ID   LEC_PEA                 Reviewed;         275 AA.
AC   P02867;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   02-SEP-2026, entry version 147.
DE   RecName: Full=Lectin;
DE   Contains:
DE     RecName: Full=Lectin beta chain;
DE   Contains:
DE     RecName: Full=Lectin alpha chain;
DE   Flags: Precursor;
GN   Name=LECA; Synonyms=PSL1;
OS   Pisum sativum (Garden pea) (Lathyrus oleraceus).
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; Lathyrus.
OX   NCBI_TaxID=3888;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=cv. Feltham First; TISSUE=Seed;
RX   PubMed=3658708; DOI=10.1093/nar/15.18.7642;
RA   Gatehouse J.A., Bown D., Evans I.M., Gatehouse L.N., Jobes D., Preston P.,
RA   Croy R.R.D.;
RT   "Sequence of the seed lectin gene from pea (Pisum sativum L.).";
RL   Nucleic Acids Res. 15:7642-7642(1987).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RX   AGRICOLA=IND91054566; DOI=10.1007/BF00015881;
RA   Kaminski P.A., Buffard D., Strosberg A.D.;
RT   "The pea lectin gene family contains only one functional gene.";
RL   Plant Mol. Biol. 9:497-507(1987).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. P1/G086;
RX   PubMed=6688253; DOI=10.1016/s0021-9258(17)44701-6;
RA   Higgins T.J.V., Chandler P.M., Zurawski G., Button S.C., Spencer D.;
RT   "The biosynthesis and primary structure of pea seed lectin.";
RL   J. Biol. Chem. 258:9544-9549(1983).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=cv. Feltham First;
RA   de Pater B.S., Pham K.T., Katagiri F., Chua N.H., Kijne J.W.;
RL   Submitted (MAY-1992) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   PROTEIN SEQUENCE OF 218-271.
RX   PubMed=728447; DOI=10.1016/0005-2795(78)90514-7;
RA   Richardson C., Behnke W.D., Freisheim J.H., Blumenthal K.M.;
RT   "The complete amino acid sequence of the alpha-subunit of pea lectin, Pisum
RT   sativum.";
RL   Biochim. Biophys. Acta 537:310-319(1978).
RN   [6]
RP   X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
RX   PubMed=3782132; DOI=10.1016/s0021-9258(18)66597-4;
RA   Einspahr H., Parks E.H., Suguna K., Subramanian E., Suddath F.L.;
RT   "The crystal structure of pea lectin at 3.0-A resolution.";
RL   J. Biol. Chem. 261:16518-16527(1986).
RN   [7]
RP   X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
RX   PubMed=8486683; DOI=10.2210/pdb1rin/pdb;
RA   Rini J.M., Hardman K.D., Einspahr H., Suddath F.L., Carver J.P.;
RT   "X-ray crystal structure of a pea lectin-trimannoside complex at 2.6-A
RT   resolution.";
RL   J. Biol. Chem. 268:10126-10132(1993).
RN   [8]
RP   X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
RA   Ruzeinikov S.N., Mikhailova I.Y., Tsygannik I.N., Pangborn W., Duax W.,
RA   Pletnev V.Z.;
RT   "The structure of the pea lectin-D-mannopyranose complex at a 2.1 A
RT   resolution.";
RL   Russ. J. Bioorg. Chem. 24:277-279(1998).
RN   [9]
RP   MUTAGENESIS.
RX   PubMed=1463840; DOI=10.1007/bf00028892;
RA   van Eijsden R.R., Hoedemaeker F.J., Diaz C.L., Lugtenberg B.J.J.,
RA   de Pater B.S., Kijne J.W.;
RT   "Mutational analysis of pea lectin. Substitution of Asn125 for Asp in the
RT   monosaccharide-binding site eliminates mannose/glucose-binding activity.";
RL   Plant Mol. Biol. 20:1049-1058(1992).
CC   -!- FUNCTION: D-mannose specific lectin.
CC   -!- SUBUNIT: Tetramer of two alpha and two beta chains.
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; Y00440; CAA68497.1; -; Genomic_DNA.
DR   EMBL; M18160; AAA33676.1; -; mRNA.
DR   EMBL; J01254; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; X66368; CAA47011.1; -; Genomic_DNA.
DR   PIR; A26844; LNPM.
DR   PDB; 1BQP; X-ray; 2.10 A; A/C=31-211, B/D=218-264.
DR   PDB; 1HKD; X-ray; 2.09 A; A/C=31-211, B/D=218-269.
DR   PDB; 1OFS; X-ray; 1.80 A; A/C=31-217, B/D=218-265.
DR   PDB; 1RIN; X-ray; 2.60 A; A/C=31-210, B/D=218-266.
DR   PDB; 2BQP; X-ray; 1.90 A; A/B=31-264.
DR   PDB; 2LTN; X-ray; 1.70 A; A/C=31-211, B/D=218-269.
DR   PDB; 5T7P; X-ray; 2.16 A; A/B=31-266.
DR   AlphaFoldDB; P02867; -.
DR   MDposit; P02867; -.
DR   MDRepo; P02867; -.
DR   PCDDB; P02867; -.
DR   SMR; P02867; -.
DR   MINT; P02867; -.
DR   Allergome; 8818; Pis s Agglutinin.
DR   UniLectin; P02867; -.
DR   GlyCosmos; P02867; 1 site, No reported glycans.
DR   EnsemblPlants; Psat7g231520.1; Psat7g231520.1.cds1; Psat7g231520.
DR   EnsemblPlants; PSAT_LOCUS29525_t1; CAL5211070.1; PSAT_LOCUS29525.
DR   Gramene; Psat7g231520.1; Psat7g231520.1.cds1; Psat7g231520.
DR   Gramene; PSAT_LOCUS29525_t1; CAL5211070.1; PSAT_LOCUS29525.
DR   OrthoDB; 2014373at2759; -.
DR   EvolutionaryTrace; P02867; -.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
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   PDBsum; 1BQP; -.
DR   PDBsum; 1HKD; -.
DR   PDBsum; 1OFS; -.
DR   PDBsum; 1RIN; -.
DR   PDBsum; 2BQP; -.
DR   PDBsum; 2LTN; -.
DR   PDBsum; 5T7P; -.
PE   1: Evidence at protein level;
KW   3D-structure; Calcium; Direct protein sequencing; Glycoprotein; Lectin;
KW   Manganese; Mannose-binding; Metal-binding; Signal.
FT   SIGNAL          1..30
FT   CHAIN           31..217
FT                   /note="Lectin beta chain"
FT                   /id="PRO_0000017623"
FT   CHAIN           218..275
FT                   /note="Lectin alpha chain"
FT                   /id="PRO_0000017624"
FT   BINDING         149
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   BINDING         151
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         151
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
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"
FT   BINDING         159
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         159
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   BINDING         166
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        217
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        269
FT                   /note="Missing (in Ref. 4)"
FT                   /evidence="ECO:0000305"
FT   STRAND          32..40
FT                   /evidence="ECO:0007829|PDB:2LTN"
FT   STRAND          48..52
FT                   /evidence="ECO:0007829|PDB:2LTN"
FT   STRAND          55..57
FT                   /evidence="ECO:0007829|PDB:1OFS"
FT   STRAND          58..64
FT                   /evidence="ECO:0007829|PDB:2LTN"
FT   STRAND          71..78
FT                   /evidence="ECO:0007829|PDB:2LTN"
FT   TURN            85..87
FT                   /evidence="ECO:0007829|PDB:2LTN"
FT   STRAND          92..102
FT                   /evidence="ECO:0007829|PDB:2LTN"
FT   STRAND          104..108
FT                   /evidence="ECO:0007829|PDB:1HKD"
FT   STRAND          112..119
FT                   /evidence="ECO:0007829|PDB:2LTN"
FT   HELIX           128..130
FT                   /evidence="ECO:0007829|PDB:2LTN"
FT   TURN            131..133
FT                   /evidence="ECO:0007829|PDB:2LTN"
FT   HELIX           141..143
FT                   /evidence="ECO:0007829|PDB:1OFS"
FT   STRAND          146..151
FT                   /evidence="ECO:0007829|PDB:2LTN"
FT   TURN            156..158
FT                   /evidence="ECO:0007829|PDB:2LTN"
FT   STRAND          166..175
FT                   /evidence="ECO:0007829|PDB:2LTN"
FT   STRAND          177..181
FT                   /evidence="ECO:0007829|PDB:2LTN"
FT   STRAND          190..197
FT                   /evidence="ECO:0007829|PDB:2LTN"
FT   TURN            198..201
FT                   /evidence="ECO:0007829|PDB:2LTN"
FT   STRAND          202..209
FT                   /evidence="ECO:0007829|PDB:2LTN"
FT   STRAND          219..226
FT                   /evidence="ECO:0007829|PDB:2LTN"
FT   HELIX           229..232
FT                   /evidence="ECO:0007829|PDB:2LTN"
FT   STRAND          235..244
FT                   /evidence="ECO:0007829|PDB:2LTN"
FT   STRAND          246..248
FT                   /evidence="ECO:0007829|PDB:1OFS"
FT   STRAND          251..263
FT                   /evidence="ECO:0007829|PDB:2LTN"
SQ   SEQUENCE   275 AA;  30270 MW;  FD7BE8E00A811222 CRC64;
     MASLQTQMIS FYAIFLSILL TTILFFKVNS TETTSFLITK FSPDQQNLIF QGDGYTTKEK
     LTLTKAVKNT VGRALYSSPI HIWDRETGNV ANFVTSFTFV INAPNSYNVA DGFTFFIAPV
     DTKPQTGGGY LGVFNSAEYD KTTQTVAVEF DTFYNAAWDP SNRDRHIGID VNSIKSVNTK
     SWKLQNGEEA NVVIAFNAAT NVLTVSLTYP NSLEEENVTS YTLSDVVSLK DVVPEWVRIG
     FSATTGAEYA AHEVLSWSFH SELSGTSSSK QAADA
//