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Protein

Lectin alpha chain

Gene
N/A
Organism
Dioclea grandiflora (Mucana)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

D-mannose/D-glucose-binding lectin. Has anti-inflammatory activity in rats. Induces histamine release in mast cells from rat. Induces lymphocyte proliferation and IFNG production. Shows toxicity against the aquatic snail B.glabrata at concentrations higher than 50 µg/ml.6 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi8Manganese1
Metal bindingi10Calcium2 Publications1
Metal bindingi10Manganese1
Metal bindingi12Calcium; via carbonyl oxygen2 Publications1
Binding sitei12Carbohydrate1 Publication1
Metal bindingi14Calcium2 Publications1
Metal bindingi19Calcium2 Publications1
Metal bindingi19Manganese1
Metal bindingi24Manganese1
Metal bindingi34ManganeseBy similarity1
Metal bindingi208CalciumBy similarity1
Binding sitei228Carbohydrate; via amide nitrogen1 Publication1

GO - Molecular functioni

  • carbohydrate binding Source: UniProtKB
  • identical protein binding Source: IntAct
  • mannose binding Source: UniProtKB-KW
  • metal ion binding Source: UniProtKB-KW
Complete GO annotation...

Keywords - Ligandi

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

Names & Taxonomyi

Protein namesi
Recommended name:
Lectin alpha chain
Cleaved into the following 2 chains:
OrganismiDioclea grandiflora (Mucana)
Taxonomic identifieri3837 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsFabalesFabaceaePapilionoideaePhaseoleaeDioclea

Pathology & Biotechi

Toxic dosei

LC(50) is 2.52 µg/ml against the brine shrimp A.salina.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000175971 – 237Lectin alpha chainAdd BLAST237
ChainiPRO_00000175981 – 118Lectin beta chainAdd BLAST118
ChainiPRO_0000017599119 – 237Lectin gamma chainAdd 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.

Interactioni

Subunit structurei

Homotetramer.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself3EBI-11191228,EBI-11191228

GO - Molecular functioni

  • identical protein binding Source: IntAct

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 strandi46 – 55Combined sources10
Turni56 – 59Combined sources4
Beta strandi60 – 67Combined sources8
Beta strandi73 – 78Combined sources6
Helixi81 – 83Combined sources3
Beta strandi87 – 96Combined sources10
Beta strandi98 – 100Combined sources3
Beta strandi105 – 116Combined sources12
Beta strandi118 – 121Combined sources4
Beta strandi124 – 132Combined sources9
Beta strandi140 – 144Combined sources5
Beta strandi150 – 152Combined sources3
Beta strandi154 – 157Combined sources4
Beta strandi161 – 163Combined sources3
Beta strandi170 – 177Combined sources8
Beta strandi187 – 198Combined sources12
Beta strandi202 – 205Combined sources4
Beta strandi209 – 216Combined sources8
Helixi227 – 229Combined sources3
Turni230 – 232Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1DGLX-ray2.40A/B1-237[»]
1VLNX-ray2.40A/B/C/D/E/F/G/H138-237[»]
2GDFX-ray2.40A/B/C/D1-237[»]
2JE9X-ray2.10A/B/C/D1-237[»]
2JECX-ray2.00A/B/C/D1-237[»]
4Z8BX-ray1.95A1-237[»]
ProteinModelPortaliP08902.
SMRiP08902.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP08902.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni99 – 100Carbohydrate binding2

Sequence similaritiesi

Belongs to the leguminous lectin family.Curated

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.

P08902-1 [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
DGNLELTKVS SSGDPQGNSV GRALFYAPVH IWESSAVVAS FDATFTFLIK
210 220 230
SPDREPADGI TFFIANTDTS IPSGSGGRLL GLFPDAN
Length:237
Mass (Da):25,567
Last modified:February 2, 2004 - v2
Checksum:iAF27C8A9B138861D
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti10D → N AA sequence (PubMed:6383825).Curated1
Sequence conflicti10D → N AA sequence (Ref. 3) Curated1
Sequence conflicti123E → A AA sequence (PubMed:6383825).Curated1
Sequence conflicti131H → N AA sequence (PubMed:6383825).Curated1
Sequence conflicti131H → N AA sequence (Ref. 3) Curated1
Sequence conflicti132K → Q AA sequence (PubMed:6383825).Curated1
Sequence conflicti132K → Q AA sequence (Ref. 3) Curated1
Sequence conflicti184S → K AA sequence (PubMed:10082964).Curated1
Sequence conflicti196T → I AA sequence (PubMed:6383825).Curated1
Sequence conflicti196T → W AA sequence (PubMed:6383825).Curated1
Sequence conflicti204R → H AA sequence (PubMed:6383825).Curated1
Sequence conflicti204R → H AA sequence (Ref. 3) Curated1

Mass spectrometryi

Molecular mass is 26602±4 Da from positions 1 - 237. Determined by ESI. 1 Publication
Molecular mass is 12872±2 Da from positions 1 - 118. Determined by ESI. 1 Publication
Molecular mass is 12752±2 Da from positions 119 - 237. Determined by ESI. 1 Publication

Sequence databases

PIRiJU0176.

Cross-referencesi

Sequence databases

PIRiJU0176.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1DGLX-ray2.40A/B1-237[»]
1VLNX-ray2.40A/B/C/D/E/F/G/H138-237[»]
2GDFX-ray2.40A/B/C/D1-237[»]
2JE9X-ray2.10A/B/C/D1-237[»]
2JECX-ray2.00A/B/C/D1-237[»]
4Z8BX-ray1.95A1-237[»]
ProteinModelPortaliP08902.
SMRiP08902.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP08902.

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_DIOGR
AccessioniPrimary (citable) accession number: P08902
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: February 2, 2004
Last modified: November 2, 2016
This is version 106 of the entry and version 2 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.
Is being tested as a molluscicide with potential application in controlling schistosomiasis. The causative agent of schistosomiasis depends on freshwater snails of the genus Biomphalaria as hosts during its larval stages.

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.