NPPB
entrez
4879
canonical
uniprot
P16860
canonical
ensembl
ENSG00000120937
resolver
ensp
ENSP00000365651
resolver
enst
ENST00000376468
resolver
genesymbol
NPPB
resolver
hgnc
HGNC:7940
resolver
uniprot
B0ZBE9
resolver
uniprot
Q6FGY0
resolver
uniprot
Q9P2Q7
resolver
uniprot_entry
ANFB_HUMAN
resolver
uniprot_sec
B0ZBE9
resolver
uniprot_sec
Q6FGY0
resolver
uniprot_sec
Q9P2Q7
resolver
amino_acid_sequence
MDPQTAPSRALLLLLFLHLAFLGGRSHPLGSPGSASDLETSGLQEQRNHLQGKLSELQVEQTSLEPLQESPRPTGVWKSREVATEGIRGHRKMVLYTLRAPRSPKMVQGSGCFGRKMDRISSSSGLGCKVLRRH
uniprot
proteins
function
FUNCTION: [Brain natriuretic peptide 32]: Cardiac hormone that plays a key role in mediating cardio-renal homeostasis (PubMed:1672777, PubMed:17372040, PubMed:1914098, PubMed:9458824). May also function as a paracrine antifibrotic factor in the heart (By similarity). Acts by specifically binding and stimulating NPR1 to produce cGMP, which in turn activates effector proteins that drive various biological responses (PubMed:1672777, PubMed:17349887, PubMed:17372040, PubMed:21098034, PubMed:25339504, PubMed:9458824). Involved in regulating the extracellular fluid volume and maintaining the fluid-electrolyte balance through natriuresis, diuresis, vasorelaxation, and inhibition of renin and aldosterone secretion (PubMed:1914098, PubMed:9458824). Binds the clearance receptor NPR3 (PubMed:16870210). {ECO:0000250|UniProtKB:P40753, ECO:0000269|PubMed:1672777, ECO:0000269|PubMed:16870210, ECO:0000269|PubMed:17349887, ECO:0000269|PubMed:17372040, ECO:0000269|PubMed:1914098, ECO:0000269|PubMed:21098034, ECO:0000269|PubMed:25339504, ECO:0000269|PubMed:9458824}.; FUNCTION: [NT-proBNP]: May affect cardio-renal homeostasis (PubMed:17372040). Able to promote the production of cGMP although its potency is very low compared to brain natriuretic peptide 32 (PubMed:17372040). {ECO:0000269|PubMed:17372040}.; FUNCTION: [BNP(3-32)]: May have a role in cardio-renal homeostasis (PubMed:17372040). Able to promote the production of cGMP (PubMed:17372040). {ECO:0000269|PubMed:17372040}.
uniprot
proteins
mass_dalton
14726
uniprot
proteins
mutagenesis
MUTAGEN 97; /note="T->A: Prevents O-glycosylation at this residue. Decreased extracellular levels of NPPB due to decreased stability after secretion whereas extracellular levels of brain natriuretic peptide 32 is increased. In HEK293 cells, proteolytic processing by CORIN or FURIN is reduced but in HL1 cells proteolytic processing is not affected."; /evidence="ECO:0000269|PubMed:21482747, ECO:0000269|PubMed:21763278"; MUTAGEN 99; /note="R->A: Loss of FURIN-mediated proteolytic processing in HEK293 cells, however processing in HL1 cells, likely mediated by CORIN, is only slightly reduced. Loss of CORIN-mediated processing in HL1 cells; when associated with A-102 and A-105."; /evidence="ECO:0000269|PubMed:21763278"; MUTAGEN 102; /note="R->A: Loss of FURIN-mediated proteolytic processing in HEK293 cells, however processing in HL1 cells, likely mediated by CORIN, is only slightly reduced. Loss of CORIN-mediated processing in HL1 cells; when associated with A-99 and A-105."; /evidence="ECO:0000269|PubMed:21763278"; MUTAGEN 105; /note="K->A: No effect on proteolytic processing in HEK293 or HL1 cells. Loss of CORIN-mediated processing in HL1 cells; when associated with A-99 and A-102."; /evidence="ECO:0000269|PubMed:21763278
uniprot
proteins
post_translational_modification
PTM: The precursor molecule is proteolytically cleaved by the endoproteases FURIN or CORIN at Arg-102 to produce brain natriuretic peptide 32 and NT-proBNP (PubMed:10880574, PubMed:20489134, PubMed:21314817, PubMed:21482747, PubMed:21763278). This likely occurs after it has been secreted into the blood, either during circulation or in the target cells (PubMed:21482747). CORIN also cleaves the precursor molecule at additional residues including Arg-99 and possibly Lys-105 (PubMed:20489134, PubMed:21763278). In patients with heart failure, processing and degradation of natriuretic peptides B occurs but is delayed, possibly due to a decrease in enzyme level or activity of CORIN and DPP4 (PubMed:25339504). {ECO:0000269|PubMed:10880574, ECO:0000269|PubMed:20489134, ECO:0000269|PubMed:21314817, ECO:0000269|PubMed:21482747, ECO:0000269|PubMed:21763278, ECO:0000269|PubMed:25339504}.; PTM: [Brain natriuretic peptide 32]: Undergoes further proteolytic cleavage by various proteases such as DPP4, MME and possibly FAP, to give rise to a variety of shorter peptides (PubMed:16254193, PubMed:19808300, PubMed:21098034, PubMed:21314817). Cleaved at Pro-104 by the prolyl endopeptidase FAP (seprase) activity (in vitro) (PubMed:21314817). Degraded by IDE (PubMed:21098034). During IDE degradation, the resulting products initially increase the activation of NPR1 and can also stimulate NPR2 to produce cGMP before the fragments are completely degraded and inactivated by IDE (in vitro) (PubMed:21098034). {ECO:0000269|PubMed:16254193, ECO:0000269|PubMed:19808300, ECO:0000269|PubMed:21098034, ECO:0000269|PubMed:21314817}.; PTM: O-glycosylated on at least seven residues (PubMed:16750161, PubMed:17349887, PubMed:20489134, PubMed:21482747, PubMed:21763278). In cardiomyocytes, glycosylation at Thr-97 is essential for the stability and processing of the extracellular natriuretic peptides B (PubMed:21482747). Glycosylation, especially at Thr-97, may also be important for brain natriuretic peptide 32 stability and/or extracellular distribution (PubMed:21763278). Glycosylation at Thr-97 appears to inhibit FURIN- or CORIN-mediated proteolytic processing, at least in HEK293 cells (PubMed:20489134, PubMed:21763278). {ECO:0000269|PubMed:16750161, ECO:0000269|PubMed:17349887, ECO:0000269|PubMed:20489134, ECO:0000269|PubMed:21482747, ECO:0000269|PubMed:21763278}.
uniprot
proteins
protein_family
Natriuretic peptide family
uniprot
proteins
pubmed
10880574
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16254193
uniprot
proteins
pubmed
16710414
uniprot
proteins
pubmed
1672777
uniprot
proteins
pubmed
16750161
uniprot
proteins
pubmed
16870210
uniprot
proteins
pubmed
17349887
uniprot
proteins
pubmed
17367664
uniprot
proteins
pubmed
17372040
uniprot
proteins
pubmed
17881654
uniprot
proteins
pubmed
18466803
uniprot
proteins
pubmed
1914098
uniprot
proteins
pubmed
19808300
uniprot
proteins
pubmed
20489134
uniprot
proteins
pubmed
21098034
uniprot
proteins
pubmed
21314817
uniprot
proteins
pubmed
2136732
uniprot
proteins
pubmed
2138890
uniprot
proteins
pubmed
21482747
uniprot
proteins
pubmed
21763278
uniprot
proteins
pubmed
2522777
uniprot
proteins
pubmed
25339504
uniprot
proteins
pubmed
2597152
uniprot
proteins
pubmed
32337544
uniprot
proteins
pubmed
9458824
uniprot
proteins
pubmed
9794555
uniprot
proteins
sequence_length
134
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: [NT-proBNP]: Secreted {ECO:0000269|PubMed:18466803, ECO:0000269|PubMed:25339504}. Note=Detected in blood. {ECO:0000269|PubMed:18466803, ECO:0000269|PubMed:25339504}.; SUBCELLULAR LOCATION: [proBNP(3-108)]: Secreted {ECO:0000269|PubMed:17367664}. Note=Detected in blood. {ECO:0000269|PubMed:17367664}.; SUBCELLULAR LOCATION: [Brain natriuretic peptide 32]: Secreted {ECO:0000269|PubMed:17367664, ECO:0000269|PubMed:18466803, ECO:0000269|PubMed:1914098, ECO:0000269|PubMed:25339504}. Note=Detected in blood. {ECO:0000269|PubMed:17367664, ECO:0000269|PubMed:18466803, ECO:0000269|PubMed:1914098, ECO:0000269|PubMed:25339504}.; SUBCELLULAR LOCATION: [BNP(3-32)]: Secreted {ECO:0000269|PubMed:17367664}. Note=Detected in blood. {ECO:0000269|PubMed:17367664}.
uniprot
proteins