ID   VNPB_OXYSC              Reviewed;         111 AA.
AC   P83228; Q4VRI2;
DT   27-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 2.
DT   25-MAY-2022, entry version 58.
DE   RecName: Full=Natriuretic peptide TNP-b;
DE   AltName: Full=Taipan natriuretic peptide;
DE   AltName: Full=Venom natriuretic peptide OxsSNPb;
DE   Flags: Precursor;
OS   Oxyuranus scutellatus scutellatus (Australian taipan) (Coastal taipan).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Elapidae; Acanthophiinae; Oxyuranus.
OX   NCBI_TaxID=8667;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Venom gland;
RA   Welton R.E., Burnell J.N.;
RL   Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   PROTEIN SEQUENCE OF 72-106, FUNCTION, SUBCELLULAR LOCATION, 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 (PubMed:15652496) and hypotensive
CC       activity (By similarity). Is only weakly active on natriuretic peptide
CC       receptor-C (NPR3). {ECO:0000250, 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:0000305|PubMed:15652496}.
CC   -!- MASS SPECTROMETRY: Mass=3661; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:15652496};
CC   -!- MISCELLANEOUS: Does not activate natriuretic peptide receptor-A (NPR1).
CC       {ECO:0000305|PubMed:15652496}.
CC   -!- SIMILARITY: Belongs to the natriuretic peptide family. {ECO:0000305}.
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DR   EMBL; AY691663; AAY47072.1; -; mRNA.
DR   AlphaFoldDB; P83228; -.
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   Pfam; PF00212; ANP; 1.
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   Signal; Toxin; Vasoactive; Vasodilator.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000255"
FT   PROPEP          28..71
FT                   /evidence="ECO:0000269|PubMed:15652496"
FT                   /id="PRO_0000334170"
FT   PEPTIDE         72..106
FT                   /note="Natriuretic peptide TNP-b"
FT                   /id="PRO_0000045073"
FT   PROPEP          107..111
FT                   /id="PRO_0000334171"
FT   REGION          51..77
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          92..111
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        80..96
FT                   /evidence="ECO:0000269|PubMed:15652496"
FT   CONFLICT        106
FT                   /note="Q -> K (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   111 AA;  11252 MW;  77DA6355F8911B08 CRC64;
     MVGLSRLAGG GLLLLLLLAL LPLALDGKPA PLPQALPEAL AGGTTALRRD VTEEQQQQLV
     AEESSGPAAG RSDPKIGDGC FGLPLDHIGS VSGLGCNRPV QNRPKQIPGG S