ID   ANFC2_ONCMY             Reviewed;         131 AA.
AC   Q8AXR2;
DT   16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   25-MAY-2022, entry version 52.
DE   RecName: Full=C-type natriuretic peptide 2;
DE   AltName: Full=C-type natriuretic peptide II;
DE   AltName: Full=CNP-22 II;
DE   Flags: Precursor;
GN   Name=cnp-1-2 {ECO:0000312|EMBL:BAC44843.1};
OS   Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC   Salmonidae; Salmoninae; Oncorhynchus.
OX   NCBI_TaxID=8022;
RN   [1] {ECO:0000305, ECO:0000312|EMBL:BAC44843.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC   TISSUE=Brain {ECO:0000269|PubMed:12568796};
RX   PubMed=12568796; DOI=10.1016/s0016-6480(02)00591-9;
RA   Inoue K., Russell M.J., Olson K.R., Takei Y.;
RT   "C-type natriuretic peptide of rainbow trout (Oncorhynchus mykiss): primary
RT   structure and vasorelaxant activities.";
RL   Gen. Comp. Endocrinol. 130:185-192(2003).
CC   -!- FUNCTION: Exhibits natriuretic and vasodepressor activity. Has a cGMP-
CC       stimulating activity (By similarity). {ECO:0000250|UniProtKB:P18145}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed in brain and to a low extent in atrium.
CC       {ECO:0000269|PubMed:12568796}.
CC   -!- SIMILARITY: Belongs to the natriuretic peptide family.
CC       {ECO:0000255|RuleBase:RU003686}.
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DR   EMBL; AB076602; BAC44843.1; -; mRNA.
DR   RefSeq; NP_001117682.1; NM_001124210.1.
DR   AlphaFoldDB; Q8AXR2; -.
DR   GeneID; 100135814; -.
DR   KEGG; omy:100135814; -.
DR   CTD; 100135814; -.
DR   OrthoDB; 1491136at2759; -.
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   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..22
FT                   /evidence="ECO:0000255"
FT   PROPEP          23..109
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000001591"
FT   PEPTIDE         110..131
FT                   /note="C-type natriuretic peptide 2"
FT                   /id="PRO_0000001592"
FT   DISULFID        115..131
FT                   /evidence="ECO:0000250|UniProtKB:P18145"
SQ   SEQUENCE   131 AA;  14472 MW;  436CF382B326A08D CRC64;
     MLYPALLCAA LLLIAPLGHT EGRTLYPSPD AIQFVEQFLD RYNDLTLDDL ENLVSSQPEE
     PSSAFTSGVK IAEYPKWADI PAQGDSTWLR LLKGTLANQK RAVTDRSRRG WNRGCFGLKL
     DRIGSMSGLG C