NDBH2_TITSE
ID NDBH2_TITSE Reviewed; 25 AA.
AC P84190; P84192;
DT 13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2006, sequence version 1.
DT 25-MAY-2022, entry version 32.
DE RecName: Full=Hypotensin-2 {ECO:0000305|PubMed:18445483};
DE AltName: Full=Hypotensin II {ECO:0000303|PubMed:18445483};
DE Short=TsHpt-II {ECO:0000303|PubMed:18445483};
DE AltName: Full=Toxin Ts14 2 {ECO:0000303|PubMed:19689419};
DE Contains:
DE RecName: Full=Hypotensin-4 {ECO:0000305|PubMed:18445483};
DE AltName: Full=Hypotensin IV {ECO:0000303|PubMed:18445483};
DE Short=TsHpt-IV {ECO:0000303|PubMed:18445483};
DE AltName: Full=Toxin Ts14 4 {ECO:0000303|PubMed:19689419};
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, SUBCELLULAR LOCATION, AND MASS SPECTROMETRY.
RC TISSUE=Venom;
RX PubMed=18445483; DOI=10.1016/j.bbrc.2008.04.104;
RA Verano-Braga T., Rocha-Resende C., Silva D.M., Ianzer D.,
RA Martin-Eauclaire M.F., Bougis P.E., de Lima M.E., Santos R.A.S.,
RA Pimenta A.M.C.;
RT "Tityus serrulatus hypotensins: a new family of peptides from scorpion
RT venom.";
RL Biochem. Biophys. Res. Commun. 371:515-520(2008).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND PHOSPHORYLATION AT SER-6.
RX PubMed=23731212; DOI=10.1021/pr4003068;
RA Verano-Braga T., Dutra A.A., Leon I.R., Melo-Braga M.N., Roepstorff P.,
RA Pimenta A.M., Kjeldsen F.;
RT "Moving pieces in a venomic puzzle: unveiling post-translationally modified
RT toxins from Tityus serrulatus.";
RL J. Proteome Res. 12:3460-3470(2013).
RN [3]
RP NOMENCLATURE.
RX PubMed=19689419; DOI=10.2174/092986609788923329;
RA Cologna C.T., Marcussi S., Giglio J.R., Soares A.M., Arantes E.C.;
RT "Tityus serrulatus scorpion venom and toxins: an overview.";
RL Protein Pept. Lett. 16:920-932(2009).
CC -!- FUNCTION: Agonist of the B2 bradykinin receptor (BDKRB2). Potentiates
CC the hypotensive effect of bradykinin (BK) and induces a direct
CC vasorelaxing effect, independently of BK, by endothelium- and nitric
CC oxide (NO)-dependent mechanisms in rat aortic ring preparations. Does
CC not inhibit the angiotensin-converting enzyme (ACE). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:18445483}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000269|PubMed:18445483}.
CC -!- PTM: The ultimate C-terminal Ala residue of TsHpt-I is quickly removed
CC by carboxypeptidase Y in (in vitro) experiments. {ECO:0000250}.
CC -!- MASS SPECTROMETRY: [Hypotensin-2]: Mass=2725.6; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:18445483};
CC -!- MASS SPECTROMETRY: [Hypotensin-4]: Mass=2654.6; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:18445483};
CC -!- SIMILARITY: Belongs to the non-disulfide-bridged peptide (NDBP)
CC superfamily. {ECO:0000305}.
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DR AlphaFoldDB; P84190; -.
DR iPTMnet; P84190; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR GO; GO:0008217; P:regulation of blood pressure; IEA:UniProtKB-KW.
PE 1: Evidence at protein level;
KW Bradykinin receptor impairing toxin; Direct protein sequencing;
KW G-protein coupled receptor impairing toxin; Hypotensive agent;
KW Phosphoprotein; Secreted; Toxin.
FT PEPTIDE 1..25
FT /note="Hypotensin-2"
FT /evidence="ECO:0000269|PubMed:18445483"
FT /id="PRO_0000239434"
FT PEPTIDE 1..24
FT /note="Hypotensin-4"
FT /evidence="ECO:0000269|PubMed:18445483"
FT /id="PRO_0000239436"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 23..24
FT /note="Important for potentiating BK effects"
FT /evidence="ECO:0000250"
FT MOD_RES 6
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:23731212"
SQ SEQUENCE 25 AA; 2726 MW; 8D99F16FE445C0C6 CRC64;
AEIDFSGIPE DIIKEIKETN AKPPA