Lectin alpha chain

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 key	Position(s)	Length	Description
Metal bindingⁱ	8 – 8	1	ManganeseBy similarity
Metal bindingⁱ	10 – 10	1	CalciumBy similarity
Metal bindingⁱ	10 – 10	1	ManganeseBy similarity
Metal bindingⁱ	12 – 12	1	Calcium; via carbonyl oxygenBy similarity
Binding siteⁱ	12 – 12	1	CarbohydrateBy similarity
Metal bindingⁱ	14 – 14	1	CalciumBy similarity
Metal bindingⁱ	19 – 19	1	CalciumBy similarity
Metal bindingⁱ	19 – 19	1	ManganeseBy similarity
Metal bindingⁱ	24 – 24	1	ManganeseBy similarity
Metal bindingⁱ	34 – 34	1	ManganeseBy similarity
Metal bindingⁱ	207 – 207	1	CalciumBy similarity
Binding siteⁱ	227 – 227	1	Carbohydrate; via amide nitrogenBy similarity

GO - Molecular functionⁱ

carbohydrate binding
Source: UniProtKB
Inferred from direct assayⁱ
- 10082964
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: Lectin beta chain Lectin gamma chain
Organismⁱ	Cratylia argentea (Cratylia floribunda)
Taxonomic identifierⁱ	83131 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Eukaryota › Viridiplantae › Streptophyta › Streptophytina › Embryophyta › Tracheophyta › Euphyllophyta › Spermatophyta › Magnoliophyta › Mesangiospermae › 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)	Length	Description	Feature identifier	Actions
Chainⁱ	1 – 236	236	Lectin alpha chain	PRO_0000017588	Add BLAST
Chainⁱ	1 – 118	118	Lectin beta chain	PRO_0000017589	Add BLAST
Chainⁱ	119 – 236	118	Lectin gamma chain	PRO_0000017590	Add 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 key	Position(s)	Length	Description
Beta strandⁱ	5 – 10	6	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:2D3P
Helixⁱ	15 – 17	3	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:2D3P
Beta strandⁱ	24 – 33	10	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:2D3P
Beta strandⁱ	35 – 39	5	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:2D3P
Beta strandⁱ	47 – 55	9	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:2D3P
Turnⁱ	56 – 59	4	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:2D3P
Beta strandⁱ	60 – 67	8	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:2D3P
Turnⁱ	68 – 70	3	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:2D3P
Beta strandⁱ	71 – 78	8	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:2D3P
Helixⁱ	81 – 83	3	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:2D3P
Beta strandⁱ	87 – 96	10	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:2D3P
Beta strandⁱ	105 – 116	12	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:2D3P
Beta strandⁱ	118 – 121	4	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:2D3P
Beta strandⁱ	123 – 132	10	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:2D3P
Beta strandⁱ	140 – 144	5	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:2D3P
Beta strandⁱ	154 – 157	4	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:2D3P
Beta strandⁱ	169 – 176	8	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:2D3P
Beta strandⁱ	186 – 197	12	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:2D3P
Beta strandⁱ	201 – 204	4	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:2D3P
Beta strandⁱ	208 – 214	7	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:2D3P
Helixⁱ	226 – 228	3	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:2D3P
Turnⁱ	229 – 231	3	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:2D3P

3D structure databases

Select the link destinations:
PDBeⁱ
RCSB PDBⁱ
PDBjⁱ

Links Updated

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. Positions 1-236.

ModBaseⁱ

Search...

MobiDBⁱ

Search...

Miscellaneous databases

EvolutionaryTraceⁱ	P81517.

EvolutionaryTraceⁱ

P81517.

Family & Domainsⁱ

Region

Feature key	Position(s)	Length	Description	Graphical view	Feature identifier	Actions
Regionⁱ	99 – 100	2	Carbohydrate bindingBy similarity

Sequence similaritiesⁱ

Belongs to the leguminous lectin family.Curated

Family and domain databases

Gene3Dⁱ	2.60.120.200. 2 hits.
InterProⁱ	IPR013320. ConA-like_dom. IPR000985. Lectin_LegA_CS. IPR019825. Lectin_legB_Mn/Ca_BS. IPR001220. Legume_lectin_dom. [Graphical view]
Pfamⁱ	PF00139. Lectin_legB. 2 hits. [Graphical view]
SUPFAMⁱ	SSF49899. SSF49899. 1 hit.
PROSITEⁱ	PS00308. 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]FASTA Add 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

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. Positions 1-236.

ModBaseⁱ

Search...

MobiDBⁱ

Search...

Protocols and materials databases

Structural Biology Knowledgebase	Search...

Structural Biology Knowledgebase

Search...

Miscellaneous databases

EvolutionaryTraceⁱ	P81517.

EvolutionaryTraceⁱ

P81517.

Family and domain databases

Gene3Dⁱ	2.60.120.200. 2 hits.
InterProⁱ	IPR013320. ConA-like_dom. IPR000985. Lectin_LegA_CS. IPR019825. Lectin_legB_Mn/Ca_BS. IPR001220. Legume_lectin_dom. [Graphical view]
Pfamⁱ	PF00139. Lectin_legB. 2 hits. [Graphical view]
SUPFAMⁱ	SSF49899. SSF49899. 1 hit.
PROSITEⁱ	PS00308. LECTIN_LEGUME_ALPHA. 1 hit. PS00307. LECTIN_LEGUME_BETA. 1 hit. [Graphical view]
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ

LECA_CRAAG

Accessionⁱ

Primary (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 statusⁱ

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant 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

PDB cross-references
Index of Protein Data Bank (PDB) cross-references
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.

UniProtKB

UniParc

Help

UniRef

Proteomes

Annotation systems

Supporting data

UniProtKB - P81517 (LECA_CRAAG)

UniProt

P81517 - LECA_CRAAG

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Secondary structure

3D structure databases

Miscellaneous databases

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Miscellaneous

Documents

Functionⁱ

GO - Molecular functionⁱ

Names & Taxonomyⁱ

Pathology & Biotechⁱ

Toxic doseⁱ

PTM / Processingⁱ

Expressionⁱ

Interactionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Sequenceⁱ

Mass spectrometryⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ