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

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	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
Inferred from direct assayⁱ
- 10082964
mannose binding Source: UniProtKB-KW
metal ion binding Source: UniProtKB-KW

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Ligand	Calcium, Lectin, Manganese, Mannose-binding, Metal-binding

Ligand

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)	DescriptionActions	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 details

Feature key	Position(s)	DescriptionActions	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: Protein Data Bank Europe More...PDBeⁱ Protein Data Bank RCSB More...RCSB PDBⁱ Protein Data Bank Japan More...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

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

Conserved Domains Database More...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
Pfam protein domain database More...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

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

Protein	Similar proteins	Organisms	Length	Cluster ID	Cluster name	Size
P81517	J9PBR3 UPI00001D73A3 UPI00005E617D P83721	Bionia pedicellata (Camptosema pedicellatum) Cratylia mollis (Camaratu bean) Cratylia argentea (Cratylia floribunda)	236	UniRef90_J9PBR3	Cluster: Lectin CPL	5

Protein	Similar proteins	Organisms	Length	Cluster ID	Cluster name	Size
P81517	C0HJY1 UPI0000D5BE25 A0A067XG71 UPI000B9D4F5A UPI0001753C69 UPI0000110D27 P81460 P55915 UPI000011025C UPI0001753C80 +9	Canavalia cathartica (Jackbean) (Canavalia virosa) Canavalia gladiata (Sword bean) (Dolichos gladiatus) Canavalia grandiflora (Jackbean) Canavalia bonariensis Canavalia ensiformis (Jack bean) (Dolichos ensiformis) Canavalia lineata (Beach bean) (Dolichos lineatus) Canavalia brasiliensis (Brazilian jack bean) Canavalia rosea (Beach bean) (Canavalia maritima) Canavalia boliviana Bionia pedicellata (Camptosema pedicellatum) And more	237	UniRef50_C0HJY1	Cluster: Concanavalin V	20

Cross-referencesⁱ

3D structure databases

Select the link destinations: Protein Data Bank Europe More...PDBeⁱ Protein Data Bank RCSB More...RCSB PDBⁱ Protein Data Bank Japan More...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...

Protocols and materials databases

Structural Biology Knowledgebase	Search...

Structural Biology Knowledgebase

Search...

Miscellaneous databases

EvolutionaryTraceⁱ	P81517

EvolutionaryTraceⁱ

P81517

Family and domain databases

Conserved Domains Database More...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
Pfam protein domain database More...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
ProtoNetⁱ	Search...

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

Miscellaneousⁱ

Keywords - Technical termⁱ

3D-structure, Direct protein sequencing

UniProtKB - P81517 (LECA_CRAAG)

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Functionⁱ

Miscellaneous

Sites

GO - Molecular functionⁱ

Keywordsⁱ

Names & Taxonomyⁱ

Pathology & Biotechⁱ

Toxic doseⁱ

PTM / Processingⁱ

Molecule processing

Post-translational modificationⁱ

Expressionⁱ

Tissue specificityⁱ

Interactionⁱ

Subunit structureⁱ

Structureⁱ

Secondary structure

3D structure databases

Miscellaneous databases

Family & Domainsⁱ

Region

Sequence similaritiesⁱ

Family and domain databases

Sequenceⁱ

Mass spectrometryⁱ

Similar proteinsⁱ

Cross-referencesⁱ

3D structure databases

Protocols and materials databases

Miscellaneous databases

Family and domain databases

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ

UniProtKB

UniParc

Help

UniRef

Proteomes

Annotation systems

Supporting data

UniProtKB - P81517 (LECA_CRAAG)

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Lectin alpha chain

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<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Miscellaneous

Sites

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Molecule processing

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<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

3D structure databases

Miscellaneous databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Region

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Family and domain databases

<p>This subsection of the ‘Sequence’ section reports information derived from mass spectrometry experiments done on the entire protein or on biologically active derived peptide(s).<p><a href='/help/mass_spectrometry' target='_top'>More...</a></p>Mass spectrometryi

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3D structure databases

Protocols and materials databases

Miscellaneous databases

Family and domain databases

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Functionⁱ

GO - Molecular functionⁱ

Names & Taxonomyⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Expressionⁱ

Interactionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Mass spectrometryⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ