ID   SLA_MACLB               Reviewed;          42 AA.
AC   P84038;
DT   19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 62.
DE   RecName: Full=Snaclec lebecetin subunit alpha;
DE   Flags: Fragment;
OS   Macrovipera lebetina (Levantine viper) (Vipera lebetina).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Viperinae; Macrovipera.
OX   NCBI_TaxID=8709;
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, FUNCTION, COFACTOR, SUBUNIT, TISSUE SPECIFICITY,
RP   SUBCELLULAR LOCATION, GLYCOSYLATION, AND MASS SPECTROMETRY.
RC   TISSUE=Venom {ECO:0000269|PubMed:14499586};
RX   PubMed=14499586; DOI=10.1016/s1570-9639(03)00232-2;
RA   Sarray S., Srairi N., Hatmi M., Luis J., Louzir H., Regaya I., Slema H.,
RA   Marvaldi J., El Ayeb M., Marrakchi N.;
RT   "Lebecetin, a potent antiplatelet C-type lectin from Macrovipera lebetina
RT   venom.";
RL   Biochim. Biophys. Acta 1651:30-40(2003).
CC   -!- FUNCTION: Binds to the platelet GPIb/IX/V receptor system and inhibits
CC       ristocetin-induced platelet aggregation in human platelet-rich plasma.
CC       Strongly inhibits platelet aggregation induced by ADP, calcium
CC       ionophore, thrombin and collagen. Does not inhibit U46619-induced
CC       platelet aggregation. {ECO:0000269|PubMed:14499586}.
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000269|PubMed:14499586};
CC   -!- SUBUNIT: Heterodimer of subunits alpha and beta; disulfide-linked.
CC       {ECO:0000269|PubMed:14499586}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:14499586}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000269|PubMed:14499586}.
CC   -!- PTM: Glycosylated. {ECO:0000269|PubMed:14499586}.
CC   -!- MASS SPECTROMETRY: Mass=15016.7; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:14499586};
CC   -!- SIMILARITY: Belongs to the snaclec family. {ECO:0000305}.
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DR   AlphaFoldDB; P84038; -.
DR   SMR; P84038; -.
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; IPR016186; C-type_lectin-like/link_sf.
DR   InterPro; IPR016187; CTDL_fold.
DR   SUPFAM; SSF56436; SSF56436; 1.
PE   1: Evidence at protein level;
KW   Calcium; Cell adhesion impairing toxin; Direct protein sequencing;
KW   Disulfide bond; Glycoprotein; Hemostasis impairing toxin;
KW   Platelet aggregation inhibiting toxin; Secreted; Toxin.
FT   CHAIN           1..>42
FT                   /note="Snaclec lebecetin subunit alpha"
FT                   /id="PRO_0000046703"
FT   DOMAIN          1..>42
FT                   /note="C-type lectin"
FT                   /evidence="ECO:0000250|UniProtKB:P23806,
FT                   ECO:0000255|PROSITE-ProRule:PRU00040"
FT   DISULFID        4..15
FT                   /evidence="ECO:0000250|UniProtKB:P23806,
FT                   ECO:0000255|PROSITE-ProRule:PRU00040"
FT   NON_TER         42
FT                   /evidence="ECO:0000303|PubMed:14499586"
SQ   SEQUENCE   42 AA;  4852 MW;  78C419D0F92280A2 CRC64;
     DQDCLPGWSS HEGHCYKVFN LDKTWEDAEK FCTEQPSNGH LV