ANFB_FELCA
ID ANFB_FELCA Reviewed; 132 AA.
AC Q9GLK4;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Natriuretic peptides B;
DE AltName: Full=Brain natriuretic factor prohormone {ECO:0000250|UniProtKB:P16860};
DE Short=preproBNP {ECO:0000303|PubMed:12119112};
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 35 {ECO:0000303|PubMed:12119112};
DE Short=BNP-35 {ECO:0000303|PubMed:12119112};
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; Synonyms=BNP;
OS Felis catus (Cat) (Felis silvestris catus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae; Felinae; Felis.
OX NCBI_TaxID=9685;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Heart atrium;
RX PubMed=12119112; DOI=10.1016/s0378-1119(02)00676-5;
RA Liu Z.L., Wiedmeyer C.E., Sisson D.D., Solter P.F.;
RT "Cloning and characterization of feline brain natriuretic peptide.";
RL Gene 292:183-190(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE.
RA Liu Z.L.;
RT "Felis catus brain natriuretic peptide (BNP) gene.";
RL Submitted (SEP-2001) to the EMBL/GenBank/DDBJ databases.
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 Ser-102 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; AF253495; AAG13661.1; -; mRNA.
DR EMBL; AF425738; AAL24812.1; -; Genomic_DNA.
DR RefSeq; NP_001009244.1; NM_001009244.1.
DR AlphaFoldDB; Q9GLK4; -.
DR STRING; 9685.ENSFCAP00000000064; -.
DR Ensembl; ENSFCAT00000072186; ENSFCAP00000058656; ENSFCAG00000000072.
DR GeneID; 493764; -.
DR KEGG; fca:493764; -.
DR CTD; 4879; -.
DR eggNOG; ENOG502SD0X; Eukaryota.
DR GeneTree; ENSGT00940000154513; -.
DR HOGENOM; CLU_158067_0_0_1; -.
DR InParanoid; Q9GLK4; -.
DR OrthoDB; 1493586at2759; -.
DR Proteomes; UP000011712; Chromosome C1.
DR Bgee; ENSFCAG00000000072; Expressed in embryonic head and 5 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: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 Disulfide bond; Hormone; Reference proteome; Secreted; Signal; Vasoactive.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..132
FT /note="Natriuretic peptides B"
FT /id="PRO_0000001529"
FT PEPTIDE 98..132
FT /note="Brain natriuretic peptide 35"
FT /evidence="ECO:0000303|PubMed:12119112"
FT /id="PRO_0000451937"
FT PEPTIDE 104..132
FT /note="Brain natriuretic peptide 29"
FT /evidence="ECO:0000250|UniProtKB:P16859"
FT /id="PRO_0000451938"
FT REGION 62..87
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 97..98
FT /note="Cleavage; by CORIN or FURIN"
FT /evidence="ECO:0000250|UniProtKB:P16860"
FT SITE 102..103
FT /note="Cleavage; by FAP"
FT /evidence="ECO:0000250|UniProtKB:P16860"
FT SITE 103..104
FT /note="Cleavage; by CORIN"
FT /evidence="ECO:0000250|UniProtKB:P16860"
FT DISULFID 110..126
FT /evidence="ECO:0000250|UniProtKB:P16860"
SQ SEQUENCE 132 AA; 14344 MW; D069B5F76A6C3510 CRC64;
MDPKTALLRA LLLLLFLHLS PLGGRSHPLG GPGPASEASA IQELLDGLRD TVSELQEAQM
ALGPLQQGHS PAESWEAQEE PPARVLAPHD NVLRALRRLG SSKMMRDSRC FGRRLDRIGS
LSGLGCNVLR RH
