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B3EWQ9

- LECA2_LABPU

UniProt

B3EWQ9 - LECA2_LABPU

Protein

Lectin alpha chain

Gene
N/A
Organism
Lablab purpureus (Hyacinth bean) (Dolichos lablab)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 9 (01 Oct 2014)
      Sequence version 1 (31 Oct 2012)
      Previous versions | rss
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    Functioni

    D-galactose-binding lectin.1 Publication

    pH dependencei

    Optimum pH is 7.4. No activity between pH 4.0 and pH 6.0, 80% activity at pH 8.0 and 20% activity at pH 9.0.1 Publication

    Temperature dependencei

    Activity stable between 4 and 40 degrees Celsius, declines at higher temperatures and is lost at 90 degrees Celsius.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei263 – 2642Cleavage1 Publication

    GO - Molecular functioni

    1. carbohydrate binding Source: InterPro

    GO - Biological processi

    1. defense response to bacterium Source: UniProtKB-KW
    2. defense response to fungus Source: UniProtKB-KW
    3. killing of cells of other organism Source: UniProtKB-KW

    Keywords - Molecular functioni

    Antibiotic, Antimicrobial, Fungicide

    Keywords - Ligandi

    Lectin

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Lectin alpha chain1 Publication
    Alternative name(s):
    DLL-II1 Publication
    Cleaved into the following chain:
    Lectin beta chain1 Publication
    OrganismiLablab purpureus (Hyacinth bean) (Dolichos lablab)
    Taxonomic identifieri35936 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsFabalesFabaceaePapilionoideaePhaseoleaeLablab

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 281281Lectin alpha chainPRO_0000420130Add
    BLAST
    Chaini1 – 263263Lectin beta chain1 PublicationPRO_0000420131Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi35 – 351N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi82 – 821N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi140 – 1401N-linked (GlcNAc...)Sequence Analysis

    Post-translational modificationi

    Glycosylated.1 Publication
    The beta chain is produced by partial proteolytic processing of the alpha chain.1 Publication

    Keywords - PTMi

    Glycoprotein

    Interactioni

    Subunit structurei

    Tetramer of 2 alpha and 2 beta chains.3 Publications

    Structurei

    Secondary structure

    1
    281
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi25 – 339
    Beta strandi39 – 413
    Beta strandi51 – 533
    Beta strandi68 – 758
    Beta strandi82 – 843
    Beta strandi87 – 9711
    Beta strandi108 – 1169
    Helixi125 – 1273
    Turni128 – 1303
    Beta strandi143 – 1475
    Beta strandi154 – 1563
    Beta strandi158 – 16912
    Beta strandi174 – 1763
    Beta strandi185 – 1917
    Turni193 – 1953
    Beta strandi197 – 2037
    Turni205 – 2073
    Beta strandi211 – 2166
    Turni220 – 2223
    Beta strandi225 – 23511
    Beta strandi237 – 2415
    Beta strandi246 – 25611
    Beta strandi258 – 2603
    Beta strandi264 – 2674
    Beta strandi270 – 2723
    Turni273 – 2753

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3UJOX-ray2.00A/B/C/D1-281[»]
    3UJQX-ray2.06A/B/C/D1-281[»]
    3UK9X-ray3.11A/B/C/D/E/F/G/H1-281[»]
    3UL2X-ray2.50A/B/C/D1-281[»]
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the leguminous lectin family.Sequence Analysis

    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.

    B3EWQ9-1 [UniParc]FASTAAdd to Basket

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    NNLISFTMKR IVLFLILLTK AASANLISFT FKRFNETNLI LQRDATVSSG    50
    KLRITKAAEN GVPTAGSLGR AFYSTPIQIW DNTTGTVAAW ATSFTFNLQA 100
    PNAASPADGL AFALVPVGSQ PKDKGGFLGL FDSKNYASSN QTVAVEFDTF 150
    YNGGWDPTER HIGIDVNSIK SIKTTSWDFA NGENAEVLIT YDSSTNLLVA 200
    SLVHPSQKTS FIVSERVDLT SVLPEWVSVG FSATTGLSKG YVETNEVLSW 250
    SFASKISINK EDEENKLLIS NLEGKAINNL A 281
    Length:281
    Mass (Da):30,422
    Last modified:October 31, 2012 - v1
    Checksum:iCC15AD7445BD170A
    GO

    Mass spectrometryi

    Molecular mass is 30746 Da from positions 1 - 281. Determined by ESI. Alpha chain.1 Publication
    Molecular mass is 28815 Da from positions 1 - 263. Determined by ESI. Beta chain.1 Publication

    Cross-referencesi

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3UJO X-ray 2.00 A/B/C/D 1-281 [» ]
    3UJQ X-ray 2.06 A/B/C/D 1-281 [» ]
    3UK9 X-ray 3.11 A/B/C/D/E/F/G/H 1-281 [» ]
    3UL2 X-ray 2.50 A/B/C/D 1-281 [» ]
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    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. "Complete primary structure of a newly characterized galactose-specific lectin from the seeds of Dolichos lablab."
      Rameshwaram N.R., Karanam N.K., Scharf C., Volker U., Nadimpalli S.K.
      Glycoconj. J. 26:161-172(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE, SUBUNIT, MASS SPECTROMETRY.
      Tissue: Seed1 Publication.
    2. "Affinity purification, physicochemical and immunological characterization of a galactose-specific lectin from the seeds of Dolichos lablab (Indian lablab beans)."
      Latha V.L., Rao R.N., Nadimpalli S.K.
      Protein Expr. Purif. 45:296-306(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 1-10, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, GLYCOSYLATION.
      Tissue: Seed1 Publication.
    3. "Crystallization and preliminary X-ray crystallographic analysis of a galactose-specific lectin from Dolichos lablab."
      Latha V.L., Kulkarni K.A., Rao R.N., Kumar N.S., Suguna K.
      Acta Crystallogr. F 62:163-165(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: CRYSTALLIZATION, PRELIMINARY X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS), SUBUNIT.
      Tissue: Seed1 Publication.

    Entry informationi

    Entry nameiLECA2_LABPU
    AccessioniPrimary (citable) accession number: B3EWQ9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 31, 2012
    Last sequence update: October 31, 2012
    Last modified: October 1, 2014
    This is version 9 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant Protein Annotation Program

    Miscellaneousi

    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