ID   ANF_OREMO               Reviewed;         140 AA.
AC   Q805E9;
DT   05-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   25-MAY-2022, entry version 52.
DE   RecName: Full=Natriuretic peptides A;
DE   AltName: Full=Prepronatriodilatin;
DE   Contains:
DE     RecName: Full=Atrial natriuretic factor;
DE              Short=ANF;
DE     AltName: Full=Atrial natriuretic peptide;
DE              Short=ANP;
DE   Contains:
DE     RecName: Full=ANP-24;
DE   Flags: Precursor;
GN   Name=nppa; Synonyms=anp;
OS   Oreochromis mossambicus (Mozambique tilapia) (Tilapia mossambica).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC   Pseudocrenilabrinae; Oreochromini; Oreochromis.
OX   NCBI_TaxID=8127;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Heart;
RX   PubMed=15072558; DOI=10.1677/jme.0.0320547;
RA   Kawakoshi A., Hyodo S., Inoue K., Kobayashi Y., Takei Y.;
RT   "Four natriuretic peptides (ANP, BNP, VNP and CNP) coexist in the sturgeon:
RT   identification of BNP in fish lineage.";
RL   J. Mol. Endocrinol. 32:547-555(2004).
CC   -!- FUNCTION: Hormone playing a key role in cardiovascular homeostasis
CC       through regulation of natriuresis, diuresis, and vasodilation. Has a
CC       cGMP-stimulating activity (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- PTM: Cleaved upon secretion to produce the functional hormone.
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the natriuretic peptide family. {ECO:0000305}.
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DR   EMBL; AB087283; BAC55024.1; -; mRNA.
DR   AlphaFoldDB; Q805E9; -.
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: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; IPR002407; Natriuretic_peptide_atrial.
DR   Pfam; PF00212; ANP; 1.
DR   PRINTS; PR00711; ANATPEPTIDE.
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; Secreted;
KW   Signal; Vasoactive.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   PROPEP          22..113
FT                   /id="PRO_0000001521"
FT   PEPTIDE         114..140
FT                   /note="Atrial natriuretic factor"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000391789"
FT   PEPTIDE         116..140
FT                   /note="ANP-24"
FT                   /id="PRO_0000001522"
FT   REGION          59..102
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        64..102
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   SITE            113..114
FT                   /note="Cleavage"
FT                   /evidence="ECO:0000250"
FT   DISULFID        119..135
FT                   /evidence="ECO:0000250|UniProtKB:P18144"
SQ   SEQUENCE   140 AA;  15577 MW;  5F2D214FA560DB0F CRC64;
     MRTEFLWGVL ALLCQQTLVS GHILGRPSSA NDLAQLKSLL ERFEETLDEV VQKEDLEAYY
     EDMNQDPKSS QTSQGWDQEG NQEPLISEKA QPLTEGKTVN QRSRLQDLLM ATRKRTSGCF
     GARMDRIGNA SGLGCNSGRG