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B3EWQ9 (LECA2_LABPU) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 8. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Lectin alpha chain
Alternative name(s):
DLL-II

Cleaved into the following chain:

  1. Lectin beta chain
OrganismLablab purpureus (Hyacinth bean) (Dolichos lablab)
Taxonomic identifier35936 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsFabalesFabaceaePapilionoideaePhaseoleaeLablab

Protein attributes

Sequence length281 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

D-galactose-binding lectin. Ref.2

Subunit structure

Tetramer of 2 alpha and 2 beta chains. Ref.1 Ref.2 Ref.3

Post-translational modification

Glycosylated. Ref.2

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

Sequence similarities

Belongs to the leguminous lectin family.

Biophysicochemical properties

pH dependence:

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. Ref.2

Temperature dependence:

Activity stable between 4 and 40 degrees Celsius, declines at higher temperatures and is lost at 90 degrees Celsius. Ref.2

Mass spectrometry

Molecular mass is 30746 Da from positions 1 - 281. Determined by ESI. Alpha chain. Ref.1

Molecular mass is 28815 Da from positions 1 - 263. Determined by ESI. Beta chain. Ref.1

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 281281Lectin alpha chain
PRO_0000420130
Chain1 – 263263Lectin beta chain Ref.1
PRO_0000420131

Sites

Site263 – 2642Cleavage Ref.1

Amino acid modifications

Glycosylation351N-linked (GlcNAc...) Potential
Glycosylation821N-linked (GlcNAc...) Potential
Glycosylation1401N-linked (GlcNAc...) Potential

Secondary structure

................................................... 281
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
B3EWQ9 [UniParc].

Last modified October 31, 2012. Version 1.
Checksum: CC15AD7445BD170A

FASTA28130,422
        10         20         30         40         50         60 
NNLISFTMKR IVLFLILLTK AASANLISFT FKRFNETNLI LQRDATVSSG KLRITKAAEN 

        70         80         90        100        110        120 
GVPTAGSLGR AFYSTPIQIW DNTTGTVAAW ATSFTFNLQA PNAASPADGL AFALVPVGSQ 

       130        140        150        160        170        180 
PKDKGGFLGL FDSKNYASSN QTVAVEFDTF YNGGWDPTER HIGIDVNSIK SIKTTSWDFA 

       190        200        210        220        230        240 
NGENAEVLIT YDSSTNLLVA SLVHPSQKTS FIVSERVDLT SVLPEWVSVG FSATTGLSKG 

       250        260        270        280 
YVETNEVLSW SFASKISINK EDEENKLLIS NLEGKAINNL A 

« Hide

References

[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.
+Additional computationally mapped references.

Cross-references

3D structure databases

PDBe
RCSB PDB
PDBj
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[»]
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D2.60.120.200. 1 hit.
InterProIPR008985. 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]
PfamPF00139. Lectin_legB. 1 hit.
[Graphical view]
PIRSFPIRSF002690. L-type_lectin_plant. 1 hit.
SUPFAMSSF49899. SSF49899. 1 hit.
PROSITEPS00308. LECTIN_LEGUME_ALPHA. 1 hit.
PS00307. LECTIN_LEGUME_BETA. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameLECA2_LABPU
AccessionPrimary (citable) accession number: B3EWQ9
Entry history
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 statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references