Aliases for NPR2 Gene
- Natriuretic Peptide Receptor 2 2 3 5
- Atrial Natriuretic Peptide Receptor Type B 3 4
- Guanylate Cyclase 2B 2 3
- Guanylate Cyclase B 3 4
- EC 126.96.36.199 4 61
- ANPR-B 3 4
- ANPRB 3 4
- ANP-B 3 4
- NPR-B 3 4
- GC-B 3 4
- Natriuretic Peptide Receptor B/Guanylate Cyclase B (Atrionatriuretic Peptide Receptor B) 3
- Atrial Natriuretic Peptide B-Type Receptor 3
- Acromesomelic Dysplasia, Maroteaux Type 2
External Ids for NPR2 Gene
Previous HGNC Symbols for NPR2 Gene
Previous GeneCards Identifiers for NPR2 Gene
This gene encodes natriuretic peptide receptor B, one of two integral membrane receptors for natriuretic peptides. Both NPR1 and NPR2 contain five functional domains: an extracellular ligand-binding domain, a single membrane-spanning region, and intracellularly a protein kinase homology domain, a helical hinge region involved in oligomerization, and a carboxyl-terminal guanylyl cyclase catalytic domain. The protein is the primary receptor for C-type natriuretic peptide (CNP), which upon ligand binding exhibits greatly increased guanylyl cyclase activity. Mutations in this gene are the cause of acromesomelic dysplasia Maroteaux type. [provided by RefSeq, Jul 2008]
GeneCards Summary for NPR2 Gene
NPR2 (Natriuretic Peptide Receptor 2) is a Protein Coding gene. Diseases associated with NPR2 include Acromesomelic Dysplasia, Maroteaux Type and Epiphyseal Chondrodysplasia, Miura Type. Among its related pathways are Signaling in Gap Junctions and Cardiac conduction. GO annotations related to this gene include identical protein binding and protein kinase activity. An important paralog of this gene is NPR1.
UniProtKB/Swiss-Prot for NPR2 Gene
Receptor for the C-type natriuretic peptide NPPC/CNP hormone. Has guanylate cyclase activity upon binding of its ligand. May play a role in the regulation of skeletal growth.
Natriuretic peptide (NP) receptors are single transmembrane catalytic receptors with intracellular guanylyl cyclase activity. There are three isoforms of NP receptors; NPR1-3, which have conserved catalytic and regulatory domains and divergent ligand binding domains.