SLAB_PROFL
ID SLAB_PROFL Reviewed; 148 AA.
AC Q8AV98; Q9PRT1;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 25-MAY-2022, entry version 68.
DE RecName: Full=Snaclec flavocetin-A subunit beta;
DE Short=FL-A subunit beta;
DE Flags: Precursor;
OS Protobothrops flavoviridis (Habu) (Trimeresurus flavoviridis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Protobothrops.
OX NCBI_TaxID=88087;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 24-45; 46-53; 61-79;
RP 80-85; 86-102; 103-109; 114-125; 126-139 AND 140-145.
RC TISSUE=Venom, and Venom gland;
RX PubMed=10942790; DOI=10.1016/s0049-3848(00)00234-6;
RA Shin Y., Okuyama I., Hasegawa J., Morita T.;
RT "Molecular cloning of glycoprotein Ib-binding protein, flavocetin-A, which
RT inhibits platelet aggregation.";
RL Thromb. Res. 99:239-247(2000).
RN [2]
RP PROTEIN SEQUENCE OF 24-60, AND FUNCTION.
RC TISSUE=Venom;
RX PubMed=7599152; DOI=10.1016/0304-4165(95)00052-d;
RA Taniuchi Y., Kawasaki T., Fujimura Y., Suzuki M., Titani K., Sakai Y.,
RA Kaku S., Hisamichi N., Satoh N., Takenaka T.;
RT "Flavocetin-A and -B, two high molecular mass glycoprotein Ib binding
RT proteins with high affinity purified from Trimeresurus flavoviridis venom,
RT inhibit platelet aggregation at high shear stress.";
RL Biochim. Biophys. Acta 1244:331-338(1995).
RN [3]
RP FUNCTION.
RX PubMed=10688335; DOI=10.1016/s0049-3848(99)00143-7;
RA Taniuchi Y., Kawasaki T., Fujimura Y.;
RT "The high molecular mass, glycoprotein Ib-binding protein flavocetin-A
RT induces only small platelet aggregates in vitro.";
RL Thromb. Res. 97:69-75(2000).
RN [4]
RP CRYSTALLIZATION.
RX PubMed=10531492; DOI=10.1107/s0907444999009622;
RA Fukuda K., Mizuno H., Atoda H., Morita T.;
RT "Crystallization and preliminary x-ray studies of flavocetin-A, a platelet
RT glycoprotein Ib-binding protein from the habu snake venom.";
RL Acta Crystallogr. D 55:1911-1913(1999).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 24-148, SUBUNIT, AND DISULFIDE
RP BONDS.
RX PubMed=10684640; DOI=10.1021/bi992134z;
RA Fukuda K., Mizuno H., Atoda H., Morita T.;
RT "Crystal structure of flavocetin-A, a platelet glycoprotein Ib-binding
RT protein, reveals a novel cyclic tetramer of C-type lectin-like
RT heterodimers.";
RL Biochemistry 39:1915-1923(2000).
CC -!- FUNCTION: Strong platelet aggregation inhibitor. Binds specifically to
CC platelet glycoprotein Ibalpha (GP1BA) with high affinity and inhibits
CC vWF-dependent platelet aggregation (PubMed:7599152). Has also been
CC observed to induce small agglutinates in washed platelets by binding to
CC GPIb (PubMed:10688335). {ECO:0000269|PubMed:10688335,
CC ECO:0000269|PubMed:7599152}.
CC -!- SUBUNIT: Tetramer of heterodimers of alpha and beta subunits
CC (alphabeta)(4); disulfide-linked. {ECO:0000269|PubMed:10684640}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- MISCELLANEOUS: Has no effect on ADP- and collagen-induced platelet
CC aggregation in platelet rich plasma. {ECO:0000305|PubMed:7599152}.
CC -!- SIMILARITY: Belongs to the snaclec family. {ECO:0000305}.
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DR EMBL; AY149340; AAN72437.1; -; mRNA.
DR PIR; S55679; S55679.
DR PDB; 1C3A; X-ray; 2.50 A; B=24-148.
DR PDBsum; 1C3A; -.
DR AlphaFoldDB; Q8AV98; -.
DR SMR; Q8AV98; -.
DR EvolutionaryTrace; Q8AV98; -.
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 inhibiting toxin;
KW Secreted; Signal; Toxin.
FT SIGNAL 1..23
FT /evidence="ECO:0000269|PubMed:10942790,
FT ECO:0000269|PubMed:7599152"
FT CHAIN 24..148
FT /note="Snaclec flavocetin-A subunit beta"
FT /id="PRO_0000355294"
FT DOMAIN 34..145
FT /note="C-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 26
FT /note="Interchain (with C-158 in subunit alpha of
FT tetrameric partner)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040,
FT ECO:0000269|PubMed:10684640"
FT DISULFID 27..38
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040,
FT ECO:0000269|PubMed:10684640"
FT DISULFID 55..144
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040,
FT ECO:0000269|PubMed:10684640"
FT DISULFID 100
FT /note="Interchain (with C-104 in subunit alpha of
FT heterodimeric partner)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040,
FT ECO:0000269|PubMed:10684640"
FT DISULFID 121..136
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040,
FT ECO:0000269|PubMed:10684640"
FT CONFLICT 43..44
FT /note="QQ -> PP (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 32..34
FT /evidence="ECO:0007829|PDB:1C3A"
FT STRAND 37..46
FT /evidence="ECO:0007829|PDB:1C3A"
FT HELIX 48..58
FT /evidence="ECO:0007829|PDB:1C3A"
FT HELIX 70..84
FT /evidence="ECO:0007829|PDB:1C3A"
FT STRAND 88..90
FT /evidence="ECO:0007829|PDB:1C3A"
FT STRAND 98..100
FT /evidence="ECO:0007829|PDB:1C3A"
FT STRAND 102..104
FT /evidence="ECO:0007829|PDB:1C3A"
FT STRAND 120..129
FT /evidence="ECO:0007829|PDB:1C3A"
FT STRAND 131..135
FT /evidence="ECO:0007829|PDB:1C3A"
FT STRAND 140..147
FT /evidence="ECO:0007829|PDB:1C3A"
SQ SEQUENCE 148 AA; 16932 MW; 26379A49C6CB1E34 CRC64;
MGQFIFVSFG FLVVATSLSG TEAGFCCPLG WSSYDEHCYQ VFQQKMNWED AEKFCTQQHK
GSHLVSFHSS EEVDFVTSKT FPILKYDFVW IGLSNVWNEC TKEWSDGTKL DYKAWSGGSD
CIVSKTTDNQ WLSMDCSSKR YVVCKFQA
