VNPA_OXYSC
ID VNPA_OXYSC Reviewed; 35 AA.
AC P83225;
DT 27-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 25-MAY-2022, entry version 53.
DE RecName: Full=Natriuretic peptide TNP-a;
DE AltName: Full=Taipan natriuretic peptide;
DE AltName: Full=Venom natriuretic peptide OxsSNPa;
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 {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 (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:0000269|PubMed:15652496}.
CC -!- MASS SPECTROMETRY: Mass=3651; 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR AlphaFoldDB; P83225; -.
DR SMR; P83225; -.
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 Toxin; Vasoactive; Vasodilator.
FT PEPTIDE 1..35
FT /note="Natriuretic peptide TNP-a"
FT /id="PRO_0000045070"
FT DISULFID 9..25
FT /evidence="ECO:0000269|PubMed:15652496"
SQ SEQUENCE 35 AA; 3653 MW; A89AC295E8D3E3F2 CRC64;
SDSKIGDGCF GLPLDHIGSV SGLGCNRPVQ NRPKK