SL1A_BOTJA
ID SL1A_BOTJA Reviewed; 142 AA.
AC Q9PSM6; Q9PRQ8;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 65.
DE RecName: Full=Snaclec GPIB-binding protein subunit alpha;
DE Short=GPIb-BP subunit alpha;
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 1-42, 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 -!- MISCELLANEOUS: Does not induce platelet aggregation or serotonin
CC release from platelets. {ECO:0000305|PubMed:8585016}.
CC -!- SIMILARITY: Belongs to the snaclec family. {ECO:0000305}.
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DR AlphaFoldDB; Q9PSM6; -.
DR SMR; Q9PSM6; -.
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..142
FT /note="Snaclec GPIB-binding protein subunit alpha"
FT /id="PRO_0000355254"
FT DOMAIN 13..137
FT /note="C-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 6..17
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 39..136
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 88
FT /note="Interchain (with C-75 in subunit alpha)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 111..128
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
SQ SEQUENCE 142 AA; 16720 MW; E28EFDEBEF922004 CRC64;
DTPFECPSDW STHRQYCYKF FQQKESWDDR SEYDAERFCS EQAKGGHLVS IESDEEADFV
AQLVAPNIGK SKYYVWIGLR IENKKQQCSS KWSDYSSVSY ENLVRGNVKK CFALEKKQGF
RKWVNIDCVE GNPFVCKFIR PR
