SLB_TRIPP
ID SLB_TRIPP Reviewed; 123 AA.
AC P0DJL3;
DT 29-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2013, sequence version 1.
DT 25-MAY-2022, entry version 22.
DE RecName: Full=Snaclec purpureotin subunit beta;
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; P0DJL3; -.
DR SMR; P0DJL3; -.
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; IPR016187; CTDL_fold.
DR Pfam; PF00059; Lectin_C; 1.
DR SMART; SM00034; CLECT; 1.
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..123
FT /note="Snaclec purpureotin subunit beta"
FT /id="PRO_0000422429"
FT DOMAIN 9..120
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..119
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 75
FT /note="Interchain (with C-79 in subunit alpha)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 96..111
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
SQ SEQUENCE 123 AA; 14498 MW; AF66C4AFD75CA547 CRC64;
DCPSDWSSYD LYCYKVFQQR MNWEDAEKFC RQQHTGSHLL SFHSSEEVDF VVSKTLPILK
ADFVWIGLTD VWSACRLQWS DGTELKYNAW TAESECIASK TTDNQWWTRS CSRTYPFVCK
LEV