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Protein Domain : IPR018297

Name  Adenylyl cyclase class-3/4/guanylyl cyclase, conserved site Short Name  A/G_cyclase_CS
Type  Conserved_site Description  Guanylate cyclases () [, , , ]catalyze the formation of cyclic GMP (cGMP) from GTP. cGMP acts asan 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 particular fraction of eukaryotic cells. The soluble and plasma membrane-bound forms differ in structure, regulation and other properties. Most currently known plasma membrane-bound forms are receptors for small polypeptides. The topology of such proteins is the following: they have a N-terminal extracellular domain which acts as the ligand binding region, then a transmembrane domain, followed by a large cytoplasmic C-terminal region that can be subdivided into two domains: a protein kinase-like domain that appears important for proper signalling and a cyclase catalytic domain. This topology is schematically represented below. +-----------------------xxxxx----------------------+------------+| Ligand-binding XXXXX Protein Kinase like | Cyclase |+-----------------------xxxxx----------------------+------------+Extracellular Transmembrane CytoplasmicThe known guanylate cyclase receptors are: The sea-urchins receptors for speract and resact, which are small peptides that stimulate sperm motility and metabolism. The receptors for natriuretic peptides (ANF). Two forms of ANF receptors with guanylate cyclase activity are currently known: GC-A (or ANP-A) which seems specific to atrial natriuretic peptide (ANP), and GC-B (or ANP-B) which seems to be stimulated more effectively by brain natriuretic peptide (BNP) than by ANP. The receptor for Escherichia coli heat-stable enterotoxin (GC-C). The endogenous ligand for this intestinal receptor seems to be a small peptide called guanylin. Retinal guanylate cyclase (retGC) which probably plays a specific functional role in the rods and/or cones of photoreceptors. It is not known if this protein acts as receptor, but its structure is similar to that of the other plasma membrane-bound GCs. The soluble forms of guanylate cyclase are cytoplasmic heterodimers. The two subunits, alpha and beta are proteins of from 70 to 82 Kd which are highly related. Two forms of beta subunits are currently known: beta-1 which seems to be expressed in lung and brain, and beta-2 which is more abundant in kidney and liver. The membrane and cytoplasmic forms of guanylate cyclase share a conserved domain which is probably important for the catalytic activity of the enzyme. Such a domain is also found twice in the different forms of membrane-bound adenylate cyclases (also known as class-III) [, ]from mammals, slime mold or Drosophila.

Publication Counts Displayer

0 Child Features

0 Contains

1 Cross References

Identifier
Source . Name

Subject . Primary Identifier
PS00452 PROSITE IPR018297

3 Data Sets

Name URL
TrEMBL data set http://www.ebi.ac.uk/trembl/
InterPro data set  
InterPro GO Annotation data set  

1 Found In

DB identifier Name Short Name Type
IPR001054 Adenylyl cyclase class-3/4/guanylyl cyclase A/G_cyclase Domain

3 GO Annotation


Subject . Secondary Identifier

Subject . Name

Subject . Symbol

Ontology Term . Identifier

Ontology Term . Name
Adenylyl cyclase class-3/4/guanylyl cyclase, conserved site   GO:0016849 phosphorus-oxygen lyase activity
Adenylyl cyclase class-3/4/guanylyl cyclase, conserved site   GO:0009190 cyclic nucleotide biosynthetic process
Adenylyl cyclase class-3/4/guanylyl cyclase, conserved site   GO:0035556 intracellular signal transduction

3 Ontology Annotations


Subject . Secondary Identifier

Subject . Name

Subject . Symbol

Ontology Term . Identifier

Ontology Term . Name
Adenylyl cyclase class-3/4/guanylyl cyclase, conserved site   GO:0016849 phosphorus-oxygen lyase activity
Adenylyl cyclase class-3/4/guanylyl cyclase, conserved site   GO:0009190 cyclic nucleotide biosynthetic process
Adenylyl cyclase class-3/4/guanylyl cyclase, conserved site   GO:0035556 intracellular signal transduction

0 Parent Features

308 Proteins

DB identifier Primary Accession
Organism . Name
FBpp0082745 Q9VEU5 Drosophila melanogaster
FBpp0099492 Q9VXU0 Drosophila melanogaster
FBpp0290537 Q8IRF5 Drosophila melanogaster
FBpp0271905 Q9W2P1 Drosophila melanogaster
FBpp0271904 Q8MLX0 Drosophila melanogaster
FBpp0099611 A1ZB47 Drosophila melanogaster
FBpp0291487 Q7JQ32 Drosophila melanogaster
FBpp0084819 Q07093 Drosophila melanogaster
FBpp0073809 P32870 Drosophila melanogaster
FBpp0082641 Q9VF17 Drosophila melanogaster
FBpp0074666 Q9VW60 Drosophila melanogaster
FBpp0293332 M9NFA6 Drosophila melanogaster
FBpp0085252 Q9V9R3 Drosophila melanogaster
FBpp0072753 Q9W038 Drosophila melanogaster
FBpp0085115 Q9VA09 Drosophila melanogaster
FBpp0293331 C7LAF5 Drosophila melanogaster
FBpp0110263 Q9VEU6 Drosophila melanogaster
FBpp0291649 Q8IQK2 Drosophila melanogaster
FBpp0291650 Q9VU79 Drosophila melanogaster
FBpp0305810 M9PHL3 Drosophila melanogaster
FBpp0309409 M9PJN1 Drosophila melanogaster
FBpp0305812 M9PEL4 Drosophila melanogaster
FBpp0305813 M9PH52 Drosophila melanogaster
FBpp0110261 Q0KI72 Drosophila melanogaster
FBpp0290535 E1JIB3 Drosophila melanogaster
FBpp0290536 Q9W037 Drosophila melanogaster
FBpp0111769 A8DYZ3 Drosophila melanogaster
FBpp0294032 M9NF51 Drosophila melanogaster
FBpp0290915 Q9VP76 Drosophila melanogaster
FBpp0310220 Q07553 Drosophila melanogaster