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