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P02867 (LEC_PEA) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 102. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Lectin

Cleaved into the following 2 chains:

  1. Lectin beta chain
  2. Lectin alpha chain
Gene names
Name:LECA
Synonyms:PSL1
OrganismPisum sativum (Garden pea)
Taxonomic identifier3888 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsFabalesFabaceaePapilionoideaeFabeaePisum

Protein attributes

Sequence length275 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

D-mannose specific lectin.

Subunit structure

Tetramer of two alpha and two beta chains.

Miscellaneous

Binds one manganese (or another transition metal) ion and one calcium ion. The metal ions are essential for the saccharide-binding and cell-agglutinating activities.

Sequence similarities

Belongs to the leguminous lectin family.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3030
Chain31 – 217187Lectin beta chain
PRO_0000017623
Chain218 – 27558Lectin alpha chain
PRO_0000017624

Sites

Metal binding1491Manganese By similarity
Metal binding1511Calcium By similarity
Metal binding1511Manganese By similarity
Metal binding1531Calcium; via carbonyl oxygen By similarity
Metal binding1551Calcium By similarity
Metal binding1591Calcium By similarity
Metal binding1591Manganese By similarity
Metal binding1661Manganese By similarity

Amino acid modifications

Glycosylation2171N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict2691Missing Ref.4

Secondary structure

............................................. 275
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P02867 [UniParc].

Last modified July 21, 1986. Version 1.
Checksum: FD7BE8E00A811222

FASTA27530,270
        10         20         30         40         50         60 
MASLQTQMIS FYAIFLSILL TTILFFKVNS TETTSFLITK FSPDQQNLIF QGDGYTTKEK 

        70         80         90        100        110        120 
LTLTKAVKNT VGRALYSSPI HIWDRETGNV ANFVTSFTFV INAPNSYNVA DGFTFFIAPV 

       130        140        150        160        170        180 
DTKPQTGGGY LGVFNSAEYD KTTQTVAVEF DTFYNAAWDP SNRDRHIGID VNSIKSVNTK 

       190        200        210        220        230        240 
SWKLQNGEEA NVVIAFNAAT NVLTVSLTYP NSLEEENVTS YTLSDVVSLK DVVPEWVRIG 

       250        260        270 
FSATTGAEYA AHEVLSWSFH SELSGTSSSK QAADA 

« Hide

References

[1]"Sequence of the seed lectin gene from pea (Pisum sativum L.)."
Gatehouse J.A., Bown D., Evans I.M., Gatehouse L.N., Jobes D., Preston P., Croy R.R.D.
Nucleic Acids Res. 15:7642-7642(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: cv. Feltham First.
Tissue: Seed.
[2]"The pea lectin gene family contains only one functional gene."
Kaminski P.A., Buffard D., Strosberg A.D.
Plant Mol. Biol. 9:497-507(1987) [AGRICOLA] [Europe PMC]
Cited for: NUCLEOTIDE SEQUENCE.
[3]"The biosynthesis and primary structure of pea seed lectin."
Higgins T.J.V., Chandler P.M., Zurawski G., Button S.C., Spencer D.
J. Biol. Chem. 258:9544-9549(1983) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: cv. P1/G086.
[4]de Pater B.S., Pham K.T., Katagiri F., Chua N.H., Kijne J.W.
Submitted (MAY-1992) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE.
Strain: cv. Feltham First.
[5]"The complete amino acid sequence of the alpha-subunit of pea lectin, Pisum sativum."
Richardson C., Behnke W.D., Freisheim J.H., Blumenthal K.M.
Biochim. Biophys. Acta 537:310-319(1978) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 218-271.
[6]"The crystal structure of pea lectin at 3.0-A resolution."
Einspahr H., Parks E.H., Suguna K., Subramanian E., Suddath F.L.
J. Biol. Chem. 261:16518-16527(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
[7]"X-ray crystal structure of a pea lectin-trimannoside complex at 2.6-A resolution."
Rini J.M., Hardman K.D., Einspahr H., Suddath F.L., Carver J.P.
J. Biol. Chem. 268:10126-10132(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
[8]"The structure of the pea lectin-D-mannopyranose complex at a 2.1 A resolution."
Ruzeinikov S.N., Mikhailova I.Y., Tsygannik I.N., Pangborn W., Duax W., Pletnev V.Z.
Russ. J. Bioorg. Chem. 24:277-279(1998)
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
[9]"Mutational analysis of pea lectin. Substitution of Asn125 for Asp in the monosaccharide-binding site eliminates mannose/glucose-binding activity."
van Eijsden R.R., Hoedemaeker F.J., Diaz C.L., Lugtenberg B.J.J., de Pater B.S., Kijne J.W.
Plant Mol. Biol. 20:1049-1058(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Y00440 Genomic DNA. Translation: CAA68497.1.
M18160 mRNA. Translation: AAA33676.1.
J01254 mRNA. No translation available.
X66368 Genomic DNA. Translation: CAA47011.1.
PIRLNPM. A26844.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1BQPX-ray2.10A/C31-211[»]
B/D218-264[»]
1HKDX-ray2.09A/C31-211[»]
B/D218-269[»]
1OFSX-ray1.80A/C31-217[»]
B/D218-265[»]
1RINX-ray2.60A/C31-210[»]
B/D218-266[»]
2BQPX-ray1.90A/B31-264[»]
2LTNX-ray1.70A/C31-211[»]
B/D218-269[»]
ProteinModelPortalP02867.
SMRP02867. Positions 31-266.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

MINTMINT-1508409.

Protein family/group databases

Allergome8818. Pis s Agglutinin.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D2.60.120.200. 1 hit.
InterProIPR008985. ConA-like_lec_gl_sf.
IPR013320. ConA-like_subgrp.
IPR016363. Lectin.
IPR000985. Lectin_LegA_CS.
IPR019825. Lectin_legB_Mn/Ca_BS.
IPR001220. Legume_lectin_dom.
[Graphical view]
PfamPF00139. Lectin_legB. 1 hit.
[Graphical view]
PIRSFPIRSF002690. L-type_lectin_plant. 1 hit.
SUPFAMSSF49899. SSF49899. 1 hit.
PROSITEPS00308. LECTIN_LEGUME_ALPHA. 1 hit.
PS00307. LECTIN_LEGUME_BETA. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP02867.

Entry information

Entry nameLEC_PEA
AccessionPrimary (citable) accession number: P02867
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: February 19, 2014
This is version 102 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references