ID   SLA_BOTIN               Reviewed;         132 AA.
AC   P0C929;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-MAY-2009, sequence version 1.
DT   25-MAY-2022, entry version 33.
DE   RecName: Full=Snaclec bothroinsularin subunit alpha;
DE            Short=BIN;
OS   Bothrops insularis (Golden lancehead) (Lachesis insularis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Crotalinae; Bothrops.
OX   NCBI_TaxID=8723;
RN   [1]
RP   PROTEIN SEQUENCE, FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, AND TISSUE
RP   SPECIFICITY.
RC   TISSUE=Venom;
RX   PubMed=18221976; DOI=10.1016/j.toxicon.2007.11.026;
RA   Oliveira-Carvalho A.L., Guimaraes P.R., Abreu P.A., Dutra D.L.S.,
RA   Junqueira-de-Azevedo I.L.M., Rodrigues C.R., Ho P.L., Castro H.C.,
RA   Zingali R.B.;
RT   "Identification and characterization of a new member of snake venom
RT   thrombin inhibitors from Bothrops insularis using a proteomic approach.";
RL   Toxicon 51:659-671(2008).
CC   -!- FUNCTION: Thrombin and prothrombin (F2) inhibitor. The IC(50) of
CC       thrombin-induced platelet aggregation and fibrinocoagulation is 62 and
CC       35 nM, respectively. Its inhibitory activity is at least 10-fold lower
CC       than that observed for other thrombin inhibitors.
CC       {ECO:0000269|PubMed:18221976}.
CC   -!- SUBUNIT: Heterodimer of subunits alpha and beta; disulfide-linked.
CC       {ECO:0000269|PubMed:18221976}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:18221976}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000269|PubMed:18221976}.
CC   -!- SIMILARITY: Belongs to the snaclec family. {ECO:0000305}.
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DR   AlphaFoldDB; P0C929; -.
DR   SMR; P0C929; -.
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   Blood coagulation cascade inhibiting toxin; Direct protein sequencing;
KW   Disulfide bond; Hemostasis impairing toxin;
KW   Platelet aggregation inhibiting toxin; Secreted; Toxin.
FT   CHAIN           1..132
FT                   /note="Snaclec bothroinsularin subunit alpha"
FT                   /id="PRO_0000370637"
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 beta chain)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   DISULFID        102..119
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
SQ   SEQUENCE   132 AA;  15209 MW;  581DB6ECE54408A2 CRC64;
     DCPSDWSPYG QYCYKFFQQK MNWADAERFC SEQAKGGHLV SFQSDGETDF VVNLVTEKIQ
     SSDLYAWIGL RVQNKEKQCS SKWSDGSSVS YENVVGRTVK KCFALEKEQE FFVWINIYCG
     QQNPFVCKSP PP