CONA_CANGL
ID CONA_CANGL Reviewed; 290 AA.
AC P14894;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1990, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Concanavalin-A;
DE Short=Con A;
DE Flags: Precursor;
OS Canavalia gladiata (Sword bean) (Dolichos gladiatus).
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=3824;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Seedling;
RX PubMed=2404793; DOI=10.1016/0014-5793(90)80083-u;
RA Yamauchi D., Minamikawa T.;
RT "Structure of the gene encoding concanavalin A from Canavalia gladiata and
RT its expression in Escherichia coli cells.";
RL FEBS Lett. 260:127-130(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Seed;
RA Yamauchi D., Nakamura K., Asahi T., Minamikawa T.;
RT "Nucleotide sequence of cDNA for concanavalin A from Canavalia gladiata
RT seeds.";
RL Plant Cell Physiol. 30:147-150(1989).
RN [3]
RP PROTEIN SEQUENCE OF 164-183, AND FUNCTION.
RC TISSUE=Fruit;
RX PubMed=15935326; DOI=10.1016/j.abb.2005.05.004;
RA Wong J.H., Ng T.B.;
RT "Isolation and characterization of a glucose/mannose/rhamnose-specific
RT lectin from the knife bean Canavalia gladiata.";
RL Arch. Biochem. Biophys. 439:91-98(2005).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 30-281 IN COMPLEX WITH
RP ALPHA-AMINOBUTYRIC ACID; ALPHA-METHYL-MANNOSIDE; CALCIUM AND MANGANESE
RP IONS, IDENTIFICATION BY MASS SPECTROMETRY, AND SUBUNIT.
RX PubMed=17683532; DOI=10.1186/1472-6807-7-52;
RA Delatorre P., Rocha B.A.M., Souza E.P., Oliveira T.M., Bezerra G.A.,
RA Moreno F.B.M.B., Freitas B.T., Santi-Gadelha T., Sampaio A.H.,
RA Azevedo W.F. Jr., Cavada B.S.;
RT "Structure of a lectin from Canavalia gladiata seeds: new structural
RT insights for old molecules.";
RL BMC Struct. Biol. 7:52-52(2007).
CC -!- FUNCTION: Glucose/D-mannose/rhamnose specific lectin. Has
CC hemagglutinating activity towards rabbit erythrocytes. Has mitogenic
CC activity towards murine splenocytes that is inhibited by glucose.
CC Inhibits HIV-1 reverse transcriptase with an IC(50) of 35 uM. Has a
CC potent antiproliferative activity against L1210 leukemia cells in vitro
CC that is not inhibited by glucose. Inhibits translation in cell-free
CC rabbit reticulocyte system with an IC(50) of 2.08 uM. Lacks anti-fungal
CC activity against M.arachidicola, B.cenera and F.oxysporum.
CC {ECO:0000269|PubMed:15935326}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:17683532}.
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 Asn-148, Asn-163, and Asn-281 is
CC followed by transposition and ligation (By formation of a new peptide
CC bond) of 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}.
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DR EMBL; X16041; CAA34163.1; -; Genomic_DNA.
DR PIR; A34139; A34139.
DR PDB; 1WUV; X-ray; 2.30 A; A/D/G/J=28-148.
DR PDB; 2D7F; X-ray; 2.31 A; A/F/L/S=28-148.
DR PDB; 2EF6; X-ray; 2.10 A; A/B/C/D=28-148.
DR PDB; 2OVU; X-ray; 1.50 A; A=28-148.
DR PDB; 2P2K; X-ray; 1.98 A; A/B/C/D=28-148.
DR PDBsum; 1WUV; -.
DR PDBsum; 2D7F; -.
DR PDBsum; 2EF6; -.
DR PDBsum; 2OVU; -.
DR PDBsum; 2P2K; -.
DR AlphaFoldDB; P14894; -.
DR SMR; P14894; -.
DR UniLectin; P14894; -.
DR EvolutionaryTrace; P14894; -.
DR GO; GO:0005537; F:mannose binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0048029; F:monosaccharide binding; IDA:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0051781; P:positive regulation of cell division; IEA:UniProtKB-KW.
DR GO; GO:0045840; P:positive regulation of mitotic nuclear division; IDA:UniProtKB.
DR GO; GO:0050688; P:regulation of defense response to virus; 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; Antiviral protein; Calcium; Direct protein sequencing;
KW Glycoprotein; Hemagglutinin; Lectin; Manganese; Mannose-binding;
KW Metal-binding; Mitogen; Signal.
FT SIGNAL 1..29
FT CHAIN 30..148
FT /note="Concanavalin-A, 2nd part"
FT /id="PRO_0000017573"
FT PROPEP 149..163
FT /evidence="ECO:0000269|PubMed:15935326"
FT /id="PRO_0000017574"
FT CHAIN 164..281
FT /note="Concanavalin-A, 1st part"
FT /id="PRO_0000017575"
FT PROPEP 282..290
FT /id="PRO_0000017576"
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:17683532"
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:17683532"
FT BINDING 177
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:17683532"
FT BINDING 182
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:17683532"
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 /evidence="ECO:0000305"
FT STRAND 28..32
FT /evidence="ECO:0007829|PDB:2OVU"
FT STRAND 34..43
FT /evidence="ECO:0007829|PDB:2OVU"
FT STRAND 51..55
FT /evidence="ECO:0007829|PDB:2OVU"
FT STRAND 61..63
FT /evidence="ECO:0007829|PDB:2P2K"
FT STRAND 65..68
FT /evidence="ECO:0007829|PDB:2OVU"
FT STRAND 81..88
FT /evidence="ECO:0007829|PDB:2OVU"
FT STRAND 97..109
FT /evidence="ECO:0007829|PDB:2OVU"
FT STRAND 113..116
FT /evidence="ECO:0007829|PDB:2OVU"
FT STRAND 120..127
FT /evidence="ECO:0007829|PDB:2OVU"
FT HELIX 138..140
FT /evidence="ECO:0007829|PDB:2OVU"
FT TURN 141..143
FT /evidence="ECO:0007829|PDB:2OVU"
SQ SEQUENCE 290 AA; 31421 MW; 3A1C9E9ADADA3580 CRC64;
MAISKKSSLF LPIFTFITMF LMVVNKVSSS THETNALHFM FNQFSKDQKD LILQGDATTG
TDGNLELTRV SSNGSPQGSS VGRALFYAPV HIWESSAVVA SFDATFTFLI KSPDSHPADG
IAFFISNIDS SIPSGSTGRL LGLFPDANVI RNSTTIDFNA AYNADTIVAV ELDTYPNTDI
GDPNYPHIGI DIKSVRSKKT AKWNMQNGKV GTAHIIYNSV GKRLSAVVSY PNGDSATVSY
DVDLDNVLPE WVRVGLSAST GLYKETNTIL SWSFTSKLKS NEIPDIATVV
