ANFB_BOVIN
ID ANFB_BOVIN Reviewed; 129 AA.
AC P13204; F1MWE9;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2012, sequence version 3.
DT 03-AUG-2022, entry version 128.
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:0000250|UniProtKB:P07634};
DE AltName: Full=Iso-ANP {ECO:0000250|UniProtKB:P13205};
DE Contains:
DE RecName: Full=Aldosterone secretion inhibitory factor {ECO:0000303|PubMed:2532709};
DE Short=ASIF {ECO:0000303|PubMed:2532709};
DE Contains:
DE RecName: Full=Brain natriuretic peptide 26 {ECO:0000250|UniProtKB:P07634};
DE Short=BNP-26 {ECO:0000250|UniProtKB:P07634};
DE Contains:
DE RecName: Full=Brain natriuretic peptide 29 {ECO:0000250|UniProtKB:O46541};
DE Short=BNP-29 {ECO:0000250|UniProtKB:O46541};
DE Flags: Precursor;
GN Name=NPPB;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hereford;
RX PubMed=19393038; DOI=10.1186/gb-2009-10-4-r42;
RA Zimin A.V., Delcher A.L., Florea L., Kelley D.R., Schatz M.C., Puiu D.,
RA Hanrahan F., Pertea G., Van Tassell C.P., Sonstegard T.S., Marcais G.,
RA Roberts M., Subramanian P., Yorke J.A., Salzberg S.L.;
RT "A whole-genome assembly of the domestic cow, Bos taurus.";
RL Genome Biol. 10:R42.01-R42.10(2009).
RN [2]
RP PROTEIN SEQUENCE OF 27-129, AND SUBCELLULAR LOCATION.
RX PubMed=2532709; DOI=10.1210/mend-3-11-1823;
RA Nguyen T.T., Lazure C., Babinski K., Chretien M., de Lean A., Ong H.;
RT "Purification and primary structure of pro-aldosterone secretion inhibitory
RT factor from bovine adrenal chromaffin cells.";
RL Mol. Endocrinol. 3:1823-1829(1989).
RN [3]
RP PROTEIN SEQUENCE OF 95-129, AND SUBCELLULAR LOCATION.
RX PubMed=2537187; DOI=10.1210/endo-124-3-1591;
RA Nguyen T.T., Lazure C., Babinski K., Chretien M., Ong H., de Lean A.;
RT "Aldosterone secretion inhibitory factor: a novel neuropeptide in bovine
RT chromaffin cells.";
RL Endocrinology 124:1591-1593(1989).
CC -!- FUNCTION: Cardiac hormone that plays a key role in mediating cardio-
CC renal homeostasis (By similarity). May also function as a paracrine
CC antifibrotic factor in the heart (By similarity). Acts by specifically
CC binding and stimulating NPR1 to produce cGMP, which in turn activates
CC effector proteins that drive various biological responses. Involved in
CC regulating the extracellular fluid volume and maintaining the fluid-
CC electrolyte balance through natriuresis, diuresis, vasorelaxation, and
CC inhibition of renin and aldosterone secretion. Binds the clearance
CC receptor NPR3 (By similarity). {ECO:0000250|UniProtKB:P16860,
CC ECO:0000250|UniProtKB:P40753}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P16860}.
CC Note=Detected in blood. {ECO:0000250|UniProtKB:P16860}.
CC -!- SUBCELLULAR LOCATION: [Aldosterone secretion inhibitory factor]:
CC Secreted {ECO:0000269|PubMed:2532709, ECO:0000269|PubMed:2537187}.
CC -!- PTM: The precursor molecule is proteolytically cleaved, possibly by
CC FURIN or CORIN, to produce the active peptide (By similarity). May
CC undergo further proteolytic cleavage by various proteases such as DPP4,
CC MME and possibly FAP, to give rise to a variety of shorter peptides (By
CC similarity). May be cleaved at Pro-99 by the prolyl endopeptidase FAP
CC (seprase) activity (in vitro) (By similarity). May be degraded by IDE
CC (By similarity). During IDE degradation, the resulting products
CC initially increase the activation of NPR1 and can also stimulate NPR2
CC to produce cGMP before the fragments are completely degraded and
CC inactivated by IDE (in vitro) (By similarity).
CC {ECO:0000250|UniProtKB:P16860}.
CC -!- SIMILARITY: Belongs to the natriuretic peptide family. {ECO:0000305}.
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DR EMBL; DAAA02042958; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; A41403; A41403.
DR RefSeq; NP_001160042.1; NM_001166570.1.
DR AlphaFoldDB; P13204; -.
DR BMRB; P13204; -.
DR STRING; 9913.ENSBTAP00000028974; -.
DR PaxDb; P13204; -.
DR Ensembl; ENSBTAT00000028974; ENSBTAP00000028974; ENSBTAG00000021739.
DR GeneID; 508734; -.
DR KEGG; bta:508734; -.
DR CTD; 4879; -.
DR VEuPathDB; HostDB:ENSBTAG00000021739; -.
DR VGNC; VGNC:32211; NPPB.
DR eggNOG; ENOG502SD0X; Eukaryota.
DR GeneTree; ENSGT00940000154513; -.
DR HOGENOM; CLU_158067_0_0_1; -.
DR InParanoid; P13204; -.
DR OMA; PTGVWKA; -.
DR OrthoDB; 1493586at2759; -.
DR TreeFam; TF106304; -.
DR Proteomes; UP000009136; Chromosome 16.
DR Bgee; ENSBTAG00000021739; Expressed in cardiac atrium and 35 other tissues.
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..26
FT /evidence="ECO:0000269|PubMed:2532709"
FT CHAIN 27..129
FT /note="Natriuretic peptides B"
FT /id="PRO_0000001523"
FT PEPTIDE 95..129
FT /note="Aldosterone secretion inhibitory factor"
FT /evidence="ECO:0000269|PubMed:2537187"
FT /id="PRO_0000001524"
FT PEPTIDE 101..129
FT /note="Brain natriuretic peptide 29"
FT /evidence="ECO:0000250|UniProtKB:O46541"
FT /id="PRO_0000451934"
FT PEPTIDE 104..129
FT /note="Brain natriuretic peptide 26"
FT /evidence="ECO:0000250|UniProtKB:P07634"
FT /id="PRO_0000001525"
FT SITE 97..98
FT /note="Cleavage; by CORIN or FURIN"
FT /evidence="ECO:0000250|UniProtKB:P16860"
FT SITE 99..100
FT /note="Cleavage; by FAP"
FT /evidence="ECO:0000250|UniProtKB:P16860"
FT SITE 100..101
FT /note="Cleavage; by CORIN"
FT /evidence="ECO:0000250|UniProtKB:P16860"
FT DISULFID 107..123
SQ SEQUENCE 129 AA; 14113 MW; E03CFFF01BC3D24B CRC64;
MDPQTALSRA LLLLLFLHLS LLGCRSHPVG GPGPVSELPG LQELLDRLRD RVSELQAEQL
RVEPLQQGQG LEETWDSPAA APAGFLGPHH SILRALRGPK MMRDSGCFGR RLDRIGSLSG
LGCNVLRRY
