Q3UEI1 (PDE4C_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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

Gene names

Name:

Pde4c

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [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 › Mus › Mus

Protein attributes

Sequence length	686 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 By similarity.
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 By similarity.
Pathway	Purine metabolism; 3',5'-cyclic AMP degradation; AMP from 3',5'-cyclic AMP: step 1/1.
Subunit structure	Part of a complex containing AKAP5, ADCY5, ADCY6 and PKD2.
Subcellular location	Cell projection › cilium Ref.4.
Sequence similarities	Belongs to the cyclic nucleotide phosphodiesterase family. PDE4 subfamily.

Ontologies

Keywords
Cellular component	Cell projection Cilium
Coding sequence diversity	Alternative splicing
Ligand	Metal-binding cAMP
Molecular function	Hydrolase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cAMP catabolic process Inferred from electronic annotation. Source: UniProtKB-UniPathway signal transduction Inferred from electronic annotation. Source: InterPro
Cellular_component	primary cilium Inferred from direct assay Ref.4. Source: UniProtKB
Molecular_function	3',5'-cyclic-nucleotide phosphodiesterase activity Inferred from electronic annotation. Source: EC metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q3UEI1-1)

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 2 (identifier: Q3UEI1-2)

The sequence of this isoform differs from the canonical sequence as follows:
     537-570: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 686	686	cAMP-specific 3',5'-cyclic phosphodiesterase 4C		PRO_0000198812
Regions
	Nucleotide binding	389 – 393	5	cAMP By similarity
	Compositional bias	659 – 668	10	Poly-Glu
Sites
	Active site	389	1	Proton donor By similarity
	Metal binding	393	1	Divalent metal cation 1 By similarity
	Metal binding	429	1	Divalent metal cation 1 By similarity
	Metal binding	430	1	Divalent metal cation 1 By similarity
	Metal binding	430	1	Divalent metal cation 2 By similarity
	Metal binding	547	1	Divalent metal cation 1 By similarity
	Binding site	430	1	cAMP By similarity
	Binding site	547	1	cAMP By similarity
	Binding site	598	1	cAMP By similarity
	Site	550	1	Binds AMP, but not cAMP By similarity
Amino acid modifications
	Modified residue	299	1	Phosphoserine Ref.3
Natural variations
	Alternative sequence	537 – 570	34	Missing in isoform 2.		VSP_016663

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified October 11, 2005. Version 1. Checksum: 4B510001564A2A08	FASTA	686	76,090
	10 20 30 40 50 60 MRRSGTALSF LWTERVREPV DSGVAPVSPL GGGVILRRFS GTLLLPPLSS RLGSSGEAES 70 80 90 100 110 120 AAHVVFTIGT QGTQRNLGSA QSSFDLENGL PGGKGLLDAQ SGPSLGRALQ PPVHHVQRRE 130 140 150 160 170 180 SFLYRSDSDH EPSPKAVSRT SSAASDLHGE DMIVTPFAQV LASLRTVRNN VAALAHGPGS 190 200 210 220 230 240 ATRQVLLGTP PHSSQQAAPT EDSGLQLVQE TLEELDWCLE QLETLQTRRS VGEMASNKFK 250 260 270 280 290 300 RMLNRELSYL SETSRSGNQV SEYISQTFLD QQAEVELPQP PTEDDPWPMA QITELRRSSH 310 320 330 340 350 360 TSLPTAAIPR FGVQTDQEEQ LAKELEDTNK WGLDVFKVAE LSGNRPLTAV IFSVFQERDL 370 380 390 400 410 420 LKTFQIPADT LLAYLLTLEG HYHSDVAYHN SMHAADVVQS AHVLLGTPAL EAVFTDLEVL 430 440 450 460 470 480 AAIFACAIHD VDHPGVSNQF LINTNSELAL MYNDSSVLEN HHLAVGFKLL QGENCDIFRN 490 500 510 520 530 540 LSTKQRLSLR RMVIDMVLAT DMSKHMSLLA DLKTMVETKK VTSLGVLLLD NYSDRIQVLQ 550 560 570 580 590 600 SLVHCADLSN PAKPLPLYRQ WTERIMAEFF QQGDRERESG LDISPMCDKH TASMEKSQVG 610 620 630 640 650 660 FIDYIAQPLW ETWADLVHPD AQELLDTLED NREWYQSRIP CSPPHTMGSD RFKFELTLEE 670 680 AEEEEEEEDE GQCTALNRES SELPST
	Isoform 2 [UniParc]. Checksum: 75B22BC077830AA9	FASTA	652	72,106
	10 20 30 40 50 60 MRRSGTALSF LWTERVREPV DSGVAPVSPL GGGVILRRFS GTLLLPPLSS RLGSSGEAES 70 80 90 100 110 120 AAHVVFTIGT QGTQRNLGSA QSSFDLENGL PGGKGLLDAQ SGPSLGRALQ PPVHHVQRRE 130 140 150 160 170 180 SFLYRSDSDH EPSPKAVSRT SSAASDLHGE DMIVTPFAQV LASLRTVRNN VAALAHGPGS 190 200 210 220 230 240 ATRQVLLGTP PHSSQQAAPT EDSGLQLVQE TLEELDWCLE QLETLQTRRS VGEMASNKFK 250 260 270 280 290 300 RMLNRELSYL SETSRSGNQV SEYISQTFLD QQAEVELPQP PTEDDPWPMA QITELRRSSH 310 320 330 340 350 360 TSLPTAAIPR FGVQTDQEEQ LAKELEDTNK WGLDVFKVAE LSGNRPLTAV IFSVFQERDL 370 380 390 400 410 420 LKTFQIPADT LLAYLLTLEG HYHSDVAYHN SMHAADVVQS AHVLLGTPAL EAVFTDLEVL 430 440 450 460 470 480 AAIFACAIHD VDHPGVSNQF LINTNSELAL MYNDSSVLEN HHLAVGFKLL QGENCDIFRN 490 500 510 520 530 540 LSTKQRLSLR RMVIDMVLAT DMSKHMSLLA DLKTMVETKK VTSLGVLLLD NYSDRIQQGD 550 560 570 580 590 600 RERESGLDIS PMCDKHTASM EKSQVGFIDY IAQPLWETWA DLVHPDAQEL LDTLEDNREW 610 620 630 640 650 YQSRIPCSPP HTMGSDRFKF ELTLEEAEEE EEEEDEGQCT ALNRESSELP ST

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Strain: C57BL/6J. Tissue: Liver.
[2]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Strain: FVB/N. Tissue: Kidney.
[3]	"Large-scale phosphorylation analysis of mouse liver." Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-299, MASS SPECTROMETRY. Tissue: Liver.
[4]	"Polycystin-2 and phosphodiesterase 4C are components of a ciliary A-kinase anchoring protein complex that is disrupted in cystic kidney diseases." Choi Y.H., Suzuki A., Hajarnis S., Ma Z., Chapin H.C., Caplan M.J., Pontoglio M., Somlo S., Igarashi P. Proc. Natl. Acad. Sci. U.S.A. 108:10679-10684(2011) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION, INTERACTION WITH AKAP5; ADCY5; ADCY6 AND PKD2.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AK149514 mRNA. Translation: BAE28930.1. BC030873 mRNA. Translation: AAH30873.1.
IPI	IPI00111678. IPI00653801.
RefSeq	NP_963901.1. NM_201607.2.
UniGene	Mm.255180.
3D structure databases
ProteinModelPortal	Q3UEI1.
SMR	Q3UEI1. Positions 317-640.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q3UEI1. 1 interaction.
STRING	10090.ENSMUSP00000105722.
PTM databases
PhosphoSite	Q3UEI1.
Proteomic databases
PaxDb	Q3UEI1.
PRIDE	Q3UEI1.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000034307; ENSMUSP00000034307; ENSMUSG00000031842. ENSMUST00000110095; ENSMUSP00000105722; ENSMUSG00000031842.
GeneID	110385.
KEGG	mmu:110385.
UCSC	uc009mbg.1. mouse. uc009mbh.1. mouse.
Organism-specific databases
CTD	5143.
MGI	MGI:99556. Pde4c.
Phylogenomic databases
eggNOG	NOG122287.
GeneTree	ENSGT00690000101692.
HOGENOM	HOG000236297.
HOVERGEN	HBG108239.
InParanoid	Q3UEI1.
KO	K01120.
OMA	AIMFSIF.
OrthoDB	EOG4ZGPBT.
Enzyme and pathway databases
UniPathway	UPA00762; UER00747.
Gene expression databases
ArrayExpress	Q3UEI1.
Bgee	Q3UEI1.
CleanEx	MM_PDE4C.
Genevestigator	Q3UEI1.
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	Q3UEI1.
ChEMBL	CHEMBL2550.
ChiTaRS	PDE4C. mouse.
NextBio	363905.
SOURCE	Search...

Entry information

Entry name

PDE4C_MOUSE

Accession

Primary (citable) accession number: Q3UEI1
Secondary accession number(s): Q8K0P4

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 20, 2005
Last sequence update:	October 11, 2005
Last modified:	April 3, 2013
This is version 64 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program