Reviewed, UniProtKB/Swiss-Prot P0C1Q2 (PDE11_MOUSE)

Names and origin

Protein names

Recommended name:
    Dual 3',5'-cyclic-AMP and -GMP phosphodiesterase 11A
    EC=3.1.4.17
    EC=3.1.4.35
Alternative name(s):
    cAMP and cGMP phosphodiesterase 11A

Gene names

Name:

Pde11a

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

Protein attributes

Sequence length	933 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Plays a role in signal transduction by regulating the intracellular concentration of cyclic nucleotides cAMP and cGMP. Catalyzes the hydrolysis of both cAMP and cGMP to 5'-AMP and 5'-GMP, respectively By similarity. Ref.2
Catalytic activity	Guanosine 3',5'-cyclic phosphate + H2O = guanosine 5'-phosphate. 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 3-isobutyl-1-methylxanthine (IBMX), zaprinast and dipyridamole. cGMP acts as an allosteric activator By similarity.
Subcellular location	Cytoplasm › cytosol By similarity.
Tissue specificity	Expressed in testis and developing spermatoza. Ref.2
Domain	The tandem GAF domains bind cGMP, and regulate enzyme activity. The binding of cGMP leading to stimulate the enzyme activity By similarity.
Disruption phenotype	Mice live well and have no impaired fertility. They do however display reduced sperm concentration, rate of forward progression and percentage of live spermatozoa. Pre-ejaculated sperm display increased premature/spontaneous capacitance. Ref.2
Sequence similarities	Belongs to the cyclic nucleotide phosphodiesterase family. Contains 2 GAF domains.

Ontologies

Keywords
Cellular component	Cytoplasm
Domain	Repeat
Ligand	Metal-binding cAMP cGMP
Molecular function	Hydrolase
PTM	Phosphoprotein
Technical term	Allosteric enzyme
Gene Ontology (GO)
Biological process	signal transduction Inferred from electronic annotation. Source: InterPro
Cellular component	cytosol Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	3',5'-cyclic-GMP phosphodiesterase activity Inferred from electronic annotation. Source: EC metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 933	933	Dual 3',5'-cyclic-AMP and -GMP phosphodiesterase 11A		PRO_0000247041
Regions
	Domain	217 – 370	154	GAF 1
	Domain	402 – 558	157	GAF 2
	Region	640 – 905	266	Catalytic By similarity
Sites
	Active site	664	1	Proton donor By similarity
	Metal binding	668	1	Divalent metal cation 1 By similarity
	Metal binding	704	1	Divalent metal cation 1 By similarity
	Metal binding	705	1	Divalent metal cation 1 By similarity
	Metal binding	705	1	Divalent metal cation 2 By similarity
	Metal binding	708	1	Divalent metal cation 2 By similarity
	Metal binding	734	1	Divalent metal cation 2 By similarity
	Metal binding	816	1	Divalent metal cation 1 By similarity
	Binding site	869	1	cAMP or cGMP By similarity
Amino acid modifications
	Modified residue	162	1	Phosphoserine Ref.3

Sequences

	Sequence		Length	Mass (Da)
	P0C1Q2-1 [UniParc]. Last modified July 25, 2006. Version 1. Checksum: 07B7CA1E4F905755	FASTA	933	104,563
	10 20 30 40 50 60 MAASRLDFGE VETFLDRHPE LFEDYLMRKG KQELVDKWLQ RHTSGQGASS LRPALAGASS 70 80 90 100 110 120 LAQSNAKGSP GIGGGAGPQG SAHSHPTPGG GESAGVPLSP SWASGSRGDG SLQRRASQKE 130 140 150 160 170 180 LRKSFARSKA IHVNRTYDEQ VTSRAQEPLS SVRRRALLRK ASSLPPTTAH ILSALLESRV 190 200 210 220 230 240 NLPQYPPTAI DYKCHLKKHN ERQFFLELVK DISNDLDLTS LSYKILIFVC LMVDADRCSL 250 260 270 280 290 300 FLVEGAAAGK KTLVSKFFDV HAGTPLLPCS STENSNEVQV PWGKGIIGYV GEHGETVNIP 310 320 330 340 350 360 DAYQDRRFND EIDKLTGYKT KSLLCMPIRN SDGEIIGVAQ AINKVPEGAP FTEDDEKVMQ 370 380 390 400 410 420 MYLPFCGIAI SNAQLFAASR KEYERSRALL EVVNDLFEEQ TDLEKIVKKI MHRAQTLLKC 430 440 450 460 470 480 ERCSVLLLED IESPVVKFTK SFELMSPKCS ADAENSFKES VEKSSYSDWL INNSIAELVA 490 500 510 520 530 540 STGLPVNVSD AYQDPRFDAE ADQISGFHIR SVLCVPIWNS NHQIIGVAQV LNRLDGKPFD 550 560 570 580 590 600 DADQRLFEAF VIFCGLGINN TIMYDQVKKS WAKQSVALDV LSYHATCSKA EVDKFKAANI 610 620 630 640 650 660 PLVSELAIDD IHFDDFSLDV DAMITAALRM FMELGMVQKF KIDYETLCRW LLTVRKNYRM 670 680 690 700 710 720 VLYHNWRHAF NVCQLMFAML TTAGFQEILT EVEILAVIVG CLCHDLDHRG TNNAFQAKSD 730 740 750 760 770 780 SALAQLYGTS ATLEHHHFNH AVMILQSEGH NIFANLSSKE YSDLMQLLKQ SILATDLTLY 790 800 810 820 830 840 FERRTEFFEL VRKGDYDWSI TSHRDVFRSM LMTACDLGAV TKPWEISRQV AELVTSEFFE 850 860 870 880 890 900 QGDRERSELK LTPSAIFDRN RKDELPRLQL EWIDSICMPL YQALVKVNAK LKPMLDSVAA 910 920 930 NRRKWEELHQ KRLQVSAASP DPASPMVAGE DRL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Lineage-specific biology revealed by a finished genome assembly of the mouse." Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P. PLoS Biol. 7:E1000112-E1000112(2009) [PubMed: 19468303] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: C57BL/6J.
[2]	"Phosphodiesterase 11 (PDE11) regulation of spermatozoa physiology." Wayman C., Phillips S., Lunny C., Webb T., Fawcett L., Baxendale R., Burgess G. Int. J. Impot. Res. 17:216-223(2005) [PubMed: 15800654] [Abstract] Cited for: TISSUE SPECIFICITY, FUNCTION, DISRUPTION PHENOTYPE.
[3]	"Solid tumor proteome and phosphoproteome analysis by high resolution mass spectrometry." Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J., Faessler R., Mann M. J. Proteome Res. 7:5314-5326(2008) [PubMed: 18973353] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-162, MASS SPECTROMETRY.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AL772341, AL845373, AL929133 Genomic DNA. Translation: CAM16587.1. AL845373, AL772341, AL929133 Genomic DNA. Translation: CAM17618.1. AL929133, AL772341, AL845373 Genomic DNA. Translation: CAM23980.1. AL929589 Genomic DNA. No translation available.
IPI	IPI00753837.
RefSeq	NP_001074502.1.
UniGene	Mm.246613
3D structure databases
SMR	P0C1Q2. Positions 205-570, 589-912.
ModBase	Search...
PTM databases
PhosphoSite	P0C1Q2.
Proteomic databases
PRIDE	P0C1Q2.
Genome annotation databases
Ensembl	ENSMUST00000099992; ENSMUSP00000097572; ENSMUSG00000075270; Mus musculus. [Genome view]
GeneID	241489.
KEGG	mmu:241489.
UCSC	uc008kex.1. mouse.
Organism-specific databases
CTD	241489.
MGI	MGI:3036251. Pde11a.
Phylogenomic databases
HOGENOM	HBG444971.
HOVERGEN	P0C1Q2.
InParanoid	P0C1Q2.
OMA	VEKWLQR.
OrthoDB	EOG9QNQG7.
PhylomeDB	P0C1Q2.
Enzyme and pathway databases
BRENDA	3.1.4.17. 244. 3.1.4.35. 244.
Gene expression databases
ArrayExpress	P0C1Q2.
Bgee	P0C1Q2.
CleanEx	MM_PDE11A.
Genevestigator	P0C1Q2.
Family and domain databases
InterPro	IPR003018. GAF. IPR003607. Metal-dep_PHydrolase_HD_dom. IPR002073. PDEase. [Graphical view]
Pfam	PF01590. GAF. 2 hits. PF00233. PDEase_I. 1 hit. [Graphical view]
PRINTS	PR00387. PDIESTERASE1.
SMART	SM00065. GAF. 2 hits. SM00471. HDc. 1 hit. [Graphical view]
PROSITE	PS00126. PDEASE_I. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	385015.
SOURCE	Search...

Entry information

Entry name

PDE11_MOUSE

Accession

Primary (citable) accession number: P0C1Q2
Secondary accession number(s): A2AKR2

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 25, 2006
Last sequence update:	July 25, 2006
Last modified:	January 19, 2010
This is version 31 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)