ID   SLA_BOTAS               Reviewed;          62 AA.
AC   P0DJC8;
DT   25-JAN-2012, integrated into UniProtKB/Swiss-Prot.
DT   25-JAN-2012, sequence version 1.
DT   25-MAY-2022, entry version 33.
DE   RecName: Full=Snaclec aspercetin subunit alpha;
DE   Flags: Fragment;
OS   Bothrops asper (Terciopelo).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Crotalinae; Bothrops.
OX   NCBI_TaxID=8722;
RN   [1]
RP   PROTEIN SEQUENCE, FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RC   TISSUE=Venom;
RX   PubMed=11341509;
RA   Rucavado A., Soto M., Kamiguti A.S., Theakston R.D., Fox J.W.,
RA   Escalante T., Gutierrez J.M.;
RT   "Characterization of aspercetin, a platelet aggregating component from the
RT   venom of the snake Bothrops asper which induces thrombocytopenia and
RT   potentiates metalloproteinase-induced hemorrhage.";
RL   Thromb. Haemost. 85:710-715(2001).
CC   -!- FUNCTION: Snaclec that binds to von Willebrand factor (VWF) and induces
CC       its interaction with GPIbalpha (GP1BA) (via the vWF A1 domain),
CC       resulting in platelet aggregation. Intravenous injection in mice
CC       induces a dose-dependent drop in platelet count (thrombocytopenia).
CC       Pretreatment by intravenous injection by this protein in mice
CC       potentiates the hemorrhagic lesion in the skin provoked by the
CC       metalloproteinase BaP1 intradermally injected. This result is not
CC       observed when both BaP1 and this protein are injected simultaneously.
CC       {ECO:0000269|PubMed:11341509}.
CC   -!- SUBUNIT: Heterodimer; disulfide-linked. {ECO:0000269|PubMed:11341509}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:11341509}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC   -!- SIMILARITY: Belongs to the snaclec family. {ECO:0000305}.
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DR   AlphaFoldDB; P0DJC8; -.
DR   SMR; P0DJC8; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.10.100.10; -; 1.
DR   InterPro; IPR001304; C-type_lectin-like.
DR   InterPro; IPR016186; C-type_lectin-like/link_sf.
DR   InterPro; IPR016187; CTDL_fold.
DR   SUPFAM; SSF56436; SSF56436; 1.
DR   PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Hemostasis impairing toxin;
KW   Platelet aggregation activating toxin; Secreted; Toxin.
FT   CHAIN           1..>62
FT                   /note="Snaclec aspercetin subunit alpha"
FT                   /id="PRO_0000415317"
FT   DOMAIN          9..>62
FT                   /note="C-type lectin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   DISULFID        2..13
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   DISULFID        30..?
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   UNSURE          2
FT                   /note="Assigned by comparison with orthologs"
FT   UNSURE          30
FT                   /note="Assigned by comparison with orthologs"
FT   NON_TER         62
SQ   SEQUENCE   62 AA;  7084 MW;  C1ADA87D39A81446 CRC64;
     DCPSGWSSYE GHCYRFFHPP KDWADAERFC TEQAKGGALV SIQRFGEEDF VSNLITKNLQ
     RG