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Protein

Concanavalin-A

Gene
N/A
Organism
Canavalia ensiformis (Jack bean) (Dolichos ensiformis)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

D-mannose specific lectin.

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.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi119CalciumBy similarity1
Binding sitei119Carbohydrate1
Binding sitei139Carbohydrate; via amide nitrogen1
Metal bindingi171Manganese1
Metal bindingi173Calcium1 Publication1
Metal bindingi173Manganese1
Metal bindingi175Calcium; via carbonyl oxygen1 Publication1
Metal bindingi177Calcium1 Publication1
Metal bindingi182Calcium1 Publication1
Metal bindingi182Manganese1
Metal bindingi187Manganese1

GO - Molecular functioni

Keywordsi

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

Protein family/group databases

UniLectiniP02866

Names & Taxonomyi

Protein namesi
Recommended name:
Concanavalin-A
Short name:
Con A
OrganismiCanavalia ensiformis (Jack bean) (Dolichos ensiformis)
Taxonomic identifieri3823 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsFabalesFabaceaePapilionoideae50 kb inversion cladeNPAAA cladeindigoferoid/millettioid cladePhaseoleaeCanavalia

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL5820

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 291 PublicationAdd BLAST29
ChainiPRO_000001757730 – 148Concanavalin-A, 2nd partAdd BLAST119
PropeptideiPRO_0000017578149 – 1631 PublicationAdd BLAST15
ChainiPRO_0000017579164 – 281Concanavalin-A, 1st partAdd BLAST118
PropeptideiPRO_0000017580282 – 2909

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi152N-linked (GlcNAc...) asparagine1

Post-translational modificationi

The mature chain consists of residues 164-281 followed by 30-148. To form a mature chain the precursor undergoes further post-translational modification after removal of the signal sequence; cleavage after Asn at positions 148, 163, and 281 is followed by transposition and ligation (By formation of a new peptide bond) of residues 164-281 and 30-148.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei148 – 149Cleavage2
Sitei163 – 164Cleavage2
Sitei281 – 282Cleavage2

Keywords - PTMi

Glycoprotein

Interactioni

Subunit structurei

Homotetramer.1 Publication

Protein-protein interaction databases

IntActiP02866, 109 interactors

Chemistry databases

BindingDBiP02866

Structurei

Secondary structure

1290
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

ProteinModelPortaliP02866
SMRiP02866
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP02866

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni262 – 263Carbohydrate binding2

Sequence similaritiesi

Belongs to the leguminous lectin family.Curated

Keywords - Domaini

Signal

Family and domain databases

CDDicd06899 lectin_legume_LecRK_Arcelin_Co, 1 hit
InterProiView protein in InterPro
IPR013320 ConA-like_dom_sf
IPR016363 L-lectin
IPR000985 Lectin_LegA_CS
IPR019825 Lectin_legB_Mn/Ca_BS
IPR001220 Legume_lectin_dom
PfamiView protein in Pfam
PF00139 Lectin_legB, 1 hit
PIRSFiPIRSF002690 L-type_lectin_plant, 1 hit
SUPFAMiSSF49899 SSF49899, 1 hit
PROSITEiView 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.

P02866-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MAISKKSSLF LPIFTFITMF LMVVNKVSSS THETNALHFM FNQFSKDQKD
60 70 80 90 100
LILQGDATTG TDGNLELTRV SSNGSPQGSS VGRALFYAPV HIWESSAVVA
110 120 130 140 150
SFEATFTFLI KSPDSHPADG IAFFISNIDS SIPSGSTGRL LGLFPDANVI
160 170 180 190 200
RNSTTIDFNA AYNADTIVAV ELDTYPNTDI GDPSYPHIGI DIKSVRSKKT
210 220 230 240 250
AKWNMQNGKV GTAHIIYNSV DKRLSAVVSY PNADSATVSY DVDLDNVLPE
260 270 280 290
WVRVGLSAST GLYKETNTIL SWSFTSKLKS NEIPDIATVV
Length:290
Mass (Da):31,480
Last modified:October 3, 2003 - v2
Checksum:i0F2F7DBBCF547E42
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti33E → Q AA sequence (PubMed:1112814).Curated1
Sequence conflicti35N → D AA sequence (PubMed:1112814).Curated1
Sequence conflicti62D → E in CAA25787 (PubMed:3965973).Curated1
Sequence conflicti66E → R in CAA25787 (PubMed:3965973).Curated1
Sequence conflicti77Q → E AA sequence (PubMed:1112814).Curated1
Sequence conflicti98 – 101VVAS → TVSA AA sequence (PubMed:1112814).Curated4
Sequence conflicti107T → A AA sequence (PubMed:1112814).Curated1
Sequence conflicti207N → D AA sequence (PubMed:1112813).Curated1
Sequence conflicti245 – 246DN → ND AA sequence (PubMed:1112813).Curated2

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X01632 mRNA Translation: CAA25787.1
AF308777 mRNA Translation: AAL09432.1
PIRiA03357 CVJBP

Similar proteinsi

Cross-referencesi

Web resourcesi

Worthington enzyme manual
Functional Glycomics Gateway - Glycan Binding

Con A (Canavalia ensiformis)

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X01632 mRNA Translation: CAA25787.1
AF308777 mRNA Translation: AAL09432.1
PIRiA03357 CVJBP

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1APNX-ray2.50A/B28-148[»]
1BXHX-ray2.75A/B/C/D148-164[»]
1C57neutron diffraction2.40A148-164[»]
1CESX-ray2.70A/B28-148[»]
1CJPX-ray2.78A/B/C/D30-148[»]
1CN1X-ray3.20A/B30-281[»]
1CONX-ray2.00A28-148[»]
1CVNX-ray2.30A/B/C/D30-148[»]
1DQ0X-ray1.70A28-148[»]
1DQ1X-ray2.15A28-148[»]
1DQ2X-ray2.05A/B28-148[»]
1DQ4X-ray2.90A/B28-148[»]
1DQ5X-ray2.00A28-148[»]
1DQ6X-ray1.90A28-148[»]
1ENQX-ray2.50A/B/C/D30-148[»]
1ENRX-ray1.83A28-148[»]
1ENSX-ray2.80A/B30-148[»]
1GICX-ray2.00A/B28-148[»]
1GKBX-ray1.56A/B148-164[»]
1HQWX-ray2.40A30-148[»]
1I3HX-ray1.20A28-148[»]
1JBCX-ray1.15A28-148[»]
1JN2X-ray1.90P28-148[»]
1JOJX-ray3.00A/B/C/D28-148[»]
1JUIX-ray2.75A/B/C/D28-148[»]
1JW6X-ray1.93A28-148[»]
1JYCX-ray2.75A/B/C/D28-148[»]
1JYIX-ray2.75A/B/C/D28-148[»]
1NLSX-ray0.94A28-148[»]
1NXDX-ray1.901/2/3/4148-164[»]
1ONAX-ray2.35A/B/C/D30-148[»]
1QGLX-ray2.66A/B30-148[»]
1QNYX-ray1.80A28-148[»]
1SCRX-ray2.00A28-148[»]
1SCSX-ray1.60A28-148[»]
1TEIX-ray2.70A/B/C/D/E/F/G/H28-148[»]
1VALX-ray3.00A/B/C/D30-148[»]
1VAMX-ray2.75A/B/C/D30-148[»]
1XQNneutron diffraction2.50A28-148[»]
2CNAX-ray2.00A28-148[»]
2CTVX-ray1.95A28-148[»]
2ENRX-ray2.35A28-148[»]
2UU8X-ray0.94A148-164[»]
2YZ4neutron diffraction2.20A28-148[»]
3CNAX-ray2.40A30-281[»]
3D4KX-ray1.80A/B/C/D148-164[»]
3ENRX-ray2.40A/B148-164[»]
3NWKX-ray2.09A/B/C/D148-164[»]
4P9WX-ray2.11A/B/C/D28-148[»]
4P9XX-ray2.06A/B/C/D28-148[»]
4P9YX-ray1.89A/B28-148[»]
4PF5X-ray2.04A/B28-148[»]
5CNAX-ray2.00A/B/C/D28-148[»]
5O6NX-ray1.35A148-164[»]
5WEYOther1.80A148-164[»]
5Z5YX-ray1.89A/B148-164[»]
5ZACX-ray2.59A/B/C/D148-164[»]
ProteinModelPortaliP02866
SMRiP02866
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP02866, 109 interactors

Chemistry databases

BindingDBiP02866
ChEMBLiCHEMBL5820

Protein family/group databases

UniLectiniP02866

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP02866

Family and domain databases

CDDicd06899 lectin_legume_LecRK_Arcelin_Co, 1 hit
InterProiView protein in InterPro
IPR013320 ConA-like_dom_sf
IPR016363 L-lectin
IPR000985 Lectin_LegA_CS
IPR019825 Lectin_legB_Mn/Ca_BS
IPR001220 Legume_lectin_dom
PfamiView protein in Pfam
PF00139 Lectin_legB, 1 hit
PIRSFiPIRSF002690 L-type_lectin_plant, 1 hit
SUPFAMiSSF49899 SSF49899, 1 hit
PROSITEiView protein in PROSITE
PS00308 LECTIN_LEGUME_ALPHA, 1 hit
PS00307 LECTIN_LEGUME_BETA, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiCONA_CANEN
AccessioniPrimary (citable) accession number: P02866
Secondary accession number(s): Q947H0
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: October 3, 2003
Last modified: September 12, 2018
This is version 143 of the entry and version 2 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. SIMILARITY comments
    Index of protein domains and families
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

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