P02866 (CONA_CANEN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names	Recommended name: Concanavalin-A Short name=Con A Cleaved into the following chain: Concanavalin, 1st part
Organism	Canavalia ensiformis (Jack bean) (Dolichos ensiformis)
Taxonomic identifier	3823 [NCBI]
Taxonomic lineage	cellular organisms › Eukaryota › Viridiplantae › Streptophyta › Streptophytina › Embryophyta › Tracheophyta › Euphyllophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › fabids › Fabales › Fabaceae › Papilionoideae › Phaseoleae › Canavalia

Protein attributes

Sequence length	290 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 other 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.

Ontologies

Keywords
Domain	Signal
Ligand	Calcium Lectin Manganese Mannose-binding Metal-binding
PTM	Glycoprotein
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Molecular_function	mannose binding Inferred from electronic annotation. Source: UniProtKB-KW metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 29

29

Ref.3

Chain

30 – 148

119

Concanavalin-A

PRO_0000017577

Propeptide

149 – 163

15

PRO_0000017578

Chain

164 – 281

118

Concanavalin, 1st part

PRO_0000017579

Propeptide

282 – 290

9

PRO_0000017580

Regions

Region

262 – 263

2

Carbohydrate binding

Sites

Metal binding

119

1

Calcium By similarity

Metal binding

171

1

Manganese

Metal binding

173

1

Calcium

Metal binding

173

1

Manganese

Metal binding

175

1

Calcium; via carbonyl oxygen

Metal binding

177

1

Calcium

Metal binding

182

1

Calcium

Metal binding

182

1

Manganese

Metal binding

187

1

Manganese

Binding site

119

1

Carbohydrate

Binding site

139

1

Carbohydrate; via amide nitrogen

Site

148 – 149

2

Cleavage

Site

163 – 164

2

Cleavage

Site

281 – 282

2

Cleavage

Amino acid modifications

Glycosylation

152

1

N-linked (GlcNAc...)

Experimental info

Sequence conflict

33

1

E → Q AA sequence Ref.3

Sequence conflict

35

1

N → D AA sequence Ref.3

Sequence conflict

62

1

D → E in CAA25787. Ref.1

Sequence conflict

66

1

E → R in CAA25787. Ref.1

Sequence conflict

77

1

Q → E AA sequence Ref.3

Sequence conflict

98 – 101

4

VVAS → TVSA AA sequence Ref.3

Sequence conflict

107

1

T → A AA sequence Ref.3

Sequence conflict

207

1

N → D AA sequence Ref.4

Sequence conflict

245 – 246

2

DN → ND AA sequence Ref.4

Secondary structure

1

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290

Helix Strand Turn

Details...

Beta strand

30 – 32

3

Beta strand

34 – 42

9

Beta strand

51 – 55

5

Helix

61 – 63

3

Beta strand

64 – 68

5

Turn

72 – 74

3

Beta strand

81 – 88

8

Beta strand

97 – 109

13

Beta strand

113 – 116

4

Beta strand

120 – 126

7

Helix

138 – 140

3

Turn

141 – 143

3

Beta strand

167 – 173

7

Helix

178 – 180

3

Beta strand

184 – 186

3

Beta strand

187 – 196

10

Beta strand

198 – 202

5

Beta strand

210 – 218

9

Turn

219 – 222

4

Beta strand

223 – 229

7

Beta strand

231 – 233

3

Beta strand

236 – 241

6

Helix

244 – 246

3

Beta strand

250 – 259

10

Beta strand

261 – 263

3

Beta strand

268 – 281

14

Sequences

	Sequence		Length	Mass (Da)
	P02866 [UniParc]. Last modified October 3, 2003. Version 2. Checksum: 0F2F7DBBCF547E42	FASTA	290	31,480
	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

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.

Web resources

Worthington enzyme manual

Functional Glycomics Gateway - Glycan Binding

Con A (Canavalia ensiformis)

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X01632 mRNA. Translation: CAA25787.1.
AF308777 mRNA. Translation: AAL09432.1.

PIR

CVJBP. A03357.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1APN	X-ray	2.50	A/B	30-281	[»]
1BXH	X-ray	2.75	A/B/C/D	30-281	[»]
1C57	neutron diffraction	2.40	A	30-281	[»]
1CES	X-ray	2.70	A/B	30-281	[»]
1CJP	X-ray	2.78	A/B/C/D	30-281	[»]
1CN1	X-ray	3.20	A/B	30-281	[»]
1CON	X-ray	2.00	A	30-281	[»]
1CVN	X-ray	2.30	A/B/C/D	30-281	[»]
1DQ0	X-ray	1.70	A	30-281	[»]
1DQ1	X-ray	2.15	A	30-281	[»]
1DQ2	X-ray	2.05	A/B	30-281	[»]
1DQ4	X-ray	2.90	A/B	30-281	[»]
1DQ5	X-ray	2.00	A	30-281	[»]
1DQ6	X-ray	1.90	A	30-281	[»]
1ENQ	X-ray	2.50	A/B/C/D	30-281	[»]
1ENR	X-ray	1.83	A	30-281	[»]
1ENS	X-ray	2.80	A/B	30-281	[»]
1GIC	X-ray	2.00	A/B	30-281	[»]
1GKB	X-ray	1.56	A/B	30-281	[»]
1HQW	X-ray	2.40	A	30-281	[»]
1I3H	X-ray	1.20	A	30-281	[»]
1JBC	X-ray	1.15	A	30-281	[»]
1JN2	X-ray	1.90	P	30-281	[»]
1JOJ	X-ray	3.00	A/B/C/D	30-281	[»]
1JUI	X-ray	2.75	A/B/C/D	30-281	[»]
1JW6	X-ray	1.93	A	30-281	[»]
1JYC	X-ray	2.75	A/B/C/D	30-281	[»]
1JYI	X-ray	2.75	A/B/C/D	30-281	[»]
1NLS	X-ray	0.94	A	30-281	[»]
1NXD	X-ray	1.90	1/2/3/4	30-281	[»]
1ONA	X-ray	2.35	A/B/C/D	30-281	[»]
1QGL	X-ray	2.66	A/B	30-281	[»]
1QNY	X-ray	1.80	A	30-281	[»]
1SCR	X-ray	2.00	A	30-281	[»]
1SCS	X-ray	1.60	A	30-281	[»]
1TEI	X-ray	2.70	A/B/C/D/E/F/G/H	30-281	[»]
1VAL	X-ray	3.00	A/B/C/D	30-281	[»]
1VAM	X-ray	2.75	A/B/C/D	30-281	[»]
1XQN	neutron diffraction	2.50	A	30-281	[»]
2CNA	X-ray	2.00	A	30-281	[»]
2CTV	X-ray	1.95	A	30-281	[»]
2ENR	X-ray	2.35	A	30-281	[»]
2UU8	X-ray	0.94	A	30-281	[»]
2YZ4	neutron diffraction	2.20	A	30-281	[»]
3CNA	X-ray	2.40	A	30-281	[»]
3D4K	X-ray	1.80	A/B/C/D	30-281	[»]
3ENR	X-ray	2.40	A/B	30-281	[»]
3NWK	X-ray	2.09	A/B/C/D	30-281	[»]
5CNA	X-ray	2.00	A/B/C/D	30-281	[»]

ProteinModelPortal

P02866.

SMR

P02866. Positions 28-281.

ModBase

Search...

Protein-protein interaction databases

IntAct

P02866. 106 interactions.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Family and domain databases

Gene3D

2.60.120.200. 1 hit.

InterPro

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]

Pfam

PF00139. Lectin_legB. 1 hit.
[Graphical view]

PIRSF

PIRSF002690. L-type_lectin_plant. 1 hit.

SUPFAM

SSF49899. ConA_like_lec_gl. 1 hit.

PROSITE

PS00308. LECTIN_LEGUME_ALPHA. 1 hit.
PS00307. LECTIN_LEGUME_BETA. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

P02866.

ChEMBL

CHEMBL5820.

EvolutionaryTrace

P02866.

Entry information

Entry name

CONA_CANEN

Accession

Primary (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:	April 3, 2013
This is version 118 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program