, U01279 Unassigned DNA. Translation: AAA18925.1. U01280 , U01278, U01282, U01283, U01284, U01285, U01286, U01287, U01279 Unassigned DNA. Translation: AAA18924.1. U09455 mRNA. Translation: AAA20401.1. AF031373 mRNA. Translation: AAB95266.1. AF536979 mRNA. Translation: AAN10121.1. AY388961 mRNA. Translation: AAQ90405.1. AF536974 mRNA. Translation: AAN10116.1.
IPI	IPI00203378. IPI00230929. IPI00337259. IPI00391626. IPI00515793. IPI00515813. IPI00515827.
PIR	B53109. I61259.
RefSeq	NP_001106799.1. NM_001113328.1. NP_001106800.1. NM_001113329.1. NP_001106803.1. NM_001113332.1. NP_001106805.1. NM_001113334.1. NP_058728.1. NM_017032.1.
UniGene	Rn.163460. Rn.95959.
3D structure databases
ProteinModelPortal	P14270.
SMR	P14270. Positions 376-736.
ModBase	Search...
Protein-protein interaction databases
STRING	10116.ENSRNOP00000015138.
PTM databases
PhosphoSite	P14270.
Proteomic databases
PRIDE	P14270.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSRNOT00000015138; ENSRNOP00000015138; ENSRNOG00000042536. ENSRNOT00000067546; ENSRNOP00000062384; ENSRNOG00000042536.
GeneID	24627.
KEGG	rno:24627.
Organism-specific databases
CTD	5144.
RGD	3281. Pde4d.
Phylogenomic databases
eggNOG	NOG122287.
GeneTree	ENSGT00690000101692.
HOVERGEN	HBG108239.
KO	K01120.
Enzyme and pathway databases
UniPathway	UPA00762; UER00747.
Gene expression databases
Genevestigator	P14270.
Family and domain databases
Gene3D	1.10.1300.10. 1 hit.
InterPro	IPR003607. HD/PDEase_dom. IPR023088. PDEase. IPR002073. PDEase_catalytic_dom. IPR023174. PDEase_CS. [Graphical view]
Pfam	PF00233. PDEase_I. 1 hit. [Graphical view]
PRINTS	PR00387. PDIESTERASE1.
SMART	SM00471. HDc. 1 hit. [Graphical view]
PROSITE	PS00126. PDEASE_I. 1 hit. [Graphical view]
ProtoNet	Search...
Other
BindingDB	P14270.
ChEMBL	CHEMBL2712.
NextBio	603898.

Entry information

Entry name

PDE4D_RAT

Accession

Primary (citable) accession number: P14270
Secondary accession number(s): O35470 , Q6TRI0, Q8CG04, Q8CG06

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 1, 1990
Last sequence update:	January 4, 2005
Last modified:	April 3, 2013
This is version 115 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program