ID   SL1B_BOTJA              Reviewed;         123 AA.
AC   Q9PSM5; Q9PRQ7;
DT   25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   25-MAY-2022, entry version 66.
DE   RecName: Full=Snaclec GPIB-binding protein subunit beta;
DE            Short=GPIb-BP subunit beta;
OS   Bothrops jararaca (Jararaca) (Bothrops jajaraca).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Crotalinae; Bothrops.
OX   NCBI_TaxID=8724;
RN   [1]
RP   PROTEIN SEQUENCE, AND GPIB-BINDING SITE.
RC   TISSUE=Venom;
RX   PubMed=8631868; DOI=10.1074/jbc.271.18.10635;
RA   Kawasaki T., Fujimura Y., Usami Y., Suzuki M., Miura S., Sakurai Y.,
RA   Makita K., Taniuchi Y., Hirano K., Titani K.;
RT   "Complete amino acid sequence and identification of the platelet
RT   glycoprotein Ib-binding site of jararaca GPIb-BP, a snake venom protein
RT   isolated from Bothrops jararaca.";
RL   J. Biol. Chem. 271:10635-10639(1996).
RN   [2]
RP   PROTEIN SEQUENCE OF 1-33, FUNCTION, AND SUBUNIT.
RC   TISSUE=Venom;
RX   PubMed=8585016;
RA   Fujimura Y., Ikeda Y., Miura S., Yoshida E., Shima H., Nishida S.,
RA   Suzuki M., Titani K., Taniuchi Y., Kawasaki T.;
RT   "Isolation and characterization of jararaca GPIb-BP, a snake venom
RT   antagonist specific to platelet glycoprotein Ib.";
RL   Thromb. Haemost. 74:743-750(1995).
CC   -!- FUNCTION: Binds to platelet GPIb (subunit alpha) (GP1BA) and functions
CC       as a receptor blocker for vWF binding to GPIb. The platelet GPIb-
CC       binding site resides on the GPIB-BP subunit beta and not on the alpha
CC       subunit. At a final concentration of 104 nM totally abolishes vWF-
CC       dependent shear-induced platelet aggregation (SIPA) at a high shear
CC       stress, but had no effect on SIPA at a low shear stress.
CC       {ECO:0000269|PubMed:8585016}.
CC   -!- SUBUNIT: Heterodimer of subunits alpha and beta; disulfide-linked.
CC       {ECO:0000269|PubMed:8585016}.
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; Q9PSM5; -.
DR   SMR; Q9PSM5; -.
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 inhibiting toxin; Secreted; Toxin.
FT   CHAIN           1..123
FT                   /note="Snaclec GPIB-binding protein subunit beta"
FT                   /id="PRO_0000355255"
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-88 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;  14298 MW;  18B6A1ADF845A00B CRC64;
     DCPSDWSPYG GHCYKLFKQR MNWADAENLC AQQRKESHLV SFHSSEEVDF LVLLTFPILG
     PDLYWTGLSN IWNGCSFEWS DGTKVNYNAW ASESECVASK TTDNQWWSFP CTRLQYFVCE
     FQA