HKS_HELSS
ID HKS_HELSS Reviewed; 10 AA.
AC P86446;
DT 23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 23-MAR-2010, sequence version 1.
DT 26-FEB-2020, entry version 14.
DE RecName: Full=Helokinestatin-1;
OS Heloderma suspectum suspectum (Reticulate Gila monster).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Anguimorpha; Neoanguimorpha; Helodermatidae; Heloderma.
OX NCBI_TaxID=709964;
RN [1] {ECO:0000305}
RP PROTEIN SEQUENCE, FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP MASS SPECTROMETRY.
RC TISSUE=Venom {ECO:0000269|PubMed:18078686};
RX PubMed=18078686; DOI=10.1016/j.peptides.2007.10.025;
RA Kwok H.F., Chen T., O'Rourke M., Ivanyi C., Hirst D., Shaw C.;
RT "Helokinestatin: a new bradykinin B2 receptor antagonist decapeptide from
RT lizard venom.";
RL Peptides 29:65-72(2008).
CC -!- FUNCTION: Helokinestatin antagonizes the vasodilatory actions of
CC bradykinin at the B2 bradykinin receptor (BDKRB2) in a dose-dependent
CC manner. {ECO:0000269|PubMed:18078686}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:18078686}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000269|PubMed:18078686}.
CC -!- MASS SPECTROMETRY: Mass=1122.62; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:18078686};
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DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
PE 1: Evidence at protein level;
KW Bradykinin receptor impairing toxin; Direct protein sequencing;
KW G-protein coupled receptor impairing toxin; Secreted; Toxin; Vasoactive.
FT PEPTIDE 1..10
FT /note="Helokinestatin-1"
FT /id="PRO_0000392452"
FT UNSURE 7
FT /note="L or I"
FT /evidence="ECO:0000269|PubMed:18078686"
SQ SEQUENCE 10 AA; 1123 MW; 3150E9C73776CB47 CRC64;
GPPYQPLVPR