Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P02870

- LEC_LENCU

UniProt

P02870 - LEC_LENCU

Protein

Lectin

Gene
N/A
Organism
Lens culinaris (Lentil) (Cicer lens)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 103 (01 Oct 2014)
      Sequence version 2 (21 Feb 2006)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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

    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 – 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.
    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.
    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

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti46 – 461K → Q AA sequence (PubMed:7240155)Curated
    Sequence conflicti47 – 537NLIFQGD → GGRGNSI in AAS55887. 1 PublicationCurated
    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:
    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: October 1, 2014
    This is version 103 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