ID   LEC1_MEDTR              Reviewed;         277 AA.
AC   Q01806;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1993, sequence version 1.
DT   03-AUG-2022, entry version 103.
DE   RecName: Full=Lectin 1;
DE   Flags: Precursor;
GN   Name=LEC1;
OS   Medicago truncatula (Barrel medic) (Medicago tribuloides).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; Hologalegina; IRL clade; Trifolieae; Medicago.
OX   NCBI_TaxID=3880;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=cv. Jemalong;
RX   PubMed=1511126; DOI=10.1007/bf00040532;
RA   Bauchrowitz M.A., Barker D.G., Nadaud I., Rouge P., Lescure B.;
RT   "Lectin genes from the legume Medicago truncatula.";
RL   Plant Mol. Biol. 19:1011-1017(1992).
CC   -!- FUNCTION: Lectin that may be involved in a cell recognition process.
CC   -!- MISCELLANEOUS: Binds one manganese (or another transition metal) ion
CC       and one calcium ion. The metal ions are essential for the saccharide-
CC       binding and cell-agglutinating activities.
CC   -!- SIMILARITY: Belongs to the leguminous lectin family. {ECO:0000305}.
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DR   EMBL; X60386; CAA42937.1; -; Genomic_DNA.
DR   PIR; S25296; S25296.
DR   RefSeq; XP_003627476.1; XM_003627428.2.
DR   AlphaFoldDB; Q01806; -.
DR   SMR; Q01806; -.
DR   STRING; 3880.AET01952; -.
DR   EnsemblPlants; AET01952; AET01952; MTR_8g023510.
DR   GeneID; 11445681; -.
DR   Gramene; AET01952; AET01952; MTR_8g023510.
DR   eggNOG; ENOG502QTX3; Eukaryota.
DR   HOGENOM; CLU_000288_62_2_1; -.
DR   OMA; LFDNATY; -.
DR   OrthoDB; 1377709at2759; -.
DR   ExpressionAtlas; Q01806; differential.
DR   GO; GO:0005537; F:mannose binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0009610; P:response to symbiotic fungus; IEA:UniProt.
DR   CDD; cd06899; lectin_legume_LecRK_Arcelin_ConA; 1.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR016363; L-lectin.
DR   InterPro; IPR000985; Lectin_LegA_CS.
DR   InterPro; IPR019825; Lectin_legB_Mn/Ca_BS.
DR   InterPro; IPR001220; Legume_lectin_dom.
DR   Pfam; PF00139; Lectin_legB; 1.
DR   PIRSF; PIRSF002690; L-type_lectin_plant; 1.
DR   SUPFAM; SSF49899; SSF49899; 1.
DR   PROSITE; PS00308; LECTIN_LEGUME_ALPHA; 1.
DR   PROSITE; PS00307; LECTIN_LEGUME_BETA; 1.
PE   3: Inferred from homology;
KW   Calcium; Glycoprotein; Lectin; Manganese; Mannose-binding; Metal-binding;
KW   Signal.
FT   SIGNAL          1..30
FT                   /evidence="ECO:0000255"
FT   CHAIN           31..277
FT                   /note="Lectin 1"
FT                   /id="PRO_0000017621"
FT   BINDING         152
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   BINDING         154
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         154
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   BINDING         158
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         161
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         161
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   BINDING         167
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        143
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        269
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   277 AA;  30550 MW;  2F87F7FEDA560254 CRC64;
     MSFSSSNFYV ILSISLTVFI LLFNINKVNS TELTSFTITK FSQDQKNLIF QGNAITTSTG
     KLQLTKAVKN SIGRALYSAP IHIWDSKTGD VANFETLFTF AITAPYSSNV ADGLAFFIAP
     VDTQPQNIGR AGFLGVFNSE TYNKSIQTVA VEIDTFHNTW DPKINRHIGI NVNCIKSIST
     TSWVLENGRE ANVLVRFDAH TNVLSVVLSY PGLPDSYILS DVVPLKDIVP EWVRIGFSAA
     TGAEFAEHDI RYWSFHSELS LVFNNNNANV SSSVQSA