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P02870 (LEC_LENCU) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 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·Web links·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
OrganismLens culinaris (Lentil) (Cicer lens)
Taxonomic identifier3864 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsFabalesFabaceaePapilionoideaeFabeaeLens

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 By similarity.

Subunit structure

Heterotetramer of two alpha and two beta chains.

Post-translational modification

The mature form consists of two chains, alpha and beta, produced by cleavage of the immature protein. These remain cleaved, yet fold together to form one subunit. Ref.4 Ref.6 Ref.7

Miscellaneous

Binds two manganese (or other transition metal) ions and two calcium ions per heterotetramer. The metal ions are essential for the saccharide-binding activity.

Sequence similarities

Belongs to the leguminous lectin family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3030 Ref.2
Chain31 – 210180Lectin beta chain
PRO_0000017619
Propeptide211 – 2177
PRO_0000223477
Chain218 – 26952Lectin alpha chain
PRO_0000017620
Propeptide270 – 2756
PRO_0000223478

Sites

Metal binding1491Manganese
Metal binding1511Calcium
Metal binding1511Manganese
Metal binding1531Calcium; via carbonyl oxygen
Metal binding1551Calcium
Metal binding1591Calcium
Metal binding1591Manganese
Metal binding1661Manganese
Binding site1111Glucose
Binding site1291Glucose; via amide nitrogen
Binding site2461Glucose; via amide nitrogen
Binding site2471Glucose; via amide nitrogen
Site210 – 2112Cleavage
Site217 – 2182Cleavage

Experimental info

Sequence conflict461K → Q AA sequence Ref.2
Sequence conflict47 – 537NLIFQGD → GGRGNSI in AAS55887. Ref.1
Sequence conflict57 – 604TKGK → GKEG AA sequence Ref.2
Sequence conflict66 – 716AVKSTV → VSKETG AA sequence Ref.2
Sequence conflict881G → V AA sequence Ref.2
Sequence conflict96 – 10611SFTFVIDAPSS → NGSQVFRESPNG AA sequence Ref.2
Sequence conflict1121E → G AA sequence Ref.2
Sequence conflict135 – 1362NS → YNG AA sequence Ref.2
Sequence conflict2521H → Q AA sequence Ref.3
Sequence conflict260 – 2689HSELGGTSS → NSQLGHTSK AA sequence Ref.3

Secondary structure

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

Details...

Sequences

Sequence LengthMass (Da)Tools
P02870 [UniParc].

Last modified February 21, 2006. Version 2.
Checksum: 194756B9F1A069C5

FASTA27530,352
        10         20         30         40         50         60 
MASLQTQMIS FYLIFLSILL TTIFFFKVNS TETTSFSITK FSPDQKNLIF QGDGYTTKGK 

        70         80         90        100        110        120 
LTLTKAVKST VGRALYSTPI HIWDRDTGNV ANFVTSFTFV IDAPSSYNVA DEFTFFIAPV 

       130        140        150        160        170        180 
DTKPQTGGGY LGVFNSKEYD KTSQTVAVEF DTFYNAAWDP SNKERHIGID VNSIKSVNTK 

       190        200        210        220        230        240 
SWNLQNGERA NVVIAFNAAT NVLTVTLTYP NSLEEENVTS YTLNEVVPLK DVVPEWVRIG 

       250        260        270 
FSATTGAEFA AHEVHSWSFH SELGGTSSSK QAADA 

« Hide

References

[1]Qureshi I.A., Koundal K.R.
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA], NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 47-275.
[2]"The structure of the lentil (Lens culinaris) lectin. Amino acid sequence determination and prediction of the secondary structure."
Foriers A., Lebrun E., van Rapenbusch R., de Neve R., Strosberg A.D.
J. Biol. Chem. 256:5550-5560(1981) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 31-187.
Tissue: Seed.
[3]"Common ancestor for concanavalin A and lentil lectin?"
Foriers A., de Neve R., Kanarek L., Strosberg A.D.
Proc. Natl. Acad. Sci. U.S.A. 75:1136-1139(1978) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 218-269.
[4]"Crystal structure determination and refinement at 2.3-A resolution of the lentil lectin."
Loris R., Steyaert J., Maes D., Lisgarten J., Pickersgill R., Wyns L.
Biochemistry 32:8772-8781(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: PARTIAL NUCLEOTIDE SEQUENCE [GENOMIC DNA], X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 31-210 AND 218-269 IN COMPLEX WITH ZINC AND MANGANESE IONS, CLEAVAGE SITE.
Tissue: Seed.
[5]Erratum
Loris R., Steyaert J., Maes D., Lisgarten J., Pickersgill R., Wyns L.
Biochemistry 32:14229-14229(1993) [PubMed] [Europe PMC] [Abstract]
[6]"Structural analysis of two crystal forms of lentil lectin at 1.8 A resolution."
Loris R., Van Overberge D., Dao-Thi M.H., Poortmans F., Maene N., Wyns L.
Proteins 20:330-346(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 31-210 AND 218-269 IN COMPLEX WITH SUCROSE; ZINC AND MANGANESE IONS, CLEAVAGE SITE.
[7]"NMR, molecular modeling, and crystallographic studies of lentil lectin-sucrose interaction."
Casset F., Hamelryck T., Loris R., Brisson J.R., Tellier C., Dao-Thi M.H., Wyns L., Poortmans F., Perez S., Imberty A.
J. Biol. Chem. 270:25619-25628(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 31-210 AND 218-269 IN COMPLEX WITH SUCROSE; ZINC AND MANGANESE IONS, CLEAVAGE SITE.
Tissue: Seed.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY547295 Genomic DNA. Translation: AAS55887.1.
DQ005103 mRNA. Translation: AAY21161.1.
PIRA48694.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1LEMX-ray3.00A31-211[»]
B218-269[»]
1LENX-ray1.80A/C31-211[»]
B/D218-269[»]
1LESX-ray1.90A/C31-211[»]
B/D218-269[»]
2LALX-ray1.80A/C31-211[»]
B/D218-269[»]
ProteinModelPortalP02870.
SMRP02870. Positions 31-263.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

MINTMINT-1508422.

Protein family/group databases

Allergome8816. Len c 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

EvolutionaryTraceP02870.

Entry information

Entry nameLEC_LENCU
AccessionPrimary (citable) accession number: P02870
Secondary accession number(s): Q4ZJ64, Q6QDC0
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: February 21, 2006
Last modified: July 9, 2014
This is version 102 of the entry and version 2 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