SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P02866

- CONA_CANEN

UniProt

P02866 - CONA_CANEN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

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 – 1191Calcium By similarity
Binding sitei119 – 1191Carbohydrate
Binding sitei139 – 1391Carbohydrate; via amide nitrogen
Sitei148 – 1492Cleavage
Sitei163 – 1642Cleavage
Metal bindingi171 – 1711Manganese
Metal bindingi173 – 1731Calcium
Metal bindingi173 – 1731Manganese
Metal bindingi175 – 1751Calcium; via carbonyl oxygen
Metal bindingi177 – 1771Calcium
Metal bindingi182 – 1821Calcium
Metal bindingi182 – 1821Manganese
Metal bindingi187 – 1871Manganese
Sitei281 – 2822Cleavage

GO - Molecular functioni

  1. mannose binding Source: UniProtKB-KW
  2. metal ion binding Source: UniProtKB-KW
  3. protein binding Source: UniProtKB
Complete GO annotation...

Keywords - Ligandi

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

Names & Taxonomyi

Protein namesi
Recommended name:
Concanavalin-A
Short name:
Con A
Cleaved into the following chain:
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-APRO_0000017577Add
BLAST
Propeptidei149 – 16315PRO_0000017578Add
BLAST
Chaini164 – 281118Concanavalin, 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[»]
5CNAX-ray2.00A/B/C/D28-148[»]
ProteinModelPortaliP02866.
SMRiP02866. Positions 28-281.

Miscellaneous databases

EvolutionaryTraceiP02866.

Family & Domainsi

Region

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

Sequence similaritiesi

Belongs to the leguminous lectin family.

Keywords - Domaini

Signal

Family and domain databases

Gene3Di2.60.120.200. 1 hit.
InterProiIPR008985. 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]
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

MAISKKSSLF LPIFTFITMF LMVVNKVSSS THETNALHFM FNQFSKDQKD    50
LILQGDATTG TDGNLELTRV SSNGSPQGSS VGRALFYAPV HIWESSAVVA 100
SFEATFTFLI KSPDSHPADG IAFFISNIDS SIPSGSTGRL LGLFPDANVI 150
RNSTTIDFNA AYNADTIVAV ELDTYPNTDI GDPSYPHIGI DIKSVRSKKT 200
AKWNMQNGKV GTAHIIYNSV DKRLSAVVSY PNADSATVSY DVDLDNVLPE 250
WVRVGLSAST GLYKETNTIL SWSFTSKLKS NEIPDIATVV 290
Length:290
Mass (Da):31,480
Last modified:October 3, 2003 - v2
Checksum:i0F2F7DBBCF547E42
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti33 – 331E → Q AA sequence 1 Publication
Sequence conflicti35 – 351N → D AA sequence 1 Publication
Sequence conflicti62 – 621D → E in CAA25787. 1 Publication
Sequence conflicti66 – 661E → R in CAA25787. 1 Publication
Sequence conflicti77 – 771Q → E AA sequence 1 Publication
Sequence conflicti98 – 1014VVAS → TVSA AA sequence 1 Publication
Sequence conflicti107 – 1071T → A AA sequence 1 Publication
Sequence conflicti207 – 2071N → D AA sequence 1 Publication
Sequence conflicti245 – 2462DN → ND AA sequence 1 Publication

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 [» ]
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 IPR008985. 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 ]
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: July 9, 2014
This is version 126 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

Similar proteinsi