Reviewed, UniProtKB/Swiss-Prot Q1KKS3 (PDE11_FUGRU)

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

Fugu rubripes (Japanese pufferfish) (Takifugu rubripes)

Taxonomic identifier

31033 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Actinopterygii › Neopterygii › Teleostei › Euteleostei › Neoteleostei › Acanthomorpha › Acanthopterygii › Percomorpha › Tetraodontiformes › Tetradontoidea › Tetraodontidae › Takifugu

Protein attributes

Sequence length	903 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

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.
Catalytic activity	Guanosine 3',5'-cyclic phosphate + H2O = guanosine 5'-phosphate. Adenosine 3',5'-cyclic phosphate + H2O = adenosine 5'-phosphate.
Cofactor	Divalent cations 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.
Domain	The tandem GAF domains bind cGMP, and regulate enzyme activity. The binding of cGMP leading to stimulate the enzyme activity By similarity.
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
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 – 903	903	Dual 3',5'-cyclic-AMP and -GMP phosphodiesterase 11A		PRO_0000247043
Regions
	Domain	175 – 324	150	GAF 1
	Domain	356 – 512	157	GAF 2
	Region	594 – 859	266	Catalytic By similarity
Sites
	Metal binding	622	1	Divalent metal cation 1 By similarity
	Metal binding	658	1	Divalent metal cation 1 By similarity
	Metal binding	659	1	Divalent metal cation 1 By similarity
	Metal binding	659	1	Divalent metal cation 2 By similarity
	Metal binding	662	1	Divalent metal cation 2 By similarity
	Metal binding	688	1	Divalent metal cation 2 By similarity
	Metal binding	770	1	Divalent metal cation 1 By similarity
	Binding site	823	1	cAMP or cGMP By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q1KKS3-1 [UniParc]. Last modified May 30, 2006. Version 1. Checksum: 0B12D6E7897E2E26	FASTA	903	102,019
	10 20 30 40 50 60 MAVPKMVFSD VESFLDSHPE LFEDYLNRKG SSSMVEKWLK NHQAGKSEAE PKEEKSSVCK 70 80 90 100 110 120 DSWASKCDGL QRRASQKELR KTFARSKAIN VNRTYDEHVN SRAQEPLTSM RRRALLRKAS 130 140 150 160 170 180 SLPPTTAHIL SALLESRVNI PQYPSTAVDF KYYLKEHNER EFFLELVKDI SNDLDLTSLS 190 200 210 220 230 240 YKILVFVCIM VDADRCSLFL VEGTGNKKTL VSKFFDVHAG TTVLPSMNSG EVQVPWGKGI 250 260 270 280 290 300 IGYVAEHGET VNIPDAYQDR RFSDEIDKLT GYKTKSLLCM PIQNSDGEII GVAQAINKSS 310 320 330 340 350 360 SGELFTEDDE KVLQMYLPFC GIAISNAQLF AASRKEYDRS RALLEVVNDL FEEQTDLEKI 370 380 390 400 410 420 VRKIMHRAQT LLKCERCSVQ LLEDIESPVV KFTKSFELLS PKCSADAESS FKDSMEKSSY 430 440 450 460 470 480 SDWLINNSIA ELVASTGLPV NISDAYQDPR FDAEADQFSD FHIRSVLCVP IWNSNHQIIG 490 500 510 520 530 540 VAQVLNRLDG KPFDDADQRL FEAFVIFCGL GINNTIMYDQ VKKSWAKQSV ALDVLSYHAT 550 560 570 580 590 600 CSKTEVDKFK AANIPLVCEL GIDKLSFDDF SLDVDAMITA ALRMFIELGM VQKFKIDYET 610 620 630 640 650 660 LCRWLLTVRK NYRMVLYHNW RHAFNVCQCM FAMLTTAGFQ ETLTDVEILA LIVGCVCHDL 670 680 690 700 710 720 DHRGTNNAFQ AKTGSALSLL YGTSATLEHH HFNHAVMILQ SEGHNIFCNL SSTEYSDLMQ 730 740 750 760 770 780 LLKQSILATD LTLYFENRNS FFELVSIGEY NWNVKTHRDM CRSMMMTACD LGAVTKPWDI 790 800 810 820 830 840 SRKVAELVTS EFFEQGDRER SELKLTPSAI FDRNRKDELP GLQLEWIDGI CAPLYETLVK 850 860 870 880 890 900 LNPKLQPMVD MINANRVKWE ELDKKRQHDH GASVPASPCS AAEGSETGGV PCCSNNTPPT HVS

References

[1]

"Highly conserved syntenic blocks at the vertebrate Hox loci and conserved regulatory elements within and outside Hox gene clusters." Lee A.P., Koh E.G.L., Tay A., Brenner S., Venkatesh B. Proc. Natl. Acad. Sci. U.S.A. 103:6994-6999(2006) [PubMed: 16636282] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	DQ481668 Genomic DNA. Translation: ABF22471.1.
3D structure databases
ModBase	Search...
Phylogenomic databases
HOVERGEN	Q1KKS3.
Enzyme and pathway databases
BRENDA	3.1.4.17. 281122. 3.1.4.35. 281122.
Family and domain databases
InterPro	IPR003018. GAF. IPR003607. Met-dep_phosphohydro_HD. 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...

Entry information

Entry name

PDE11_FUGRU

Accession

Primary (citable) accession number: Q1KKS3

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 25, 2006
Last sequence update:	May 30, 2006
Last modified:	June 16, 2009
This is version 16 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)