ID   SLA_DABSI               Reviewed;         154 AA.
AC   Q38L02;
DT   25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT   22-NOV-2005, sequence version 1.
DT   25-MAY-2022, entry version 51.
DE   RecName: Full=Snaclec dabocetin subunit alpha;
DE   AltName: Full=C-type lectin-like 8;
DE   Flags: Precursor;
OS   Daboia siamensis (Eastern Russel's viper) (Daboia russelii siamensis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Viperinae; Daboia.
OX   NCBI_TaxID=343250;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 24-38; 45-51; 85-94;
RP   100-119 AND 132-143, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC   TISSUE=Venom, and Venom gland;
RX   PubMed=16330060; DOI=10.1016/j.toxicon.2005.10.002;
RA   Zhong S.-R., Jin Y., Wu J.-B., Chen R.-Q., Jia Y.-H., Wang W.-Y.,
RA   Xiong Y.-L., Zhang Y.;
RT   "Characterization and molecular cloning of dabocetin, a potent antiplatelet
RT   C-type lectin-like protein from Daboia russellii siamensis venom.";
RL   Toxicon 47:104-112(2006).
CC   -!- FUNCTION: Inhibits ristocetin-induced platelet aggregation via binding
CC       to platelet glycoprotein Ibalpha (GP1BA).
CC   -!- SUBUNIT: Heterodimer of subunits alpha and beta; disulfide-linked.
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   EMBL; DQ218272; ABA86561.1; -; mRNA.
DR   AlphaFoldDB; Q38L02; -.
DR   SMR; Q38L02; -.
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   Direct protein sequencing; Disulfide bond; Hemostasis impairing toxin;
KW   Platelet aggregation inhibiting toxin; Secreted; Signal; Toxin.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000269|PubMed:16330060"
FT   CHAIN           24..154
FT                   /note="Snaclec dabocetin subunit alpha"
FT                   /id="PRO_0000355264"
FT   DOMAIN          32..149
FT                   /note="C-type lectin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   DISULFID        25..36
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   DISULFID        53..148
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   DISULFID        102
FT                   /note="Interchain (with C-100 in subunit beta)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   DISULFID        123..140
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
SQ   SEQUENCE   154 AA;  17507 MW;  DD7C58425CDB76AC CRC64;
     MGRFISVSFG LLVVFLSLSG TGADCPSEWS SHEGHCYKVF KLLKTWEDAE KFCTQQANGW
     HLASIESVEE ANFVAQLASE TLTKSKYHAW IGLRDQSKRQ QCSSHWTDGS AVSYETVTKY
     TKCFGLNKET KYHEWITLPC GDKNPFICKS WVLH