ID   SLB_BOTAS               Reviewed;          62 AA.
AC   P0DJC9;
DT   25-JAN-2012, integrated into UniProtKB/Swiss-Prot.
DT   25-JAN-2012, sequence version 1.
DT   25-MAY-2022, entry version 27.
DE   RecName: Full=Snaclec aspercetin subunit beta;
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. Intramuscular and intravenous
CC       injections in mice induce a dose-dependent drop in platelet count
CC       (thrombocytopenia). Pretreatment by intravenous injection by this
CC       protein in mice potentiates the hemorrhagic lesion in the skin provoked
CC       by the metalloproteinase BaP1 intradermally injected. This result is
CC       not observed when both BaP1 and this protein are injected
CC       simultaneously. {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; P0DJC9; -.
DR   SMR; P0DJC9; -.
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 beta"
FT                   /id="PRO_0000415318"
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;  7164 MW;  592C2267E398DB39 CRC64;
     DCPSDWSSYE GHCYRVFKPP KDWADAERFC SQQAKGGHLV SIERFGREDF VSNLITKNLQ
     RG