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Protein

Lectin

Gene
N/A
Organism
Lens culinaris (Lentil) (Cicer lens)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

D-mannose specific lectin.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei111 – 1111Glucose
Binding sitei129 – 1291Glucose; via amide nitrogen
Metal bindingi149 – 1491Manganese
Metal bindingi151 – 1511Calcium
Metal bindingi151 – 1511Manganese
Metal bindingi153 – 1531Calcium; via carbonyl oxygen
Metal bindingi155 – 1551Calcium
Metal bindingi159 – 1591Calcium
Metal bindingi159 – 1591Manganese
Metal bindingi166 – 1661Manganese
Sitei210 – 2112Cleavage
Sitei217 – 2182Cleavage
Binding sitei246 – 2461Glucose; via amide nitrogen
Binding sitei247 – 2471Glucose; via amide nitrogen

GO - Molecular functioni

  • calcium ion binding Source: UniProtKB
  • carbohydrate binding Source: UniProtKB
  • manganese ion binding Source: UniProtKB
  • mannose binding Source: UniProtKB-KW

GO - Biological processi

  • carbohydrate mediated signaling Source: UniProtKB
Complete GO annotation...

Keywords - Ligandi

Calcium, Lectin, Manganese, Mannose-binding, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Lectin
Cleaved into the following 2 chains:
OrganismiLens culinaris (Lentil) (Cicer lens)
Taxonomic identifieri3864 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsFabalesFabaceaePapilionoideaeFabeaeLens

Pathology & Biotechi

Protein family/group databases

Allergomei8816. Len c Agglutinin.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 30301 PublicationAdd
BLAST
Chaini31 – 210180Lectin beta chainPRO_0000017619Add
BLAST
Propeptidei211 – 21771 PublicationPRO_0000223477
Chaini218 – 26952Lectin alpha chainPRO_0000017620Add
BLAST
Propeptidei270 – 2756PRO_0000223478

Post-translational modificationi

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.3 Publications

Interactioni

Subunit structurei

Heterotetramer of two alpha and two beta chains.3 Publications

Protein-protein interaction databases

MINTiMINT-1508422.

Structurei

Secondary structure

1
275
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi32 – 4110Combined sources
Beta strandi48 – 525Combined sources
Beta strandi55 – 573Combined sources
Beta strandi59 – 646Combined sources
Beta strandi71 – 788Combined sources
Turni85 – 873Combined sources
Beta strandi92 – 10211Combined sources
Beta strandi104 – 1085Combined sources
Beta strandi112 – 1198Combined sources
Helixi128 – 1303Combined sources
Turni131 – 1333Combined sources
Turni141 – 1433Combined sources
Beta strandi146 – 1516Combined sources
Turni156 – 1583Combined sources
Beta strandi166 – 17510Combined sources
Beta strandi177 – 1815Combined sources
Beta strandi189 – 1979Combined sources
Turni198 – 2014Combined sources
Beta strandi202 – 2098Combined sources
Beta strandi219 – 2268Combined sources
Helixi229 – 2324Combined sources
Beta strandi235 – 24410Combined sources
Beta strandi246 – 2483Combined sources
Beta strandi251 – 26313Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP02870.
SMRiP02870. Positions 31-263.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP02870.

Family & Domainsi

Sequence similaritiesi

Belongs to the leguminous lectin family.Curated

Keywords - Domaini

Signal

Family and domain databases

Gene3Di2.60.120.200. 1 hit.
InterProiIPR013320. ConA-like_dom.
IPR016363. Lectin.
IPR000985. Lectin_LegA_CS.
IPR019825. Lectin_legB_Mn/Ca_BS.
IPR001220. Legume_lectin_dom.
[Graphical view]
PfamiPF00139. Lectin_legB. 1 hit.
[Graphical view]
PIRSFiPIRSF002690. L-type_lectin_plant. 1 hit.
SUPFAMiSSF49899. SSF49899. 1 hit.
PROSITEiPS00308. LECTIN_LEGUME_ALPHA. 1 hit.
PS00307. LECTIN_LEGUME_BETA. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P02870-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASLQTQMIS FYLIFLSILL TTIFFFKVNS TETTSFSITK FSPDQKNLIF
60 70 80 90 100
QGDGYTTKGK LTLTKAVKST VGRALYSTPI HIWDRDTGNV ANFVTSFTFV
110 120 130 140 150
IDAPSSYNVA DEFTFFIAPV DTKPQTGGGY LGVFNSKEYD KTSQTVAVEF
160 170 180 190 200
DTFYNAAWDP SNKERHIGID VNSIKSVNTK SWNLQNGERA NVVIAFNAAT
210 220 230 240 250
NVLTVTLTYP NSLEEENVTS YTLNEVVPLK DVVPEWVRIG FSATTGAEFA
260 270
AHEVHSWSFH SELGGTSSSK QAADA
Length:275
Mass (Da):30,352
Last modified:February 21, 2006 - v2
Checksum:i194756B9F1A069C5
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti46 – 461K → Q AA sequence (PubMed:7240155).Curated
Sequence conflicti47 – 537NLIFQGD → GGRGNSI in AAS55887 (Ref. 1) Curated
Sequence conflicti57 – 604TKGK → GKEG AA sequence (PubMed:7240155).Curated
Sequence conflicti66 – 716AVKSTV → VSKETG AA sequence (PubMed:7240155).Curated
Sequence conflicti88 – 881G → V AA sequence (PubMed:7240155).Curated
Sequence conflicti96 – 10611SFTFVIDAPSS → NGSQVFRESPNG AA sequence (PubMed:7240155).CuratedAdd
BLAST
Sequence conflicti112 – 1121E → G AA sequence (PubMed:7240155).Curated
Sequence conflicti135 – 1362NS → YNG AA sequence (PubMed:7240155).Curated
Sequence conflicti252 – 2521H → Q AA sequence (PubMed:274705).Curated
Sequence conflicti260 – 2689HSELGGTSS → NSQLGHTSK AA sequence (PubMed:274705).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY547295 Genomic DNA. Translation: AAS55887.1.
DQ005103 mRNA. Translation: AAY21161.1.
PIRiA48694.

Cross-referencesi

Web resourcesi

ProZyme technical fact sheet
Functional Glycomics Gateway - Glycan Binding

LcH

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY547295 Genomic DNA. Translation: AAS55887.1.
DQ005103 mRNA. Translation: AAY21161.1.
PIRiA48694.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP02870.
SMRiP02870. Positions 31-263.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

MINTiMINT-1508422.

Protein family/group databases

Allergomei8816. Len c Agglutinin.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP02870.

Family and domain databases

Gene3Di2.60.120.200. 1 hit.
InterProiIPR013320. ConA-like_dom.
IPR016363. Lectin.
IPR000985. Lectin_LegA_CS.
IPR019825. Lectin_legB_Mn/Ca_BS.
IPR001220. Legume_lectin_dom.
[Graphical view]
PfamiPF00139. Lectin_legB. 1 hit.
[Graphical view]
PIRSFiPIRSF002690. L-type_lectin_plant. 1 hit.
SUPFAMiSSF49899. SSF49899. 1 hit.
PROSITEiPS00308. LECTIN_LEGUME_ALPHA. 1 hit.
PS00307. LECTIN_LEGUME_BETA. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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. 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. "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.
  6. "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.

Entry informationi

Entry nameiLEC_LENCU
AccessioniPrimary (citable) accession number: P02870
Secondary accession number(s): Q4ZJ64, Q6QDC0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: February 21, 2006
Last modified: November 26, 2014
This is version 105 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

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.

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.