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P02866 (CONA_CANEN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 126. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Concanavalin-A

Short name=Con A

Cleaved into the following chain:

  1. Concanavalin, 1st part
OrganismCanavalia ensiformis (Jack bean) (Dolichos ensiformis)
Taxonomic identifier3823 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsFabalesFabaceaePapilionoideaePhaseoleaeCanavalia

Protein attributes

Sequence length290 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

D-mannose specific lectin.

Subunit structure

Homotetramer. Ref.8

Post-translational modification

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.

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.

Sequence similarities

Belongs to the leguminous lectin family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2929 Ref.3
Chain30 – 148119Concanavalin-A
PRO_0000017577
Propeptide149 – 16315
PRO_0000017578
Chain164 – 281118Concanavalin, 1st part
PRO_0000017579
Propeptide282 – 2909
PRO_0000017580

Regions

Region262 – 2632Carbohydrate binding

Sites

Metal binding1191Calcium By similarity
Metal binding1711Manganese
Metal binding1731Calcium
Metal binding1731Manganese
Metal binding1751Calcium; via carbonyl oxygen
Metal binding1771Calcium
Metal binding1821Calcium
Metal binding1821Manganese
Metal binding1871Manganese
Binding site1191Carbohydrate
Binding site1391Carbohydrate; via amide nitrogen
Site148 – 1492Cleavage
Site163 – 1642Cleavage
Site281 – 2822Cleavage

Amino acid modifications

Glycosylation1521N-linked (GlcNAc...)

Experimental info

Sequence conflict331E → Q AA sequence Ref.3
Sequence conflict351N → D AA sequence Ref.3
Sequence conflict621D → E in CAA25787. Ref.1
Sequence conflict661E → R in CAA25787. Ref.1
Sequence conflict771Q → E AA sequence Ref.3
Sequence conflict98 – 1014VVAS → TVSA AA sequence Ref.3
Sequence conflict1071T → A AA sequence Ref.3
Sequence conflict2071N → D AA sequence Ref.4
Sequence conflict245 – 2462DN → ND AA sequence Ref.4

Secondary structure

............................................... 290
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P02866 [UniParc].

Last modified October 3, 2003. Version 2.
Checksum: 0F2F7DBBCF547E42

FASTA29031,480
        10         20         30         40         50         60 
MAISKKSSLF LPIFTFITMF LMVVNKVSSS THETNALHFM FNQFSKDQKD LILQGDATTG 

        70         80         90        100        110        120 
TDGNLELTRV SSNGSPQGSS VGRALFYAPV HIWESSAVVA SFEATFTFLI KSPDSHPADG 

       130        140        150        160        170        180 
IAFFISNIDS SIPSGSTGRL LGLFPDANVI RNSTTIDFNA AYNADTIVAV ELDTYPNTDI 

       190        200        210        220        230        240 
GDPSYPHIGI DIKSVRSKKT AKWNMQNGKV GTAHIIYNSV DKRLSAVVSY PNADSATVSY 

       250        260        270        280        290 
DVDLDNVLPE WVRVGLSAST GLYKETNTIL SWSFTSKLKS NEIPDIATVV 

« Hide

References

[1]"Polypeptide ligation occurs during post-translational modification of concanavalin A."
Carrington D.M., Auffret A., Hanke D.E.
Nature 313:64-67(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]Ramis C., Gomord V.
Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: cv. U-02.
[3]"The covalent and three-dimensional structure of concanavalin A. II. Amino acid sequence of cyanogen bromide fragment F3."
Cunningham B.A., Wang J.L., Waxdal M.J., Edelman G.M.
J. Biol. Chem. 250:1503-1512(1975) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 30-148.
[4]"The covalent and three-dimensional structural of concanavalin A. I. Amino acid sequence of cyanogen bromide fragments F1 and F2."
Wang J.L., Cunningham B.A., Waxdal M.J., Edelman G.M.
J. Biol. Chem. 250:1490-1502(1975) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 164-281.
[5]"Structure of concanavalin A at 2.4-A resolution."
Hardman K.D., Ainsworth C.F.
Biochemistry 11:4910-4919(1972) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
[6]"The covalent and three-dimensional structure of concanavalin A. III. Structure of the monomer and its interactions with metals and saccharides."
Becker J.W., Reeke G.N. Jr., Wang J.L., Cunningham B.A., Edelman G.M.
J. Biol. Chem. 250:1513-1524(1975) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
[7]"The covalent and three-dimensional structure of concanavalin A. IV. Atomic coordinates, hydrogen bonding, and quaternary structure."
Reeke G.N. Jr., Becker J.W., Edelman G.M.
J. Biol. Chem. 250:1525-1547(1975) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
[8]"The structure of the saccharide-binding site of concanavalin A."
Derewenda Z., Yariv J., Helliwell J.R., Kalb A.J., Dodson E.J., Papiz M.Z., Wan T., Campbell J.
EMBO J. 8:2189-2193(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 164-290 IN COMPLEX WITH METHYL-ALPHA-D-MANNOPYRANOSIDE; CALCIUM AND MANGANESE IONS, SUBUNIT.
[9]"Atomic resolution structure of concanavalin A at 120 K."
Parkin S., Rupp B., Hope H.
Acta Crystallogr. D 52:1161-1168(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.2 ANGSTROMS).
[10]"The structural features of concanavalin A governing non-proline peptide isomerization."
Bouckaert J., Dewallef Y., Poortmans F., Wyns L., Loris R.
J. Biol. Chem. 275:19778-19787(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X01632 mRNA. Translation: CAA25787.1.
AF308777 mRNA. Translation: AAL09432.1.
PIRCVJBP. A03357.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
5CNAX-ray2.00A/B/C/D28-148[»]
ProteinModelPortalP02866.
SMRP02866. Positions 28-281.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP02866. 109 interactions.

Chemistry

BindingDBP02866.
ChEMBLCHEMBL5820.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D2.60.120.200. 1 hit.
InterProIPR008985. ConA-like_lec_gl_sf.
IPR013320. ConA-like_subgrp.
IPR016363. Lectin.
IPR000985. Lectin_LegA_CS.
IPR019825. Lectin_legB_Mn/Ca_BS.
IPR001220. Legume_lectin_dom.
[Graphical view]
PfamPF00139. Lectin_legB. 1 hit.
[Graphical view]
PIRSFPIRSF002690. L-type_lectin_plant. 1 hit.
SUPFAMSSF49899. SSF49899. 1 hit.
PROSITEPS00308. LECTIN_LEGUME_ALPHA. 1 hit.
PS00307. LECTIN_LEGUME_BETA. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP02866.

Entry information

Entry nameCONA_CANEN
AccessionPrimary (citable) accession number: P02866
Secondary accession number(s): Q947H0
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: October 3, 2003
Last modified: July 9, 2014
This is version 126 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references