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LEC2_MEDTR
ID   LEC2_MEDTR              Reviewed;         280 AA.
AC   Q01807;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1993, sequence version 1.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=Truncated lectin 2;
DE   Flags: Precursor;
GN   Name=LEC2;
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   -!- MISCELLANEOUS: Lec2 is probably non functional, since a frameshift
CC       mutation leads to premature translation termination after only 98 AA.
CC       The sequence below ignores this frameshift mutation.
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; X60387; CAA42938.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q01807; -.
DR   SMR; Q01807; -.
DR   GO; GO:0030246; F:carbohydrate 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; Metal-binding; Signal.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000255"
FT   CHAIN           27..280
FT                   /note="Truncated lectin 2"
FT                   /id="PRO_0000017622"
FT   BINDING         148
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   BINDING         150
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         150
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   BINDING         152
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         154
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         158
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         158
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   BINDING         170
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        163
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        272
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   280 AA;  30473 MW;  DB68690AD8015E81 CRC64;
     MSSSNFSCIL SISLTFFILL LNKVNSAETT SFSITKFVPD QKNLIFQGDA KTASTGKLEL
     SKAVKNSIGR ALYSAPIHIW DSKTGSVANF QTTFTFTITA PNTYNVADGL AFFIAPIDTK
     PKSIHHGGYL GVFDSKTYKK SIQTVAVEID TFYNAQWDPN PGNISSTGRH IGIDVNSIKS
     ISTVPWSLEN NKKANVAIGF NGATNVLSVD VEYPLIRHYT LSHVVPLKDV VPEWVRIGFS
     SSTGAEYSAH DILSWSFDSK LNLGFENNIN ANVSSSTQAA
 
 
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