CONA_CANLI
ID CONA_CANLI Reviewed; 237 AA.
AC P81460;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-1998, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Concanavalin-A;
DE Short=Con A;
OS Canavalia lineata (Beach bean) (Dolichos lineatus).
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=28957;
RN [1]
RP PROTEIN SEQUENCE.
RX PubMed=7764031; DOI=10.1016/0031-9422(93)85008-f;
RA Fujimura S., Terada S., Jayavardhanan K.K., Panikkar K.R., Kimoto E.;
RT "Primary structures of concanavalin A-like lectins from seeds of two
RT species of Canavalia.";
RL Phytochemistry 33:985-987(1993).
CC -!- FUNCTION: Glucose/D-mannose specific lectin.
CC -!- SUBUNIT: Homotetramer.
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR PIR; A59415; A59415.
DR PDB; 2CWM; X-ray; 1.95 A; A=1-237.
DR PDB; 2CY6; X-ray; 2.00 A; A/D=1-237.
DR PDB; 2CYF; X-ray; 1.80 A; A=1-237.
DR PDB; 3SNM; X-ray; 2.15 A; A=1-237.
DR PDB; 4DPN; X-ray; 2.55 A; A/D=1-237.
DR PDB; 4I30; X-ray; 1.89 A; A=1-237.
DR PDB; 4TYS; X-ray; 3.25 A; A/B/C/D/E/F=1-237.
DR PDB; 4TZD; X-ray; 3.20 A; A/D=1-237.
DR PDB; 5BYN; X-ray; 2.65 A; A/B=1-237.
DR PDBsum; 2CWM; -.
DR PDBsum; 2CY6; -.
DR PDBsum; 2CYF; -.
DR PDBsum; 3SNM; -.
DR PDBsum; 4DPN; -.
DR PDBsum; 4I30; -.
DR PDBsum; 4TYS; -.
DR PDBsum; 4TZD; -.
DR PDBsum; 5BYN; -.
DR AlphaFoldDB; P81460; -.
DR SMR; P81460; -.
DR UniLectin; P81460; -.
DR EvolutionaryTrace; P81460; -.
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; IPR000985; Lectin_LegA_CS.
DR InterPro; IPR019825; Lectin_legB_Mn/Ca_BS.
DR InterPro; IPR001220; Legume_lectin_dom.
DR Pfam; PF00139; Lectin_legB; 2.
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; Lectin; Manganese;
KW Mannose-binding; Metal-binding.
FT CHAIN 1..237
FT /note="Concanavalin-A"
FT /id="PRO_0000105087"
FT BINDING 8
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 10
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 10
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 12
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000250"
FT BINDING 12
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 14
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 19
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 19
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 24
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 99..100
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000250"
FT BINDING 208
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 228
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000250"
FT STRAND 4..10
FT /evidence="ECO:0007829|PDB:4I30"
FT HELIX 15..17
FT /evidence="ECO:0007829|PDB:4I30"
FT STRAND 24..33
FT /evidence="ECO:0007829|PDB:4I30"
FT STRAND 35..39
FT /evidence="ECO:0007829|PDB:4I30"
FT STRAND 46..55
FT /evidence="ECO:0007829|PDB:4I30"
FT TURN 56..59
FT /evidence="ECO:0007829|PDB:4I30"
FT STRAND 60..66
FT /evidence="ECO:0007829|PDB:4I30"
FT STRAND 72..78
FT /evidence="ECO:0007829|PDB:4I30"
FT HELIX 81..83
FT /evidence="ECO:0007829|PDB:4I30"
FT STRAND 87..96
FT /evidence="ECO:0007829|PDB:4I30"
FT STRAND 98..100
FT /evidence="ECO:0007829|PDB:2CY6"
FT STRAND 105..116
FT /evidence="ECO:0007829|PDB:4I30"
FT STRAND 124..132
FT /evidence="ECO:0007829|PDB:4I30"
FT STRAND 140..144
FT /evidence="ECO:0007829|PDB:4I30"
FT STRAND 150..152
FT /evidence="ECO:0007829|PDB:4I30"
FT STRAND 154..157
FT /evidence="ECO:0007829|PDB:4I30"
FT TURN 161..163
FT /evidence="ECO:0007829|PDB:3SNM"
FT STRAND 170..177
FT /evidence="ECO:0007829|PDB:4I30"
FT STRAND 187..199
FT /evidence="ECO:0007829|PDB:4I30"
FT STRAND 203..205
FT /evidence="ECO:0007829|PDB:4I30"
FT STRAND 209..216
FT /evidence="ECO:0007829|PDB:4I30"
FT HELIX 227..229
FT /evidence="ECO:0007829|PDB:4I30"
FT TURN 230..232
FT /evidence="ECO:0007829|PDB:4I30"
SQ SEQUENCE 237 AA; 25497 MW; 2D31C2BD3D30D66A CRC64;
ADTIVAVELD TYPNTDIGDP SYPHIGIDIK SVRSKKTAKW NMQNGKVGTA HIIYNSVGKR
LSAVVSYPNG DSATVSYDVD LDNVLPEWVR VGLSASTGLY KETNTILSWS FTSKLKSNST
HETNALHFVF NQFSKDQKDL ILQGDATTGT DGNLELTRVS SNGSPQGNSV GRALFYAPVH
IWESSAVVAS FDATFTFLIK SSDSHPADGI AFFISNIDSS IPSGSTGRLL GLFPDAN
