SRTXB_ATRBI
ID SRTXB_ATRBI Reviewed; 21 AA.
AC P80163;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1993, sequence version 1.
DT 25-MAY-2022, entry version 70.
DE RecName: Full=Bibrotoxin;
DE Short=BTX;
OS Atractaspis bibronii (Bibron's mole viper) (Southern stiletto snake).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Lamprophiidae; Atractaspidinae; Atractaspis.
OX NCBI_TaxID=61304;
RN [1]
RP PROTEIN SEQUENCE, AND FUNCTION.
RC TISSUE=Venom;
RX PubMed=8416802; DOI=10.1016/0014-5793(93)81142-m;
RA Becker A., Dowdle E.B., Hechler U., Kauser K., Donner P., Schleuning W.-D.;
RT "Bibrotoxin, a novel member of the endothelin/sarafotoxin peptide family,
RT from the venom of the burrowing asp Atractaspis bibroni.";
RL FEBS Lett. 315:100-103(1993).
CC -!- FUNCTION: Vasoconstrictor activity. These toxins cause cardiac arrest
CC probably as a result of coronary vasospasm. May act by displaying
CC agonistic activities towards endothelin-1 and -2 receptors (EDNRA and
CC EDNRB). {ECO:0000269|PubMed:8416802}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- SIMILARITY: Belongs to the endothelin/sarafotoxin family.
CC {ECO:0000305}.
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DR PIR; S27039; S27039.
DR AlphaFoldDB; P80163; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR GO; GO:0019229; P:regulation of vasoconstriction; IEA:InterPro.
DR GO; GO:0042310; P:vasoconstriction; IEA:UniProtKB-KW.
DR InterPro; IPR019764; Endothelin_toxin_CS.
DR InterPro; IPR001928; Endothln-like_toxin.
DR Pfam; PF00322; Endothelin; 1.
DR SMART; SM00272; END; 1.
DR PROSITE; PS00270; ENDOTHELIN; 1.
PE 1: Evidence at protein level;
KW Cardiotoxin; Direct protein sequencing; Disulfide bond;
KW G-protein coupled receptor impairing toxin; Secreted; Toxin; Vasoactive;
KW Vasoconstrictor.
FT PEPTIDE 1..21
FT /note="Bibrotoxin"
FT /id="PRO_0000043645"
FT SITE 21
FT /note="Endothelin-receptor binding site"
FT /evidence="ECO:0000250"
FT DISULFID 1..15
FT /evidence="ECO:0000250"
FT DISULFID 3..11
FT /evidence="ECO:0000250"
SQ SEQUENCE 21 AA; 2511 MW; 83A5DFB81D036AE2 CRC64;
CSCADMTDKE CLYFCHQDVI W