ID   ANFC4_ORYLA             Reviewed;         121 AA.
AC   Q800I7;
DT   16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 81.
DE   RecName: Full=C-type natriuretic peptide 4;
DE   Flags: Precursor;
GN   Name=cnp-4 {ECO:0000312|EMBL:BAC65998.1};
OS   Oryzias latipes (Japanese rice fish) (Japanese killifish).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Beloniformes; Adrianichthyidae; Oryziinae;
OC   Oryzias.
OX   NCBI_TaxID=8090;
RN   [1] {ECO:0000305, ECO:0000312|EMBL:BAC65998.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND SYNTHESIS.
RC   TISSUE=Brain {ECO:0000312|EMBL:BAC65998.1};
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:0000269|PubMed:12893874, ECO:0000303|PubMed:12893874}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Brain, spinal cord, spleen, heart and fin, and to a
CC       lower extent in gill and ovary. {ECO:0000269|PubMed:12893874}.
CC   -!- SIMILARITY: Belongs to the natriuretic peptide family.
CC       {ECO:0000255|RuleBase:RU003686}.
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DR   EMBL; AB091699; BAC65998.1; -; mRNA.
DR   RefSeq; NP_001098154.1; NM_001104684.2.
DR   AlphaFoldDB; Q800I7; -.
DR   STRING; 8090.ENSORLP00000008805; -.
DR   Ensembl; ENSORLT00000041713; ENSORLP00000037865; ENSORLG00000022637.
DR   GeneID; 100049239; -.
DR   KEGG; ola:100049239; -.
DR   CTD; 4880; -.
DR   eggNOG; ENOG502S2QY; Eukaryota.
DR   GeneTree; ENSGT00390000015492; -.
DR   HOGENOM; CLU_160791_0_0_1; -.
DR   InParanoid; Q800I7; -.
DR   OMA; SHFLACG; -.
DR   OrthoDB; 1491136at2759; -.
DR   TreeFam; TF106305; -.
DR   Proteomes; UP000001038; Chromosome 4.
DR   Proteomes; UP000265180; Unplaced.
DR   Proteomes; UP000265200; Unplaced.
DR   Bgee; ENSORLG00000022637; Expressed in heart and 3 other tissues.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005179; F:hormone activity; IBA:GO_Central.
DR   GO; GO:0051427; F:hormone receptor binding; IBA:GO_Central.
DR   GO; GO:0006182; P:cGMP biosynthetic process; IBA:GO_Central.
DR   GO; GO:0007168; P:receptor guanylyl cyclase signaling pathway; IBA:GO_Central.
DR   InterPro; IPR000663; Natr_peptide.
DR   InterPro; IPR030480; Natr_peptide_CS.
DR   InterPro; IPR002408; Natriuretic_peptide_brain.
DR   Pfam; PF00212; ANP; 1.
DR   PRINTS; PR00712; BNATPEPTIDE.
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;
KW   Reference proteome; Secreted; Signal; Vasoactive.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   PROPEP          23..96
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000001599"
FT   PEPTIDE         97..121
FT                   /note="C-type natriuretic peptide 4"
FT                   /id="PRO_0000001600"
FT   REGION          80..109
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        105..121
FT                   /evidence="ECO:0000250|UniProtKB:P18145"
SQ   SEQUENCE   121 AA;  13457 MW;  EFD7FD534B137009 CRC64;
     MNLSYLVACG LLVTFLSDKM DAQPLTPAQQ KSLRSLLGEE LAEFLESGEN ENRLDDVRSR
     MRLLRDLRVD TRARGMWARL LNDQPASRRH KSGSKKGGST SRSGCFGHKM DRIGTISGMG
     C