Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
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)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 bindingi207CalciumBy similarity1
Binding sitei227Carbohydrate; via amide nitrogenBy similarity1

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)DescriptionActionsGraphical viewLength
ChainiPRO_00000175881 – 236Lectin alpha chainAdd BLAST236
ChainiPRO_00000175891 – 118Lectin beta chainAdd BLAST118
ChainiPRO_0000017590119 – 236Lectin gamma chainAdd BLAST118

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

1236
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi5 – 10Combined sources6
Helixi15 – 17Combined sources3
Beta strandi24 – 33Combined sources10
Beta strandi35 – 39Combined sources5
Beta strandi47 – 55Combined sources9
Turni56 – 59Combined sources4
Beta strandi60 – 67Combined sources8
Turni68 – 70Combined sources3
Beta strandi71 – 78Combined sources8
Helixi81 – 83Combined sources3
Beta strandi87 – 96Combined sources10
Beta strandi105 – 116Combined sources12
Beta strandi118 – 121Combined sources4
Beta strandi123 – 132Combined sources10
Beta strandi140 – 144Combined sources5
Beta strandi154 – 157Combined sources4
Beta strandi169 – 176Combined sources8
Beta strandi186 – 197Combined sources12
Beta strandi201 – 204Combined sources4
Beta strandi208 – 214Combined sources7
Helixi226 – 228Combined sources3
Turni229 – 231Combined sources3

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP81517.

Family & Domainsi

Region

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

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2D3PX-ray2.80A/B/C/D1-236[»]
2D3RX-ray2.90A/B/C/D1-236[»]
ProteinModelPortaliP81517.
SMRiP81517.
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...

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: November 2, 2016
This is version 85 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.