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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)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi8 – 81Manganese
Metal bindingi10 – 101Calcium
Metal bindingi10 – 101Manganese
Metal bindingi12 – 121Calcium; via carbonyl oxygen
Binding sitei12 – 121Carbohydrate1 Publication
Metal bindingi14 – 141Calcium
Metal bindingi19 – 191Calcium
Metal bindingi19 – 191Manganese
Metal bindingi24 – 241Manganese
Metal bindingi34 – 341ManganeseBy similarity
Metal bindingi208 – 2081CalciumBy similarity
Binding sitei228 – 2281Carbohydrate; via amide nitrogen1 Publication

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)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 237237Concanavalin-BrPRO_0000105085Add
BLAST

Interactioni

Subunit structurei

Homotetramer.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 strandi48 – 558Combined sources
Turni56 – 594Combined sources
Beta strandi60 – 667Combined sources
Beta strandi68 – 703Combined sources
Beta strandi72 – 787Combined sources
Helixi81 – 833Combined sources
Beta strandi87 – 9610Combined sources
Beta strandi98 – 1003Combined sources
Beta strandi108 – 1169Combined sources
Turni118 – 1203Combined sources
Beta strandi124 – 1329Combined sources
Beta strandi140 – 1445Combined sources
Beta strandi150 – 1523Combined sources
Beta strandi154 – 1574Combined sources
Turni161 – 1633Combined sources
Beta strandi170 – 1778Combined sources
Beta strandi187 – 19711Combined sources
Beta strandi203 – 2053Combined 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
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. Positions 1-237.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP55915.

Family & Domainsi

Region

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

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
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. Positions 1-237.
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: October 14, 2015
This is version 91 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.