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Protein

Lectin alpha chain

Gene
N/A
Organism
Dioclea sclerocarpa (Dioclea reflexa var. glabrescens)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

D-mannose/D-glucose-binding lectin. Has hemagglutinating activity towards rabbit erythrocytes.1 Publication

pH dependencei

Optimum pH is 6-8 for hemagglutinating activity. Activity is reduced to 50% at pH 8.5.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi8ManganeseBy similarity1
Metal bindingi10CalciumBy similarity1
Metal bindingi10ManganeseBy similarity1
Metal bindingi12Calcium; via carbonyl oxygenBy similarity1
Binding sitei12CarbohydrateBy similarity1
Metal bindingi14CalciumBy similarity1
Metal bindingi19CalciumBy similarity1
Metal bindingi19ManganeseBy similarity1
Metal bindingi24ManganeseBy similarity1
Metal bindingi34ManganeseBy similarity1
Metal bindingi208CalciumBy similarity1
Binding sitei228Carbohydrate; via amide nitrogenBy similarity1

GO - Molecular functioni

  • calcium ion binding Source: UniProtKB
  • glucose binding Source: UniProtKB
  • manganese ion binding Source: UniProtKB
  • mannose binding Source: UniProtKB
Complete GO annotation...

Keywords - Ligandi

Calcium, Lectin, Manganese, Mannose-binding, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Lectin alpha chain1 Publication
Alternative name(s):
DSL1 Publication
Cleaved into the following 2 chains:
Lectin beta chain1 Publication
Lectin gamma chain1 Publication
OrganismiDioclea sclerocarpa (Dioclea reflexa var. glabrescens)
Taxonomic identifieri1176036 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsFabalesFabaceaePapilionoideaePhaseoleaeDioclea

Subcellular locationi

  • Vacuolealeurone grain By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Vacuole

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004179341 – 237Lectin alpha chainAdd BLAST237
ChainiPRO_00004179351 – 118Lectin beta chain1 PublicationAdd BLAST118
ChainiPRO_0000417936119 – 237Lectin gamma chain1 PublicationAdd BLAST119

Post-translational modificationi

The beta and gamma chains are produced by partial proteolytic processing of the lectin alpha chain by an asparaginyl endopeptidase. Mixture of 60% alpha lectin and 40% of its beta and gamma proteolytic fragments.1 Publication

Interactioni

Subunit structurei

Homotetramer.By similarity

Structurei

Secondary structure

1237
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi4 – 10Combined sources7
Helixi15 – 17Combined sources3
Beta strandi24 – 33Combined sources10
Beta strandi35 – 39Combined sources5
Beta strandi48 – 55Combined sources8
Turni56 – 59Combined sources4
Beta strandi60 – 67Combined sources8
Beta strandi72 – 78Combined sources7
Helixi81 – 84Combined sources4
Beta strandi87 – 96Combined sources10
Beta strandi98 – 100Combined sources3
Beta strandi105 – 117Combined sources13
Beta strandi124 – 132Combined sources9
Beta strandi140 – 144Combined sources5
Beta strandi170 – 177Combined sources8
Beta strandi186 – 198Combined sources13
Beta strandi202 – 205Combined sources4
Beta strandi209 – 215Combined sources7
Helixi227 – 229Combined sources3
Turni230 – 232Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4NOTX-ray2.35A1-237[»]
SMRiB3EWJ2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni99 – 100Carbohydrate bindingBy similarity2

Sequence similaritiesi

Belongs to the leguminous lectin family.Sequence analysis

Family and domain databases

Gene3Di2.60.120.200. 2 hits.
InterProiIPR013320. ConA-like_dom.
IPR000985. Lectin_LegA_CS.
IPR019825. Lectin_legB_Mn/Ca_BS.
IPR001220. Legume_lectin_dom.
[Graphical view]
PfamiPF00139. Lectin_legB. 2 hits.
[Graphical view]
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.

B3EWJ2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
ADTIVAVELD SYPNTDIGDP NYPHIGIDIK SIRSKSTARW NMQTGKVGTV
60 70 80 90 100
HISYNSVAKR LSAVVSYSGS SSTTVSYDVD LNNVLPEWVR VGLSATTGLY
110 120 130 140 150
KETNTILSWS FTSKLKTNSI ADENSLHFSF HKFSQNPKDL ILQGDAFTDS
160 170 180 190 200
DGNLQLTKVS SSGDPQGNSV GRALFYAPVH IWEKSAVVAS FDATFTFLIK
210 220 230
SPDREPADGI TFFIANTDTS IPSGSGGRLL GLFPDAN
Length:237
Mass (Da):25,607
Last modified:June 13, 2012 - v1
Checksum:iF33FD269ABF01D6A
GO

Mass spectrometryi

Molecular mass is 25606±2 Da from positions 1 - 237. Determined by ESI. Alpha chain.1 Publication
Molecular mass is 12873±2 Da from positions 1 - 118. Determined by ESI. Beta chain.1 Publication
Molecular mass is 12752±2 Da from positions 119 - 237. Determined by ESI. Gamma chain.1 Publication

Cross-referencesi

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4NOTX-ray2.35A1-237[»]
SMRiB3EWJ2.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

Gene3Di2.60.120.200. 2 hits.
InterProiIPR013320. ConA-like_dom.
IPR000985. Lectin_LegA_CS.
IPR019825. Lectin_legB_Mn/Ca_BS.
IPR001220. Legume_lectin_dom.
[Graphical view]
PfamiPF00139. Lectin_legB. 2 hits.
[Graphical view]
SUPFAMiSSF49899. SSF49899. 1 hit.
PROSITEiPS00308. LECTIN_LEGUME_ALPHA. 1 hit.
PS00307. LECTIN_LEGUME_BETA. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiLECA_DIOSC
AccessioniPrimary (citable) accession number: B3EWJ2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 13, 2012
Last sequence update: June 13, 2012
Last modified: November 2, 2016
This is version 15 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Miscellaneous

Binds one manganese (or another transition metal) ion and one calcium ion. The metal ions are essential for the saccharide-binding and cell-agglutinating activities.

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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.