Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

B3EWQ9

- LECA2_LABPU

UniProt

B3EWQ9 - LECA2_LABPU

(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)

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: UniProtKB-KW

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 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 – 339Combined sources
Beta strandi39 – 413Combined sources
Beta strandi51 – 533Combined sources
Beta strandi68 – 758Combined sources
Beta strandi82 – 843Combined sources
Beta strandi87 – 9711Combined sources
Beta strandi108 – 1169Combined sources
Helixi125 – 1273Combined sources
Turni128 – 1303Combined sources
Beta strandi143 – 1475Combined sources
Beta strandi154 – 1563Combined sources
Beta strandi158 – 16912Combined sources
Beta strandi174 – 1763Combined sources
Beta strandi185 – 1917Combined sources
Turni193 – 1953Combined sources
Beta strandi197 – 2037Combined sources
Turni205 – 2073Combined sources
Beta strandi211 – 2166Combined sources
Turni220 – 2223Combined sources
Beta strandi225 – 23511Combined sources
Beta strandi237 – 2415Combined sources
Beta strandi246 – 25611Combined sources
Beta strandi258 – 2603Combined sources
Beta strandi264 – 2674Combined sources
Beta strandi270 – 2723Combined sources
Turni273 – 2753Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
InterProiIPR013320. ConA-like_dom.
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

        10         20         30         40         50
NNLISFTMKR IVLFLILLTK AASANLISFT FKRFNETNLI LQRDATVSSG
60 70 80 90 100
KLRITKAAEN GVPTAGSLGR AFYSTPIQIW DNTTGTVAAW ATSFTFNLQA
110 120 130 140 150
PNAASPADGL AFALVPVGSQ PKDKGGFLGL FDSKNYASSN QTVAVEFDTF
160 170 180 190 200
YNGGWDPTER HIGIDVNSIK SIKTTSWDFA NGENAEVLIT YDSSTNLLVA
210 220 230 240 250
SLVHPSQKTS FIVSERVDLT SVLPEWVSVG FSATTGLSKG YVETNEVLSW
260 270 280
SFASKISINK EDEENKLLIS NLEGKAINNL A
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:
PDBei
RCSB PDBi
PDBji
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 IPR013320. ConA-like_dom.
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 29, 2014
This is version 10 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