ID   ANFC_ANGJA              Reviewed;         131 AA.
AC   P18145;
DT   01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 2.
DT   25-MAY-2022, entry version 83.
DE   RecName: Full=C-type natriuretic peptide;
DE   AltName: Full=BNP-like peptide CNP-22;
DE   Flags: Precursor;
GN   Name=cnp;
OS   Anguilla japonica (Japanese eel).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Anguilliformes; Anguillidae;
OC   Anguilla.
OX   NCBI_TaxID=7937;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP   STAGE.
RC   TISSUE=Brain;
RX   PubMed=11353677; DOI=10.1152/ajpregu.2001.280.6.r1727;
RA   Takei Y., Inoue K., Ando K., Ihara T., Katafuchi T., Kashiwagi M.,
RA   Hirose S.;
RT   "Enhanced expression and release of C-type natriuretic peptide in
RT   freshwater eels.";
RL   Am. J. Physiol. 280:R1727-1735(2001).
RN   [2]
RP   PROTEIN SEQUENCE OF 110-131, AND FUNCTION.
RC   TISSUE=Brain;
RX   PubMed=2143379; DOI=10.1016/0006-291x(90)92174-x;
RA   Takei Y., Takahashi A., Watanabe T.X., Nakajima K., Sakakibara S.,
RA   Takao T., Shimonishi Y.;
RT   "Amino acid sequence and relative biological activity of a natriuretic
RT   peptide isolated from eel brain.";
RL   Biochem. Biophys. Res. Commun. 170:883-891(1990).
CC   -!- FUNCTION: Hormone which plays a role in endochondral ossification
CC       through regulation of cartilaginous growth plate chondrocytes
CC       proliferation and differentiation. May also be vasoactive and
CC       natriuretic. May be important for freshwater adaptation.
CC       {ECO:0000269|PubMed:11353677, ECO:0000269|PubMed:2143379}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Highly expressed in brain and liver, and moderately
CC       in gut, gills and heart. Expressed to a low level in atrium, ventricle
CC       and liver of fresh water eels. {ECO:0000269|PubMed:11353677}.
CC   -!- DEVELOPMENTAL STAGE: Expression is generally higher in freshwater eels
CC       than in saltwater ones, except in brain, where the levels are the same.
CC       {ECO:0000269|PubMed:11353677}.
CC   -!- SIMILARITY: Belongs to the natriuretic peptide family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; D88022; BAA13529.1; -; mRNA.
DR   PIR; A35418; A35418.
DR   AlphaFoldDB; P18145; -.
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; IPR002406; C_natriurtcpep.
DR   InterPro; IPR000663; Natr_peptide.
DR   InterPro; IPR030480; Natr_peptide_CS.
DR   Pfam; PF00212; ANP; 1.
DR   PRINTS; PR00713; CNATPEPTIDE.
DR   PRINTS; PR00710; NATPEPTIDES.
DR   SMART; SM00183; NAT_PEP; 1.
DR   PROSITE; PS00263; NATRIURETIC_PEPTIDE; 1.
PE   1: Evidence at protein level;
KW   Cleavage on pair of basic residues; Direct protein sequencing;
KW   Disulfide bond; Hormone; Secreted; Signal; Vasoactive.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   PROPEP          21..109
FT                   /evidence="ECO:0000269|PubMed:2143379"
FT                   /id="PRO_0000001579"
FT   PEPTIDE         110..131
FT                   /note="C-type natriuretic peptide"
FT                   /id="PRO_0000001580"
FT   DISULFID        115..131
SQ   SEQUENCE   131 AA;  14725 MW;  0E19C1B259838079 CRC64;
     MMCKALVFAV LLLAVPLERA DSRALRTPVD AIQFVEQFLE HYNDLLNIDD LENQTGDQLE
     SPQPLSSGLK VAEYPKWVDV PSQNDNTWFR LLRGALANRK RALPDRAKRG WNRGCFGLKL
     DRIGSLSGLG C