ANFB_CANLF
ID ANFB_CANLF Reviewed; 140 AA.
AC P16859;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1990, sequence version 1.
DT 25-MAY-2022, entry version 104.
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=Brain natriuretic peptide 34;
DE Short=BNP-34;
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:0000305|PubMed:2597152};
DE Short=BNP(1-32) {ECO:0000305|PubMed:2597152};
DE Short=BNP-32 {ECO:0000305|PubMed:2597152};
DE AltName: Full=Brain natriuretic peptide {ECO:0000303|PubMed:2597152};
DE Short=BNP {ECO:0000303|PubMed:2597152};
DE Contains:
DE RecName: Full=Brain natriuretic peptide 29;
DE Short=BNP-29;
DE Flags: Precursor;
GN Name=NPPB;
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2597152; DOI=10.1016/s0006-291x(89)80015-4;
RA Seilhamer J.J., Arfsten A., Miller J.A., Lundquist P., Scarborough R.M.,
RA Lewicki J.A., Porter J.G.;
RT "Human and canine gene homologs of porcine brain natriuretic peptide.";
RL Biochem. Biophys. Res. Commun. 165:650-658(1989).
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: [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: Brain and also in atria, but at much lower levels
CC than ANP.
CC -!- PTM: The precursor molecule is proteolytically cleaved by the
CC endoproteases FURIN or CORIN at Arg-108 to produce the brain
CC natriuretic peptide 32. CORIN also cleaves the precursor molecule at
CC additional residues including Arg-105, Arg-108 and possibly Lys-111.
CC {ECO:0000250|UniProtKB:P16860}.
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-110 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M31777; AAA30832.1; -; Genomic_DNA.
DR PIR; B36736; B36736.
DR AlphaFoldDB; P16859; -.
DR STRING; 9612.ENSCAFP00000024316; -.
DR PaxDb; P16859; -.
DR eggNOG; ENOG502SD0X; Eukaryota.
DR InParanoid; P16859; -.
DR Proteomes; UP000002254; Unplaced.
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: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: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 2: Evidence at transcript level;
KW Cleavage on pair of basic residues; Disulfide bond; Hormone;
KW Reference proteome; Secreted; Signal; Vasoactive.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..140
FT /note="Natriuretic peptides B"
FT /id="PRO_0000001526"
FT PEPTIDE 27..108
FT /note="NT-proBNP"
FT /evidence="ECO:0000250|UniProtKB:P16860"
FT /id="PRO_0000451935"
FT PEPTIDE 107..140
FT /note="Brain natriuretic peptide 34"
FT /id="PRO_0000001527"
FT PEPTIDE 109..140
FT /note="Brain natriuretic peptide 32"
FT /evidence="ECO:0000250|UniProtKB:P16860"
FT /id="PRO_0000451936"
FT PEPTIDE 112..140
FT /note="Brain natriuretic peptide 29"
FT /id="PRO_0000001528"
FT REGION 71..94
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 105..106
FT /note="Cleavage; by CORIN"
FT /evidence="ECO:0000250|UniProtKB:P16860"
FT SITE 108..109
FT /note="Cleavage; by FURIN or CORIN"
FT /evidence="ECO:0000250|UniProtKB:P16860"
FT SITE 110..111
FT /note="Cleavage; by FAP"
FT /evidence="ECO:0000250|UniProtKB:P16860"
FT SITE 111..112
FT /note="Cleavage; by CORIN"
FT /evidence="ECO:0000250|UniProtKB:P16860"
FT DISULFID 118..134
FT /evidence="ECO:0000250|UniProtKB:P16860"
SQ SEQUENCE 140 AA; 14966 MW; 6128B6F4D0FD49D9 CRC64;
MEPCAALPRA LLLLLFLHLS PLGGRPHPLG GRSPASEASE ASEASGLWAV QELLGRLKDA
VSELQAEQLA LEPLHRSHSP AEAPEAGGTP RGVLAPHDSV LQALRRLRSP KMMHKSGCFG
RRLDRIGSLS GLGCNVLRKY
