ID   SLAG_MACLB              Reviewed;         157 AA.
AC   B4XSZ1;
DT   16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   25-MAY-2022, entry version 35.
DE   RecName: Full=Snaclec A16;
DE   AltName: Full=C-type lectin A16;
DE   Flags: Precursor;
OS   Macrovipera lebetina (Levantine viper) (Vipera lebetina).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Viperinae; Macrovipera.
OX   NCBI_TaxID=8709;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=19059426; DOI=10.1016/j.toxicon.2008.11.006;
RA   Jebali J., Bazaa A., Sarray S., Benhaj K., Karboul A., El Ayeb M.,
RA   Marrakchi N., Gargouri A.;
RT   "C-type lectin protein isoforms of Macrovipera lebetina: cDNA cloning and
RT   genetic diversity.";
RL   Toxicon 53:228-237(2009).
CC   -!- FUNCTION: Interferes with one step of hemostasis (modulation of
CC       platelet aggregation, or coagulation cascade, for example).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Heterodimer; disulfide-linked. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC   -!- MISCELLANEOUS: Shows greater sequence similarity to the alpha than beta
CC       subunits compared to other heterodimer snaclecs.
CC   -!- SIMILARITY: Belongs to the snaclec family. {ECO:0000305}.
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DR   EMBL; EU085453; ABW82663.1; -; mRNA.
DR   AlphaFoldDB; B4XSZ1; -.
DR   SMR; B4XSZ1; -.
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   2: Evidence at transcript level;
KW   Disulfide bond; Hemostasis impairing toxin; Secreted; Signal; Toxin.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000250"
FT   CHAIN           24..157
FT                   /note="Snaclec A16"
FT                   /id="PRO_0000356332"
FT   DOMAIN          34..150
FT                   /note="C-type lectin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   DISULFID        27..38
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   DISULFID        55..149
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   DISULFID        103
FT                   /note="Interchain"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   DISULFID        124..141
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
SQ   SEQUENCE   157 AA;  17778 MW;  77EF2CA39D2C009C CRC64;
     MGRLISVSFG LLVVFLSLSG TGADQDCLPG WSFYEGHCYK VFNVKKTWED AEKFCQKQSN
     GKHLATIEWL GKANFVADLV TLMNSDPDLD WIGLRVEDKR QQCSSHWTDG SAVSYENVVH
     NTKCFGLDQK TGYRTWVALR CELAYHFICM SRVPRGA