ID   TSNP_TITSE              Reviewed;          21 AA.
AC   P0DMD6;
DT   19-MAR-2014, integrated into UniProtKB/Swiss-Prot.
DT   19-MAR-2014, sequence version 1.
DT   25-MAY-2022, entry version 12.
DE   RecName: Full=Natriuretic peptide TsNP;
OS   Tityus serrulatus (Brazilian scorpion).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC   Scorpiones; Buthida; Buthoidea; Buthidae; Tityus.
OX   NCBI_TaxID=6887;
RN   [1]
RP   PROTEIN SEQUENCE, FUNCTION, MASS SPECTROMETRY, AND 3D-STRUCTURE MODELING.
RC   TISSUE=Venom;
RX   PubMed=23911732; DOI=10.1016/j.toxicon.2013.07.016;
RA   Alves R.S., Ximenes R.M., Jorge A.R., Nascimento N.R., Martins R.D.,
RA   Rabello M.M., Hernandes M.Z., Toyama D.O., Toyama M.H., Martins A.M.,
RA   Havt A., Monteiro H.S.;
RT   "Isolation, homology modeling and renal effects of a C-type natriuretic
RT   peptide from the venom of the Brazilian yellow scorpion (Tityus
RT   serrulatus).";
RL   Toxicon 74:19-26(2013).
CC   -!- FUNCTION: Scorpion venom natriuretic peptide that increases the
CC       perfusion pressure, glomerular filtration rate and urinary flow in the
CC       isolated perfused rat kidney assay. Induces a decrease of the
CC       percentages of renal transport for sodium, potassium and chloride and
CC       an increase of the urinary cGMP concentration. Also down-regulates the
CC       mRNA expression of natriuretic peptide receptor-A (NPR1) in the kidneys
CC       whereas it up-regulates those of NPR-B (NPR2), NPR-C (NPR3) and
CC       guanylyl cyclase C (GUCY2C) mRNAs. May exhibit hypotensive and
CC       vasodepressor activities. {ECO:0000269|PubMed:23911732}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC   -!- MASS SPECTROMETRY: Mass=2190.64; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:23911732};
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; P0DMD6; -.
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   PRINTS; PR00710; NATPEPTIDES.
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..21
FT                   /note="Natriuretic peptide TsNP"
FT                   /id="PRO_0000425736"
FT   DISULFID        5..21
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   21 AA;  2191 MW;  FC309C0BC16D1865 CRC64;
     KLSGCFGFKL DRIGTMSGLG C