ID LEC_LENCU Reviewed; 275 AA. AC P02870; Q4ZJ64; Q6QDC0; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 21-FEB-2006, sequence version 2. DT 04-NOV-2026, entry version 146. 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 (Lentil) (Cicer lens). 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=3864; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF RP 47-275. RA Qureshi I.A., Koundal K.R.; RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases. RN [2] RP PROTEIN SEQUENCE OF 31-187. RC TISSUE=Seed; RX PubMed=7240155; DOI=10.1016/s0021-9258(19)69237-9; RA Foriers A., Lebrun E., van Rapenbusch R., de Neve R., Strosberg A.D.; RT "The structure of the lentil (Lens culinaris) lectin. Amino acid sequence RT determination and prediction of the secondary structure."; RL J. Biol. Chem. 256:5550-5560(1981). RN [3] RP PROTEIN SEQUENCE OF 218-269. RX PubMed=274705; DOI=10.1073/pnas.75.3.1136; RA Foriers A., de Neve R., Kanarek L., Strosberg A.D.; RT "Common ancestor for concanavalin A and lentil lectin?"; RL Proc. Natl. Acad. Sci. U.S.A. 75:1136-1139(1978). RN [4] RP PARTIAL NUCLEOTIDE SEQUENCE [GENOMIC DNA], X-RAY CRYSTALLOGRAPHY AND RP 218-269 IN COMPLEX WITH ZINC AND MANGANESE IONS, AND CLEAVAGE SITE. RC TISSUE=Seed; RX PubMed=8364026; DOI=10.1021/bi00085a007; RA Loris R., Steyaert J., Maes D., Lisgarten J., Pickersgill R., Wyns L.; RT "Crystal structure determination and refinement at 2.3-A resolution of the RT lentil lectin."; RL Biochemistry 32:8772-8781(1993). RN [5] RP ERRATUM OF PUBMED:8364026. RX PubMed=8260509; DOI=10.1021/bi00214a024; RA Loris R., Steyaert J., Maes D., Lisgarten J., Pickersgill R., Wyns L.; RL Biochemistry 32:14229-14229(1993). RN [6] RP X-RAY CRYSTALLOGRAPHY AND 218-269 IN COMPLEX WITH SUCROSE; ZINC AND RP MANGANESE IONS, AND CLEAVAGE SITE. RX PubMed=7731952; DOI=10.1002/prot.340200406; RA Loris R., Van Overberge D., Dao-Thi M.H., Poortmans F., Maene N., Wyns L.; RT "Structural analysis of two crystal forms of lentil lectin at 1.8 A RT resolution."; RL Proteins 20:330-346(1994). RN [7] RP X-RAY CRYSTALLOGRAPHY AND 218-269 IN COMPLEX WITH SUCROSE; ZINC AND RP MANGANESE IONS, AND CLEAVAGE SITE. RC TISSUE=Seed; RX PubMed=7592736; DOI=10.1074/jbc.270.43.25619; RA Casset F., Hamelryck T., Loris R., Brisson J.R., Tellier C., Dao-Thi M.H., RA Wyns L., Poortmans F., Perez S., Imberty A.; RT "NMR, molecular modeling, and crystallographic studies of lentil lectin- RT sucrose interaction."; RL J. Biol. Chem. 270:25619-25628(1995). CC -!- FUNCTION: D-mannose specific lectin. {ECO:0000250}. CC -!- SUBUNIT: Heterotetramer of two alpha and two beta chains. CC {ECO:0000269|PubMed:7592736, ECO:0000269|PubMed:7731952, CC ECO:0000269|PubMed:8364026}. 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. {ECO:0000269|PubMed:7592736, CC ECO:0000269|PubMed:7731952, ECO:0000269|PubMed:8364026}. 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. CC -!- SIMILARITY: Belongs to the leguminous lectin family. {ECO:0000305}. CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - Glycan Binding; CC Note=LcH; CC URL="https://www.functionalglycomics.org/glycan-array/1004579"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AY547295; AAS55887.1; -; Genomic_DNA. DR EMBL; DQ005103; AAY21161.1; -; mRNA. DR PIR; A48694; A48694. DR PDB; 1LEM; X-ray; 3.00 A; A=31-211, B=218-269. DR PDB; 1LEN; X-ray; 1.80 A; A/C=31-211, B/D=218-269. DR PDB; 1LES; X-ray; 1.90 A; A/C=31-211, B/D=218-269. DR PDB; 2LAL; X-ray; 1.80 A; A/C=31-211, B/D=218-269. DR AlphaFoldDB; P02870; -. DR SMR; P02870; -. DR Allergome; 8816; Len c Agglutinin. DR UniLectin; P02870; -. DR EvolutionaryTrace; P02870; -. DR GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB. DR GO; GO:0030246; F:carbohydrate binding; IDA:UniProtKB. DR GO; GO:0030145; F:manganese ion binding; IDA:UniProtKB. DR GO; GO:0009756; P:carbohydrate mediated signaling; TAS:UniProtKB. DR CDD; cd06899; lectin_legume_LecRK_Arcelin_ConA; 1. DR FunFam; 2.60.120.200:FF:000237; Mannose/glucose-specific lectin; 1. DR Gene3D; 2.60.120.200; -; 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 InterPro; IPR050258; Leguminous_Lectin. DR PANTHER; PTHR32401; CONCANAVALIN A-LIKE LECTIN FAMILY PROTEIN; 1. DR PANTHER; PTHR32401:SF45; LECTIN; 1. DR Pfam; PF00139; Lectin_legB; 1. DR PIRSF; PIRSF002690; L-type_lectin_plant; 1. DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1. DR PROSITE; PS00308; LECTIN_LEGUME_ALPHA; 1. DR PROSITE; PS00307; LECTIN_LEGUME_BETA; 1. DR PCDDB; P02870; -. PE 1: Evidence at protein level; KW 3D-structure; Calcium; Direct protein sequencing; Lectin; Manganese; KW Mannose-binding; Metal-binding; Signal. FT SIGNAL 1..30 FT /evidence="ECO:0000269|PubMed:7240155" FT CHAIN 31..210 FT /note="Lectin beta chain" FT /id="PRO_0000017619" FT PROPEP 211..217 FT /evidence="ECO:0000269|PubMed:274705" FT /id="PRO_0000223477" FT CHAIN 218..269 FT /note="Lectin alpha chain" FT /id="PRO_0000017620" FT PROPEP 270..275 FT /id="PRO_0000223478" FT BINDING 111 FT /ligand="D-glucose" FT /ligand_id="ChEBI:CHEBI:4167" FT BINDING 129 FT /ligand="D-glucose" FT /ligand_id="ChEBI:CHEBI:4167" FT BINDING 149 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT BINDING 151 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT BINDING 151 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT BINDING 153 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT BINDING 155 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT BINDING 159 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT BINDING 159 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT BINDING 166 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT BINDING 246 FT /ligand="D-glucose" FT /ligand_id="ChEBI:CHEBI:4167" FT BINDING 247 FT /ligand="D-glucose" FT /ligand_id="ChEBI:CHEBI:4167" FT SITE 210..211 FT /note="Cleavage" FT SITE 217..218 FT /note="Cleavage" FT CONFLICT 46 FT /note="K -> Q (in Ref. 2; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 47..53 FT /note="NLIFQGD -> GGRGNSI (in Ref. 1; AAS55887)" FT /evidence="ECO:0000305" FT CONFLICT 57..60 FT /note="TKGK -> GKEG (in Ref. 2; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 66..71 FT /note="AVKSTV -> VSKETG (in Ref. 2; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 88 FT /note="G -> V (in Ref. 2; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 96..106 FT /note="SFTFVIDAPSS -> NGSQVFRESPNG (in Ref. 2; AA FT sequence)" FT /evidence="ECO:0000305" FT CONFLICT 112 FT /note="E -> G (in Ref. 2; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 135..136 FT /note="NS -> YNG (in Ref. 2; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 252 FT /note="H -> Q (in Ref. 3; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 260..268 FT /note="HSELGGTSS -> NSQLGHTSK (in Ref. 3; AA sequence)" FT /evidence="ECO:0000305" FT STRAND 32..41 FT /evidence="ECO:0007829|PDB:1LEN" FT STRAND 48..52 FT /evidence="ECO:0007829|PDB:1LEN" FT STRAND 55..57 FT /evidence="ECO:0007829|PDB:1LEN" FT STRAND 59..64 FT /evidence="ECO:0007829|PDB:1LEN" FT STRAND 71..78 FT /evidence="ECO:0007829|PDB:1LEN" FT TURN 85..87 FT /evidence="ECO:0007829|PDB:1LEN" FT STRAND 92..102 FT /evidence="ECO:0007829|PDB:1LEN" FT STRAND 104..108 FT /evidence="ECO:0007829|PDB:1LEM" FT STRAND 112..119 FT /evidence="ECO:0007829|PDB:1LEN" FT HELIX 128..130 FT /evidence="ECO:0007829|PDB:1LEN" FT TURN 131..133 FT /evidence="ECO:0007829|PDB:1LEN" FT TURN 141..143 FT /evidence="ECO:0007829|PDB:1LEN" FT STRAND 146..151 FT /evidence="ECO:0007829|PDB:1LEN" FT TURN 156..158 FT /evidence="ECO:0007829|PDB:1LEN" FT STRAND 166..175 FT /evidence="ECO:0007829|PDB:1LEN" FT STRAND 177..181 FT /evidence="ECO:0007829|PDB:1LEN" FT STRAND 189..197 FT /evidence="ECO:0007829|PDB:1LEN" FT TURN 198..201 FT /evidence="ECO:0007829|PDB:1LEN" FT STRAND 202..209 FT /evidence="ECO:0007829|PDB:1LEN" FT STRAND 219..226 FT /evidence="ECO:0007829|PDB:1LEN" FT HELIX 229..232 FT /evidence="ECO:0007829|PDB:1LEN" FT STRAND 235..244 FT /evidence="ECO:0007829|PDB:1LEN" FT STRAND 246..248 FT /evidence="ECO:0007829|PDB:1LES" FT STRAND 251..263 FT /evidence="ECO:0007829|PDB:1LEN" SQ SEQUENCE 275 AA; 30352 MW; 194756B9F1A069C5 CRC64; MASLQTQMIS FYLIFLSILL TTIFFFKVNS TETTSFSITK FSPDQKNLIF QGDGYTTKGK LTLTKAVKST VGRALYSTPI HIWDRDTGNV ANFVTSFTFV IDAPSSYNVA DEFTFFIAPV DTKPQTGGGY LGVFNSKEYD KTSQTVAVEF DTFYNAAWDP SNKERHIGID VNSIKSVNTK SWNLQNGERA NVVIAFNAAT NVLTVTLTYP NSLEEENVTS YTLNEVVPLK DVVPEWVRIG FSATTGAEFA AHEVHSWSFH SELGGTSSSK QAADA //