SLA_CRODU
ID SLA_CRODU Reviewed; 158 AA.
AC O93426;
DT 15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 25-MAY-2022, entry version 90.
DE RecName: Full=Snaclec convulxin subunit alpha;
DE Short=CVX-alpha;
DE Flags: Precursor;
OS Crotalus durissus terrificus (South American rattlesnake).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Crotalus.
OX NCBI_TaxID=8732;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 24-48; 61-68; 108-120;
RP 139-145 AND 149-153.
RC TISSUE=Venom, and Venom gland;
RX PubMed=9657980; DOI=10.1042/bj3330389;
RA Leduc M., Bon C.;
RT "Cloning of subunits of convulxin, a collagen-like platelet-aggregating
RT protein from Crotalus durissus terrificus venom.";
RL Biochem. J. 333:389-393(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Venom gland;
RA Radis-Baptista G., Camargo A.C.M., Yamane T.;
RL Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PROTEIN SEQUENCE OF 24-43, AND FUNCTION.
RC TISSUE=Venom;
RX PubMed=9153205; DOI=10.1074/jbc.272.21.13576;
RA Polgar J., Clemetson J.M., Kehrel B.E., Wiedemann M., Magnenat E.M.,
RA Wells T.N., Clemetson K.J.;
RT "Platelet activation and signal transduction by convulxin, a C-type lectin
RT from Crotalus durissus terrificus (tropical rattlesnake) venom via the
RT p62/GPVI collagen receptor.";
RL J. Biol. Chem. 272:13576-13583(1997).
RN [4]
RP FUNCTION.
RX PubMed=16102113; DOI=10.1111/j.1538-7836.2005.01481.x;
RA Lu Q., Clemetson J.M., Clemetson K.J.;
RT "Translocation of GPIb and Fc receptor gamma-chain to cytoskeleton in
RT mucetin-activated platelets.";
RL J. Thromb. Haemost. 3:2065-2076(2005).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 24-158.
RX PubMed=14521935; DOI=10.1016/j.bbrc.2003.09.032;
RA Murakami M.T., Zela S.P., Gava L.M., Michelan-Duarte S., Cintra A.C.O.,
RA Arni R.K.;
RT "Crystal structure of the platelet activator convulxin, a disulfide-linked
RT alpha4beta4 cyclic tetramer from the venom of Crotalus durissus
RT terrificus.";
RL Biochem. Biophys. Res. Commun. 310:478-482(2003).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 26-158.
RX PubMed=14684891; DOI=10.1107/s0907444903021620;
RA Batuwangala T., Leduc M., Gibbins J.M., Bon C., Jones E.Y.;
RT "Structure of the snake-venom toxin convulxin.";
RL Acta Crystallogr. D 60:46-53(2004).
CC -!- FUNCTION: Snake venom lectin that activates platelets by binding to the
CC platelet collagen receptor glycoprotein VI (GP6) (PubMed:9153205). The
CC indirect activation of integrin alpha-IIb/beta-3 (ITGA2B/ITGB3) also
CC induced by the toxin is upstream the cytoskeletal translocation of
CC GPIb, FcRgamma (FCER1G) and 14-3-3zeta (YWHAZ)(PubMed:16102113).
CC {ECO:0000269|PubMed:16102113, ECO:0000269|PubMed:9153205}.
CC -!- SUBUNIT: Tetramer of heterodimers of alpha and beta subunits
CC (alphabeta)(4); disulfide-linked.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- MISCELLANEOUS: Does not act by binding to GPIb.
CC {ECO:0000305|PubMed:9153205}.
CC -!- SIMILARITY: Belongs to the snaclec family. {ECO:0000305}.
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DR EMBL; Y16348; CAA76181.1; -; mRNA.
DR EMBL; AF541882; AAQ11363.1; -; mRNA.
DR PDB; 1UMR; X-ray; 2.40 A; A/B=24-158.
DR PDB; 1UOS; X-ray; 2.70 A; A/C=24-158.
DR PDBsum; 1UMR; -.
DR PDBsum; 1UOS; -.
DR AlphaFoldDB; O93426; -.
DR SMR; O93426; -.
DR PRIDE; O93426; -.
DR EvolutionaryTrace; O93426; -.
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 3D-structure; Direct protein sequencing; Disulfide bond;
KW Hemostasis impairing toxin; Platelet aggregation activating toxin;
KW Secreted; Signal; Toxin.
FT SIGNAL 1..23
FT /evidence="ECO:0000269|PubMed:9153205,
FT ECO:0000269|PubMed:9657980"
FT CHAIN 24..158
FT /note="Snaclec convulxin subunit alpha"
FT /id="PRO_0000017528"
FT DOMAIN 34..158
FT /note="C-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 27..38
FT DISULFID 55..152
FT DISULFID 104
FT /note="Interchain (with C-100 in subunit beta)"
FT DISULFID 127..144
FT DISULFID 158
FT /note="Interchain (with C-26 in subunit beta)"
FT STRAND 32..34
FT /evidence="ECO:0007829|PDB:1UMR"
FT STRAND 37..46
FT /evidence="ECO:0007829|PDB:1UMR"
FT HELIX 48..58
FT /evidence="ECO:0007829|PDB:1UMR"
FT HELIX 70..83
FT /evidence="ECO:0007829|PDB:1UMR"
FT STRAND 90..92
FT /evidence="ECO:0007829|PDB:1UMR"
FT STRAND 94..97
FT /evidence="ECO:0007829|PDB:1UMR"
FT STRAND 100..104
FT /evidence="ECO:0007829|PDB:1UMR"
FT HELIX 121..123
FT /evidence="ECO:0007829|PDB:1UMR"
FT STRAND 127..131
FT /evidence="ECO:0007829|PDB:1UMR"
FT HELIX 132..134
FT /evidence="ECO:0007829|PDB:1UMR"
FT STRAND 138..142
FT /evidence="ECO:0007829|PDB:1UMR"
FT STRAND 148..154
FT /evidence="ECO:0007829|PDB:1UMR"
SQ SEQUENCE 158 AA; 18141 MW; 949F9C6D673E2318 CRC64;
MGRFIFVSFG LLVLFLSLSG TGAGLHCPSD WYYYDQHCYR IFNEEMNWED AEWFCTKQAK
GAHLVSIKSA KEADFVAWMV TQNIEESFSH VSIGLRVQNK EKQCSTKWSD GSSVSYDNLL
DLYITKCSLL KKETGFRKWF VASCIGKIPF VCKFPPQC
