ID   SLCIA_MACLB             Reviewed;         152 AA.
AC   W5XDM0;
DT   03-SEP-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   25-MAY-2022, entry version 15.
DE   RecName: Full=Snaclec lebecin subunit alpha;
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], PROTEIN SEQUENCE OF 24-44, FUNCTION, SUBUNIT,
RP   MASS SPECTROMETRY, AND 3D-STRUCTURE MODELING.
RC   TISSUE=Venom, and Venom gland;
RX   PubMed=24814013; DOI=10.1016/j.toxicon.2014.04.010;
RA   Jebali J., Fakhfekh E., Morgen M., Srairi-Abid N., Majdoub H., Gargouri A.,
RA   El Ayeb M., Luis J., Marrakchi N., Sarray S.;
RT   "Lebecin, a new C-type lectin like protein from Macrovipera lebetina venom
RT   with anti-tumor activity against the breast cancer cell line MDA-MB231.";
RL   Toxicon 86:16-27(2014).
CC   -!- FUNCTION: Inhibits the adhesion of MDA-MB231 human breast cancer cells
CC       to fibrinogen and fibronectin, MDA-MB231 cell migration, and the MDA-
CC       MB231 cell proliferation. This inhibition may be due to the binding to
CC       receptors of the integrin family, probably alpha-v/beta-3 (ITGAV/ITGB3)
CC       (40% inhibition of cell adhesion) and alpha-5/beta-1 (ITGA5/ITGB1) (by
CC       comparison with lebectin). {ECO:0000269|PubMed:24814013}.
CC   -!- SUBUNIT: Heterodimer with the beta subunit (AC W5XCJ6); disulfide-
CC       linked. {ECO:0000269|PubMed:24814013}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC   -!- MASS SPECTROMETRY: Mass=15820.43; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:24814013};
CC   -!- SIMILARITY: Belongs to the snaclec family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; KF836491; AHI10992.1; -; mRNA.
DR   AlphaFoldDB; W5XDM0; -.
DR   SMR; W5XDM0; -.
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   Cell adhesion impairing toxin; Direct protein sequencing; Disulfide bond;
KW   Secreted; Signal; Toxin.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000269|PubMed:24814013"
FT   CHAIN           24..152
FT                   /note="Snaclec lebecin subunit alpha"
FT                   /id="PRO_0000430178"
FT   DOMAIN          34..148
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        54..147
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   DISULFID        101
FT                   /note="Interchain (with C-102 in subunit beta)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   DISULFID        122..139
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
SQ   SEQUENCE   152 AA;  17230 MW;  D55FE27B1DB7D98C CRC64;
     MGRSISVSFG LLVVFLSLSG TGADQDCLPG WSFYEGGCYY VFDVKTWEDA EKFCQKQSNG
     KHLATIEWLG KANFVADLVT LNSDPRLDWI GLRVEDKRQQ CSSHWTDGSA VSYENVVHNT
     KCFGLDQKTG YRTWVALRCE LAYHFICSRV PR