UniProtKB - P81517 (LECA_CRAAG)
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Protein
Lectin alpha chain
Gene
N/A
Organism
Cratylia argentea (Cratylia floribunda)
Status
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
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.
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Metal bindingi | 8 | ManganeseBy similarity | 1 | |
Metal bindingi | 10 | CalciumBy similarity | 1 | |
Metal bindingi | 10 | ManganeseBy similarity | 1 | |
Metal bindingi | 12 | Calcium; via carbonyl oxygenBy similarity | 1 | |
Binding sitei | 12 | CarbohydrateBy similarity | 1 | |
Metal bindingi | 14 | CalciumBy similarity | 1 | |
Metal bindingi | 19 | CalciumBy similarity | 1 | |
Metal bindingi | 19 | ManganeseBy similarity | 1 | |
Metal bindingi | 24 | ManganeseBy similarity | 1 | |
Metal bindingi | 34 | ManganeseBy similarity | 1 | |
Metal bindingi | 207 | CalciumBy similarity | 1 | |
Binding sitei | 227 | Carbohydrate; via amide nitrogenBy similarity | 1 |
GO - Molecular functioni
- carbohydrate binding Source: UniProtKB
- mannose binding Source: UniProtKB-KW
- metal ion binding Source: UniProtKB-KW
Keywordsi
Ligand | Calcium, Lectin, Manganese, Mannose-binding, Metal-binding |
Names & Taxonomyi
Protein namesi | Recommended name: Lectin alpha chainCleaved into the following 2 chains: |
Organismi | Cratylia argentea (Cratylia floribunda) |
Taxonomic identifieri | 83131 [NCBI] |
Taxonomic lineagei | Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › Gunneridae › Pentapetalae › rosids › fabids › Fabales › Fabaceae › Papilionoideae › Phaseoleae › Cratylia |
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 key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000017588 | 1 – 236 | Lectin alpha chainAdd BLAST | 236 | |
ChainiPRO_0000017589 | 1 – 118 | Lectin beta chainAdd BLAST | 118 | |
ChainiPRO_0000017590 | 119 – 236 | Lectin gamma chainAdd BLAST | 118 |
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
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more detailsFeature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Beta strandi | 5 – 10 | Combined sources | 6 | |
Helixi | 15 – 17 | Combined sources | 3 | |
Beta strandi | 24 – 33 | Combined sources | 10 | |
Beta strandi | 35 – 39 | Combined sources | 5 | |
Beta strandi | 47 – 55 | Combined sources | 9 | |
Turni | 56 – 59 | Combined sources | 4 | |
Beta strandi | 60 – 67 | Combined sources | 8 | |
Turni | 68 – 70 | Combined sources | 3 | |
Beta strandi | 71 – 78 | Combined sources | 8 | |
Helixi | 81 – 83 | Combined sources | 3 | |
Beta strandi | 87 – 96 | Combined sources | 10 | |
Beta strandi | 105 – 116 | Combined sources | 12 | |
Beta strandi | 118 – 121 | Combined sources | 4 | |
Beta strandi | 123 – 132 | Combined sources | 10 | |
Beta strandi | 140 – 144 | Combined sources | 5 | |
Beta strandi | 154 – 157 | Combined sources | 4 | |
Beta strandi | 169 – 176 | Combined sources | 8 | |
Beta strandi | 186 – 197 | Combined sources | 12 | |
Beta strandi | 201 – 204 | Combined sources | 4 | |
Beta strandi | 208 – 214 | Combined sources | 7 | |
Helixi | 226 – 228 | Combined sources | 3 | |
Turni | 229 – 231 | Combined sources | 3 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
2D3P | X-ray | 2.80 | A/B/C/D | 1-236 | [»] | |
2D3R | X-ray | 2.90 | A/B/C/D | 1-236 | [»] | |
ProteinModelPortali | P81517 | |||||
SMRi | P81517 | |||||
ModBasei | Search... | |||||
MobiDBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P81517 |
Family & Domainsi
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 99 – 100 | Carbohydrate bindingBy similarity | 2 |
Sequence similaritiesi
Belongs to the leguminous lectin family.Curated
Family and domain databases
CDDi | cd06899 lectin_legume_LecRK_Arcelin_Co, 1 hit |
InterProi | View protein in InterPro IPR013320 ConA-like_dom_sf IPR016363 L-lectin IPR000985 Lectin_LegA_CS IPR019825 Lectin_legB_Mn/Ca_BS IPR001220 Legume_lectin_dom |
Pfami | View protein in Pfam PF00139 Lectin_legB, 2 hits |
PIRSFi | PIRSF002690 L-type_lectin_plant, 1 hit |
SUPFAMi | SSF49899 SSF49899, 1 hit |
PROSITEi | View protein in PROSITE PS00308 LECTIN_LEGUME_ALPHA, 1 hit PS00307 LECTIN_LEGUME_BETA, 1 hit |
i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
P81517-1 [UniParc]FASTAAdd to basket
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
Mass spectrometryi
Similar proteinsi
Entry informationi
Entry namei | LECA_CRAAG | |
Accessioni | P81517Primary (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: | November 22, 2017 | |
This is version 91 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Plant Protein Annotation Program |