ANFC2_ORYLA
ID ANFC2_ORYLA Reviewed; 126 AA.
AC Q8AYR5;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 25-MAY-2022, entry version 81.
DE RecName: Full=C-type natriuretic peptide 2;
DE Flags: Precursor;
GN Name=cnp-2 {ECO:0000312|EMBL:BAC15761.1};
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:BAC15761.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND SYNTHESIS.
RC TISSUE=Brain {ECO:0000269|PubMed:12893874};
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 and spinal cord.
CC {ECO:0000269|PubMed:12893874, ECO:0000305}.
CC -!- SIMILARITY: Belongs to the natriuretic peptide family.
CC {ECO:0000255|RuleBase:RU003686}.
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DR EMBL; AB081456; BAC15761.1; -; mRNA.
DR RefSeq; NP_001098152.1; NM_001104682.1.
DR AlphaFoldDB; Q8AYR5; -.
DR STRING; 8090.ENSORLP00000024353; -.
DR GeneID; 100049234; -.
DR CTD; 4879; -.
DR eggNOG; ENOG502SH05; Eukaryota.
DR HOGENOM; CLU_2048903_0_0_1; -.
DR InParanoid; Q8AYR5; -.
DR OMA; QTKMRRW; -.
DR TreeFam; TF106305; -.
DR Proteomes; UP000001038; Unplaced.
DR Proteomes; UP000265180; Chromosome 9.
DR Proteomes; UP000265200; Chromosome 9.
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..102
FT /evidence="ECO:0000250"
FT /id="PRO_0000001595"
FT PEPTIDE 103..126
FT /note="C-type natriuretic peptide 2"
FT /id="PRO_0000001596"
FT REGION 44..80
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 46..64
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 110..126
FT /evidence="ECO:0000250|UniProtKB:P18145"
SQ SEQUENCE 126 AA; 13400 MW; 9D5D7B8DDECB0F92 CRC64;
MAVCSSSSLI LLTVFLSVAV ETRPSSDRDE EQVLKSLFGP HLTSLILAPP TSNDSTEGSS
GSPEPPTPSE APVLIHGDRG TASQILRSFL RQREKTRRWG RKPMVAGGGC FGMKMDRIGS
ISGLGC
