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Protein

Lectin alpha chain

Gene
N/A
Organism
Cratylia argentea (Cratylia floribunda)
Status
Reviewed-Annotation score: Annotation score: 4 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.5 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi8 – 81ManganeseBy similarity
Metal bindingi10 – 101CalciumBy similarity
Metal bindingi10 – 101ManganeseBy similarity
Metal bindingi12 – 121Calcium; via carbonyl oxygenBy similarity
Binding sitei12 – 121CarbohydrateBy similarity
Metal bindingi14 – 141CalciumBy similarity
Metal bindingi19 – 191CalciumBy similarity
Metal bindingi19 – 191ManganeseBy similarity
Metal bindingi24 – 241ManganeseBy similarity
Metal bindingi34 – 341ManganeseBy similarity
Metal bindingi207 – 2071CalciumBy similarity
Binding sitei227 – 2271Carbohydrate; via amide nitrogenBy similarity

GO - Molecular functioni

  • carbohydrate binding Source: UniProtKB
  • 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:
OrganismiCratylia argentea (Cratylia floribunda)
Taxonomic identifieri83131 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsFabalesFabaceaePapilionoideaePhaseoleaeCratylia

Pathology & Biotechi

Toxic dosei

LC(50) is 4.75 µg/ml against the brine shrimp A.salina. LC(50) is 25.5 µg/ml against the aquatic snail B.glabrata.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 236236Lectin alpha chainPRO_0000017588Add
BLAST
Chaini1 – 118118Lectin beta chainPRO_0000017589Add
BLAST
Chaini119 – 236118Lectin gamma chainPRO_0000017590Add
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.

Expressioni

Tissue specificityi

Seed.

Interactioni

Subunit structurei

Equilibrium between homodimer and homotetramer. Oligomerization is pH-dependent with homotetramers forming at pH 6.5 and above.1 Publication

Structurei

Secondary structure

1
236
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi5 – 106Combined sources
Helixi15 – 173Combined sources
Beta strandi24 – 3310Combined sources
Beta strandi35 – 395Combined sources
Beta strandi47 – 559Combined sources
Turni56 – 594Combined sources
Beta strandi60 – 678Combined sources
Turni68 – 703Combined sources
Beta strandi71 – 788Combined sources
Helixi81 – 833Combined sources
Beta strandi87 – 9610Combined sources
Beta strandi105 – 11612Combined sources
Beta strandi118 – 1214Combined sources
Beta strandi123 – 13210Combined sources
Beta strandi140 – 1445Combined sources
Beta strandi154 – 1574Combined sources
Beta strandi169 – 1768Combined sources
Beta strandi186 – 19712Combined sources
Beta strandi201 – 2044Combined sources
Beta strandi208 – 2147Combined sources
Helixi226 – 2283Combined sources
Turni229 – 2313Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2D3PX-ray2.80A/B/C/D1-236[»]
2D3RX-ray2.90A/B/C/D1-236[»]
ProteinModelPortaliP81517.
SMRiP81517. Positions 1-236.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP81517.

Family & Domainsi

Region

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

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.

P81517-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
ADTIVAVELD TYPNTDIGDP NYQHIGINIK SIRSKATTRW NVQDGKVGTA
60 70 80 90 100
HISYNSVAKR LSAIVSYPGG SSATVSYDVD LNNILPEWVR VGLSASTGLY
110 120 130 140 150
KETNTILSWS FTSKLKTNST ADAQSLHFTF NQFSQNPKDL ILQGDASTDS
160 170 180 190 200
DGNLQLTRVS NGSPQSNSVG RALYYAPVHV WDKSAVVASF DATFTFLIKS
210 220 230
TDSDIADGIA WFIANTDSSI PHGSGGRLLG LFPDAN
Length:236
Mass (Da):25,398
Last modified:July 15, 1999 - v1
Checksum:iCA73BC77F4324251
GO

Mass spectrometryi

Molecular mass is 25397±3 Da from positions 1 - 236. Determined by ESI. 1 Publication
Molecular mass is 12847±2 Da from positions 1 - 118. Determined by ESI. 1 Publication
Molecular mass is 12568±2 Da from positions 119 - 236. Determined by ESI. 1 Publication

Cross-referencesi

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2D3PX-ray2.80A/B/C/D1-236[»]
2D3RX-ray2.90A/B/C/D1-236[»]
ProteinModelPortaliP81517.
SMRiP81517. Positions 1-236.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP81517.

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. Cited for: PROTEIN SEQUENCE, SUBUNIT, MASS SPECTROMETRY, CRYSTALLIZATION, PRELIMINARY X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS).
    Tissue: Seed.
  2. "Primary structure and kinetic interaction with glycoproteins of the lectin from seeds of Cratylia floribunda."
    Cavada B.S., Nogueira N.A.P., Farias C.M.A.S., Grangeiro T.B., Romas M.V., Thole H.H., Raida M., Rouge P., Calvete J.J.
    Protein Pept. Lett. 6:27-34(1999)
    Cited for: PROTEIN SEQUENCE.
    Tissue: Seed.
  3. Cited for: FUNCTION.
  4. "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.
  5. "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.
  6. "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.
  7. "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.
  8. "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.
  9. "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: LETHAL CONCENTRATION.

Entry informationi

Entry nameiLECA_CRAAG
AccessioniPrimary (citable) accession number: P81517
Secondary accession number(s): P81636
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: July 15, 1999
Last modified: July 6, 2016
This is version 83 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.
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.