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B3EWQ9

- LECA2_LABPU

UniProt

B3EWQ9 - LECA2_LABPU

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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

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
Complete GO annotation...

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
Complete GO annotation...

Keywords - Molecular functioni

Antibiotic, Antimicrobial, Fungicide

Keywords - Ligandi

Lectin

Names & Taxonomyi

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 281281Lectin alpha chain
PRO_0000420130Add
BLAST
Chaini1 – 263263Lectin beta chain1 Publication
PRO_0000420131Add
BLAST

Amino acid modifications

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

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

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[»]

Family & Domainsi

Sequence similaritiesi

Belongs to the leguminous lectin family.

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

« Hide

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...

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: Seed.
  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: Seed.
  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: Seed.

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: February 19, 2014
This is version 8 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

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