LEC_LENCU
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 03-AUG-2022, entry version 134.
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 (1.8
RP ANGSTROMS) OF 31-210 AND 218-269 IN COMPLEX WITH ZINC AND MANGANESE IONS,
RP 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 (1.9 ANGSTROMS) OF 31-210 AND 218-269 IN COMPLEX WITH
RP SUCROSE; ZINC AND 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 (1.9 ANGSTROMS) OF 31-210 AND 218-269 IN COMPLEX WITH
RP SUCROSE; ZINC AND 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="http://www.functionalglycomics.org/glycomics/GBPServlet?&operationType=view&cbpId=cbp_pla_other_419";
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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 PDBsum; 1LEM; -.
DR PDBsum; 1LEN; -.
DR PDBsum; 1LES; -.
DR PDBsum; 2LAL; -.
DR AlphaFoldDB; P02870; -.
DR PCDDB; P02870; -.
DR SMR; P02870; -.
DR MINT; 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:0005537; F:mannose binding; IEA:UniProtKB-KW.
DR GO; GO:0009756; P:carbohydrate mediated signaling; TAS:UniProtKB.
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 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
