ID   VNPC_OXYMI              Reviewed;          39 AA.
AC   P83230;
DT   27-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   25-MAY-2022, entry version 54.
DE   RecName: Full=Peptide TNP-c;
DE   AltName: Full=Taipan natriuretic peptide;
DE   AltName: Full=Venom natriuretic peptide OxsSNPc;
OS   Oxyuranus microlepidotus (Inland taipan) (Diemenia microlepidota).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Elapidae; Acanthophiinae; Oxyuranus.
OX   NCBI_TaxID=111177 {ECO:0000305};
RN   [1]
RP   PROTEIN SEQUENCE, FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MASS
RP   SPECTROMETRY, AND DISULFIDE BOND.
RC   TISSUE=Venom;
RX   PubMed=15652496; DOI=10.1016/j.bbrc.2004.11.171;
RA   Fry B.G., Wickramaratana J.C., Lemme S., Beuve A., Garbers D.,
RA   Hodgson W.C., Alewood P.F.;
RT   "Novel natriuretic peptides from the venom of the inland taipan (Oxyuranus
RT   microlepidotus): isolation, chemical and biological characterisation.";
RL   Biochem. Biophys. Res. Commun. 327:1011-1015(2005).
CC   -!- FUNCTION: Exhibits vasoactive and hypotensive activity (By similarity).
CC       Produces a near complete relaxation in pre-contracted aortae by
CC       activating the natriuretic peptide receptor-A (NPR1). {ECO:0000250,
CC       ECO:0000269|PubMed:15652496}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:15652496,
CC       ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000269|PubMed:15652496}.
CC   -!- MASS SPECTROMETRY: Mass=4112; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:15652496};
CC   -!- SIMILARITY: Belongs to the natriuretic peptide family. {ECO:0000305}.
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DR   AlphaFoldDB; P83230; -.
DR   SMR; P83230; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005179; F:hormone activity; IEA:InterPro.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   GO; GO:0008217; P:regulation of blood pressure; IEA:UniProtKB-KW.
DR   GO; GO:0042311; P:vasodilation; IEA:UniProtKB-KW.
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   SMART; SM00183; NAT_PEP; 1.
DR   PROSITE; PS00263; NATRIURETIC_PEPTIDE; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Hypotensive agent; Secreted;
KW   Toxin; Vasoactive; Vasodilator.
FT   PEPTIDE         1..39
FT                   /note="Peptide TNP-c"
FT                   /id="PRO_0000045075"
FT   DISULFID        9..25
FT                   /evidence="ECO:0000269|PubMed:15652496"
SQ   SEQUENCE   39 AA;  4115 MW;  1181C8B1F530C286 CRC64;
     SDSKIGNGCF GFPLDRIGSV SGLGCNRIMQ NPPKKFSGE