ID   ANFC3_TAKRU             Reviewed;         158 AA.
AC   Q805D4;
DT   16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   25-MAY-2022, entry version 73.
DE   RecName: Full=C-type natriuretic peptide 3;
DE   Flags: Precursor;
GN   Name=cnp-3 {ECO:0000312|EMBL:BAC57073.1};
OS   Takifugu rubripes (Japanese pufferfish) (Fugu rubripes).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Takifugu.
OX   NCBI_TaxID=31033;
RN   [1] {ECO:0000312|EMBL:BAC57073.1}
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Heart {ECO:0000312|EMBL:BAC57073.1};
RX   PubMed=12893874; DOI=10.1073/pnas.1632368100;
RA   Inoue K., Naruse K., Yamagami S., Mitani H., Suzuki N., Takei Y.;
RT   "Four functionally distinct C-type natriuretic peptides found in fish
RT   reveal evolutionary history of the natriuretic peptide system.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:10079-10084(2003).
CC   -!- FUNCTION: Exhibits natriuretic and vasodepressant activity. Has cGMP-
CC       stimulating activity. May help to regulate body fluid homeostasis in a
CC       variety of aquatic environments. {ECO:0000250|UniProtKB:P18145,
CC       ECO:0000303|PubMed:12893874}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the natriuretic peptide family. {ECO:0000255}.
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DR   EMBL; AB089937; BAC57073.1; -; mRNA.
DR   RefSeq; NP_001027908.1; NM_001032736.2.
DR   AlphaFoldDB; Q805D4; -.
DR   STRING; 31033.ENSTRUP00000009486; -.
DR   GeneID; 445906; -.
DR   KEGG; tru:445906; -.
DR   CTD; 567953; -.
DR   InParanoid; Q805D4; -.
DR   OrthoDB; 1491136at2759; -.
DR   Proteomes; UP000005226; Unplaced.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005179; F:hormone activity; IEA:UniProtKB-KW.
DR   InterPro; IPR002406; C_natriurtcpep.
DR   InterPro; IPR000663; Natr_peptide.
DR   InterPro; IPR030480; Natr_peptide_CS.
DR   Pfam; PF00212; ANP; 1.
DR   PRINTS; PR00713; CNATPEPTIDE.
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;
KW   Reference proteome; Secreted; Signal; Vasoactive.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   PROPEP          22..136
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000001585"
FT   PEPTIDE         137..158
FT                   /note="C-type natriuretic peptide 3"
FT                   /id="PRO_0000001586"
FT   REGION          32..95
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        47..68
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        142..158
FT                   /evidence="ECO:0000250|UniProtKB:P18145"
SQ   SEQUENCE   158 AA;  18071 MW;  24E1948EFF4410DE CRC64;
     MSLNLPGYAL FFILLVASSG AKPAPDLQIL EPPLSSLEEQ EEMQEEVQEK VQEQQEEVQE
     KVQEQQEEVQ EQQEEVQEQQ EEQQEEVQER GRGTGDVLLR AQLDSSTWAL QKDDVLMRLF
     KDLLRTSKRS RSRYKKGGLR SCFGVRLARI GSFSGLGC