SLMB_MACLB
ID SLMB_MACLB Reviewed; 127 AA.
AC C0HKZ7;
DT 23-MAY-2018, integrated into UniProtKB/Swiss-Prot.
DT 23-MAY-2018, sequence version 1.
DT 25-MAY-2022, entry version 8.
DE RecName: Full=Snaclec macrovipecetin subunit beta {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=15031.7; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:29196192};
CC -!- SIMILARITY: Belongs to the snaclec family. {ECO:0000305}.
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DR AlphaFoldDB; C0HKZ7; -.
DR SMR; C0HKZ7; -.
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..127
FT /note="Snaclec macrovipecetin subunit beta"
FT /evidence="ECO:0000269|PubMed:29196192"
FT /id="PRO_0000444295"
FT DOMAIN 11..122
FT /note="C-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 4..15
FT /evidence="ECO:0000250|UniProtKB:Q8AYA3"
FT DISULFID 32..121
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 77
FT /note="Interchain (with C-79 in subunit alpha)"
FT /evidence="ECO:0000250|UniProtKB:Q8AYA3"
FT DISULFID 98..113
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
SQ SEQUENCE 127 AA; 15026 MW; 8428F499965D8B65 CRC64;
DQDCLPGWSF YEGHCYKVFD VKKTWEDAEK FCTEQMSGGH LVSFHSSEEV DFMIKLASPI
LKFDLVWIGL SNFWRDCHWG WSDGVKLDYK AWSDKPNCYV AKTVDPQWLH RDCSRTYKFV
CKSRVPR