ANFB_PIG
ID ANFB_PIG Reviewed; 131 AA.
AC P07634;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 2.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Natriuretic peptides B;
DE AltName: Full=Brain natriuretic factor prohormone {ECO:0000250|UniProtKB:P16860};
DE Short=preproBNP {ECO:0000250|UniProtKB:P40753};
DE Short=proBNP {ECO:0000250|UniProtKB:P16860};
DE AltName: Full=Gamma-brain natriuretic peptide {ECO:0000303|PubMed:3196348};
DE AltName: Full=Iso-ANP {ECO:0000250|UniProtKB:P13205};
DE Contains:
DE RecName: Full=NT-proBNP {ECO:0000250|UniProtKB:P16860};
DE AltName: Full=NT-pro-BNP {ECO:0000250|UniProtKB:P16860};
DE AltName: Full=NT-proBNP(1-76) {ECO:0000250|UniProtKB:P16860};
DE Contains:
DE RecName: Full=Brain natriuretic peptide 32 {ECO:0000303|PubMed:2708334};
DE Short=BNP-32 {ECO:0000303|PubMed:2708334};
DE Contains:
DE RecName: Full=Brain natriuretic peptide 26 {ECO:0000303|PubMed:2708334};
DE Short=BNP-26 {ECO:0000303|PubMed:2708334};
DE Flags: Precursor;
GN Name=NPPB;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Heart atrium {ECO:0000303|PubMed:3196348};
RX PubMed=3196348; DOI=10.1016/s0006-291x(88)80062-7;
RA Maekawa K., Sudoh T., Furusawa M., Minamino N., Kangawa K., Okhubo H.,
RA Nakanishi S., Matsuo H.;
RT "Cloning and sequence analysis of cDNA encoding a precursor for porcine
RT brain natriuretic peptide.";
RL Biochem. Biophys. Res. Commun. 157:410-416(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY.
RC TISSUE=Heart atrium {ECO:0000303|PubMed:2708334};
RX PubMed=2708334; DOI=10.1016/s0021-9258(18)83482-2;
RA Porter J.G., Arfsten A., Palisi T., Scarborough R.M., Lewicki J.A.,
RA Seilhamer J.J.;
RT "Cloning of a cDNA encoding porcine brain natriuretic peptide.";
RL J. Biol. Chem. 264:6689-6692(1989).
RN [3]
RP PROTEIN SEQUENCE OF 26-131, AND TISSUE SPECIFICITY.
RC TISSUE=Heart atrium {ECO:0000269|PubMed:3196347};
RX PubMed=3196347; DOI=10.1016/s0006-291x(88)80061-5;
RA Minamino N., Kangawa K., Matsuo H.;
RT "Isolation and identification of a high molecular weight brain natriuretic
RT peptide in porcine cardiac atrium.";
RL Biochem. Biophys. Res. Commun. 157:402-409(1988).
RN [4]
RP PROTEIN SEQUENCE OF 100-131, SYNTHESIS (BRAIN NATRIURETIC PEPTIDE 32), AND
RP TISSUE SPECIFICITY (BRAIN NATRIURETIC PEPTIDE 32).
RC TISSUE=Brain {ECO:0000303|PubMed:3421965};
RX PubMed=3421965; DOI=10.1016/s0006-291x(88)80555-2;
RA Sudoh T., Minamino N., Kangawa K., Matsuo H.;
RT "Brain natriuretic peptide-32: N-terminal six amino acid extended form of
RT brain natriuretic peptide identified in porcine brain.";
RL Biochem. Biophys. Res. Commun. 155:726-732(1988).
RN [5]
RP PROTEIN SEQUENCE OF 106-131, SYNTHESIS (BRAIN NATRIURETIC PEPTIDE 26),
RP FUNCTION (BRAIN NATRIURETIC PEPTIDE 26), AND TISSUE SPECIFICITY (BRAIN
RP NATRIURETIC PEPTIDE 26).
RC TISSUE=Brain {ECO:0000303|PubMed:2964562};
RX PubMed=2964562; DOI=10.1038/332078a0;
RA Sudoh T., Kangawa K., Minamino N., Matsuo H.;
RT "A new natriuretic peptide in porcine brain.";
RL Nature 332:78-81(1988).
RN [6]
RP STRUCTURE BY NMR OF BNP-26.
RX PubMed=2146114; DOI=10.1111/j.1432-1033.1990.tb19313.x;
RA Inooka H., Kikuchi T., Endo S., Ishibashi Y., Wakimasu M., Mizuta E.;
RT "Conformation in solution of porcine brain natriuretic peptide determined
RT by combined use of nuclear magnetic resonance and distance geometry.";
RL Eur. J. Biochem. 193:127-134(1990).
RN [7]
RP STRUCTURE BY NMR OF BNP-26.
RX PubMed=1915362; DOI=10.1111/j.1432-1033.1991.tb16272.x;
RA Craik D., Munro S., Nielsen K., Shehan P., Tregear G., Wade J.;
RT "The conformation of porcine-brain natriuretic peptide by two-dimensional
RT NMR spectroscopy.";
RL Eur. J. Biochem. 201:183-191(1991).
CC -!- FUNCTION: [Brain natriuretic peptide 32]: Cardiac hormone that plays a
CC key role in mediating cardio-renal homeostasis (By similarity). May
CC also function as a paracrine antifibrotic factor in the heart (By
CC similarity). Acts by specifically binding and stimulating NPR1 to
CC produce cGMP, which in turn activates effector proteins that drive
CC various biological responses. Involved in regulating the extracellular
CC fluid volume and maintaining the fluid-electrolyte balance through
CC natriuresis, diuresis, vasorelaxation, and inhibition of renin and
CC aldosterone secretion. Binds the clearance receptor NPR3 (By
CC similarity). {ECO:0000250|UniProtKB:P16860,
CC ECO:0000250|UniProtKB:P40753}.
CC -!- FUNCTION: [Brain natriuretic peptide 26]: Plays a key role in
CC cardiovascular homeostasis through natriuresis, diuresis,
CC vasorelaxation, and inhibition of renin and aldosterone secretion
CC (PubMed:2964562). In vivo, induces vasodilation (PubMed:2964562).
CC {ECO:0000269|PubMed:2964562}.
CC -!- FUNCTION: [NT-proBNP]: May affect cardio-renal homeostasis. Able to
CC promote the production of cGMP although its potency is very low
CC compared to brain natriuretic peptide 32.
CC {ECO:0000250|UniProtKB:P16860}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P16860}.
CC Note=Detected in blood. {ECO:0000250|UniProtKB:P16860}.
CC -!- SUBCELLULAR LOCATION: [Brain natriuretic peptide 32]: Secreted
CC {ECO:0000250|UniProtKB:P16860}. Note=Detected in blood.
CC {ECO:0000250|UniProtKB:P16860}.
CC -!- TISSUE SPECIFICITY: Heart atrium. {ECO:0000269|PubMed:2708334,
CC ECO:0000269|PubMed:3196347, ECO:0000269|PubMed:3196348}.
CC -!- TISSUE SPECIFICITY: [Brain natriuretic peptide 32]: Brain (at protein
CC level). {ECO:0000269|PubMed:3421965}.
CC -!- TISSUE SPECIFICITY: [Brain natriuretic peptide 26]: Brain (at protein
CC level). {ECO:0000269|PubMed:2964562}.
CC -!- PTM: The precursor molecule is proteolytically cleaved by the
CC endoproteases FURIN or CORIN at Arg-99 to produce the active brain
CC natriuretic peptide 32 and the inactive NT-proBNP. CORIN also cleaves
CC the precursor molecule at additional residues including Arg-96 and
CC possibly Lys-102 (By similarity). Undergoes further proteolytic
CC cleavage by unknown proteases to give rise to Brain natriuretic peptide
CC 26 (PubMed:3421965). {ECO:0000250|UniProtKB:P16860,
CC ECO:0000269|PubMed:3421965}.
CC -!- PTM: [Brain natriuretic peptide 32]: Undergoes further proteolytic
CC cleavage by various proteases such as DPP4, MME and possibly FAP, to
CC give rise to a variety of shorter peptides. Cleaved at Pro-101 by the
CC prolyl endopeptidase FAP (seprase) activity (in vitro). Degraded by
CC IDE. During IDE degradation, the resulting products initially increase
CC the activation of NPR1 and can also stimulate NPR2 to produce cGMP
CC before the fragments are completely degraded and inactivated by IDE (in
CC vitro). {ECO:0000250|UniProtKB:P16860}.
CC -!- SIMILARITY: Belongs to the natriuretic peptide family. {ECO:0000305}.
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DR EMBL; M23596; AAB59258.1; -; mRNA.
DR EMBL; M25547; AAA31007.1; -; Genomic_DNA.
DR PIR; A31676; A31676.
DR PIR; A33873; A33873.
DR PIR; JC1081; JC1081.
DR RefSeq; NP_999011.1; NM_213846.1.
DR AlphaFoldDB; P07634; -.
DR BMRB; P07634; -.
DR STRING; 9823.ENSSSCP00000003722; -.
DR PaxDb; P07634; -.
DR PRIDE; P07634; -.
DR Ensembl; ENSSSCT00000003809; ENSSSCP00000003722; ENSSSCG00000003431.
DR Ensembl; ENSSSCT00015005496; ENSSSCP00015002179; ENSSSCG00015004133.
DR Ensembl; ENSSSCT00025075853; ENSSSCP00025032875; ENSSSCG00025055376.
DR Ensembl; ENSSSCT00030007142; ENSSSCP00030003197; ENSSSCG00030005226.
DR Ensembl; ENSSSCT00035021230; ENSSSCP00035007676; ENSSSCG00035016587.
DR Ensembl; ENSSSCT00040062443; ENSSSCP00040026313; ENSSSCG00040046388.
DR Ensembl; ENSSSCT00050037528; ENSSSCP00050015579; ENSSSCG00050027908.
DR Ensembl; ENSSSCT00055040307; ENSSSCP00055032068; ENSSSCG00055020462.
DR Ensembl; ENSSSCT00060101890; ENSSSCP00060044289; ENSSSCG00060074489.
DR Ensembl; ENSSSCT00070059188; ENSSSCP00070050387; ENSSSCG00070029463.
DR GeneID; 396844; -.
DR KEGG; ssc:396844; -.
DR CTD; 4879; -.
DR eggNOG; ENOG502SD0X; Eukaryota.
DR GeneTree; ENSGT00940000154513; -.
DR HOGENOM; CLU_158067_0_0_1; -.
DR InParanoid; P07634; -.
DR OMA; PTGVWKA; -.
DR OrthoDB; 1493586at2759; -.
DR TreeFam; TF106304; -.
DR Proteomes; UP000008227; Chromosome 6.
DR Proteomes; UP000314985; Chromosome 6.
DR Bgee; ENSSSCG00000003431; Expressed in heart left ventricle and 10 other tissues.
DR ExpressionAtlas; P07634; differential.
DR Genevisible; P07634; SS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0032991; C:protein-containing complex; IEA:Ensembl.
DR GO; GO:0005179; F:hormone activity; IBA:GO_Central.
DR GO; GO:0051427; F:hormone receptor binding; IBA:GO_Central.
DR GO; GO:0006182; P:cGMP biosynthetic process; ISS:UniProtKB.
DR GO; GO:0019934; P:cGMP-mediated signaling; IBA:GO_Central.
DR GO; GO:0003085; P:negative regulation of systemic arterial blood pressure; IBA:GO_Central.
DR GO; GO:0007218; P:neuropeptide signaling pathway; IBA:GO_Central.
DR GO; GO:0006457; P:protein folding; IEA:Ensembl.
DR GO; GO:0007168; P:receptor guanylyl cyclase signaling pathway; ISS:UniProtKB.
DR InterPro; IPR000663; Natr_peptide.
DR InterPro; IPR030480; Natr_peptide_CS.
DR InterPro; IPR002408; Natriuretic_peptide_brain.
DR Pfam; PF00212; ANP; 1.
DR PRINTS; PR00712; BNATPEPTIDE.
DR PRINTS; PR00710; NATPEPTIDES.
DR SMART; SM00183; NAT_PEP; 1.
DR PROSITE; PS00263; NATRIURETIC_PEPTIDE; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Disulfide bond; Hormone; Reference proteome;
KW Secreted; Signal; Vasoactive.
FT SIGNAL 1..25
FT /evidence="ECO:0000269|PubMed:3196347"
FT CHAIN 26..131
FT /note="Natriuretic peptides B"
FT /id="PRO_0000001535"
FT PEPTIDE 26..99
FT /note="NT-proBNP"
FT /evidence="ECO:0000250|UniProtKB:P16860"
FT /id="PRO_0000451941"
FT PEPTIDE 100..131
FT /note="Brain natriuretic peptide 32"
FT /evidence="ECO:0000269|PubMed:3421965"
FT /id="PRO_0000001536"
FT PEPTIDE 106..131
FT /note="Brain natriuretic peptide 26"
FT /evidence="ECO:0000269|PubMed:2708334"
FT /id="PRO_0000001537"
FT SITE 96..97
FT /note="Cleavage; by CORIN"
FT /evidence="ECO:0000250|UniProtKB:P16860"
FT SITE 99..100
FT /note="Cleavage; by FURIN or CORIN"
FT /evidence="ECO:0000250|UniProtKB:P16860"
FT SITE 101..102
FT /note="Cleavage; by FAP"
FT /evidence="ECO:0000250|UniProtKB:P16860"
FT SITE 102..103
FT /note="Cleavage; by CORIN"
FT /evidence="ECO:0000250|UniProtKB:P16860"
FT DISULFID 109..125
FT /evidence="ECO:0000250|UniProtKB:P16860"
FT VARIANT 26
FT /note="H -> Y (in a clone)"
SQ SEQUENCE 131 AA; 14512 MW; CC2F6E6E4A50C18A CRC64;
MGPRMALPRV LLLLFLHLLL LGCRSHPLGG AGLASELPGI QELLDRLRDR VSELQAERTD
LEPLRQDRGL TEAWEAREAA PTGVLGPRSS IFQVLRGIRS PKTMRDSGCF GRRLDRIGSL
SGLGCNVLRR Y
