ID   SL2_BITAR               Reviewed;          12 AA.
AC   P0C8I8;
DT   25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT   25-NOV-2008, sequence version 1.
DT   26-FEB-2020, entry version 22.
DE   RecName: Full=Snaclec bitiscetin-2;
DE   Flags: Fragment;
OS   Bitis arietans (African puff adder).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Viperinae; Bitis.
OX   NCBI_TaxID=8692;
RN   [1]
RP   PROTEIN SEQUENCE, AND FUNCTION.
RC   TISSUE=Venom;
RX   PubMed=16839359; DOI=10.1111/j.1538-7836.2006.01994.x;
RA   Obert B., Romijn R.A., Houllier A., Huizinga E.G., Girma J.P.;
RT   "Characterization of bitiscetin-2, a second form of bitiscetin from the
RT   venom of Bitis arietans: comparison of its binding site with the collagen-
RT   binding site on the von Willebrand factor A3-domain.";
RL   J. Thromb. Haemost. 4:1596-1601(2006).
RN   [2]
RP   FUNCTION.
RC   TISSUE=Venom;
RX   PubMed=10068669;
RA   Obert B., Houllier A., Meyer D., Girma J.P.;
RT   "Conformational changes in the A3 domain of von Willebrand factor modulate
RT   the interaction of the A1 domain with platelet glycoprotein Ib.";
RL   Blood 93:1959-1968(1999).
RN   [3]
RP   FUNCTION, AND SUBUNIT.
RC   TISSUE=Venom;
RX   PubMed=12069583; DOI=10.1021/bi020004b;
RA   Matsui T., Hamako J., Matsushita T., Nakayama T., Fujimura Y., Titani K.;
RT   "Binding site on human von Willebrand factor of bitiscetin, a snake venom-
RT   derived platelet aggregation inducer.";
RL   Biochemistry 41:7939-7946(2002).
CC   -!- FUNCTION: Snaclec that binds to von Willebrand factor (VWF) and induces
CC       its interaction with GPIbalpha (GP1BA), resulting in platelet
CC       aggregation. In contrary to bitiscetin, it does not bind to the A1
CC       domain. Instead, it interacts with the collagen-binding A3 domain of
CC       vWF. Also interferes with the binding of vWF to collagen.
CC       {ECO:0000269|PubMed:10068669, ECO:0000269|PubMed:12069583,
CC       ECO:0000269|PubMed:16839359}.
CC   -!- SUBUNIT: Dimer. {ECO:0000269|PubMed:12069583}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC   -!- SIMILARITY: Belongs to the snaclec family. {ECO:0000305}.
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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   Direct protein sequencing; Hemostasis impairing toxin;
KW   Platelet aggregation activating toxin; Secreted; Toxin.
FT   CHAIN           1..>12
FT                   /note="Snaclec bitiscetin-2"
FT                   /id="PRO_0000355242"
FT   DOMAIN          11..>12
FT                   /note="C-type lectin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   NON_TER         12
SQ   SEQUENCE   12 AA;  1294 MW;  4F6CDBE0EEAAB767 CRC64;
     DEGCLPDDSS RT