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Protein

Concanavalin-Br

Gene
N/A
Organism
Canavalia brasiliensis (Brazilian jack bean)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Glucose/D-mannose specific lectin. Has anti-inflammatory activity in rats. Induces histamine release in mast cells from hamster and rat. Induces lymphocyte proliferation and IFNG production. Shows toxicity against the aquatic snail B.glabrata at concentrations higher than 20 µg/ml.7 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi8Manganese1
Metal bindingi10Calcium1
Metal bindingi10Manganese1
Metal bindingi12Calcium; via carbonyl oxygen1
Binding sitei12Carbohydrate1 Publication1
Metal bindingi14Calcium1
Metal bindingi19Calcium1
Metal bindingi19Manganese1
Metal bindingi24Manganese1
Metal bindingi34ManganeseBy similarity1
Metal bindingi208CalciumBy similarity1
Binding sitei228Carbohydrate; via amide nitrogen1 Publication1

GO - Molecular functioni

Complete GO annotation...

Keywords - Ligandi

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

Names & Taxonomyi

Protein namesi
Recommended name:
Concanavalin-Br
Short name:
Con Br
OrganismiCanavalia brasiliensis (Brazilian jack bean)
Taxonomic identifieri61861 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsFabalesFabaceaePapilionoideaePhaseoleaeCanavalia

Pathology & Biotechi

Toxic dosei

LC(50) is 15.4 µg/ml against the brine shrimp A.salina.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001050851 – 237Concanavalin-BrAdd BLAST237

Interactioni

Subunit structurei

Homotetramer.1 Publication

Structurei

Secondary structure

1237
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi4 – 10Combined sources7
Helixi15 – 17Combined sources3
Beta strandi24 – 33Combined sources10
Beta strandi35 – 39Combined sources5
Beta strandi48 – 55Combined sources8
Turni56 – 59Combined sources4
Beta strandi60 – 66Combined sources7
Beta strandi68 – 70Combined sources3
Beta strandi72 – 78Combined sources7
Helixi81 – 83Combined sources3
Beta strandi87 – 96Combined sources10
Beta strandi98 – 100Combined sources3
Beta strandi108 – 116Combined sources9
Turni118 – 120Combined sources3
Beta strandi124 – 132Combined sources9
Beta strandi140 – 144Combined sources5
Beta strandi150 – 152Combined sources3
Beta strandi154 – 157Combined sources4
Turni161 – 163Combined sources3
Beta strandi170 – 177Combined sources8
Beta strandi187 – 197Combined sources11
Beta strandi203 – 205Combined sources3
Beta strandi209 – 216Combined sources8
Helixi227 – 229Combined sources3
Turni230 – 232Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1AZDX-ray3.00A/B/C/D1-237[»]
1QDCX-ray2.00A/B/C/D1-237[»]
1QDOX-ray2.80A/B/C/D1-237[»]
2CYFX-ray1.80A/C1-237[»]
3JU9X-ray2.10A1-237[»]
4H55X-ray2.07A1-237[»]
4P14X-ray2.00A1-237[»]
4PCRX-ray2.15A/D1-237[»]
ProteinModelPortaliP55915.
SMRiP55915.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP55915.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni99 – 100Carbohydrate binding2

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.

P55915-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
ADTIVAVELD TYPNTDIGDP SYPHIGIDIK SVRSKKTAKW NMQNGKVGTA
60 70 80 90 100
HIIYNSVGKR LSAVVSYPNG DSATVSYDVD LDNVLPEWVR VGLSASTGLY
110 120 130 140 150
KETNTILSWS FTSKLKSNST HETNALHFMF NQFSKDQKDL ILQGDATTGT
160 170 180 190 200
EGNLRLTRVS SNGSPQGSSV GRALFYAPVH IWESSAVVAS FEATFTFLIK
210 220 230
SPDSHPADGI AFFISNIDSS IPSGSTGRLL GLFPDAN
Length:237
Mass (Da):25,568
Last modified:November 1, 1997 - v1
Checksum:i4D62F2113A36C38F
GO

Cross-referencesi

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1AZDX-ray3.00A/B/C/D1-237[»]
1QDCX-ray2.00A/B/C/D1-237[»]
1QDOX-ray2.80A/B/C/D1-237[»]
2CYFX-ray1.80A/C1-237[»]
3JU9X-ray2.10A1-237[»]
4H55X-ray2.07A1-237[»]
4P14X-ray2.00A1-237[»]
4PCRX-ray2.15A/D1-237[»]
ProteinModelPortaliP55915.
SMRiP55915.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP55915.

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 nameiCONA_CANBR
AccessioniPrimary (citable) accession number: P55915
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: November 2, 2016
This is version 93 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.