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NPR1

Guanylyl cyclases, catalyzing the production of cGMP from GTP, are classified as soluble and membrane forms (Garbers and Lowe, 1994 [PubMed 7982997]). The membrane guanylyl cyclases, often termed guanylyl cyclases A through F, form a family of cell-surface receptors with a similar topographic structure: an extracellular ligand-binding domain, a single membrane-spanning domain, and an intracellular region that contains a protein kinase-like domain and a cyclase catalytic domain. GC-A and GC-B function as receptors for natriuretic peptides; they are also referred to as atrial natriuretic peptide receptor A (NPR1) and type B (NPR2; MIM 108961). Also see NPR3 (MIM 108962), which encodes a protein with only the ligand-binding transmembrane and 37-amino acid cytoplasmic domains. NPR1 is a membrane-bound guanylate cyclase that serves as the receptor for both atrial and brain natriuretic peptides (ANP (MIM 108780) and BNP (MIM 600295), respectively).
Protein class

Enzymes, FDA approved drug targets, Metabolic proteins, Transporters

Predicted location

Membrane

Single cell type specificity

Group enriched (Hepatic stellate cells, Adipocytes, Endothelial cells)

Immune cell specificity

Not detected in immune cells

Cell line specificity

Cell line enriched (ASC diff)

Interaction

Homodimer.

Molecular function

Lyase, Receptor, Vasoactive

More Types Infomation

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For Research Use Only. Not For Clinical Use.

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