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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)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi8 – 81Manganese
Metal bindingi10 – 101Calcium2 Publications
Metal bindingi10 – 101Manganese
Metal bindingi12 – 121Calcium; via carbonyl oxygen2 Publications
Binding sitei12 – 121Carbohydrate1 Publication
Metal bindingi14 – 141Calcium2 Publications
Metal bindingi19 – 191Calcium2 Publications
Metal bindingi19 – 191Manganese
Metal bindingi24 – 241Manganese
Metal bindingi34 – 341ManganeseBy similarity
Metal bindingi208 – 2081CalciumBy similarity
Binding sitei228 – 2281Carbohydrate; via amide nitrogen1 Publication

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)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 237237Lectin alpha chainPRO_0000017597Add
BLAST
Chaini1 – 118118Lectin beta chainPRO_0000017598Add
BLAST
Chaini119 – 237119Lectin gamma chainPRO_0000017599Add
BLAST

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

1
237
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 107Combined sources
Helixi15 – 173Combined sources
Beta strandi24 – 3310Combined sources
Beta strandi35 – 395Combined sources
Beta strandi46 – 5510Combined sources
Turni56 – 594Combined sources
Beta strandi60 – 678Combined sources
Beta strandi73 – 786Combined sources
Helixi81 – 833Combined sources
Beta strandi87 – 9610Combined sources
Beta strandi98 – 1003Combined sources
Beta strandi105 – 11612Combined sources
Beta strandi118 – 1214Combined sources
Beta strandi124 – 1329Combined sources
Beta strandi140 – 1445Combined sources
Beta strandi150 – 1523Combined sources
Beta strandi154 – 1574Combined sources
Beta strandi161 – 1633Combined sources
Beta strandi170 – 1778Combined sources
Beta strandi187 – 19812Combined sources
Beta strandi202 – 2054Combined sources
Beta strandi209 – 2168Combined sources
Helixi227 – 2293Combined sources
Turni230 – 2323Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 1-237.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP08902.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni99 – 1002Carbohydrate binding

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti10 – 101D → N AA sequence (PubMed:6383825).Curated
Sequence conflicti10 – 101D → N AA sequence (Ref. 3) Curated
Sequence conflicti123 – 1231E → A AA sequence (PubMed:6383825).Curated
Sequence conflicti131 – 1311H → N AA sequence (PubMed:6383825).Curated
Sequence conflicti131 – 1311H → N AA sequence (Ref. 3) Curated
Sequence conflicti132 – 1321K → Q AA sequence (PubMed:6383825).Curated
Sequence conflicti132 – 1321K → Q AA sequence (Ref. 3) Curated
Sequence conflicti184 – 1841S → K AA sequence (PubMed:10082964).Curated
Sequence conflicti196 – 1961T → I AA sequence (PubMed:6383825).Curated
Sequence conflicti196 – 1961T → W AA sequence (PubMed:6383825).Curated
Sequence conflicti204 – 2041R → H AA sequence (PubMed:6383825).Curated
Sequence conflicti204 – 2041R → H AA sequence (Ref. 3) Curated

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
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. Positions 1-237.
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...

Publicationsi

  1. "The complete amino acid sequence of the major alpha subunit of the lectin from the seeds of Dioclea grandiflora (Mart)."
    Richardson M., Campos F.D.A.P., Moreira R.A., Ainouz I.L., Begbie R., Watt W.B., Pusztai A.
    Eur. J. Biochem. 144:101-111(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE.
    Tissue: Seed.
  2. Cited for: PROTEIN SEQUENCE, MASS SPECTROMETRY.
    Tissue: Seed.
  3. "The isolation and amino acid sequence of the beta- and gamma-subunits of the lectin from the seeds of Dioclea grandiflora."
    Ainouz I.L., Moreira R.A., Campos F.D.A.P., Richardson M., Begbie R., Stewart J.C., Watt W.B., Pusztai A.
    Phytochemistry 26:1435-1440(1987)
    Cited for: PROTEIN SEQUENCE OF 1-23; 37-107; 110-151; 159-184 AND 201-237.
    Tissue: Seed.
  4. Cited for: FUNCTION.
  5. "Histamine release induced by glucose (mannose)-specific lectins isolated from Brazilian beans. Comparison with concanavalin A."
    Gomes J.C., Ferreira R.R., Cavada B.S., Moreira R.A., Oliveira J.T.
    Agents Actions 41:132-135(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CALCIUM-BINDING.
  6. "Anti-inflammatory effect of glucose-mannose binding lectins isolated from Brazilian beans."
    Assreuy A.M., Shibuya M.D., Martins G.J., De Souza M.L., Cavada B.S., Moreira R.A., Oliveira J.T., Ribeiro R.A., Flores C.A.
    Mediators Inflamm. 6:201-210(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  7. "Diocleinae lectins are a group of proteins with conserved binding sites for the core trimannoside of asparagine-linked oligosaccharides and differential specificities for complex carbohydrates."
    Dam T.K., Cavada B.S., Grangeiro T.B., Santos C.F., de Sousa F.A.M., Oscarson S., Brewer C.F.
    J. Biol. Chem. 273:12082-12088(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  8. "Demonstration of a conserved histidine and two water ligands at the Mn2+ site in Diocleinae lectins by pulsed EPR spectroscopy."
    Lee H.C., Goroncy A.K., Peisach J., Cavada B.S., Grangeiro T.B., Ramos M.V., Sampaio A.H., Dam T.K., Brewer C.F.
    Biochemistry 39:2340-2346(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: MANGANESE-BINDING.
  9. "Thermodynamic binding studies of lectins from the diocleinae subtribe to deoxy analogs of the core trimannoside of asparagine-linked oligosaccharides."
    Dam T.K., Cavada B.S., Grangeiro T.B., Santos C.F., Ceccatto V.M., de Sousa F.A., Oscarson S., Brewer C.F.
    J. Biol. Chem. 275:16119-16126(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  10. "Toxicity of some glucose/mannose-binding lectins to Biomphalaria glabrata and Artemia salina."
    dos Santos A.F., Cavada B.S., da Rocha B.A., do Nascimento K.S., Sant'Ana A.E.
    Bioresour. Technol. 101:794-798(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, LETHAL CONCENTRATION.
  11. Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEX WITH CALCIUM AND MANGANESE IONS.
  12. "Crystal structure of the lectin from Dioclea grandiflora complexed with core trimannoside of asparagine-linked carbohydrates."
    Rozwarski D.A., Swami B.M., Brewer C.F., Sacchettini J.C.
    J. Biol. Chem. 273:32818-32825(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEX WITH CARBOHYDRATE; CALCIUM AND MANGANESE IONS.

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: January 20, 2016
This is version 104 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.