ID   LEC_ALLCE               Reviewed;         164 AA.
AC   C0HJM8; Q38687;
DT   29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2017, sequence version 2.
DT   25-MAY-2022, entry version 12.
DE   RecName: Full=Lectin {ECO:0000303|PubMed:8106012};
DE   Flags: Precursor; Fragment;
OS   Allium cepa (Onion).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Asparagales; Amaryllidaceae;
OC   Allioideae; Allieae; Allium.
OX   NCBI_TaxID=4679;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=8106012; DOI=10.1007/bf00029011;
RA   Van Damme E.J., Smeets K., Engelborghs I., Aelbers H., Balzarini J.,
RA   Pusztai A., van Leuven F., Goldstein I.J., Peumans W.J.;
RT   "Cloning and characterization of the lectin cDNA clones from onion, shallot
RT   and leek.";
RL   Plant Mol. Biol. 23:365-376(1993).
RN   [2]
RP   PROTEIN SEQUENCE OF N-TERMINUS, FUNCTION, SUBUNIT, AND LACK OF
RP   GLYCOSYLATION.
RC   TISSUE=Bulb;
RX   PubMed=25887266; DOI=10.1016/j.intimp.2015.04.009;
RA   Prasanna V.K., Venkatesh Y.P.;
RT   "Characterization of onion lectin (Allium cepa agglutinin) as an
RT   immunomodulatory protein inducing Th1-type immune response in vitro.";
RL   Int. Immunopharmacol. 26:304-313(2015).
CC   -!- FUNCTION: Mannose-specific lectin. Induces a Th1-type immune response
CC       in vitro. Causes a 4-fold increase in the proliferation of murine
CC       thymocytes and a significant increase in the production of nitric oxide
CC       at 24 hours in a macrophage cell line. Stimulates the production of the
CC       pro-inflammatory cytokines TNF and IL12 by rat peritoneal macrophages
CC       in a dose-dependent manner and of the cytokines IFNG and IL2 in murine
CC       thymocytes. Has hemagglutination activity towards rabbit erythrocytes.
CC       {ECO:0000269|PubMed:25887266}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:25887266}.
CC   -!- PTM: Not glycosylated. {ECO:0000269|PubMed:25887266}.
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DR   EMBL; L12171; AAC37359.1; -; mRNA.
DR   PIR; S39487; S39487.
DR   AlphaFoldDB; C0HJM8; -.
DR   SMR; C0HJM8; -.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR   CDD; cd00028; B_lectin; 1.
DR   Gene3D; 2.90.10.10; -; 1.
DR   InterPro; IPR001480; Bulb-type_lectin_dom.
DR   InterPro; IPR036426; Bulb-type_lectin_dom_sf.
DR   SMART; SM00108; B_lectin; 1.
DR   SUPFAM; SSF51110; SSF51110; 1.
DR   PROSITE; PS50927; BULB_LECTIN; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Hemagglutinin; Lectin; Signal.
FT   SIGNAL          <1..15
FT                   /evidence="ECO:0000269|PubMed:25887266"
FT   CHAIN           16..164
FT                   /note="Lectin"
FT                   /evidence="ECO:0000269|PubMed:25887266"
FT                   /id="PRO_0000439160"
FT   DOMAIN          16..125
FT                   /note="Bulb-type lectin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00038"
FT   DISULFID        44..68
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00038"
FT   CONFLICT        20
FT                   /note="V -> L (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   NON_TER         1
FT                   /evidence="ECO:0000312|EMBL:AAC37359.1"
SQ   SEQUENCE   164 AA;  17537 MW;  ACBDB1CDC5B2C357 CRC64;
     TVATILTILA STCMARNVLV NNEGLYAGQS LVVEQYTFIM QDDCNLVLYE YSTPIWASNT
     GVTGKNGCRA VMQADGNFVV YDVKGRAVWA SNSRRGNGNY ILVLQKDRNV VIYGSDIWST
     GTYRKKVGGT VVMAMNGTVD GGSVVGPVTV NQNVTAVRKV AAAA