ID   SLA_TRIPP               Reviewed;         133 AA.
AC   P0DJL2;
DT   29-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2013, sequence version 1.
DT   25-MAY-2022, entry version 21.
DE   RecName: Full=Snaclec purpureotin subunit alpha;
OS   Trimeresurus purpureomaculatus (Mangrove pit viper) (Cryptelytrops
OS   purpureomaculatus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Crotalinae; Trimeresurus.
OX   NCBI_TaxID=101163;
RN   [1]
RP   PROTEIN SEQUENCE, FUNCTION, AND SUBUNIT.
RC   TISSUE=Venom;
RX   PubMed=15019836; DOI=10.1016/j.abb.2004.01.015;
RA   Li X., Zheng L., Kong C., Kolatkar P.R., Chung M.C.;
RT   "Purpureotin: a novel di-dimeric C-type lectin-like protein from
RT   Trimeresurus purpureomaculatus venom is stabilized by noncovalent
RT   interactions.";
RL   Arch. Biochem. Biophys. 424:53-62(2004).
CC   -!- FUNCTION: Snaclec that induces platelet aggregation without any
CC       cofactor in a dose-dependent manner. Its platelet aggregation effect is
CC       blocked by echicetin, suggesting it is a GPIb-binding protein which
CC       binds to the same or a closely related GPIb site on platelets as
CC       echicetin. {ECO:0000269|PubMed:15019836}.
CC   -!- SUBUNIT: Homodimer (non-covalently linked) of heterodimer of alpha and
CC       beta subunits (disulfide-linked). {ECO:0000269|PubMed:15019836}.
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   AlphaFoldDB; P0DJL2; -.
DR   SMR; P0DJL2; -.
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.
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; IPR018378; C-type_lectin_CS.
DR   InterPro; IPR016187; CTDL_fold.
DR   Pfam; PF00059; Lectin_C; 1.
DR   SMART; SM00034; CLECT; 1.
DR   SUPFAM; SSF56436; SSF56436; 1.
DR   PROSITE; PS00615; C_TYPE_LECTIN_1; 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..133
FT                   /note="Snaclec purpureotin subunit alpha"
FT                   /id="PRO_0000422428"
FT   DOMAIN          9..128
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..127
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   DISULFID        79
FT                   /note="Interchain (with C-75 in subunit beta)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   DISULFID        102..119
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
SQ   SEQUENCE   133 AA;  15613 MW;  383A6C14DB3DC4AE CRC64;
     DCPSDWSSFK QYCYQIIKQL KTWEDAERFC LDQMKGAHLV SIESYREAVF VAELLSENVK
     TTKYHVWIGL SVQNKGQQCS SEWSDGSTVS YENLVKPNPK KCFVLKKESE FRTWSNVYCE
     QKHIFMCKFL GSR