ID   CRVP_BOTCO              Reviewed;          15 AA.
AC   P0DMG5;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   23-FEB-2022, entry version 10.
DE   RecName: Full=Cysteine-rich venom protein Bco13;
DE   Flags: Fragment;
OS   Bothrops cotiara (Cotiara) (Rhinocerophis cotiara).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Crotalinae; Bothrops.
OX   NCBI_TaxID=8727;
RN   [1]
RP   PROTEIN SEQUENCE.
RC   TISSUE=Venom;
RX   PubMed=18760386; DOI=10.1016/j.jprot.2008.07.007;
RA   Tashima A.K., Sanz L., Camargo A.C., Serrano S.M., Calvete J.J.;
RT   "Snake venomics of the Brazilian pitvipers Bothrops cotiara and Bothrops
RT   fonsecai. Identification of taxonomy markers.";
RL   J. Proteomics 71:473-485(2008).
CC   -!- FUNCTION: Weakly blocks contraction of smooth muscle elicited by high
CC       potassium-induced depolarization, but does not block caffeine-
CC       stimulated contraction. May target voltage-gated calcium channels on
CC       smooth muscle (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC   -!- PTM: Contains 8 disulfide bonds. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the CRISP family. {ECO:0000305}.
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DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005246; F:calcium channel regulator activity; IEA:UniProtKB-KW.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Calcium channel impairing toxin; Direct protein sequencing; Disulfide bond;
KW   Ion channel impairing toxin; Neurotoxin; Secreted; Toxin.
FT   CHAIN           1..>15
FT                   /note="Cysteine-rich venom protein Bco13"
FT                   /id="PRO_0000428805"
FT   NON_TER         15
SQ   SEQUENCE   15 AA;  1734 MW;  8C87D005E932DFAA CRC64;
     SVDFDSESPR KPEIQ