ANFB_RAT
ID ANFB_RAT Reviewed; 121 AA.
AC P13205;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 3.
DT 03-AUG-2022, entry version 147.
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:2673236};
DE AltName: Full=Iso-ANP {ECO:0000303|PubMed:2144113};
DE Contains:
DE RecName: Full=Brain natriuretic peptide 45 {ECO:0000303|PubMed:2673236};
DE Short=BNP-45 {ECO:0000303|PubMed:2673236};
DE AltName: Full=5 kDa cardiac natriuretic peptide {ECO:0000303|PubMed:2673236};
DE AltName: Full=Brain natriuretic peptide {ECO:0000303|PubMed:2522776};
DE Short=BNP {ECO:0000303|PubMed:2522776};
DE Flags: Precursor;
GN Name=Nppb;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Heart atrium {ECO:0000303|PubMed:2522776};
RX PubMed=2522776; DOI=10.1016/0006-291x(89)92268-7;
RA Kojima M., Minamino N., Kangawa K., Matsuo H.;
RT "Cloning and sequence analysis of cDNA encoding a precursor for rat brain
RT natriuretic peptide.";
RL Biochem. Biophys. Res. Commun. 159:1420-1426(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2144113; DOI=10.1016/0006-291x(90)91409-l;
RA Roy R.N., Flynn T.G.;
RT "Organization of the gene for iso-rANP, a rat B-type natriuretic peptide.";
RL Biochem. Biophys. Res. Commun. 171:416-423(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
RX PubMed=1837590; DOI=10.1210/mend-5-9-1292;
RA Dagnino L., Drouin J., Nemer M.;
RT "Differential expression of natriuretic peptide genes in cardiac and
RT extracardiac tissues.";
RL Mol. Endocrinol. 5:1292-1300(1991).
RN [4]
RP PROTEIN SEQUENCE OF 27-121 AND 77-121, AND TISSUE SPECIFICITY.
RC TISSUE=Heart atrium {ECO:0000303|PubMed:2673236};
RX PubMed=2673236; DOI=10.1016/0006-291x(89)92125-6;
RA Abuyara M., Hino J., Minamino N., Kangawa K., Matsuo H.;
RT "Isolation and identification of rat brain natriuretic peptides in cardiac
RT atrium.";
RL Biochem. Biophys. Res. Commun. 163:226-232(1989).
RN [5]
RP PROTEIN SEQUENCE OF 77-121, AND SUBCELLULAR LOCATION (BRAIN NATRIURETIC
RP PEPTIDE 45).
RC TISSUE=Heart atrium {ECO:0000303|PubMed:2528349};
RX PubMed=2528349; DOI=10.1016/0006-291x(89)92126-8;
RA Kambayashi Y., Nakao K., Itoh H., Hosoda K., Saito Y., Yamada T.,
RA Mukoyama M., Arai H., Shirikami G., Suga S., Ogawa Y., Jougasaki M.,
RA Minamino N., Kangawa K., Matsuo H., Inouye K., Imura H.;
RT "Isolation and sequence determination of rat cardiac natriuretic peptide.";
RL Biochem. Biophys. Res. Commun. 163:233-240(1989).
RN [6]
RP PROTEIN SEQUENCE OF 77-121, FUNCTION, AND DISULFIDE BOND.
RC TISSUE=Heart atrium {ECO:0000303|PubMed:2525380};
RX PubMed=2525380; DOI=10.1016/0006-291x(89)92675-2;
RA Flynn T.G., Brar A., Tremblay L., Sarda I., Lyons C., Jennings D.B.;
RT "Isolation and characterization of iso-rANP, a new natriuretic peptide from
RT rat atria.";
RL Biochem. Biophys. Res. Commun. 161:830-837(1989).
RN [7]
RP PROTEIN SEQUENCE OF 99-115, FUNCTION (BRAIN NATRIURETIC PEPTIDE 45), AND
RP SUBCELLULAR LOCATION (BRAIN NATRIURETIC PEPTIDE 45).
RX PubMed=2525379; DOI=10.1016/0006-291x(89)92661-2;
RA Itoh H., Nakao K., Kambayashi Y., Hosoda K., Saito Y., Yamada T.,
RA Mukoyama M., Arai H., Shirakami G., Suga S., Yoshida I., Inouye K.,
RA Imura H.;
RT "Occurrence of a novel cardiac natriuretic peptide in rats.";
RL Biochem. Biophys. Res. Commun. 161:732-739(1989).
RN [8]
RP FUNCTION, TISSUE SPECIFICITY, INDUCTION BY MECHANICAL STRETCH, AND
RP PROTEOLYTIC PROCESSING BY FURIN.
RX PubMed=9252368; DOI=10.1074/jbc.272.33.20545;
RA Sawada Y., Suda M., Yokoyama H., Kanda T., Sakamaki T., Tanaka S.,
RA Nagai R., Abe S., Takeuchi T.;
RT "Stretch-induced hypertrophic growth of cardiocytes and processing of
RT brain-type natriuretic peptide are controlled by proprotein-processing
RT endoprotease furin.";
RL J. Biol. Chem. 272:20545-20554(1997).
CC -!- FUNCTION: [Brain natriuretic peptide 45]: Cardiac hormone that plays a
CC key role in mediating cardio-renal homeostasis (PubMed:2525380,
CC PubMed:9252368). May also function as a paracrine antifibrotic factor
CC in the heart (By similarity). Acts by specifically binding and
CC stimulating NPR1 to produce cGMP, which in turn activates effector
CC proteins that drive various biological responses (By similarity).
CC Likely involved in regulating the extracellular fluid volume and
CC maintaining the fluid-electrolyte balance through natriuresis,
CC diuresis, kaluresis and chloruresis (PubMed:2525380, PubMed:9252368).
CC {ECO:0000250|UniProtKB:P40753, ECO:0000269|PubMed:2525380,
CC ECO:0000269|PubMed:9252368}.
CC -!- SUBCELLULAR LOCATION: [Brain natriuretic peptide 45]: Secreted
CC {ECO:0000269|PubMed:2525379, ECO:0000269|PubMed:2528349}.
CC -!- TISSUE SPECIFICITY: Expressed in the atria and ventricles, but at much
CC lower levels than NPPA (PubMed:1837590). Expression levels in the
CC ventricles are slightly higher than in the atria (PubMed:1837590). Very
CC low levels of expression detected in the brain, hypothalamaus, lung and
CC aorta (PubMed:1837590). {ECO:0000269|PubMed:1837590}.
CC -!- TISSUE SPECIFICITY: [Brain natriuretic peptide 45]: Atria (at protein
CC level) (PubMed:2673236). Cardiocytes (at protein level)
CC (PubMed:9252368). {ECO:0000269|PubMed:2673236,
CC ECO:0000269|PubMed:9252368}.
CC -!- DEVELOPMENTAL STAGE: Expressed in the atria and ventricles throughout
CC postnatal development and in adults. {ECO:0000269|PubMed:1837590}.
CC -!- INDUCTION: Up-regulated in cardiocytes in response to stretching for
CC 48hr. {ECO:0000269|PubMed:9252368}.
CC -!- PTM: The precursor molecule is proteolytically cleaved by the
CC endoprotease Furin to produce brain natriuretic peptide 45
CC (PubMed:9252368). May undergo further proteolytic cleavage by various
CC proteases such as DPP4, MME and possibly FAP, to give rise to a variety
CC of shorter peptides (By similarity). May be cleaved at Ser-91 by the
CC prolyl endopeptidase FAP (seprase) activity (in vitro) (By similarity).
CC May be degraded by IDE (By similarity). During IDE degradation, the
CC resulting products initially increase the activation of NPR1 and can
CC also stimulate NPR2 to produce cGMP before the fragments are completely
CC degraded and inactivated by IDE (in vitro) (By similarity).
CC {ECO:0000250|UniProtKB:P16860, ECO:0000269|PubMed:9252368}.
CC -!- SIMILARITY: Belongs to the natriuretic peptide family. {ECO:0000305}.
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DR EMBL; M25297; AAA57269.1; -; mRNA.
DR EMBL; M60731; AAA41456.1; -; Genomic_DNA.
DR EMBL; M60266; AAA41455.1; -; Genomic_DNA.
DR PIR; A30162; A30162.
DR RefSeq; NP_113733.1; NM_031545.1.
DR AlphaFoldDB; P13205; -.
DR STRING; 10116.ENSRNOP00000010778; -.
DR PaxDb; P13205; -.
DR Ensembl; ENSRNOT00000010779; ENSRNOP00000010778; ENSRNOG00000008141.
DR GeneID; 25105; -.
DR KEGG; rno:25105; -.
DR CTD; 4879; -.
DR RGD; 3194; Nppb.
DR eggNOG; ENOG502SD0X; Eukaryota.
DR GeneTree; ENSGT00940000154513; -.
DR HOGENOM; CLU_158067_0_0_1; -.
DR InParanoid; P13205; -.
DR OMA; PTGVWKA; -.
DR OrthoDB; 1493586at2759; -.
DR PhylomeDB; P13205; -.
DR TreeFam; TF106304; -.
DR PRO; PR:P13205; -.
DR Proteomes; UP000002494; Chromosome 5.
DR Bgee; ENSRNOG00000008141; Expressed in heart and 1 other tissue.
DR Genevisible; P13205; RN.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0005615; C:extracellular space; IDA:RGD.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:RGD.
DR GO; GO:0032991; C:protein-containing complex; ISO:RGD.
DR GO; GO:0030133; C:transport vesicle; IDA:RGD.
DR GO; GO:0005179; F:hormone activity; IDA:RGD.
DR GO; GO:0051427; F:hormone receptor binding; ISO:RGD.
DR GO; GO:0005102; F:signaling receptor binding; ISO:RGD.
DR GO; GO:0014898; P:cardiac muscle hypertrophy in response to stress; ISO:RGD.
DR GO; GO:0061049; P:cell growth involved in cardiac muscle cell development; IEP:RGD.
DR GO; GO:0071260; P:cellular response to mechanical stimulus; IEP:RGD.
DR GO; GO:0006182; P:cGMP biosynthetic process; ISO:RGD.
DR GO; GO:0019934; P:cGMP-mediated signaling; IBA:GO_Central.
DR GO; GO:0007507; P:heart development; IEP:RGD.
DR GO; GO:0006954; P:inflammatory response; IEP:RGD.
DR GO; GO:0030308; P:negative regulation of cell growth; IDA:RGD.
DR GO; GO:1904055; P:negative regulation of cholangiocyte proliferation; IDA:RGD.
DR GO; GO:0048662; P:negative regulation of smooth muscle cell proliferation; IDA:RGD.
DR GO; GO:0003085; P:negative regulation of systemic arterial blood pressure; IDA:RGD.
DR GO; GO:0007218; P:neuropeptide signaling pathway; IBA:GO_Central.
DR GO; GO:0010753; P:positive regulation of cGMP-mediated signaling; IDA:RGD.
DR GO; GO:1903816; P:positive regulation of collecting lymphatic vessel constriction; IDA:RGD.
DR GO; GO:0035815; P:positive regulation of renal sodium excretion; IDA:RGD.
DR GO; GO:0035810; P:positive regulation of urine volume; IDA:RGD.
DR GO; GO:0006457; P:protein folding; ISO:RGD.
DR GO; GO:0007168; P:receptor guanylyl cyclase signaling pathway; ISS:UniProtKB.
DR GO; GO:0051592; P:response to calcium ion; IEP:RGD.
DR GO; GO:0001666; P:response to hypoxia; IEP:RGD.
DR GO; GO:0032496; P:response to lipopolysaccharide; IEP:RGD.
DR GO; GO:0014070; P:response to organic cyclic compound; IEP:RGD.
DR GO; GO:0043434; P:response to peptide hormone; IEP:RGD.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEP:RGD.
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 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:2673236"
FT PEPTIDE 27..121
FT /note="Natriuretic peptides B"
FT /id="PRO_0000001538"
FT PEPTIDE 77..121
FT /note="Brain natriuretic peptide 45"
FT /evidence="ECO:0000269|PubMed:2528349,
FT ECO:0000269|PubMed:2673236, ECO:0000269|PubMed:9252368"
FT /id="PRO_0000001539"
FT SITE 76..77
FT /note="Cleavage; by FURIN"
FT /evidence="ECO:0000269|PubMed:9252368"
FT SITE 91..92
FT /note="Cleavage; by FAP"
FT /evidence="ECO:0000250|UniProtKB:P16860"
FT DISULFID 99..115
FT /evidence="ECO:0000269|PubMed:2525380"
FT CONFLICT 15
FT /note="L -> V (in Ref. 2; AAA41456)"
FT /evidence="ECO:0000305"
FT CONFLICT 120
FT /note="L -> Q (in Ref. 6; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 121 AA; 13656 MW; B5D4151ED18C7294 CRC64;
MDLQKVLPQM ILLLLFLNLS PLGGHSHPLG SPSQSPEQST MQKLLELIRE KSEEMAQRQL
SKDQGPTKEL LKRVLRSQDS AFRIQERLRN SKMAHSSSCF GQKIDRIGAV SRLGCDGLRL
F
