SLTB_PROMU
ID SLTB_PROMU Reviewed; 144 AA.
AC Q5FZI5;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 25-MAY-2022, entry version 51.
DE RecName: Full=Snaclec trimecetin subunit beta;
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 24-48,
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; AY871786; AAW69916.1; -; Genomic_DNA.
DR AlphaFoldDB; Q5FZI5; -.
DR SMR; Q5FZI5; -.
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..144
FT /note="Snaclec trimecetin subunit beta"
FT /id="PRO_0000355300"
FT DOMAIN 32..143
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..142
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 98
FT /note="Interchain (with C-102 in subunit alpha)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 119..134
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
SQ SEQUENCE 144 AA; 16635 MW; 778BF08645FCFCEC CRC64;
MGRFIFVSFG LLVVFLSLSG TAADCPSDWS SFRRYCYQVF QQKMNWEDAE KFCTQQHRGS
HLVSFHSSEE VDFVVSKTLP ILKANFVWMG LSNVWNECAK EWSDGTKLDY KAWSGQSDCI
TSKTTDNQWL SMDCSSKRYV VCKF