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BNP receptor; basic (brain) natriuretic peptide [BNP] receptor; atrial natriuretic peptide receptor B; ANP-B; ANPRB; GC-B; guanylate cyclase B; NPR-B; atrial natriuretic peptide B-type receptor (NPR2, ANPRB)
Function:
- receptor for
a) atrial natriuretic peptide (ANP)
b) brain natriuretic peptide (BNP)
c) C-type natriuretic peptide (CNP)
- has guanylate cyclase activity on binding of ligand
- activation order seems to be CNP > BNP > ANP
- phosphorylation of the protein kinase-like domain is required for full activation by CNP (putative)
Structure:
- belongs to the adenylyl cyclase class-4/ guanylyl cyclase family
- contains 1 guanylate cyclase domain
- contains 1 protein kinase domain
Compartment: membrane
Alternative splicing: named isoforms=2
Expression:
- may be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay
Pathology:
- defects in NPR2 are the cause of acromesomelic dysplasia Maroteaux type
Related
basic (brain) natriuretic peptide (BNP, B-type)
General
glycoprotein
guanyl cyclase or guanylate cyclase
natriuretic peptide receptor
phosphoprotein
Properties
SIZE: entity length = 1047 aa
MW = 117 kD
COMPARTMENT: cellular membrane
MOTIF: signal sequence {1-22}
N-glycosylation site {N24}
N-glycosylation site {N35}
cysteine residue {C75}
MODIFICATION: cysteine residue {C101}
cysteine residue {C101}
MODIFICATION: cysteine residue {C75}
N-glycosylation site {N161}
N-glycosylation site {N195}
N-glycosylation site {N244}
N-glycosylation site {N277}
N-glycosylation site {N349}
cysteine residue {C439}
MODIFICATION: cysteine residue {C-INTERCHAIN}
cysteine residue {C448}
MODIFICATION: cysteine residue {C-INTERCHAIN}
transmembrane domain {459-478}
kinase domain
SITE: 513-786
MOTIF: ATP-binding site
NAME: ATP-binding site
Ser phosphorylation site {S513}
Thr phosphorylation site {T516}
Ser phosphorylation site {S518}
Ser phosphorylation site {S523}
Ser phosphorylation site {S526}
Guanylate cyclase {861-991}
Database Correlations
OMIM correlations
MORBIDMAP 108961
UniProt P20594
PFAM correlations
Kegg hsa:4882
ENZYME 4.6.1.2
References
UniProt :accession P20594