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PROSITE documentation PDOC00430

Natriuretic peptides receptors signature





Description

Natriuretic peptides are hormones involved in the regulation of fluid and electrolyte homeostasis. These hormones stimulate the intracellular production of cyclic GMP as a second messenger.

Currently, three types of natriuretic peptide receptors are known [1,2]. Two express guanylate cyclase activity: 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 third receptor (ANP-C) is probably responsible for the clearance of ANP from the circulation and does not play a role in signal transduction.

GC-A and GC-B are plasma membrane-bound proteins that share the following topology: an 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 (see <PDOC00100>) that appears important for proper signalling and a guanylate cyclase catalytic domain (see <PDOC00425>). The topology of ANP-C is different: like GC-A and -B it possesses an extracellular ligand-binding region and a transmembrane domain, but its cytoplasmic domain is very short.

We developed a pattern from the ligand-binding region of natriuretic peptide receptors based on a highly conserved region located in the N-terminal part of the domain.

Last update:

May 1991 / First entry.

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Technical section

PROSITE method (with tools and information) covered by this documentation:

ANF_RECEPTORS, PS00458; Natriuretic peptides receptors signature  (PATTERN)


References

1AuthorsGarbers D.L.
TitleThe guanylyl cyclase receptor family.
SourceNew Biol. 2:499-504(1990).
PubMed ID1982420

2AuthorsSchulz S. Chinkers M. Garbers D.L.
TitleThe guanylate cyclase/receptor family of proteins.
SourceFASEB J. 3:2026-2035(1989).
PubMed ID2568301



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