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

Complete GO annotation...

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. 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

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        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

Similar proteinsⁱ

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

Entry	Cluster members	Organisms	Length	Cluster ID	Cluster name	Size
P81517	C0HJY1 UPI0000D5BE25 A0A067XG71 UPI0001753C69 UPI0000110D27 P81460 P55915 UPI000011025C UPI0001753C80 A0A023GPI8 +8	Canavalia cathartica (Jackbean) (Canavalia virosa) Canavalia gladiata (Sword bean) (Dolichos gladiatus) Canavalia grandiflora (Jackbean) 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) Cratylia argentea (Cratylia floribunda) And more	237	UniRef50_C0HJY1	Cluster: Concanavalin V	19

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. 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:	August 30, 2017
	This is version 90 of the entry and version 1 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Plant Protein Annotation Program

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

Documents

UniProtKB

UniParc

Help

UniRef

Proteomes

Annotation systems

Supporting data

UniProtKB - P81517 (LECA_CRAAG)

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Lectin alpha chain

Select a section on the left to see content.

<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

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<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 section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including length and molecular weight.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<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

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Documents

Functionⁱ

GO - Molecular functionⁱ

Names & Taxonomyⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Expressionⁱ

Interactionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Sequenceⁱ

Mass spectrometryⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ