ID   VNPA_PSETE              Reviewed;          40 AA.
AC   Q3SAF6;
DT   22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   25-MAY-2022, entry version 43.
DE   RecName: Full=Natriuretic peptide PtNP-a;
DE   Flags: Precursor; Fragment;
OS   Pseudonaja textilis (Eastern brown snake).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Elapidae; Acanthophiinae; Pseudonaja.
OX   NCBI_TaxID=8673;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC   TISSUE=Venom gland;
RX   PubMed=16908092; DOI=10.1016/j.biochi.2006.06.014;
RA   St Pierre L., Flight S., Masci P.P., Hanchard K.J., Lewis R.J.,
RA   Alewood P.F., de Jersey J., Lavin M.F.;
RT   "Cloning and characterisation of natriuretic peptides from the venom glands
RT   of Australian elapids.";
RL   Biochimie 88:1923-1931(2006).
CC   -!- FUNCTION: Snake venom natriuretic peptide that exhibits hypotensive and
CC       vasodepressor activity (By similarity). Recombinant PtNP-a demonstrates
CC       a dose-dependent stimulation of cGMP production via the natriuretic
CC       peptide receptor-A (NPR1). It also inhibits the angiotensin converting
CC       enzyme (ACE). {ECO:0000250, ECO:0000269|PubMed:16908092}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC   -!- MISCELLANEOUS: Recombinant PtNP-a does not inhibit platelet
CC       aggregation. {ECO:0000305|PubMed:16908092}.
CC   -!- SIMILARITY: Belongs to the natriuretic peptide family. {ECO:0000305}.
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DR   EMBL; DQ116724; AAZ82819.1; -; mRNA.
DR   AlphaFoldDB; Q3SAF6; -.
DR   Proteomes; UP000472273; Unplaced.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005179; F:hormone activity; IEA:InterPro.
DR   GO; GO:0008191; F:metalloendopeptidase inhibitor activity; IEA:UniProtKB-KW.
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   2: Evidence at transcript level;
KW   Disulfide bond; Hypotensive agent; Metalloenzyme inhibitor;
KW   Metalloprotease inhibitor; Protease inhibitor; Reference proteome;
KW   Secreted; Toxin; Vasoactive; Vasodilator.
FT   PEPTIDE         <1..35
FT                   /note="Natriuretic peptide PtNP-a"
FT                   /id="PRO_5000140402"
FT   PROPEP          36..40
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000344372"
FT   REGION          17..40
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        20..40
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        9..25
FT                   /evidence="ECO:0000250"
FT   NON_TER         1
SQ   SEQUENCE   40 AA;  4063 MW;  21D63ABF7BA64FB9 CRC64;
     SGSKIGNGCF GLPLDRISNT SGMGCRNPIQ NRPKSTPGGS