LEC_LENCC
ID LEC_LENCC Reviewed; 275 AA.
AC Q93WH6; Q93X50;
DT 21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 2.
DT 03-AUG-2022, entry version 69.
DE RecName: Full=Lectin;
DE Contains:
DE RecName: Full=Lectin beta chain;
DE Contains:
DE RecName: Full=Lectin alpha chain;
DE Flags: Precursor;
OS Lens culinaris subsp. culinaris (Cultivated lentil) (Lens esculenta).
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; Fabeae; Lens.
OX NCBI_TaxID=362247;
RN [1] {ECO:0000312|EMBL:CAC42123.2}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Eston {ECO:0000312|EMBL:CAC42124.2}, and
RC cv. Laird {ECO:0000312|EMBL:CAC42123.2};
RC TISSUE=Leaf {ECO:0000312|EMBL:CAC42123.2};
RX PubMed=15067396; DOI=10.1007/s00122-003-1520-9;
RA Galasso I., Lioi L., Lanave C., Bollini R., Sparvoli F.;
RT "Identification and isolation of lectin nucleotide sequences and species
RT relationships in the genus Lens (Miller).";
RL Theor. Appl. Genet. 108:1098-1102(2004).
CC -!- FUNCTION: D-mannose specific lectin. {ECO:0000250|UniProtKB:P02867}.
CC -!- SUBUNIT: Heterotetramer of two alpha and two beta chains.
CC {ECO:0000250}.
CC -!- PTM: The mature form consists of two chains, alpha and beta, produced
CC by cleavage of the immature protein. These remain cleaved, yet fold
CC together to form one subunit (By similarity).
CC {ECO:0000250|UniProtKB:P02870}.
CC -!- MISCELLANEOUS: Binds two manganese (or other transition metal) ions and
CC two calcium ions per heterotetramer. The metal ions are essential for
CC the saccharide-binding activity (By similarity).
CC {ECO:0000250|UniProtKB:P02870}.
CC -!- SIMILARITY: Belongs to the leguminous lectin family. {ECO:0000255}.
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DR EMBL; AJ318216; CAC42122.1; -; Genomic_DNA.
DR EMBL; AJ318217; CAC42123.2; -; Genomic_DNA.
DR EMBL; AJ318218; CAC42124.2; -; Genomic_DNA.
DR AlphaFoldDB; Q93WH6; -.
DR SMR; Q93WH6; -.
DR GO; GO:0005537; F:mannose binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; Lectin; Manganese; Mannose-binding; Metal-binding; Signal.
FT SIGNAL 1..30
FT /evidence="ECO:0000250|UniProtKB:P02870"
FT CHAIN 31..210
FT /note="Lectin beta chain"
FT /evidence="ECO:0000250|UniProtKB:P02870"
FT /id="PRO_0000223510"
FT PROPEP 211..217
FT /evidence="ECO:0000250|UniProtKB:P02870"
FT /id="PRO_0000223511"
FT CHAIN 218..269
FT /note="Lectin alpha chain"
FT /evidence="ECO:0000250|UniProtKB:P02870"
FT /id="PRO_0000223512"
FT PROPEP 270..275
FT /evidence="ECO:0000250|UniProtKB:P02870"
FT /id="PRO_0000223513"
FT BINDING 111
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /evidence="ECO:0000250|UniProtKB:P02870"
FT BINDING 129
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /evidence="ECO:0000250"
FT BINDING 149
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:P02870"
FT BINDING 151
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P02870"
FT BINDING 151
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:P02870"
FT BINDING 153
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 155
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P02870"
FT BINDING 159
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P02870"
FT BINDING 159
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:P02870"
FT BINDING 166
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:P02870"
FT BINDING 246
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /evidence="ECO:0000250"
FT BINDING 247
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /evidence="ECO:0000250"
FT SITE 210..211
FT /note="Cleavage"
FT /evidence="ECO:0000250|UniProtKB:P02870"
FT SITE 217..218
FT /note="Cleavage"
FT /evidence="ECO:0000250|UniProtKB:P02870"
FT CONFLICT 46
FT /note="K -> Q (in Ref. 1; CAC42122)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 275 AA; 30280 MW; 4345F4322F1C75F0 CRC64;
MASLQTQMIS FYLIFLSILL TTIFFFKVNS TETTSFSITK FSPDQKNLIF QGDGYTTKGK
LTLTKAVKST VGRALYSTPI HIWDRDTGNV ANFVTSFTFV IDAPSSYNVA DGFTFFIAPV
DTKPQTGGGY LGVFNSKEYD KTSQTVAVEF DTFYNAAWDP SNKERHIGID VNSIKSVNTK
SWNLQNGERA NVVIAFNAAT NVLTVTLTYP NSLEEENVTS YTLNEVVPLK DVVPEWVRIG
FSATTGAEFA AHEVHSWSFH SELGGTSSSK QAADA
