NDBH1_TITSE
ID NDBH1_TITSE Reviewed; 72 AA.
AC P84189; A0A218QWX8; A0A218QWX9; P84191;
DT 13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 25-MAY-2022, sequence version 2.
DT 03-AUG-2022, entry version 34.
DE RecName: Full=Hypotensin-1 {ECO:0000305|PubMed:18445483};
DE AltName: Full=Anti-hypertensive peptide {ECO:0000303|PubMed:27732900};
DE AltName: Full=Hypotensin I {ECO:0000303|PubMed:18445483};
DE Short=TsHpt-I {ECO:0000303|PubMed:18445483};
DE AltName: Full=Tityustoxin-14 1 {ECO:0000305|PubMed:19689419};
DE Short=Hypotensin toxin Ts14.1 {ECO:0000312|EMBL:QPD99051.1};
DE Short=Ts14 1 {ECO:0000303|PubMed:19689419};
DE Contains:
DE RecName: Full=Hypotensin-3 {ECO:0000305|PubMed:18445483};
DE AltName: Full=Hypotensin III {ECO:0000303|PubMed:18445483};
DE Short=TsHpt-III {ECO:0000303|PubMed:18445483};
DE AltName: Full=Toxin Ts14 3 {ECO:0000303|PubMed:19689419};
DE Flags: Precursor;
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 NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Venom gland;
RX DOI=10.4236/ojgen.2012.24027;
RA Alvarenga E.R., Mendes T.M., Magalhaes B.F., Siqueira F.F., Dantas A.E.,
RA Barroca T.M., Horta C.C., Kalapothakis E.;
RT "Transcriptome analysis of the Tityus serrulatus scorpion venom gland.";
RL O. J. Gen. 2:210-220(2012).
RN [2] {ECO:0000312|EMBL:JAW06987.1, ECO:0000312|EMBL:JAW06992.1, ECO:0000312|EMBL:JAW07038.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Venom gland;
RX PubMed=29561852; DOI=10.1371/journal.pone.0193739;
RA de Oliveira U.C., Nishiyama M.Y. Jr., Dos Santos M.B.V.,
RA Santos-da-Silva A.P., Chalkidis H.M., Souza-Imberg A., Candido D.M.,
RA Yamanouye N., Dorce V.A.C., Junqueira-de-Azevedo I.L.M.;
RT "Proteomic endorsed transcriptomic profiles of venom glands from Tityus
RT obscurus and T. serrulatus scorpions.";
RL PLoS ONE 13:e0193739-e0193739(2018).
RN [3] {ECO:0000312|EMBL:QPD99051.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Venom gland;
RX PubMed=33181162; DOI=10.1016/j.toxicon.2020.11.001;
RA Kalapothakis Y., Miranda K., Pereira A.H., Witt A.S.A., Marani C.,
RA Martins A.P., Leal H.G., Campos-Junior E., Pimenta A.M.C., Borges A.,
RA Chavez-Olortegui C., Kalapothakis E.;
RT "Novel components of Tityus serrulatus venom: a transcriptomic approach.";
RL Toxicon 189:91-104(2021).
RN [4]
RP PROTEIN SEQUENCE OF 36-60, FUNCTION, SUBCELLULAR LOCATION, PTM, AND MASS
RP 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 [5]
RP PROTEIN SEQUENCE OF 36-51, AND SUBCELLULAR LOCATION.
RC TISSUE=Venom;
RX PubMed=18718845; DOI=10.1016/j.toxicon.2008.07.010;
RA Rates B., Ferraz K.K., Borges M.H., Richardson M., De Lima M.E.,
RA Pimenta A.M.;
RT "Tityus serrulatus venom peptidomics: assessing venom peptide diversity.";
RL Toxicon 52:611-618(2008).
RN [6]
RP FUNCTION, AND SYNTHESIS OF ANALOGS.
RX PubMed=20417225; DOI=10.1016/j.toxicon.2010.04.006;
RA Verano-Braga T., Figueiredo-Rezende F., Melo M.N., Lautner R.Q.,
RA Gomes E.R.M., Mata-Machado L.T., Murari A., Rocha-Resende C.,
RA Elena de Lima M., Guatimosim S., Santos R.A.S., Pimenta A.M.C.;
RT "Structure-function studies of Tityus serrulatus hypotensin-I (TsHpt-I): a
RT new agonist of B(2) kinin receptor.";
RL Toxicon 56:1162-1171(2010).
RN [7]
RP PROTEIN SEQUENCE OF 36-49, MASS SPECTROMETRY, AND PHOSPHORYLATION AT
RP SER-41.
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 [8]
RP FUNCTION.
RX PubMed=27732900; DOI=10.1016/j.peptides.2016.10.002;
RA Cassini-Vieira P., Felipetto M., Prado L.B., Verano-Braga T., Andrade S.P.,
RA Santos R.A.S., Teixeira M.M., de Lima M.E., Pimenta A.M.C., Barcelos L.S.;
RT "Ts14 from Tityus serrulatus boosts angiogenesis and attenuates
RT inflammation and collagen deposition in sponge-induced granulation tissue
RT in mice.";
RL Peptides 98:63-69(2017).
RN [9]
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)
CC (PubMed:18445483, PubMed:20417225). Potentiates the hypotensive effect
CC of bradykinin (BK) and induces a direct vasorelaxing effect independent
CC of BK, by endothelium- and nitric oxide (NO)-dependent mechanisms in
CC rat aortic ring preparations (PubMed:18445483, PubMed:20417225). Also
CC exerts proangiogenic, antiinflammatory, and antifibrogenic activities
CC (PubMed:27732900). {ECO:0000269|PubMed:18445483,
CC ECO:0000269|PubMed:20417225, ECO:0000269|PubMed:27732900}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:18445483,
CC ECO:0000269|PubMed:18718845}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000305|PubMed:18445483, ECO:0000305|PubMed:18718845}.
CC -!- PTM: Hypotensin-1 undergoes enzymatic cleavages by carboxypeptidases,
CC endopeptidases, and aminopeptidases resulting in at least 46 fragments
CC of this protein. {ECO:0000269|PubMed:23731212}.
CC -!- MASS SPECTROMETRY: [Hypotensin-1]: Mass=2726.08; Method=Electrospray;
CC Note=Hypotensin-1.; Evidence={ECO:0000269|PubMed:18445483};
CC -!- MASS SPECTROMETRY: [Hypotensin-3]: Mass=2655.06; Method=Electrospray;
CC Note=Hypotensin-3.; Evidence={ECO:0000269|PubMed:18445483};
CC -!- MISCELLANEOUS: Does not inhibit the angiotensin-converting enzyme
CC (ACE). {ECO:0000305|PubMed:18445483}.
CC -!- SIMILARITY: Belongs to the non-disulfide-bridged peptide (NDBP)
CC superfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=JAW06987.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; GEUW01000058; JAW06987.1; ALT_INIT; Transcribed_RNA.
DR EMBL; GEUW01000053; JAW06992.1; -; Transcribed_RNA.
DR EMBL; GEUW01000007; JAW07038.1; -; Transcribed_RNA.
DR EMBL; MT450715; QPD99051.1; -; mRNA.
DR AlphaFoldDB; P84189; -.
DR iPTMnet; P84189; -.
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; Signal; Toxin.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT PROPEP 25..35
FT /evidence="ECO:0000305|PubMed:18445483"
FT /id="PRO_0000455426"
FT PEPTIDE 36..60
FT /note="Hypotensin-1"
FT /evidence="ECO:0000269|PubMed:18445483"
FT /id="PRO_0000239433"
FT PEPTIDE 36..59
FT /note="Hypotensin-3"
FT /evidence="ECO:0000269|PubMed:18445483"
FT /id="PRO_0000239435"
FT PROPEP 61..72
FT /evidence="ECO:0000305|PubMed:18445483"
FT /id="PRO_0000455427"
FT REGION 53..72
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 58..59
FT /note="Important for potentiating BK effects"
FT MOD_RES 41
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:23731212"
SQ SEQUENCE 72 AA; 8164 MW; 8800BDD8F4FB3CE9 CRC64;
MKMMIPVIFS ILLLIFSLSS TAMSLEDEQE NMEERAEIDF SGIPEDIIKQ IKETNAKPPA
RFDPAAFEKS DD
