ID   NDB11_TITSE             Reviewed;          13 AA.
AC   Q9TWR4;
DT   01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   29-SEP-2021, entry version 33.
DE   RecName: Full=Bradykinin-potentiating peptide T {ECO:0000303|PubMed:8212046};
DE            Short=BPP-T {ECO:0000303|PubMed:8212046};
DE   AltName: Full=Non-disulfide-bridged peptide 1.1 {ECO:0000303|PubMed:24184590, ECO:0000303|PubMed:8212046};
DE            Short=NDBP-1.1 {ECO:0000303|PubMed:24184590, ECO:0000303|PubMed:8212046};
DE   AltName: Full=Ts10 {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, FUNCTION, AND SUBCELLULAR LOCATION.
RC   TISSUE=Venom;
RX   PubMed=8212046; DOI=10.1016/0041-0101(93)90253-f;
RA   Ferreira L.A.F., Alves E.W., Henriques O.B.;
RT   "Peptide T, a novel bradykinin potentiator isolated from Tityus serrulatus
RT   scorpion venom.";
RL   Toxicon 31:941-947(1993).
RN   [2]
RP   NOMENCLATURE.
RX   PubMed=16036557; DOI=10.1080/15216540500058899;
RA   Zeng X.C., Corzo G., Hahin R.;
RT   "Scorpion venom peptides without disulfide bridges.";
RL   IUBMB Life 57:13-21(2005).
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).
RN   [4]
RP   NOMENCLATURE.
RX   PubMed=24184590; DOI=10.1016/j.peptides.2013.10.021;
RA   Almaaytah A., Albalas Q.;
RT   "Scorpion venom peptides with no disulfide bridges: a review.";
RL   Peptides 51:35-45(2014).
CC   -!- FUNCTION: Potentiates the contractile activity of bradykinin on the
CC       isolated guinea-pig ileum. Inhibits the hydrolysis of bradykinin by
CC       angiotensin-converting enzyme (ACE) and also inhibits the conversion of
CC       angiotensin I to angiotensin II by kininase II from guinea-pig ileum
CC       tissue. Also increases the depressor effect of bradykinin on arterial
CC       blood pressure in the anaesthetized rat. {ECO:0000269|PubMed:8212046}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:8212046}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the non-disulfide-bridged peptide (NDBP)
CC       superfamily. Scorpion BPP (group 1) family. {ECO:0000305}.
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DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0008191; F:metalloendopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR   GO; GO:0008217; P:regulation of blood pressure; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Hypotensive agent; Metalloenzyme inhibitor;
KW   Metalloprotease inhibitor; Protease inhibitor; Secreted.
FT   PEPTIDE         1..13
FT                   /note="Bradykinin-potentiating peptide T"
FT                   /id="PRO_0000343196"
SQ   SEQUENCE   13 AA;  1604 MW;  35770B0644FC02D7 CRC64;
     KKDGYPVEYD RAY