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P02870

- LEC_LENCU

UniProt

P02870 - LEC_LENCU

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Protein

Lectin

Gene
N/A
Organism
Lens culinaris (Lentil) (Cicer lens)
Status
Reviewed - 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

  1. calcium ion binding Source: UniProtKB
  2. carbohydrate binding Source: UniProtKB
  3. manganese ion binding Source: UniProtKB
  4. mannose binding Source: UniProtKB-KW

GO - Biological processi

  1. 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 – 2177PRO_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.

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 – 4110
Beta strandi48 – 525
Beta strandi55 – 573
Beta strandi59 – 646
Beta strandi71 – 788
Turni85 – 873
Beta strandi92 – 10211
Beta strandi104 – 1085
Beta strandi112 – 1198
Helixi128 – 1303
Turni131 – 1333
Turni141 – 1433
Beta strandi146 – 1516
Turni156 – 1583
Beta strandi166 – 17510
Beta strandi177 – 1815
Beta strandi189 – 1979
Turni198 – 2014
Beta strandi202 – 2098
Beta strandi219 – 2268
Helixi229 – 2324
Beta strandi235 – 24410
Beta strandi246 – 2483
Beta strandi251 – 26313

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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.

Miscellaneous databases

EvolutionaryTraceiP02870.

Family & Domainsi

Sequence similaritiesi

Belongs to the leguminous lectin family.

Keywords - Domaini

Signal

Family and domain databases

Gene3Di2.60.120.200. 1 hit.
InterProiIPR008985. 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]
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

MASLQTQMIS FYLIFLSILL TTIFFFKVNS TETTSFSITK FSPDQKNLIF    50
QGDGYTTKGK LTLTKAVKST VGRALYSTPI HIWDRDTGNV ANFVTSFTFV 100
IDAPSSYNVA DEFTFFIAPV DTKPQTGGGY LGVFNSKEYD KTSQTVAVEF 150
DTFYNAAWDP SNKERHIGID VNSIKSVNTK SWNLQNGERA NVVIAFNAAT 200
NVLTVTLTYP NSLEEENVTS YTLNEVVPLK DVVPEWVRIG FSATTGAEFA 250
AHEVHSWSFH SELGGTSSSK QAADA 275
Length:275
Mass (Da):30,352
Last modified:February 21, 2006 - v2
Checksum:i194756B9F1A069C5
GO

Sequence conflict

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

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
AY547295 Genomic DNA. Translation: AAS55887.1 .
DQ005103 mRNA. Translation: AAY21161.1 .
PIRi A48694.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1LEM X-ray 3.00 A 31-211 [» ]
B 218-269 [» ]
1LEN X-ray 1.80 A/C 31-211 [» ]
B/D 218-269 [» ]
1LES X-ray 1.90 A/C 31-211 [» ]
B/D 218-269 [» ]
2LAL X-ray 1.80 A/C 31-211 [» ]
B/D 218-269 [» ]
ProteinModelPortali P02870.
SMRi P02870. Positions 31-263.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

MINTi MINT-1508422.

Protein family/group databases

Allergomei 8816. Len c Agglutinin.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Miscellaneous databases

EvolutionaryTracei P02870.

Family and domain databases

Gene3Di 2.60.120.200. 1 hit.
InterProi IPR008985. 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 ]
Pfami PF00139. Lectin_legB. 1 hit.
[Graphical view ]
PIRSFi PIRSF002690. L-type_lectin_plant. 1 hit.
SUPFAMi SSF49899. SSF49899. 1 hit.
PROSITEi PS00308. LECTIN_LEGUME_ALPHA. 1 hit.
PS00307. LECTIN_LEGUME_BETA. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: July 9, 2014
This is version 102 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

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