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InterPro: IPR001054 Adenylyl cyclase class-3/4/guanylyl cyclase

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4145 proteins

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Architectures
Accession List
Matches in BioMart

Accession

IPR001054 A/G_cyclase

Type

Domain

Signatures Help

Database	ID	Name	Proteins
Gene3D	G3DSA:3.30.70.1230	A/G_cyclase	3825
Pfam	PF00211	Guanylate_cyc	3873
PROSITE profile	PS50125	GUANYLATE_CYCLASE_2	3893
SMART	SM00044	CYCc	3795
SuperFamily	SSF55073	A/G_cyclase	4073
Signatures in BioMart

InterPro Relationships Help

Found in

IPR016577 Adenylate cylcase, type 10

Contains

IPR018297 Adenylyl cyclase class-3/4/guanylyl cyclase, conserved site

GO Term annotation Help

Process

GO:0007242 intracellular signaling cascade
GO:0009190 cyclic nucleotide biosynthetic process

Function

GO:0016849 phosphorus-oxygen lyase activity

InterPro annotation

Entry Details in BioMart

Abstract

Guanylate cyclases (EC:4.6.1.2) catalyse the formation of cyclic GMP (cGMP) from GTP. cGMP acts as an intracellular messenger, activating cGMP-dependent kinases and regulating cGMP-sensitive ion channels. The role of cGMP as a second messenger in vascular smooth muscle relaxation and retinal photo-transduction is well established. Guanylate cyclase is found both in the soluble and particulate fractions of eukaryotic cells. The soluble and plasma membrane-bound forms differ in structure, regulation and other properties [1, 2, 3, 4]. Most currently known plasma membrane-bound forms are receptors for small polypeptides. The soluble forms of guanylate cyclase are cytoplasmic heterodimers having alpha and beta subunits.

In all characterised eukaryote guanylyl- and adenylyl cyclases, cyclic nucleotide synthesis is carried out by the conserved class III cyclase domain.

Structural links Help

PDB - click here

SCOP: d.58.29.1

CATH: 3.30.70.1230

Database links Help

PDBe-motif: PS00452

Enzyme: EC:4.6.1

PROSITE doc: PDOC00425

PANDIT: PF00211

Blocks: IPB001054

Pfam Clan: CL0276.4

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR001054

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

O02298 Soluble guanylate cyclase gcy-35

O43306 Adenylate cyclase type 6

O54865 Guanylate cyclase soluble subunit beta-1

P08678 Adenylate cyclase

P32870 Ca(2+)/calmodulin-responsive adenylate cyclase

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR000159	Ras-association
IPR018297	Adenylyl cyclase class-3/4/guanylyl cyclase, conserved site
IPR009398	Adenylate cyclase-like
IPR001611	Leucine-rich repeat
IPR014045	Protein phosphatase 2C, N-terminal
IPR001932	Protein phosphatase 2C-related
IPR011644	Haem NO binding
IPR013716	Adenylate cyclase G-alpha binding
IPR001054	Adenylyl cyclase class-3/4/guanylyl cyclase
	SWISS-MODEL
	ModBase

Publications Open in usermanual
1.	Yuen PS, Garbers DL. Guanylyl cyclase-linked receptors. Annu. Rev. Neurosci. 15 193-225 1992 [PubMed: 1349465] http://dx.doi.org/10.1146/annurev.ne.15.030192.001205
2.	Garbers DL. Guanylyl cyclase receptors and their endocrine, paracrine, and autocrine ligands. Cell 71 1-4 1992 [PubMed: 1356629] http://dx.doi.org/10.1016/0092-8674(92)90258-E
3.	Koesling D, Bohme E, Schultz G. Guanylyl cyclases, a growing family of signal-transducing enzymes. FASEB J. 5 2785-91 1991 [PubMed: 1680765] http://www.fasebj.org/cgi/content/abstract/5/13/2785
4.	Garbers DL. The guanylyl cyclase receptor family. New Biol. 2 499-504 1990 [PubMed: 1982420]

Additional Reading Open in usermanual
	Barzu O, Danchin A. Adenylyl cyclases: a heterogeneous class of ATP-utilizing enzymes. Prog. Nucleic Acid Res. Mol. Biol. 49 1994 241-83 [PubMed: 7863008]
	Iyengar R. Molecular and functional diversity of mammalian Gs-stimulated adenylyl cyclases. FASEB J. 7 1993 768-75 [PubMed: 8330684] http://www.fasebj.org/cgi/content/abstract/7/9/768
	Mou TC, Gille A, Suryanarayana S, Richter M, Seifert R, Sprang SR. Broad specificity of mammalian adenylyl cyclase for interaction with 2',3'-substituted purine- and pyrimidine nucleotide inhibitors. Mol. Pharmacol. 70 2006 878-86 [PubMed: 16766715] http://dx.doi.org/10.1124/mol.106.026427
	Mou TC, Gille A, Fancy DA, Seifert R, Sprang SR. Structural basis for the inhibition of mammalian membrane adenylyl cyclase by 2 '(3')-O-(N-Methylanthraniloyl)-guanosine 5 '-triphosphate. J. Biol. Chem. 280 2005 7253-61 [PubMed: 15591060] http://dx.doi.org/10.1074/jbc.M409076200
	Bieger B, Essen LO. Structural analysis of adenylate cyclases from Trypanosoma brucei in their monomeric state. EMBO J. 20 2001 433-45 [PubMed: 11157750] http://dx.doi.org/10.1093/emboj/20.3.433
	Steegborn C, Litvin TN, Levin LR, Buck J, Wu H. Bicarbonate activation of adenylyl cyclase via promotion of catalytic active site closure and metal recruitment. Nat. Struct. Mol. Biol. 12 2005 32-7 [PubMed: 15619637] http://dx.doi.org/10.1038/nsmb880
	Tesmer JJ, Dessauer CW, Sunahara RK, Murray LD, Johnson RA, Gilman AG, Sprang SR. Molecular basis for P-site inhibition of adenylyl cyclase. Biochemistry 39 2000 14464-71 [PubMed: 11087399] http://dx.doi.org/10.1021/bi0015562

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