ID   SLMA_MACLB              Reviewed;         131 AA.
AC   C0HKZ6;
DT   23-MAY-2018, integrated into UniProtKB/Swiss-Prot.
DT   23-MAY-2018, sequence version 1.
DT   25-MAY-2022, entry version 6.
DE   RecName: Full=Snaclec macrovipecetin subunit alpha {ECO:0000303|PubMed:29196192};
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 {ECO:0000303|PubMed:29196192};
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, SUBUNIT, SUBCELLULAR LOCATION, AND MASS SPECTROMETRY.
RC   TISSUE=Venom {ECO:0000303|PubMed:29196192};
RX   PubMed=29196192; DOI=10.1016/j.bbagen.2017.11.019;
RA   Hammouda M.B., Riahi-Chebbi I., Souid S., Othman H., Aloui Z.,
RA   Srairi-Abid N., Karoui H., Gasmi A., Magnenat E.M., Wells T.N.C.,
RA   Clemetson K.J., Rodriguez-Lopez J.N., Essafi-Benkhadir K.;
RT   "Macrovipecetin, a C-type lectin from Macrovipera lebetina venom, inhibits
RT   proliferation migration and invasion of SK-MEL-28 human melanoma cells and
RT   enhances their sensitivity to cisplatin.";
RL   Biochim. Biophys. Acta 1862:600-614(2018).
CC   -!- FUNCTION: Interferes with one step of hemostasis (modulation of
CC       platelet aggregation, or coagulation cascade, for example).
CC       {ECO:0000305}.
CC   -!- SUBUNIT: Heterodimer of subunits alpha and beta; disulfide-linked.
CC       {ECO:0000269|PubMed:29196192}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:29196192}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:29196192}.
CC   -!- MASS SPECTROMETRY: Mass=15422.7; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:29196192};
CC   -!- SIMILARITY: Belongs to the snaclec family. {ECO:0000305}.
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DR   AlphaFoldDB; C0HKZ6; -.
DR   SMR; C0HKZ6; -.
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   Secreted; Toxin.
FT   CHAIN           1..131
FT                   /note="Snaclec macrovipecetin subunit alpha"
FT                   /evidence="ECO:0000269|PubMed:29196192"
FT                   /id="PRO_0000444294"
FT   DOMAIN          9..126
FT                   /note="C-type lectin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   DISULFID        2..13
FT                   /evidence="ECO:0000250|UniProtKB:Q8JIV9"
FT   DISULFID        30..125
FT                   /evidence="ECO:0000250|UniProtKB:Q8JIV9"
FT   DISULFID        79
FT                   /note="Interchain (with C-77 in subunit beta)"
FT                   /evidence="ECO:0000250|UniProtKB:Q8JIV9"
FT   DISULFID        100..117
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
SQ   SEQUENCE   131 AA;  15418 MW;  2DC63A9500F4466E CRC64;
     DCPSDWSSHE EHCYKVFRLF KTWEEAEKFC TQQVNGWHLA SIESVEEANF LAELVPKTLI
     KSKYHVWIGL RDQSERQQCS SHWTDGSAVS YEKVVRFTKC FGLNKDKGYL EWVTLPCEDK
     NPFICKSWVP H