CONA_CANEN
ID CONA_CANEN Reviewed; 290 AA.
AC P02866; Q947H0;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2003, sequence version 2.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Concanavalin-A;
DE Short=Con A;
DE Flags: Precursor;
OS Canavalia ensiformis (Jack bean) (Dolichos ensiformis).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Canavalia.
OX NCBI_TaxID=3823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3965973; DOI=10.1038/313064a0;
RA Carrington D.M., Auffret A., Hanke D.E.;
RT "Polypeptide ligation occurs during post-translational modification of
RT concanavalin A.";
RL Nature 313:64-67(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. U-02;
RA Ramis C., Gomord V.;
RL Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PROTEIN SEQUENCE OF 30-148.
RX PubMed=1112814; DOI=10.1016/s0021-9258(19)41841-3;
RA Cunningham B.A., Wang J.L., Waxdal M.J., Edelman G.M.;
RT "The covalent and three-dimensional structure of concanavalin A. II. Amino
RT acid sequence of cyanogen bromide fragment F3.";
RL J. Biol. Chem. 250:1503-1512(1975).
RN [4]
RP PROTEIN SEQUENCE OF 164-281.
RX PubMed=1112813; DOI=10.1016/s0021-9258(19)41840-1;
RA Wang J.L., Cunningham B.A., Waxdal M.J., Edelman G.M.;
RT "The covalent and three-dimensional structural of concanavalin A. I. Amino
RT acid sequence of cyanogen bromide fragments F1 and F2.";
RL J. Biol. Chem. 250:1490-1502(1975).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
RX PubMed=4638345; DOI=10.1021/bi00776a006;
RA Hardman K.D., Ainsworth C.F.;
RT "Structure of concanavalin A at 2.4-A resolution.";
RL Biochemistry 11:4910-4919(1972).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
RX PubMed=1112815; DOI=10.1016/s0021-9258(19)41842-5;
RA Becker J.W., Reeke G.N. Jr., Wang J.L., Cunningham B.A., Edelman G.M.;
RT "The covalent and three-dimensional structure of concanavalin A. III.
RT Structure of the monomer and its interactions with metals and
RT saccharides.";
RL J. Biol. Chem. 250:1513-1524(1975).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
RX PubMed=1112816; DOI=10.1016/s0021-9258(19)41843-7;
RA Reeke G.N. Jr., Becker J.W., Edelman G.M.;
RT "The covalent and three-dimensional structure of concanavalin A. IV. Atomic
RT coordinates, hydrogen bonding, and quaternary structure.";
RL J. Biol. Chem. 250:1525-1547(1975).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 164-290 IN COMPLEX WITH
RP METHYL-ALPHA-D-MANNOPYRANOSIDE; CALCIUM AND MANGANESE IONS, AND SUBUNIT.
RX PubMed=2792084; DOI=10.1002/j.1460-2075.1989.tb08341.x;
RA Derewenda Z., Yariv J., Helliwell J.R., Kalb A.J., Dodson E.J., Papiz M.Z.,
RA Wan T., Campbell J.;
RT "The structure of the saccharide-binding site of concanavalin A.";
RL EMBO J. 8:2189-2193(1989).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (1.2 ANGSTROMS).
RX PubMed=15299577; DOI=10.1107/s0907444996009237;
RA Parkin S., Rupp B., Hope H.;
RT "Atomic resolution structure of concanavalin A at 120 K.";
RL Acta Crystallogr. D 52:1161-1168(1996).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).
RX PubMed=10748006; DOI=10.1074/jbc.m001251200;
RA Bouckaert J., Dewallef Y., Poortmans F., Wyns L., Loris R.;
RT "The structural features of concanavalin A governing non-proline peptide
RT isomerization.";
RL J. Biol. Chem. 275:19778-19787(2000).
CC -!- FUNCTION: D-mannose specific lectin.
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:2792084}.
CC -!- PTM: The mature chain consists of residues 164-281 followed by 30-148.
CC To form a mature chain the precursor undergoes further post-
CC translational modification after removal of the signal sequence;
CC cleavage after Asn at positions 148, 163, and 281 is followed by
CC transposition and ligation (By formation of a new peptide bond) of
CC residues 164-281 and 30-148.
CC -!- MISCELLANEOUS: Binds one manganese (or another transition metal) ion
CC and one calcium ion. The metal ions are essential for the saccharide-
CC binding and cell-agglutinating activities.
CC -!- SIMILARITY: Belongs to the leguminous lectin family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Worthington enzyme manual;
CC URL="http://www.worthington-biochem.com/CONA/";
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - Glycan Binding;
CC Note=Con A (Canavalia ensiformis);
CC URL="http://www.functionalglycomics.org/glycomics/GBPServlet?&operationType=view&cbpId=cbp_pla_other_414";
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DR EMBL; X01632; CAA25787.1; -; mRNA.
DR EMBL; AF308777; AAL09432.1; -; mRNA.
DR PIR; A03357; CVJBP.
DR PDB; 1APN; X-ray; 2.50 A; A/B=28-148.
DR PDB; 1BXH; X-ray; 2.75 A; A/B/C/D=148-164.
DR PDB; 1C57; Neutron; 2.40 A; A=148-164.
DR PDB; 1CES; X-ray; 2.70 A; A/B=28-148.
DR PDB; 1CJP; X-ray; 2.78 A; A/B/C/D=30-148.
DR PDB; 1CN1; X-ray; 3.20 A; A/B=30-281.
DR PDB; 1CON; X-ray; 2.00 A; A=28-148.
DR PDB; 1CVN; X-ray; 2.30 A; A/B/C/D=30-148.
DR PDB; 1DQ0; X-ray; 1.70 A; A=28-148.
DR PDB; 1DQ1; X-ray; 2.15 A; A=28-148.
DR PDB; 1DQ2; X-ray; 2.05 A; A/B=28-148.
DR PDB; 1DQ4; X-ray; 2.90 A; A/B=28-148.
DR PDB; 1DQ5; X-ray; 2.00 A; A=28-148.
DR PDB; 1DQ6; X-ray; 1.90 A; A=28-148.
DR PDB; 1ENQ; X-ray; 2.50 A; A/B/C/D=30-148.
DR PDB; 1ENR; X-ray; 1.83 A; A=28-148.
DR PDB; 1ENS; X-ray; 2.80 A; A/B=30-148.
DR PDB; 1GIC; X-ray; 2.00 A; A/B=28-148.
DR PDB; 1GKB; X-ray; 1.56 A; A/B=148-164.
DR PDB; 1HQW; X-ray; 2.40 A; A=30-148.
DR PDB; 1I3H; X-ray; 1.20 A; A=28-148.
DR PDB; 1JBC; X-ray; 1.15 A; A=28-148.
DR PDB; 1JN2; X-ray; 1.90 A; P=28-148.
DR PDB; 1JOJ; X-ray; 3.00 A; A/B/C/D=28-148.
DR PDB; 1JUI; X-ray; 2.75 A; A/B/C/D=28-148.
DR PDB; 1JW6; X-ray; 1.93 A; A=28-148.
DR PDB; 1JYC; X-ray; 2.75 A; A/B/C/D=28-148.
DR PDB; 1JYI; X-ray; 2.75 A; A/B/C/D=28-148.
DR PDB; 1NLS; X-ray; 0.94 A; A=28-148.
DR PDB; 1NXD; X-ray; 1.90 A; 1/2/3/4=148-164.
DR PDB; 1ONA; X-ray; 2.35 A; A/B/C/D=30-148.
DR PDB; 1QGL; X-ray; 2.66 A; A/B=30-148.
DR PDB; 1QNY; X-ray; 1.80 A; A=28-148.
DR PDB; 1SCR; X-ray; 2.00 A; A=28-148.
DR PDB; 1SCS; X-ray; 1.60 A; A=28-148.
DR PDB; 1TEI; X-ray; 2.70 A; A/B/C/D/E/F/G/H=28-148.
DR PDB; 1VAL; X-ray; 3.00 A; A/B/C/D=30-148.
DR PDB; 1VAM; X-ray; 2.75 A; A/B/C/D=30-148.
DR PDB; 1XQN; Neutron; 2.50 A; A=28-148.
DR PDB; 2CNA; X-ray; 2.00 A; A=28-148.
DR PDB; 2CTV; X-ray; 1.95 A; A=28-148.
DR PDB; 2ENR; X-ray; 2.35 A; A=28-148.
DR PDB; 2UU8; X-ray; 0.94 A; A=148-164.
DR PDB; 2YZ4; Neutron; 2.20 A; A=28-148.
DR PDB; 3CNA; X-ray; 2.40 A; A=30-281.
DR PDB; 3D4K; X-ray; 1.80 A; A/B/C/D=148-164.
DR PDB; 3ENR; X-ray; 2.40 A; A/B=148-164.
DR PDB; 3NWK; X-ray; 2.09 A; A/B/C/D=148-164.
DR PDB; 4P9W; X-ray; 2.11 A; A/B/C/D=28-148.
DR PDB; 4P9X; X-ray; 2.06 A; A/B/C/D=28-148.
DR PDB; 4P9Y; X-ray; 1.89 A; A/B=28-148.
DR PDB; 4PF5; X-ray; 2.04 A; A/B=28-148.
DR PDB; 5CNA; X-ray; 2.00 A; A/B/C/D=28-148.
DR PDB; 5O6N; X-ray; 1.35 A; A=148-164.
DR PDB; 5WEY; Other; 1.80 A; A=148-164.
DR PDB; 5Z5L; X-ray; 2.30 A; A/B/C/D=148-164.
DR PDB; 5Z5N; X-ray; 2.04 A; A/B/C/D=148-164.
DR PDB; 5Z5P; X-ray; 1.40 A; A/B=148-164.
DR PDB; 5Z5Y; X-ray; 1.89 A; A/B=148-164.
DR PDB; 5ZAC; X-ray; 2.59 A; A/B/C/D=148-164.
DR PDB; 6AHG; X-ray; 2.83 A; A/B/C=148-164.
DR PDB; 6H2M; X-ray; 1.93 A; A=148-164.
DR PDB; 6XT6; X-ray; 2.10 A; A/B=30-290.
DR PDB; 7MG1; X-ray; 2.00 A; A=148-164.
DR PDB; 7MG2; X-ray; 1.80 A; A=148-164.
DR PDB; 7MG3; X-ray; 1.60 A; A=148-164.
DR PDB; 7MG4; X-ray; 2.00 A; A=148-164.
DR PDB; 7MG5; X-ray; 2.10 A; A/B=148-164.
DR PDB; 7MG6; X-ray; 1.70 A; A/B=148-164.
DR PDB; 7MG7; X-ray; 1.75 A; A/B=148-164.
DR PDB; 7MG8; X-ray; 3.00 A; A/B=148-164.
DR PDB; 7MG9; X-ray; 2.55 A; A/B=148-164.
DR PDB; 7MGA; X-ray; 2.00 A; A/B=148-164.
DR PDB; 7MGB; X-ray; 2.45 A; A/B/C/D=148-164.
DR PDB; 7MGC; X-ray; 2.92 A; A/B/C/D=148-164.
DR PDB; 7MGD; X-ray; 2.05 A; A/B/C/D=148-164.
DR PDBsum; 1APN; -.
DR PDBsum; 1BXH; -.
DR PDBsum; 1C57; -.
DR PDBsum; 1CES; -.
DR PDBsum; 1CJP; -.
DR PDBsum; 1CN1; -.
DR PDBsum; 1CON; -.
DR PDBsum; 1CVN; -.
DR PDBsum; 1DQ0; -.
DR PDBsum; 1DQ1; -.
DR PDBsum; 1DQ2; -.
DR PDBsum; 1DQ4; -.
DR PDBsum; 1DQ5; -.
DR PDBsum; 1DQ6; -.
DR PDBsum; 1ENQ; -.
DR PDBsum; 1ENR; -.
DR PDBsum; 1ENS; -.
DR PDBsum; 1GIC; -.
DR PDBsum; 1GKB; -.
DR PDBsum; 1HQW; -.
DR PDBsum; 1I3H; -.
DR PDBsum; 1JBC; -.
DR PDBsum; 1JN2; -.
DR PDBsum; 1JOJ; -.
DR PDBsum; 1JUI; -.
DR PDBsum; 1JW6; -.
DR PDBsum; 1JYC; -.
DR PDBsum; 1JYI; -.
DR PDBsum; 1NLS; -.
DR PDBsum; 1NXD; -.
DR PDBsum; 1ONA; -.
DR PDBsum; 1QGL; -.
DR PDBsum; 1QNY; -.
DR PDBsum; 1SCR; -.
DR PDBsum; 1SCS; -.
DR PDBsum; 1TEI; -.
DR PDBsum; 1VAL; -.
DR PDBsum; 1VAM; -.
DR PDBsum; 1XQN; -.
DR PDBsum; 2CNA; -.
DR PDBsum; 2CTV; -.
DR PDBsum; 2ENR; -.
DR PDBsum; 2UU8; -.
DR PDBsum; 2YZ4; -.
DR PDBsum; 3CNA; -.
DR PDBsum; 3D4K; -.
DR PDBsum; 3ENR; -.
DR PDBsum; 3NWK; -.
DR PDBsum; 4P9W; -.
DR PDBsum; 4P9X; -.
DR PDBsum; 4P9Y; -.
DR PDBsum; 4PF5; -.
DR PDBsum; 5CNA; -.
DR PDBsum; 5O6N; -.
DR PDBsum; 5WEY; -.
DR PDBsum; 5Z5L; -.
DR PDBsum; 5Z5N; -.
DR PDBsum; 5Z5P; -.
DR PDBsum; 5Z5Y; -.
DR PDBsum; 5ZAC; -.
DR PDBsum; 6AHG; -.
DR PDBsum; 6H2M; -.
DR PDBsum; 6XT6; -.
DR PDBsum; 7MG1; -.
DR PDBsum; 7MG2; -.
DR PDBsum; 7MG3; -.
DR PDBsum; 7MG4; -.
DR PDBsum; 7MG5; -.
DR PDBsum; 7MG6; -.
DR PDBsum; 7MG7; -.
DR PDBsum; 7MG8; -.
DR PDBsum; 7MG9; -.
DR PDBsum; 7MGA; -.
DR PDBsum; 7MGB; -.
DR PDBsum; 7MGC; -.
DR PDBsum; 7MGD; -.
DR AlphaFoldDB; P02866; -.
DR PCDDB; P02866; -.
DR SMR; P02866; -.
DR IntAct; P02866; 109.
DR BindingDB; P02866; -.
DR ChEMBL; CHEMBL5820; -.
DR UniLectin; P02866; -.
DR ABCD; P02866; 6 sequenced antibodies.
DR EvolutionaryTrace; P02866; -.
DR GO; GO:0005537; F:mannose binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd06899; lectin_legume_LecRK_Arcelin_ConA; 1.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR016363; L-lectin.
DR InterPro; IPR000985; Lectin_LegA_CS.
DR InterPro; IPR019825; Lectin_legB_Mn/Ca_BS.
DR InterPro; IPR001220; Legume_lectin_dom.
DR Pfam; PF00139; Lectin_legB; 1.
DR PIRSF; PIRSF002690; L-type_lectin_plant; 1.
DR SUPFAM; SSF49899; SSF49899; 1.
DR PROSITE; PS00308; LECTIN_LEGUME_ALPHA; 1.
DR PROSITE; PS00307; LECTIN_LEGUME_BETA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium; Direct protein sequencing; Glycoprotein; Lectin;
KW Manganese; Mannose-binding; Metal-binding; Signal.
FT SIGNAL 1..29
FT /evidence="ECO:0000269|PubMed:1112814"
FT CHAIN 30..148
FT /note="Concanavalin-A, 2nd part"
FT /id="PRO_0000017577"
FT PROPEP 149..163
FT /evidence="ECO:0000269|PubMed:1112813"
FT /id="PRO_0000017578"
FT CHAIN 164..281
FT /note="Concanavalin-A, 1st part"
FT /id="PRO_0000017579"
FT PROPEP 282..290
FT /id="PRO_0000017580"
FT BINDING 119
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT BINDING 119
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 139
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT BINDING 171
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT BINDING 173
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:2792084"
FT BINDING 173
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT BINDING 175
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:2792084"
FT BINDING 177
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:2792084"
FT BINDING 182
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:2792084"
FT BINDING 182
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT BINDING 187
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT BINDING 262..263
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT SITE 148..149
FT /note="Cleavage"
FT SITE 163..164
FT /note="Cleavage"
FT SITE 281..282
FT /note="Cleavage"
FT CARBOHYD 152
FT /note="N-linked (GlcNAc...) asparagine"
FT CONFLICT 33
FT /note="E -> Q (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 35
FT /note="N -> D (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 62
FT /note="D -> E (in Ref. 1; CAA25787)"
FT /evidence="ECO:0000305"
FT CONFLICT 66
FT /note="E -> R (in Ref. 1; CAA25787)"
FT /evidence="ECO:0000305"
FT CONFLICT 77
FT /note="Q -> E (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 98..101
FT /note="VVAS -> TVSA (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 107
FT /note="T -> A (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 207
FT /note="N -> D (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 245..246
FT /note="DN -> ND (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 3..8
FT /evidence="ECO:0007829|PDB:1JBC"
FT STRAND 10..12
FT /evidence="ECO:0007829|PDB:1JBC"
FT STRAND 28..32
FT /evidence="ECO:0007829|PDB:1NLS"
FT STRAND 34..42
FT /evidence="ECO:0007829|PDB:1NLS"
FT STRAND 51..55
FT /evidence="ECO:0007829|PDB:1NLS"
FT HELIX 61..63
FT /evidence="ECO:0007829|PDB:1NLS"
FT STRAND 64..68
FT /evidence="ECO:0007829|PDB:1NLS"
FT TURN 72..74
FT /evidence="ECO:0007829|PDB:1GIC"
FT STRAND 81..88
FT /evidence="ECO:0007829|PDB:1NLS"
FT STRAND 97..109
FT /evidence="ECO:0007829|PDB:1NLS"
FT STRAND 113..116
FT /evidence="ECO:0007829|PDB:1NLS"
FT STRAND 120..126
FT /evidence="ECO:0007829|PDB:1NLS"
FT HELIX 138..140
FT /evidence="ECO:0007829|PDB:1NLS"
FT TURN 141..143
FT /evidence="ECO:0007829|PDB:1NLS"
FT STRAND 167..173
FT /evidence="ECO:0007829|PDB:6XT6"
FT HELIX 178..180
FT /evidence="ECO:0007829|PDB:6XT6"
FT STRAND 187..196
FT /evidence="ECO:0007829|PDB:6XT6"
FT STRAND 198..202
FT /evidence="ECO:0007829|PDB:6XT6"
FT STRAND 209..218
FT /evidence="ECO:0007829|PDB:6XT6"
FT TURN 219..222
FT /evidence="ECO:0007829|PDB:6XT6"
FT STRAND 223..229
FT /evidence="ECO:0007829|PDB:6XT6"
FT STRAND 236..241
FT /evidence="ECO:0007829|PDB:6XT6"
FT HELIX 244..246
FT /evidence="ECO:0007829|PDB:6XT6"
FT STRAND 250..259
FT /evidence="ECO:0007829|PDB:6XT6"
FT STRAND 261..263
FT /evidence="ECO:0007829|PDB:6XT6"
FT STRAND 268..280
FT /evidence="ECO:0007829|PDB:6XT6"
SQ SEQUENCE 290 AA; 31480 MW; 0F2F7DBBCF547E42 CRC64;
MAISKKSSLF LPIFTFITMF LMVVNKVSSS THETNALHFM FNQFSKDQKD LILQGDATTG
TDGNLELTRV SSNGSPQGSS VGRALFYAPV HIWESSAVVA SFEATFTFLI KSPDSHPADG
IAFFISNIDS SIPSGSTGRL LGLFPDANVI RNSTTIDFNA AYNADTIVAV ELDTYPNTDI
GDPSYPHIGI DIKSVRSKKT AKWNMQNGKV GTAHIIYNSV DKRLSAVVSY PNADSATVSY
DVDLDNVLPE WVRVGLSAST GLYKETNTIL SWSFTSKLKS NEIPDIATVV
