ID   ANFB_MOUSE              Reviewed;         121 AA.
AC   P40753;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 2.
DT   27-MAR-2024, entry version 162.
DE   RecName: Full=Natriuretic peptides B;
DE   AltName: Full=Brain natriuretic factor prohormone {ECO:0000250|UniProtKB:P16860};
DE            Short=preproBNP {ECO:0000303|PubMed:8182124};
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 45 {ECO:0000303|PubMed:8182124};
DE     AltName: Full=5 kDa cardiac natriuretic peptide {ECO:0000250|UniProtKB:P13205};
DE     AltName: Full=BNP(77-121) {ECO:0000303|PubMed:8182124};
DE     AltName: Full=Brain natriuretic peptide {ECO:0000250|UniProtKB:P13205};
DE              Short=BNP {ECO:0000250|UniProtKB:P13205};
DE   Flags: Precursor;
GN   Name=Nppb;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION (BRAIN NATRIURETIC PEPTIDE 45),
RP   SUBCELLULAR LOCATION (BRAIN NATRIURETIC PEPTIDE 45), AND TISSUE SPECIFICITY
RP   (BRAIN NATRIURETIC PEPTIDE 45).
RC   STRAIN=BALB/cJ; TISSUE=Heart;
RX   PubMed=8182124; DOI=10.1172/jci117182;
RA   Ogawa Y., Itoh H., Tamura N., Suga S., Yoshimasa T., Uehira M., Matsuda S.,
RA   Shiono S., Nishimoto H., Nakao K.;
RT   "Molecular cloning of the complementary DNA and gene that encode mouse
RT   brain natriuretic peptide and generation of transgenic mice that
RT   overexpress the brain natriuretic peptide gene.";
RL   J. Clin. Invest. 93:1911-1921(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY (BRAIN
RP   NATRIURETIC PEPTIDE 45).
RC   STRAIN=BALB/cJ;
RX   PubMed=8097440; DOI=10.1161/01.res.72.5.984;
RA   Steinhelper M.E.;
RT   "Structure, expression, and genomic mapping of the mouse natriuretic
RT   peptide type-B gene.";
RL   Circ. Res. 72:984-992(1993).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG).
RC   TISSUE=Testis;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   FUNCTION (BRAIN NATRIURETIC PEPTIDE 45), AND DISRUPTION PHENOTYPE (BRAIN
RP   NATRIURETIC PEPTIDE 45).
RX   PubMed=10737768; DOI=10.1073/pnas.070371497;
RA   Tamura N., Ogawa Y., Chusho H., Nakamura K., Nakao K., Suda M.,
RA   Kasahara M., Hashimoto R., Katsuura G., Mukoyama M., Itoh H., Saito Y.,
RA   Tanaka I., Otani H., Katsuki M.;
RT   "Cardiac fibrosis in mice lacking brain natriuretic peptide.";
RL   Proc. Natl. Acad. Sci. U.S.A. 97:4239-4244(2000).
CC   -!- FUNCTION: [Brain natriuretic peptide 45]: Cardiac hormone that plays a
CC       key role in mediating cardio-renal homeostasis (PubMed:8182124). May
CC       also function as a paracrine antifibrotic factor in the heart
CC       (PubMed:10737768). Acts by specifically binding and stimulating NPR1 to
CC       produce cGMP, which in turn activates effector proteins that drive
CC       various biological responses (PubMed:8182124). Likely involved in
CC       regulating the extracellular fluid volume and maintaining the fluid-
CC       electrolyte balance through natriuresis, diuresis, kaluresis and
CC       chloruresis (By similarity). {ECO:0000250|UniProtKB:P13205,
CC       ECO:0000269|PubMed:10737768, ECO:0000269|PubMed:8182124}.
CC   -!- SUBCELLULAR LOCATION: [Brain natriuretic peptide 45]: Secreted
CC       {ECO:0000269|PubMed:8182124}. Note=Detected in blood.
CC       {ECO:0000269|PubMed:8182124}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=Long;
CC         IsoId=P40753-1; Sequence=Displayed;
CC       Name=Short;
CC         IsoId=P40753-2; Sequence=VSP_000263;
CC   -!- TISSUE SPECIFICITY: [Brain natriuretic peptide 45]: Expressed
CC       abundantly in the ventricle, and in a lesser extent in the atrium (at
CC       protein level). {ECO:0000269|PubMed:8182124}.
CC   -!- PTM: The precursor molecule is proteolytically cleaved by the
CC       endoprotease Furin to produce brain natriuretic peptide 45 (By
CC       similarity). 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:P13205, ECO:0000250|UniProtKB:P16860}.
CC   -!- DISRUPTION PHENOTYPE: [Brain natriuretic peptide 45]: Mice are viable
CC       and fertile and do not display gross skeletal abnormalities. Fluid-
CC       electrolyte balance and blood pressure remain normal although an
CC       increased rate of focal fibrotic lesions is observed within the cardiac
CC       ventricles. {ECO:0000269|PubMed:10737768}.
CC   -!- SIMILARITY: Belongs to the natriuretic peptide family. {ECO:0000305}.
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DR   EMBL; D16497; BAA03948.1; -; Genomic_DNA.
DR   EMBL; S58667; AAB26344.2; -; Genomic_DNA.
DR   EMBL; BC061165; AAH61165.1; -; mRNA.
DR   CCDS; CCDS18926.1; -. [P40753-1]
DR   PIR; A49144; A49144.
DR   PIR; I49548; I49548.
DR   RefSeq; NP_001274277.1; NM_001287348.1. [P40753-2]
DR   RefSeq; NP_032752.1; NM_008726.5. [P40753-1]
DR   AlphaFoldDB; P40753; -.
DR   STRING; 10090.ENSMUSP00000099521; -.
DR   PhosphoSitePlus; P40753; -.
DR   PaxDb; 10090-ENSMUSP00000099521; -.
DR   PeptideAtlas; P40753; -.
DR   Antibodypedia; 13918; 1705 antibodies from 41 providers.
DR   Ensembl; ENSMUST00000103231.5; ENSMUSP00000099521.5; ENSMUSG00000029019.9. [P40753-1]
DR   GeneID; 18158; -.
DR   KEGG; mmu:18158; -.
DR   UCSC; uc008vto.3; mouse. [P40753-1]
DR   UCSC; uc008vtp.3; mouse. [P40753-2]
DR   AGR; MGI:97368; -.
DR   CTD; 4879; -.
DR   MGI; MGI:97368; Nppb.
DR   VEuPathDB; HostDB:ENSMUSG00000029019; -.
DR   eggNOG; ENOG502SD0X; Eukaryota.
DR   GeneTree; ENSGT00940000154513; -.
DR   HOGENOM; CLU_158067_0_0_1; -.
DR   InParanoid; P40753; -.
DR   OMA; CDGFRRS; -.
DR   OrthoDB; 4262493at2759; -.
DR   PhylomeDB; P40753; -.
DR   TreeFam; TF106304; -.
DR   BioGRID-ORCS; 18158; 0 hits in 78 CRISPR screens.
DR   ChiTaRS; Nppb; mouse.
DR   PRO; PR:P40753; -.
DR   Proteomes; UP000000589; Chromosome 4.
DR   RNAct; P40753; Protein.
DR   Bgee; ENSMUSG00000029019; Expressed in cardiac muscle of left ventricle and 33 other cell types or tissues.
DR   ExpressionAtlas; P40753; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005615; C:extracellular space; ISO:MGI.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR   GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR   GO; GO:0005179; F:hormone activity; ISO:MGI.
DR   GO; GO:0051427; F:hormone receptor binding; ISO:MGI.
DR   GO; GO:0005102; F:signaling receptor binding; ISO:MGI.
DR   GO; GO:0061844; P:antimicrobial humoral immune response mediated by antimicrobial peptide; ISO:MGI.
DR   GO; GO:0097746; P:blood vessel diameter maintenance; IEA:UniProtKB-KW.
DR   GO; GO:0014898; P:cardiac muscle hypertrophy in response to stress; IDA:MGI.
DR   GO; GO:0006182; P:cGMP biosynthetic process; ISS:UniProtKB.
DR   GO; GO:0019934; P:cGMP-mediated signaling; IBA:GO_Central.
DR   GO; GO:0060976; P:coronary vasculature development; IDA:MGI.
DR   GO; GO:0001935; P:endothelial cell proliferation; IDA:MGI.
DR   GO; GO:0048872; P:homeostasis of number of cells; IDA:MGI.
DR   GO; GO:0031640; P:killing of cells of another organism; ISO:MGI.
DR   GO; GO:0000165; P:MAPK cascade; IDA:MGI.
DR   GO; GO:0030308; P:negative regulation of cell growth; ISO:MGI.
DR   GO; GO:1904055; P:negative regulation of cholangiocyte proliferation; ISO:MGI.
DR   GO; GO:0048662; P:negative regulation of smooth muscle cell proliferation; ISO:MGI.
DR   GO; GO:0003085; P:negative regulation of systemic arterial blood pressure; ISO:MGI.
DR   GO; GO:0007218; P:neuropeptide signaling pathway; IBA:GO_Central.
DR   GO; GO:0010753; P:positive regulation of cGMP-mediated signaling; ISO:MGI.
DR   GO; GO:1903816; P:positive regulation of collecting lymphatic vessel constriction; ISO:MGI.
DR   GO; GO:0035810; P:positive regulation of urine volume; ISO:MGI.
DR   GO; GO:0006457; P:protein folding; ISO:MGI.
DR   GO; GO:0007168; P:receptor guanylyl cyclase signaling pathway; ISS:UniProtKB.
DR   GO; GO:0031667; P:response to nutrient levels; IDA:MGI.
DR   GO; GO:0070482; P:response to oxygen levels; IDA:MGI.
DR   InterPro; IPR000663; Natr_peptide.
DR   InterPro; IPR030480; Natr_peptide_CS.
DR   InterPro; IPR002408; Natriuretic_peptide_brain.
DR   PANTHER; PTHR14066; ATRIAL NATRIURETIC FACTOR PRECURSOR; 1.
DR   PANTHER; PTHR14066:SF10; NATRIURETIC PEPTIDES B; 1.
DR   Pfam; PF00212; ANP; 1.
DR   PRINTS; PR00712; BNATPEPTIDE.
DR   SMART; SM00183; NAT_PEP; 1.
DR   PROSITE; PS00263; NATRIURETIC_PEPTIDE; 1.
DR   Genevisible; P40753; MM.
PE   1: Evidence at protein level;
KW   Alternative splicing; Disulfide bond; Hormone; Reference proteome;
KW   Secreted; Signal; Vasoactive.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000255"
FT   PEPTIDE         27..121
FT                   /note="Natriuretic peptides B"
FT                   /id="PRO_0000001533"
FT   PEPTIDE         77..121
FT                   /note="Brain natriuretic peptide 45"
FT                   /id="PRO_0000001534"
FT   REGION          61..89
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        61..76
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   SITE            76..77
FT                   /note="Cleavage; by FURIN"
FT                   /evidence="ECO:0000250|UniProtKB:P13205"
FT   SITE            91..92
FT                   /note="Cleavage; by FAP"
FT                   /evidence="ECO:0000250|UniProtKB:P16860"
FT   DISULFID        99..115
FT                   /evidence="ECO:0000250|UniProtKB:P16860"
FT   VAR_SEQ         43
FT                   /note="Missing (in isoform Short)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_000263"
FT   CONFLICT        27
FT                   /note="Y -> H (in Ref. 2; AAB26344)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        71
FT                   /note="P -> L (in Ref. 2; AAB26344)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   121 AA;  13756 MW;  4F62AC9445E293B9 CRC64;
     MDLLKVLSQM ILFLLFLYLS PLGGHSYPLG SPSQSPEQFK MQKLLELIRE KSEEMAQRQL
     LKDQGLTKEH PKRVLRSQGS TLRVQQRPQN SKVTHISSCF GHKIDRIGSV SRLGCNALKL
     L
//