ID   ANFC_TRISC              Reviewed;         136 AA.
AC   P55208; Q98UI7;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 2.
DT   25-MAY-2022, entry version 64.
DE   RecName: Full=C-type natriuretic peptide prohormone;
DE   AltName: Full=CNP-115;
DE   Contains:
DE     RecName: Full=CNP-39;
DE   Contains:
DE     RecName: Full=CNP-38;
DE   Contains:
DE     RecName: Full=CNP-22;
DE   Flags: Precursor;
OS   Triakis scyllium (Banded houndshark) (Hemigaleus pingi).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes;
OC   Elasmobranchii; Galeomorphii; Galeoidea; Carcharhiniformes; Triakidae;
OC   Triakis.
OX   NCBI_TaxID=30494;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Kawakoshi A., Hyodo S., Takei Y.;
RT   "C-type natriuretic peptide precursor mRNA of Triakis scyllia.";
RL   Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   PROTEIN SEQUENCE OF 22-136.
RC   TISSUE=Brain, and Heart;
RX   PubMed=1474339; DOI=10.1677/joe.0.1350317;
RA   Suzuki R., Takahashi A., Takei Y.;
RT   "Different molecular forms of C-type natriuretic peptide isolated from the
RT   brain and heart of an elasmobranch, Triakis scyllia.";
RL   J. Endocrinol. 135:317-323(1992).
CC   -!- FUNCTION: Hormone which may be vasoactive and natriuretic. Has a cGMP-
CC       stimulating activity (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: CNP-115 is differentially processed to produce CNP-
CC       38 and CNP-39 in the heart and CNP-22 in the brain.
CC   -!- SIMILARITY: Belongs to the natriuretic peptide family. {ECO:0000305}.
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DR   EMBL; AB047081; BAB32433.1; -; mRNA.
DR   AlphaFoldDB; P55208; -.
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..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..136
FT                   /note="C-type natriuretic peptide prohormone"
FT                   /id="PRO_0000001607"
FT   PEPTIDE         98..136
FT                   /note="CNP-39"
FT                   /id="PRO_0000001608"
FT   PEPTIDE         99..136
FT                   /note="CNP-38"
FT                   /id="PRO_0000001609"
FT   PEPTIDE         115..136
FT                   /note="CNP-22"
FT                   /id="PRO_0000001610"
FT   DISULFID        120..136
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   136 AA;  15143 MW;  A08BA19ED04DDB4E CRC64;
     MSGQTSFYCG LLLVLLIQAQ ARPRSDDSLQ TLSRLLEDEY GHYLPSDELN NEAQEMSPAA
     SLPEFNADQS DLELPWDRES REIGGRPFRQ EAVLARLLKD LSNNPLRFRG RSKKGPSRGC
     FGVKLDRIGA MSGLGC