SLEA_BOTJA
ID SLEA_BOTJA Reviewed; 133 AA.
AC P22029;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 2.
DT 25-MAY-2022, entry version 107.
DE RecName: Full=Snaclec botrocetin subunit alpha;
DE AltName: Full=Platelet coagglutinin;
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 DISULFIDE BONDS.
RC TISSUE=Venom;
RX PubMed=8430107; DOI=10.1073/pnas.90.3.928;
RA Usami Y., Fujimura Y., Suzuki M., Ozeki Y., Nishio K., Fukui H., Titani K.;
RT "Primary structure of two-chain botrocetin, a von Willebrand factor
RT modulator purified from the venom of Bothrops jararaca.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:928-932(1993).
RN [2]
RP PROTEIN SEQUENCE OF 1-40.
RC TISSUE=Venom;
RX PubMed=1993206; DOI=10.1021/bi00221a032;
RA Fujimura Y., Titani K., Usami Y., Suzuki M., Oyama R., Matsui T., Fukui H.,
RA Sugimoto M., Ruggeri Z.M.;
RT "Isolation and chemical characterization of two structurally and
RT functionally distinct forms of botrocetin, the platelet coagglutinin
RT isolated from the venom of Bothrops jararaca.";
RL Biochemistry 30:1957-1964(1991).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS), AND DISULFIDE BOND.
RX PubMed=11148028; DOI=10.1021/bi0021737;
RA Sen U., Vasudevan S., Subbarao G., McClintock R.A., Celikel R.,
RA Ruggeri Z.M., Varughese K.I.;
RT "Crystal structure of the von Willebrand factor modulator botrocetin.";
RL Biochemistry 40:345-352(2001).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS), AND DISULFIDE BOND.
RX PubMed=12121649; DOI=10.1016/s0969-2126(02)00787-6;
RA Fukuda K., Doggett T.A., Bankston L.A., Cruz M.A., Diacovo T.G.,
RA Liddington R.C.;
RT "Structural basis of von Willebrand factor activation by the snake toxin
RT botrocetin.";
RL Structure 10:943-950(2002).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS), AND DISULFIDE BOND.
RX PubMed=15665869; DOI=10.1038/nsmb892;
RA Fukuda K., Doggett T., Laurenzi I.J., Liddington R.C., Diacovo T.G.;
RT "The snake venom protein botrocetin acts as a biological brace to promote
RT dysfunctional platelet aggregation.";
RL Nat. Struct. Mol. Biol. 12:152-159(2005).
CC -!- FUNCTION: Snaclec that binds to von Willebrand factor (VWF) and induces
CC its interaction with GPIbalpha (GP1BA) (via the vWF A1 domain),
CC resulting in platelet aggregation.
CC -!- SUBUNIT: Heterodimer of subunits alpha and beta; disulfide-linked.
CC Botrocetin and vWF form a soluble complex.
CC {ECO:0000269|PubMed:11148028, ECO:0000269|PubMed:12121649,
CC ECO:0000269|PubMed:15665869, ECO:0000269|PubMed:8430107}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- BIOTECHNOLOGY: Is a standard reagent for testing vWF/platelet
CC interactions and detection of the defects in von Willebrand disease and
CC in GPIb-related disorders such as Bernard-Soulier syndrome.
CC -!- MISCELLANEOUS: There are two distinct forms of the vWF-dependent
CC platelet coagglutinin. The dimeric form (snaclec) is 34-fold more
CC active than the metalloprotease botrocetin in promoting vWF binding to
CC platelets (PubMed:1993206). {ECO:0000305|PubMed:1993206}.
CC -!- SIMILARITY: Belongs to the snaclec family. {ECO:0000305}.
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DR PIR; A47267; A47267.
DR PDB; 1FVU; X-ray; 1.80 A; A/C=1-133.
DR PDB; 1IJK; X-ray; 2.60 A; B=1-133.
DR PDB; 1U0N; X-ray; 2.95 A; B=1-133.
DR PDB; 1U0O; X-ray; 2.70 A; A=1-133.
DR PDBsum; 1FVU; -.
DR PDBsum; 1IJK; -.
DR PDBsum; 1U0N; -.
DR PDBsum; 1U0O; -.
DR AlphaFoldDB; P22029; -.
DR SMR; P22029; -.
DR EvolutionaryTrace; P22029; -.
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 3D-structure; Direct protein sequencing; Disulfide bond;
KW Hemostasis impairing toxin; Platelet aggregation activating toxin;
KW Secreted; Toxin.
FT CHAIN 1..133
FT /note="Snaclec botrocetin subunit alpha"
FT /id="PRO_0000046697"
FT DOMAIN 9..129
FT /note="C-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 2..13
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040,
FT ECO:0000269|PubMed:8430107"
FT DISULFID 30..128
FT DISULFID 80
FT /note="Interchain (with C-75 in beta chain)"
FT DISULFID 103..120
FT STRAND 7..9
FT /evidence="ECO:0007829|PDB:1FVU"
FT STRAND 12..21
FT /evidence="ECO:0007829|PDB:1FVU"
FT HELIX 23..33
FT /evidence="ECO:0007829|PDB:1FVU"
FT STRAND 44..46
FT /evidence="ECO:0007829|PDB:1U0N"
FT HELIX 48..59
FT /evidence="ECO:0007829|PDB:1FVU"
FT STRAND 66..73
FT /evidence="ECO:0007829|PDB:1FVU"
FT STRAND 76..80
FT /evidence="ECO:0007829|PDB:1FVU"
FT STRAND 85..87
FT /evidence="ECO:0007829|PDB:1IJK"
FT HELIX 97..99
FT /evidence="ECO:0007829|PDB:1FVU"
FT STRAND 103..107
FT /evidence="ECO:0007829|PDB:1FVU"
FT TURN 108..111
FT /evidence="ECO:0007829|PDB:1FVU"
FT STRAND 114..118
FT /evidence="ECO:0007829|PDB:1FVU"
FT STRAND 124..130
FT /evidence="ECO:0007829|PDB:1FVU"
SQ SEQUENCE 133 AA; 15215 MW; E4CF4502946AC74B CRC64;
DCPSGWSSYE GNCYKFFQQK MNWADAERFC SEQAKGGHLV SIKIYSKEKD FVGDLVTKNI
QSSDLYAWIG LRVENKEKQC SSEWSDGSSV SYENVVERTV KKCFALEKDL GFVLWINLYC
AQKNPFVCKS PPP
