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Protein

Concanavalin-A

Gene
N/A
Organism
Canavalia cathartica (Jackbean) (Canavalia virosa)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Glucose/D-mannose specific lectin.2 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.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi8ManganeseCombined sources3 Publications1
Metal bindingi10CalciumCombined sources3 Publications1
Metal bindingi10ManganeseCombined sources3 Publications1
Metal bindingi12Calcium; via carbonyl oxygenCombined sources3 Publications1
Metal bindingi14CalciumCombined sources3 Publications1
Binding sitei14CarbohydrateCombined sources2 Publications1
Metal bindingi19CalciumCombined sources3 Publications1
Metal bindingi19ManganeseCombined sources3 Publications1
Metal bindingi24Manganese; via tele nitrogenCombined sources3 Publications1
Binding sitei208CarbohydrateCombined sources2 Publications1
Binding sitei228Carbohydrate; via amide nitrogenCombined sources2 Publications1

GO - Molecular functioni

Keywordsi

LigandCalcium, Lectin, Manganese, Mannose-binding, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Concanavalin-A
Short name:
Con A
OrganismiCanavalia cathartica (Jackbean) (Canavalia virosa)
Taxonomic identifieri28958 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsFabalesFabaceaePapilionoideaePhaseoleaeCanavalia

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001050881 – 237Concanavalin-AAdd BLAST237

Post-translational modificationi

Concanavalin A-like lectins of the Diocleinae subtribe undergo proteolytic processing referred to as circular permutation. The propeptide is split into an N-terminal and a C-terminal part, the gamma and beta chain, respectively. These are then religated in beta-gamma order to form the mature alpha chain. The beta and gamma chains can often be detected in cell extracts (By similarity). Residues 1-118 of the mature chain, as displayed here, probably constitute the beta chain in the propeptide, residues 119-237 the gamma chain (Probable).By similarityCurated

Interactioni

Subunit structurei

Homotetramer.2 Publications

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 strandi46 – 55Combined sources10
Turni56 – 59Combined sources4
Beta strandi60 – 66Combined sources7
Beta strandi73 – 78Combined sources6
Helixi81 – 83Combined sources3
Beta strandi87 – 96Combined sources10
Beta strandi98 – 100Combined sources3
Beta strandi105 – 118Combined sources14
Beta strandi123 – 132Combined sources10
Beta strandi140 – 144Combined sources5
Helixi150 – 152Combined sources3
Beta strandi154 – 157Combined sources4
Beta strandi170 – 177Combined sources8
Beta strandi186 – 198Combined sources13
Beta strandi202 – 205Combined sources4
Beta strandi209 – 215Combined sources7
Helixi227 – 229Combined sources3
Turni230 – 232Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2A7AX-ray1.75A1-237[»]
2G4IX-ray2.40A1-237[»]
3QLQX-ray1.70A/B/C/D1-237[»]
4CZSX-ray1.73A/B/C/D1-237[»]
ProteinModelPortaliP81461.
SMRiP81461.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP81461.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni98 – 100Carbohydrate bindingCombined sources2 Publications3

Sequence similaritiesi

Belongs to the leguminous lectin family.Curated

Family and domain databases

InterProiView protein in InterPro
IPR013320. ConA-like_dom.
IPR016363. L-lectin.
IPR000985. Lectin_LegA_CS.
IPR019825. Lectin_legB_Mn/Ca_BS.
IPR001220. Legume_lectin_dom.
PfamiView protein in Pfam
PF00139. Lectin_legB. 2 hits.
PIRSFiPIRSF002690. L-type_lectin_plant. 2 hits.
SUPFAMiSSF49899. SSF49899. 1 hit.
PROSITEiView protein in PROSITE
PS00308. LECTIN_LEGUME_ALPHA. 1 hit.
PS00307. LECTIN_LEGUME_BETA. 1 hit.

Sequencei

Sequence statusi: Complete.

P81461-1 [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
DGNLELTRVS SNGSPQGNSV GRALFYAPVH IWESSAVVAS FDATFTFLIK
210 220 230
SPDSHPADGI AFFISNIDSS IPSGSTGRLL GLFPDAN
Length:237
Mass (Da):25,539
Last modified:December 15, 1998 - v1
Checksum:iDD31D2BFCC6EDD07
GO

Sequence databases

PIRiA59417.

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.

Entry informationi

Entry nameiCONA_CANCT
AccessioniPrimary (citable) accession number: P81461
Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: December 15, 1998
Last modified: July 5, 2017
This is version 100 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

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