ID   SLTA_PROMU              Reviewed;         156 AA.
AC   Q5FZI6;
DT   25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2005, sequence version 1.
DT   25-MAY-2022, entry version 54.
DE   RecName: Full=Snaclec trimecetin subunit alpha;
DE   Flags: Precursor;
OS   Protobothrops mucrosquamatus (Taiwan habu) (Trimeresurus mucrosquamatus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Crotalinae; Protobothrops.
OX   NCBI_TaxID=103944;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], PROTEIN SEQUENCE OF 24-43,
RP   FUNCTION, SUBUNIT, AND 3D-STRUCTURE MODELING.
RC   TISSUE=Venom, and Venom gland;
RX   PubMed=19931300; DOI=10.1016/j.toxicon.2009.11.009;
RA   Chen Y.S., Huang C.H., Chiou S.H.;
RT   "Characterization and molecular cloning of one novel C-type lectin from the
RT   venom of Taiwan habu (Trimeresurus mucrosquamatus).";
RL   Toxicon 55:762-772(2010).
RN   [2]
RP   PARTIAL PROTEIN SEQUENCE, FUNCTION, AND SUBUNIT.
RC   TISSUE=Venom;
RX   PubMed=8968958; DOI=10.1007/bf01886749;
RA   Chiou S.-H., Huang K.-F., Chow L.-P., Tsugita A., Wu S.-H.;
RT   "Isolation of a venom factor devoid of proteolytic activity from Taiwan
RT   habu (Trimeresurus mucrosquamatus): N-terminal sequence homology and no
RT   functional similarity to factors IX/X-binding proteins and botrocetin.";
RL   J. Protein Chem. 15:667-674(1996).
CC   -!- FUNCTION: Snaclec that induces platelet aggregation in either human
CC       platelet rich plasma (PRP) or washed platelet suspensions. It causes
CC       aggregation in a dose-dependent manner even in the absence of various
CC       platelet agonists such as ADP or von Willebrand factor (vWF).
CC       Interestingly, it does not induce aggregation in rabbit PRP. A
CC       monoclonal antibody against the platelet GPIb receptor blocks the
CC       aggregation induced by trimecetin, suggesting that it acts by binding
CC       to GPIb (GP1BA/GP1BB). {ECO:0000269|PubMed:19931300,
CC       ECO:0000269|PubMed:8968958}.
CC   -!- SUBUNIT: Heterodimer of subunits alpha and beta; disulfide-linked.
CC       {ECO:0000269|PubMed:19931300, ECO:0000269|PubMed:8968958}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC   -!- MISCELLANEOUS: Does not show affinity to coagulation factors IX and X
CC       in the presence of calcium ion. Also shows no inhibition on thrombin
CC       (PubMed:8968958). {ECO:0000305|PubMed:8968958}.
CC   -!- SIMILARITY: Belongs to the snaclec family. {ECO:0000305}.
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DR   EMBL; AY871785; AAW69915.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q5FZI6; -.
DR   SMR; Q5FZI6; -.
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; 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; Signal; Toxin.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000269|PubMed:19931300"
FT   CHAIN           24..156
FT                   /note="Snaclec trimecetin subunit alpha"
FT                   /id="PRO_0000355299"
FT   DOMAIN          32..151
FT                   /note="C-type lectin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   DISULFID        25..36
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   DISULFID        53..150
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   DISULFID        102
FT                   /note="Interchain (with C-98 in subunit beta)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   DISULFID        125..142
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
SQ   SEQUENCE   156 AA;  18255 MW;  2D35D822B3A0CDD1 CRC64;
     MGRFIFVSFG LLVVFLSLSG TGADCPSDWS SFRRYCYKPF KQLKTWEDAE RFCWEQVKGA
     HLVSIESSGE GDFVAQLLSE NIKTTKYHVW IGLSIQNKRQ QCRSIWSDGS SVSYENLVKP
     FSKKCFVLKK ESEFHKWFNI YCGERNLFMC KFLQPR