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Protein

Concanavalin-A

Gene
N/A
Organism
Canavalia ensiformis (Jack bean) (Dolichos ensiformis)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

D-mannose specific lectin.

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

Complete GO annotation...

Keywords - Ligandi

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

Names & Taxonomyi

Protein namesi
Recommended name:
Concanavalin-A
Short name:
Con A
OrganismiCanavalia ensiformis (Jack bean) (Dolichos ensiformis)
Taxonomic identifieri3823 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsFabalesFabaceaePapilionoideaePhaseoleaeCanavalia

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...)1

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
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi28 – 32Combined sources5
Beta strandi34 – 42Combined sources9
Beta strandi51 – 55Combined sources5
Helixi61 – 63Combined sources3
Beta strandi64 – 68Combined sources5
Turni72 – 74Combined sources3
Beta strandi81 – 88Combined sources8
Beta strandi97 – 109Combined sources13
Beta strandi113 – 116Combined sources4
Beta strandi120 – 126Combined sources7
Helixi138 – 140Combined sources3
Turni141 – 143Combined sources3
Beta strandi167 – 173Combined sources7
Helixi178 – 180Combined sources3
Beta strandi187 – 196Combined sources10
Beta strandi198 – 202Combined sources5
Beta strandi210 – 218Combined sources9
Turni219 – 222Combined sources4
Beta strandi223 – 229Combined sources7
Beta strandi231 – 233Combined sources3
Beta strandi236 – 241Combined sources6
Helixi244 – 246Combined sources3
Beta strandi250 – 259Combined sources10
Beta strandi261 – 263Combined sources3
Beta strandi268 – 281Combined sources14

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[»]
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

Gene3Di2.60.120.200. 1 hit.
InterProiIPR013320. ConA-like_dom.
IPR016363. L-lectin.
IPR000985. Lectin_LegA_CS.
IPR019825. Lectin_legB_Mn/Ca_BS.
IPR001220. Legume_lectin_dom.
[Graphical view]
PfamiPF00139. Lectin_legB. 1 hit.
[Graphical view]
PIRSFiPIRSF002690. L-type_lectin_plant. 1 hit.
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.

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.

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[»]
ProteinModelPortaliP02866.
SMRiP02866.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP02866. 109 interactors.

Chemistry databases

BindingDBiP02866.
ChEMBLiCHEMBL5820.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP02866.

Family and domain databases

Gene3Di2.60.120.200. 1 hit.
InterProiIPR013320. ConA-like_dom.
IPR016363. L-lectin.
IPR000985. Lectin_LegA_CS.
IPR019825. Lectin_legB_Mn/Ca_BS.
IPR001220. Legume_lectin_dom.
[Graphical view]
PfamiPF00139. Lectin_legB. 1 hit.
[Graphical view]
PIRSFiPIRSF002690. L-type_lectin_plant. 1 hit.
SUPFAMiSSF49899. SSF49899. 1 hit.
PROSITEiPS00308. LECTIN_LEGUME_ALPHA. 1 hit.
PS00307. LECTIN_LEGUME_BETA. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiCONA_CANEN
AccessioniPrimary (citable) accession number: P02866
Secondary accession number(s): Q947H0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: October 3, 2003
Last modified: November 2, 2016
This is version 135 of the entry and version 2 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.

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.