ID   SLB_TRIAB               Reviewed;          12 AA.
AC   P0DJL1;
DT   29-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2013, sequence version 1.
DT   25-MAY-2022, entry version 15.
DE   RecName: Full=Snaclec alboluxin subunit beta;
DE   Flags: Fragment;
OS   Trimeresurus albolabris (White-lipped pit viper) (Cryptelytrops
OS   albolabris).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Crotalinae; Trimeresurus.
OX   NCBI_TaxID=8765;
RN   [1]
RP   PROTEIN SEQUENCE, FUNCTION, AND SUBUNIT.
RC   TISSUE=Venom;
RX   PubMed=12008953;
RA   Du X.-Y., Magnenat E., Wells T.N.C., Clemetson K.J.;
RT   "Alboluxin, a snake C-type lectin from Trimeresurus albolabris venom is a
RT   potent platelet agonist acting via GPIb and GPVI.";
RL   Thromb. Haemost. 87:692-698(2002).
CC   -!- FUNCTION: Potent platelet activator that aggregates platelets via both
CC       GPIb (GP1BA/GP1BB) and GPVI (GP6). Alboluxin induces a tyrosine
CC       phosphorylation profile in platelets that resembles those produced by
CC       collagen and convulxin, involving the time dependent tyrosine
CC       phosphorylation of Fc receptor gamma chain (FCGR1A), phospholipase
CC       Cgamma2 (PLCG2), LAT and p72SYK. Inhibition of alpha-IIb/beta-3 reduces
CC       the aggregation response to alboluxin, as well as tyrosine
CC       phosphorylation of platelet proteins, showing that activation of alpha-
CC       IIb/beta-3 and binding of fibrinogen are involved in alboluxin-induced
CC       platelet aggregation and it is not simply agglutination.
CC       {ECO:0000269|PubMed:12008953}.
CC   -!- SUBUNIT: Trimer of 3 heterodimers of alpha and beta subunits;
CC       disulfide-linked. {ECO:0000269|PubMed:12008953}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC   -!- PTM: The complex may be glycosylated. {ECO:0000269|PubMed:12008953}.
CC   -!- MISCELLANEOUS: May not activate platelet via the integrin alpha-2/beta-
CC       1, since antibodies against this integrin have no effect.
CC       {ECO:0000305|PubMed:12008953}.
CC   -!- SIMILARITY: Belongs to the snaclec family. {ECO:0000305}.
CC   -!- CAUTION: The subunit alpha may be blocked, since it was impossible to
CC       sequence. {ECO:0000305|PubMed:12008953}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR   GO; GO:0044218; C:other organism cell membrane; IDA:UniProtKB.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   GO; GO:0044478; P:envenomation resulting in positive regulation of platelet aggregation in another organism; IDA:UniProtKB.
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..>12
FT                   /note="Snaclec alboluxin subunit beta"
FT                   /id="PRO_0000422427"
FT   DOMAIN          11..>12
FT                   /note="C-type lectin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   DISULFID        4..?
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   NON_TER         12
SQ   SEQUENCE   12 AA;  1478 MW;  3872D449B57AB777 CRC64;
     NFSCPPDWYA YD