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P02866

- CONA_CANEN

UniProt

P02866 - CONA_CANEN

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Protein

Concanavalin-A

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

Functioni

D-mannose specific lectin.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi119 – 1191CalciumBy similarity
Binding sitei119 – 1191Carbohydrate
Binding sitei139 – 1391Carbohydrate; via amide nitrogen
Sitei148 – 1492Cleavage
Sitei163 – 1642Cleavage
Metal bindingi171 – 1711Manganese
Metal bindingi173 – 1731Calcium1 Publication
Metal bindingi173 – 1731Manganese
Metal bindingi175 – 1751Calcium; via carbonyl oxygen1 Publication
Metal bindingi177 – 1771Calcium1 Publication
Metal bindingi182 – 1821Calcium1 Publication
Metal bindingi182 – 1821Manganese
Metal bindingi187 – 1871Manganese
Sitei281 – 2822Cleavage

GO - Molecular functioni

  1. mannose binding Source: UniProtKB-KW
  2. metal ion binding Source: UniProtKB-KW
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

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 29291 PublicationAdd
BLAST
Chaini30 – 148119Concanavalin-A, 2nd partPRO_0000017577Add
BLAST
Propeptidei149 – 163151 PublicationPRO_0000017578Add
BLAST
Chaini164 – 281118Concanavalin-A, 1st partPRO_0000017579Add
BLAST
Propeptidei282 – 2909PRO_0000017580

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi152 – 1521N-linked (GlcNAc...)

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.

Keywords - PTMi

Glycoprotein

Interactioni

Subunit structurei

Homotetramer.1 Publication

Protein-protein interaction databases

IntActiP02866. 109 interactions.

Structurei

Secondary structure

1
290
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi28 – 325
Beta strandi34 – 429
Beta strandi51 – 555
Helixi61 – 633
Beta strandi64 – 685
Turni72 – 743
Beta strandi81 – 888
Beta strandi97 – 10913
Beta strandi113 – 1164
Beta strandi120 – 1267
Helixi138 – 1403
Turni141 – 1433
Beta strandi167 – 1737
Helixi178 – 1803
Beta strandi187 – 19610
Beta strandi198 – 2025
Beta strandi210 – 2189
Turni219 – 2224
Beta strandi223 – 2297
Beta strandi231 – 2333
Beta strandi236 – 2416
Helixi244 – 2463
Beta strandi250 – 25910
Beta strandi261 – 2633
Beta strandi268 – 28114

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
5CNAX-ray2.00A/B/C/D28-148[»]
ProteinModelPortaliP02866.
SMRiP02866. Positions 28-281.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP02866.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni262 – 2632Carbohydrate binding

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. 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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti33 – 331E → Q AA sequence (PubMed:1112814)Curated
Sequence conflicti35 – 351N → D AA sequence (PubMed:1112814)Curated
Sequence conflicti62 – 621D → E in CAA25787. (PubMed:3965973)Curated
Sequence conflicti66 – 661E → R in CAA25787. (PubMed:3965973)Curated
Sequence conflicti77 – 771Q → E AA sequence (PubMed:1112814)Curated
Sequence conflicti98 – 1014VVAS → TVSA AA sequence (PubMed:1112814)Curated
Sequence conflicti107 – 1071T → A AA sequence (PubMed:1112814)Curated
Sequence conflicti207 – 2071N → D AA sequence (PubMed:1112813)Curated
Sequence conflicti245 – 2462DN → ND AA sequence (PubMed:1112813)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
X01632 mRNA. Translation: CAA25787.1 .
AF308777 mRNA. Translation: AAL09432.1 .
PIRi A03357. CVJBP.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1APN X-ray 2.50 A/B 28-148 [» ]
1BXH X-ray 2.75 A/B/C/D 148-164 [» ]
1C57 neutron diffraction 2.40 A 148-164 [» ]
1CES X-ray 2.70 A/B 28-148 [» ]
1CJP X-ray 2.78 A/B/C/D 30-148 [» ]
1CN1 X-ray 3.20 A/B 30-281 [» ]
1CON X-ray 2.00 A 28-148 [» ]
1CVN X-ray 2.30 A/B/C/D 30-148 [» ]
1DQ0 X-ray 1.70 A 28-148 [» ]
1DQ1 X-ray 2.15 A 28-148 [» ]
1DQ2 X-ray 2.05 A/B 28-148 [» ]
1DQ4 X-ray 2.90 A/B 28-148 [» ]
1DQ5 X-ray 2.00 A 28-148 [» ]
1DQ6 X-ray 1.90 A 28-148 [» ]
1ENQ X-ray 2.50 A/B/C/D 30-148 [» ]
1ENR X-ray 1.83 A 28-148 [» ]
1ENS X-ray 2.80 A/B 30-148 [» ]
1GIC X-ray 2.00 A/B 28-148 [» ]
1GKB X-ray 1.56 A/B 148-164 [» ]
1HQW X-ray 2.40 A 30-148 [» ]
1I3H X-ray 1.20 A 28-148 [» ]
1JBC X-ray 1.15 A 28-148 [» ]
1JN2 X-ray 1.90 P 28-148 [» ]
1JOJ X-ray 3.00 A/B/C/D 28-148 [» ]
1JUI X-ray 2.75 A/B/C/D 28-148 [» ]
1JW6 X-ray 1.93 A 28-148 [» ]
1JYC X-ray 2.75 A/B/C/D 28-148 [» ]
1JYI X-ray 2.75 A/B/C/D 28-148 [» ]
1NLS X-ray 0.94 A 28-148 [» ]
1NXD X-ray 1.90 1/2/3/4 148-164 [» ]
1ONA X-ray 2.35 A/B/C/D 30-148 [» ]
1QGL X-ray 2.66 A/B 30-148 [» ]
1QNY X-ray 1.80 A 28-148 [» ]
1SCR X-ray 2.00 A 28-148 [» ]
1SCS X-ray 1.60 A 28-148 [» ]
1TEI X-ray 2.70 A/B/C/D/E/F/G/H 28-148 [» ]
1VAL X-ray 3.00 A/B/C/D 30-148 [» ]
1VAM X-ray 2.75 A/B/C/D 30-148 [» ]
1XQN neutron diffraction 2.50 A 28-148 [» ]
2CNA X-ray 2.00 A 28-148 [» ]
2CTV X-ray 1.95 A 28-148 [» ]
2ENR X-ray 2.35 A 28-148 [» ]
2UU8 X-ray 0.94 A 148-164 [» ]
2YZ4 neutron diffraction 2.20 A 28-148 [» ]
3CNA X-ray 2.40 A 30-281 [» ]
3D4K X-ray 1.80 A/B/C/D 148-164 [» ]
3ENR X-ray 2.40 A/B 148-164 [» ]
3NWK X-ray 2.09 A/B/C/D 148-164 [» ]
4P9W X-ray 2.11 A/B/C/D 28-148 [» ]
4P9X X-ray 2.06 A/B/C/D 28-148 [» ]
4P9Y X-ray 1.89 A/B 28-148 [» ]
5CNA X-ray 2.00 A/B/C/D 28-148 [» ]
ProteinModelPortali P02866.
SMRi P02866. Positions 28-281.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi P02866. 109 interactions.

Chemistry

BindingDBi P02866.
ChEMBLi CHEMBL5820.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Miscellaneous databases

EvolutionaryTracei P02866.

Family and domain databases

Gene3Di 2.60.120.200. 1 hit.
InterProi IPR013320. ConA-like_dom.
IPR016363. Lectin.
IPR000985. Lectin_LegA_CS.
IPR019825. Lectin_legB_Mn/Ca_BS.
IPR001220. Legume_lectin_dom.
[Graphical view ]
Pfami PF00139. Lectin_legB. 1 hit.
[Graphical view ]
PIRSFi PIRSF002690. L-type_lectin_plant. 1 hit.
SUPFAMi SSF49899. SSF49899. 1 hit.
PROSITEi PS00308. LECTIN_LEGUME_ALPHA. 1 hit.
PS00307. LECTIN_LEGUME_BETA. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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).

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: October 29, 2014
This is version 128 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

External Data

Dasty 3