LEC_PEA
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 03-AUG-2022, entry version 136.
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).
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; Pisum.
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 PDBsum; 1BQP; -.
DR PDBsum; 1HKD; -.
DR PDBsum; 1OFS; -.
DR PDBsum; 1RIN; -.
DR PDBsum; 2BQP; -.
DR PDBsum; 2LTN; -.
DR PDBsum; 5T7P; -.
DR AlphaFoldDB; P02867; -.
DR PCDDB; P02867; -.
DR SMR; P02867; -.
DR MINT; P02867; -.
DR Allergome; 8818; Pis s Agglutinin.
DR UniLectin; P02867; -.
DR EnsemblPlants; Psat7g231520.1; Psat7g231520.1.cds1; Psat7g231520.
DR Gramene; Psat7g231520.1; Psat7g231520.1.cds1; Psat7g231520.
DR EvolutionaryTrace; P02867; -.
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 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
