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Protein

Lectin alpha chain

Gene
N/A
Organism
Dioclea guianensis
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)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi8 – 81Manganese
Metal bindingi10 – 101Calcium
Metal bindingi10 – 101Manganese
Metal bindingi12 – 121Calcium; via carbonyl oxygen
Binding sitei12 – 121CarbohydrateBy similarity
Metal bindingi14 – 141Calcium
Metal bindingi19 – 191Calcium
Metal bindingi19 – 191Manganese
Metal bindingi24 – 241Manganese
Metal bindingi34 – 341ManganeseBy similarity
Metal bindingi208 – 2081Calcium
Binding sitei228 – 2281Carbohydrate; via amide nitrogenBy similarity

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 3 chains:
OrganismiDioclea guianensis
Taxonomic identifieri99571 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsFabalesFabaceaePapilionoideaePhaseoleaeDioclea

Pathology & Biotechi

Toxic dosei

LC(50) is 5.21 µg/ml against the brine shrimp A.salina. LC(50) is 23.1 µg/ml against the aquatic snail B.glabrata.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 237237Lectin alpha chainPRO_0000017600Add
BLAST
Chaini1 – 118118Lectin beta chainPRO_0000017601Add
BLAST
Chaini119 – 237119Lectin gamma-1 chainPRO_0000017602Add
BLAST
Chaini125 – 237113Lectin gamma-2 chainPRO_0000017603Add
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.

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
237
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 107Combined sources
Helixi15 – 173Combined sources
Beta strandi24 – 3310Combined sources
Beta strandi35 – 395Combined sources
Beta strandi46 – 5510Combined sources
Turni56 – 594Combined sources
Beta strandi60 – 678Combined sources
Turni68 – 703Combined sources
Beta strandi71 – 788Combined sources
Helixi81 – 844Combined sources
Beta strandi87 – 9610Combined sources
Beta strandi105 – 11612Combined sources
Beta strandi118 – 1214Combined sources
Beta strandi123 – 13210Combined sources
Beta strandi140 – 1445Combined sources
Beta strandi154 – 1574Combined sources
Beta strandi170 – 1778Combined sources
Beta strandi187 – 19812Combined sources
Beta strandi202 – 2054Combined sources
Beta strandi209 – 2168Combined sources
Helixi227 – 2293Combined sources
Turni230 – 2323Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1H9PX-ray2.00A1-237[»]
1H9WX-ray2.00A/B1-237[»]
2JDZX-ray2.10A1-237[»]
2JE7X-ray1.65A1-237[»]
ProteinModelPortaliP81637.
SMRiP81637. Positions 1-237.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP81637.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni99 – 1002Carbohydrate bindingBy similarity

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.

P81637-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
ADTIVAVELD SYPNTDIGDP SYPHIGIDIK SIRSKSTARW NMQTGKVGTA
60 70 80 90 100
HISYNSVAKR LSAVVSYTGS SSTTVSYDVD LNNVLPEWVR VGLSATTGLY
110 120 130 140 150
KETNTILSWS FTSKLKTNSI ADANSLHFSF NQFSQNPKDL ILQSDATTDS
160 170 180 190 200
DGNLELTKVS SSGDPQGSSV GRALFYAPVH IWEKSAVVAG FDATFTFLIK
210 220 230
SPDRDPADGI TFFIANTDTS IPSGSGGRLL GLFPDAN
Length:237
Mass (Da):25,399
Last modified:July 15, 1999 - v1
Checksum:iB5D7555EAF9EE047
GO

Mass spectrometryi

Molecular mass is 25398±1 Da from positions 1 - 237. Determined by ESI. 1 Publication
Molecular mass is 12831±1 Da from positions 1 - 118. Determined by ESI. 1 Publication
Molecular mass is 12583±1 Da from positions 119 - 237. Determined by ESI. 1 Publication
Molecular mass is 12012±1 Da from positions 125 - 237. Determined by ESI. 1 Publication

Cross-referencesi

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1H9PX-ray2.00A1-237[»]
1H9WX-ray2.00A/B1-237[»]
2JDZX-ray2.10A1-237[»]
2JE7X-ray1.65A1-237[»]
ProteinModelPortaliP81637.
SMRiP81637. Positions 1-237.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP81637.

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_DIOGU
AccessioniPrimary (citable) accession number: P81637
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: July 15, 1999
Last modified: October 14, 2015
This is version 84 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.