ID   ANFB_SHEEP              Reviewed;         129 AA.
AC   O46541;
DT   26-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   25-MAY-2022, entry version 74.
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 29 {ECO:0000303|PubMed:10219521};
DE              Short=BNP-29 {ECO:0000303|PubMed:10219521};
DE   Contains:
DE     RecName: Full=Brain natriuretic peptide 26 {ECO:0000250|UniProtKB:P07634};
DE              Short=BNP-26 {ECO:0000250|UniProtKB:P07634};
DE   Flags: Precursor;
GN   Name=NPPB;
OS   Ovis aries (Sheep).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Caprinae; Ovis.
OX   NCBI_TaxID=9940;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=10219521; DOI=10.1016/s0739-7240(99)00005-3;
RA   Aitken G.D., Raizis A.M., Yandle T.G., George P.M., Espiner E.A.,
RA   Cameron V.A.;
RT   "The characterization of ovine genes for atrial, brain, and C-type
RT   natriuretic peptides.";
RL   Domest. Anim. Endocrinol. 16:115-121(1999).
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   -!- 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; AF037466; AAB92565.1; -; Genomic_DNA.
DR   RefSeq; NP_001153498.1; NM_001160026.1.
DR   AlphaFoldDB; O46541; -.
DR   BMRB; O46541; -.
DR   GeneID; 100294642; -.
DR   KEGG; oas:100294642; -.
DR   CTD; 4879; -.
DR   OrthoDB; 1493586at2759; -.
DR   Proteomes; UP000002356; Unplaced.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005179; F:hormone activity; IEA:UniProtKB-KW.
DR   GO; GO:0006182; P:cGMP biosynthetic process; ISS:UniProtKB.
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   3: Inferred from homology;
KW   Disulfide bond; Hormone; Reference proteome; Secreted; Signal; Vasoactive.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000255"
FT   CHAIN           27..129
FT                   /note="Natriuretic peptides B"
FT                   /id="PRO_0000001540"
FT   PEPTIDE         101..129
FT                   /note="Brain natriuretic peptide 29"
FT                   /evidence="ECO:0000303|PubMed:10219521"
FT                   /id="PRO_0000001541"
FT   PEPTIDE         104..129
FT                   /note="Brain natriuretic peptide 26"
FT                   /evidence="ECO:0000250|UniProtKB:P07634"
FT                   /id="PRO_0000001542"
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
FT                   /evidence="ECO:0000250|UniProtKB:P16860"
SQ   SEQUENCE   129 AA;  14118 MW;  13D4DF91D32A28EF CRC64;
     MDPQKALSRT LLLLLFLHLS LLGCRSHPLG GPGSASELPG LQELLDRLRD RVSELQAEQL
     RVEPLQQGQG LEETWDSPAA APAGFLGPHH SLLQALRGPK MMRDSGCFGR RLDRIGSLSG
     LGCNVLRRY