Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
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)DescriptionActionsGraphical viewLength
Binding sitei111Glucose1
Binding sitei129Glucose; via amide nitrogen1
Metal bindingi149Manganese1
Metal bindingi151Calcium1
Metal bindingi151Manganese1
Metal bindingi153Calcium; via carbonyl oxygen1
Metal bindingi155Calcium1
Metal bindingi159Calcium1
Metal bindingi159Manganese1
Metal bindingi166Manganese1
Binding sitei246Glucose; via amide nitrogen1
Binding sitei247Glucose; via amide nitrogen1

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)DescriptionActionsGraphical viewLength
Signal peptidei1 – 301 PublicationAdd BLAST30
ChainiPRO_000001761931 – 210Lectin beta chainAdd BLAST180
PropeptideiPRO_0000223477211 – 2171 Publication7
ChainiPRO_0000017620218 – 269Lectin alpha chainAdd BLAST52
PropeptideiPRO_0000223478270 – 2756

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei210 – 211Cleavage2
Sitei217 – 218Cleavage2

Proteomic databases

PRIDEiP02870.

Interactioni

Subunit structurei

Heterotetramer of two alpha and two beta chains.3 Publications

Protein-protein interaction databases

MINTiMINT-1508422.

Structurei

Secondary structure

1275
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi32 – 41Combined sources10
Beta strandi48 – 52Combined sources5
Beta strandi55 – 57Combined sources3
Beta strandi59 – 64Combined sources6
Beta strandi71 – 78Combined sources8
Turni85 – 87Combined sources3
Beta strandi92 – 102Combined sources11
Beta strandi104 – 108Combined sources5
Beta strandi112 – 119Combined sources8
Helixi128 – 130Combined sources3
Turni131 – 133Combined sources3
Turni141 – 143Combined sources3
Beta strandi146 – 151Combined sources6
Turni156 – 158Combined sources3
Beta strandi166 – 175Combined sources10
Beta strandi177 – 181Combined sources5
Beta strandi189 – 197Combined sources9
Turni198 – 201Combined sources4
Beta strandi202 – 209Combined sources8
Beta strandi219 – 226Combined sources8
Helixi229 – 232Combined sources4
Beta strandi235 – 244Combined sources10
Beta strandi246 – 248Combined sources3
Beta strandi251 – 263Combined sources13

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
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. L-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)DescriptionActionsGraphical viewLength
Sequence conflicti46K → Q AA sequence (PubMed:7240155).Curated1
Sequence conflicti47 – 53NLIFQGD → GGRGNSI in AAS55887 (Ref. 1) Curated7
Sequence conflicti57 – 60TKGK → GKEG AA sequence (PubMed:7240155).Curated4
Sequence conflicti66 – 71AVKSTV → VSKETG AA sequence (PubMed:7240155).Curated6
Sequence conflicti88G → V AA sequence (PubMed:7240155).Curated1
Sequence conflicti96 – 106SFTFVIDAPSS → NGSQVFRESPNG AA sequence (PubMed:7240155).CuratedAdd BLAST11
Sequence conflicti112E → G AA sequence (PubMed:7240155).Curated1
Sequence conflicti135 – 136NS → YNG AA sequence (PubMed:7240155).Curated2
Sequence conflicti252H → Q AA sequence (PubMed:274705).Curated1
Sequence conflicti260 – 268HSELGGTSS → NSQLGHTSK AA sequence (PubMed:274705).Curated9

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

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
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

MINTiMINT-1508422.

Protein family/group databases

Allergomei8816. Len c Agglutinin.

Proteomic databases

PRIDEiP02870.

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. L-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...

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 2, 2016
This is version 113 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

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 one 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.