CRVP_BOTFO
ID CRVP_BOTFO Reviewed; 15 AA.
AC P0DMG6;
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 Bfon12;
DE Short=CRVP;
DE AltName: Full=Cysteine-rich secretory protein;
DE Short=CRISP;
DE Flags: Fragment;
OS Bothrops fonsecai (Fonseca's lancehead) (Rhinocerophis fonsecai).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Bothrops.
OX NCBI_TaxID=157549;
RN [1]
RP PROTEIN SEQUENCE, AND IDENTIFICATION BY MASS SPECTROMETRY.
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 Bfon12"
FT /id="PRO_0000428806"
FT NON_TER 15
SQ SEQUENCE 15 AA; 1734 MW; 8C87D005E932DFAA CRC64;
SVDFDSESPR KPEIQ