SLB_BOTIN
ID SLB_BOTIN Reviewed; 127 AA.
AC P0C930;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 1.
DT 25-MAY-2022, entry version 32.
DE RecName: Full=Snaclec bothroinsularin subunit beta;
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; P0C930; -.
DR SMR; P0C930; -.
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; 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 Blood coagulation cascade inhibiting toxin; Direct protein sequencing;
KW Disulfide bond; Hemostasis impairing toxin;
KW Platelet aggregation inhibiting toxin; Secreted; Toxin.
FT CHAIN 1..127
FT /note="Snaclec bothroinsularin subunit beta"
FT /id="PRO_0000370638"
FT DOMAIN 9..124
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..123
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 75
FT /note="Interchain (with C-79 in alpha chain)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 100..115
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
SQ SEQUENCE 127 AA; 14874 MW; 86CF482BCF65263F CRC64;
DCPPDWSSYE GSCYRVFEQK MNWEDAEKFC TQQQTGGHLV SFQSSEEADF VVSLTSPILR
DSFVWTGLSD VWKGCRFEWS DGSDLSYKDN YQFVFSEYEC VASKTKNNKW RIIPCTKLEY
FVCEFQA