P16860 (ANFB_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Natriuretic peptides B

Alternative name(s):
Gamma-brain natriuretic peptide

Cleaved into the following 16 chains:

1. Brain natriuretic peptide 32
   Short name=BNP(1-32)
   Short name=BNP-32
2. BNP(1-30)
3. BNP(1-29)
4. BNP(1-28)
5. BNP(2-31)
6. BNP(3-32)
7. BNP(3-30)
8. BNP(3-29)
9. BNP(4-32)
10. BNP(4-31)
11. BNP(4-30)
12. BNP(4-29)
13. BNP(4-27)
14. BNP(5-32)
15. BNP(5-31)
16. BNP(5-29)

Gene names

Name:

NPPB

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	134 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Cardiac hormone which may function as a paracrine antifibrotic factor in the heart. Also plays a key role in cardiovascular homeostasis through natriuresis, diuresis, vasorelaxation, and inhibition of renin and aldosterone secretion. Specifically binds and stimulates the cGMP production of the NPR1 receptor. Binds the clearance receptor NPR3. Ref.11
Subcellular location	Secreted.
Tissue specificity	Brain and also in atria, but at much lower levels than ANP.
Pharmaceutical use	Available under the name Nesiritide (Scios). Used for the treatment of heart failure.
Sequence similarities	Belongs to the natriuretic peptide family.
Sequence caution	The sequence BAA90441.1 differs from that shown. Reason: Frameshift at position 44.

Ontologies

Keywords
Cellular component	Secreted
Coding sequence diversity	Polymorphism
Domain	Signal
Molecular function	Hormone Vasoactive
PTM	Disulfide bond Glycoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Pharmaceutical Reference proteome
Gene Ontology (GO)
Biological_process	body fluid secretion Traceable author statement PubMed 14960748. Source: UniProtKB cGMP biosynthetic process Inferred from direct assay Ref.11. Source: UniProtKB cellular response to mechanical stimulus Inferred from electronic annotation. Source: Compara heart development Inferred from electronic annotation. Source: Compara inflammatory response Inferred from electronic annotation. Source: Compara negative regulation of angiogenesis Traceable author statement PubMed 14737067. Source: UniProtKB negative regulation of cell growth Non-traceable author statement PubMed 12727915. Source: UniProtKB negative regulation of smooth muscle cell proliferation Inferred from electronic annotation. Source: Compara positive regulation of renal sodium excretion Traceable author statement PubMed 14960748. Source: UniProtKB positive regulation of urine volume Traceable author statement PubMed 14737067. Source: UniProtKB receptor guanylyl cyclase signaling pathway Inferred from direct assay Ref.11. Source: UniProtKB regulation of blood pressure Non-traceable author statement PubMed 12727915. Source: UniProtKB regulation of blood vessel size Inferred from electronic annotation. Source: UniProtKB-KW regulation of vascular permeability Traceable author statement PubMed 14737067. Source: UniProtKB regulation of vasodilation Non-traceable author statement PubMed 7601467. Source: UniProtKB response to calcium ion Inferred from electronic annotation. Source: Compara response to drug Inferred from electronic annotation. Source: Compara response to hypoxia Inferred from electronic annotation. Source: Compara response to lipopolysaccharide Inferred from electronic annotation. Source: Compara response to organic cyclic compound Inferred from electronic annotation. Source: Compara response to peptide hormone stimulus Inferred from electronic annotation. Source: Compara
Cellular_component	extracellular space Non-traceable author statement PubMed 7601467. Source: UniProtKB nucleus Inferred from electronic annotation. Source: Compara perinuclear region of cytoplasm Inferred from electronic annotation. Source: Compara
Molecular_function	diuretic hormone activity Traceable author statement PubMed 14960748. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 26

26

Ref.9

Chain

27 – 134

108

Natriuretic peptides B

PRO_0000001531

Peptide

103 – 134

32

Brain natriuretic peptide 32 Ref.10

PRO_0000001532

Peptide

103 – 132

30

BNP(1-30)

PRO_0000364993

Peptide

103 – 131

29

BNP(1-29)

PRO_0000364994

Peptide

103 – 130

28

BNP(1-28)

PRO_0000364995

Peptide

104 – 133

30

BNP(2-31)

PRO_0000364996

Peptide

105 – 134

30

BNP(3-32)

PRO_0000364997

Peptide

105 – 132

28

BNP(3-30)

PRO_0000364998

Peptide

105 – 131

27

BNP(3-29)

PRO_0000364999

Peptide

106 – 134

29

BNP(4-32)

PRO_0000365000

Peptide

106 – 133

28

BNP(4-31)

PRO_0000365001

Peptide

106 – 132

27

BNP(4-30)

PRO_0000365002

Peptide

106 – 131

26

BNP(4-29)

PRO_0000365003

Peptide

106 – 129

24

BNP(4-27)

PRO_0000365004

Peptide

107 – 134

28

BNP(5-32)

PRO_0000365005

Peptide

107 – 133

27

BNP(5-31)

PRO_0000365006

Peptide

107 – 131

25

BNP(5-29)

PRO_0000365007

Amino acid modifications

Glycosylation

62

1

O-linked (HexNAc...); Partial Ref.12

Glycosylation

63

1

O-linked (HexNAc...) Ref.12

Glycosylation

70

1

O-linked (HexNAc...) Ref.12

Glycosylation

74

1

O-linked (HexNAc...) Ref.12

Glycosylation

79

1

O-linked (HexNAc...) Ref.12

Glycosylation

84

1

O-linked (HexNAc...); Partial Ref.12

Glycosylation

97

1

O-linked (HexNAc...) Ref.12

Disulfide bond

112 ↔ 128

Ref.14

Natural variations

Natural variant

25

1

R → L.
Corresponds to variant rs5227 [ dbSNP | Ensembl ].

VAR_014580

Natural variant

47

1

R → H.
Corresponds to variant rs5229 [ dbSNP | Ensembl ].

VAR_014581

Natural variant

93

1

M → L.
Corresponds to variant rs5230 [ dbSNP | Ensembl ].

VAR_014582

Secondary structure

1

.

.

.

134

Helix Strand Turn

Details...

Beta strand

121 – 123

3

Sequences

	Sequence		Length	Mass (Da)
	P16860 [UniParc]. Last modified August 1, 1990. Version 1. Checksum: DC884D9408462146	FASTA	134	14,726
	10 20 30 40 50 60 MDPQTAPSRA LLLLLFLHLA FLGGRSHPLG SPGSASDLET SGLQEQRNHL QGKLSELQVE 70 80 90 100 110 120 QTSLEPLQES PRPTGVWKSR EVATEGIRGH RKMVLYTLRA PRSPKMVQGS GCFGRKMDRI 130 SSSSGLGCKV LRRH

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Human and canine gene homologs of porcine brain natriuretic peptide." Seilhamer J.J., Arfsten A., Miller J.A., Lundquist P., Scarborough R.M., Lewicki J.A., Porter J.G. Biochem. Biophys. Res. Commun. 165:650-658(1989) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Cloning and sequence analysis of cDNA encoding a precursor for human brain natriuretic peptide." Sudoh T., Maekawa K., Kojima M., Minamino N., Kangawa K., Matsuo H. Biochem. Biophys. Res. Commun. 159:1427-1434(1989) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]	"Silver Project." Kitano T., Kobayakawa H., Saitou N. Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]	"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)." Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y., LaBaer J. Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[5]	NHLBI resequencing and genotyping service (RS&G) Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[6]	"The DNA sequence and biological annotation of human chromosome 1." Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R. Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Pancreas and Spleen.
[9]	"Isolation and identification of human brain natriuretic peptides in cardiac atrium." Hino J., Tateyaa H., Minamino N., Kangawa K., Matsuo H. Biochem. Biophys. Res. Commun. 167:693-700(1990) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 27-58 AND 103-134.
[10]	"Isolation and sequence determination of human brain natriuretic peptide in human atrium." Kambayashi Y., Nakao K., Mukoyama M., Saito Y., Ogawa Y., Shiono S., Inouye K., Yoshida N., Imura H. FEBS Lett. 259:341-345(1990) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 103-134.
[11]	"Selective activation of the B natriuretic peptide receptor by C-type natriuretic peptide (CNP)." Koller K.J., Lowe D.G., Bennett G.L., Minamino N., Kangawa K., Matsuo H., Goeddel D.V. Science 252:120-123(1991) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[12]	"The precursor to B-type natriuretic peptide is an O-linked glycoprotein." Schellenberger U., O'Rear J., Guzzetta A., Jue R.A., Protter A.A., Pollitt N.S. Arch. Biochem. Biophys. 451:160-166(2006) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION AT THR-62; SER-63; SER-70; THR-74; SER-79; THR-84 AND THR-97.
[13]	"Detection of endogenous B-type natriuretic peptide at very low concentrations in patients with heart failure." Niederkofler E.E., Kiernan U.A., O'Rear J., Menon S., Saghir S., Protter A.A., Nelson R.W., Schellenberger U. Circ. Heart Fail. 1:258-264(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEOLYTIC PROCESSING, MASS SPECTROMETRY.
[14]	"Structural determinants of natriuretic peptide receptor specificity and degeneracy." He X.-L., Dukkipati A., Garcia K.C. J. Mol. Biol. 361:698-714(2006) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 111-131 IN COMPLEX WITH NPR3, DISULFIDE BOND.
+	Additional computationally mapped references.

Web resources

Wikipedia

Brain natriuretic peptide entry

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M31776 Genomic DNA. Translation: AAA35603.1.
M25296 mRNA. Translation: AAA36355.1.
AB037521 Genomic DNA. Translation: BAA90441.1. Frameshift.
CR541976 mRNA. Translation: CAG46774.1.
CR542003 mRNA. Translation: CAG46800.1.
EU326309 Genomic DNA. Translation: ACA05917.1.
AL021155 Genomic DNA. Translation: CAA15956.1.
CH471130 Genomic DNA. Translation: EAW71718.1.
BC025785 mRNA. Translation: AAH25785.1.

IPI

IPI00031101.

PIR

AWHUB. A36736.

RefSeq

NP_002512.1. NM_002521.2.

UniGene

Hs.219140.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1YK1	X-ray	2.90	E	111-131	[»]
3N56	X-ray	3.10	C/D	103-134	[»]

ProteinModelPortal

P16860.

SMR

P16860. Positions 104-132.

ModBase

Search...

Protein-protein interaction databases

IntAct

P16860. 1 interaction.

MINT

MINT-1434895.

STRING

9606.ENSP00000365651.

PTM databases

PhosphoSite

P16860.

Polymorphism databases

DMDM

113836.

Proteomic databases

PaxDb

P16860.

PRIDE

P16860.

Protocols and materials databases

DNASU

4879.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000376468; ENSP00000365651; ENSG00000120937.

GeneID

4879.

KEGG

hsa:4879.

UCSC

uc001atj.3. human.

Organism-specific databases

CTD

4879.

GeneCards

GC01M011918.

HGNC

HGNC:7940. NPPB.

MIM

600295. gene.

neXtProt

NX_P16860.

PharmGKB

PA31734.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG67899.

HOGENOM

HOG000206568.

HOVERGEN

HBG004227.

KO

K12335.

OMA

YTLRAPR.

OrthoDB

EOG4SQWZC.

Gene expression databases

Bgee

P16860.

CleanEx

HS_NPPB.

Genevestigator

P16860.

GermOnline

ENSG00000120937. Homo sapiens.

Family and domain databases

InterPro

IPR000663. Natr_peptide.
IPR002408. Natriuretic_peptide_brain.
[Graphical view]

Pfam

PF00212. ANP. 1 hit.
[Graphical view]

PRINTS

PR00712. BNATPEPTIDE.

SMART

SM00183. NAT_PEP. 1 hit.
[Graphical view]

PROSITE

PS00263. NATRIURETIC_PEPTIDE. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

DrugBank

DB01136. Carvedilol.
DB04899. Nesiritide.
DB00624. Testosterone.

EvolutionaryTrace

P16860.

GenomeRNAi

4879.

NextBio

18780.

PMAP-CutDB

P16860.

SOURCE

Search...

Entry information

Entry name

ANFB_HUMAN

Accession

Primary (citable) accession number: P16860
Secondary accession number(s): B0ZBE9, Q6FGY0, Q9P2Q7

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1990
Last sequence update:	August 1, 1990
Last modified:	April 3, 2013
This is version 135 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.