CONA_CANCT
ID CONA_CANCT Reviewed; 237 AA.
AC P81461;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-1998, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Concanavalin-A;
DE Short=Con A;
OS Canavalia cathartica (Jackbean) (Canavalia virosa).
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=28958;
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).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEX WITH CALCIUM AND MANGANESE
RP IONS.
RX PubMed=17327674; DOI=10.1107/s0907444906055624;
RA Mueller-Dieckmann C., Panjikar S., Schmidt A., Mueller S., Kuper J.,
RA Geerlof A., Wilmanns M., Singh R.K., Tucker P.A., Weiss M.S.;
RT "On the routine use of soft X-rays in macromolecular crystallography. Part
RT IV. Efficient determination of anomalous substructures in biomacromolecules
RT using longer X-ray wavelengths.";
RL Acta Crystallogr. D 63:366-380(2007).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) IN COMPLEX WITH CALCIUM; MANGANESE
RP AND CARBOHYDRATE, FUNCTION, AND SUBUNIT.
RX DOI=10.1002/adfm.201200423;
RA Trastoy B., Bonsor D.A., Perez-Ojeda M.E., Jimeno M.L., Mendez-Ardoy A.,
RA Fernandez J.M.G., Sundberg E.J., Chiara J.L.;
RT "Synthesis and biophysical study of disassembling nanohybrid bioconjugates
RT with a cubix oactasilsesquioxane core.";
RL Adv. Mater. 22:3191-3201(2012).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.72 ANGSTROMS) IN COMPLEX WITH CALCIUM; MANGANESE
RP AND GLYCOPROTEIN, FUNCTION, AND SUBUNIT.
RX PubMed=25860443; DOI=10.1021/ja511237n;
RA Ng S., Lin E., Kitov P.I., Tjhung K.F., Gerlits O.O., Deng L., Kasper B.,
RA Sood A., Paschal B.M., Zhang P., Ling C.C., Klassen J.S., Noren C.J.,
RA Mahal L.K., Woods R.J., Coates L., Derda R.;
RT "Genetically encoded fragment-based discovery of glycopeptide ligands for
RT carbohydrate-binding proteins.";
RL J. Am. Chem. Soc. 137:5248-5251(2015).
CC -!- FUNCTION: Glucose/D-mannose specific lectin.
CC {ECO:0000269|PubMed:25860443, ECO:0000269|Ref.3}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:25860443,
CC ECO:0000269|Ref.3}.
CC -!- PTM: Concanavalin A-like lectins of the Diocleinae subtribe undergo
CC proteolytic processing referred to as circular permutation. The
CC propeptide is split into an N-terminal and a C-terminal part, the gamma
CC and beta chain, respectively. These are then religated in beta-gamma
CC order to form the mature alpha chain. The beta and gamma chains can
CC often be detected in cell extracts (By similarity). Residues 1-118 of
CC the mature chain, as displayed here, probably constitute the beta chain
CC in the propeptide, residues 119-237 the gamma chain (Probable).
CC {ECO:0000250|UniProtKB:C0HK27, ECO:0000305}.
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 {ECO:0000305|PubMed:17327674}.
CC -!- SIMILARITY: Belongs to the leguminous lectin family. {ECO:0000305}.
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DR PIR; A59417; A59417.
DR PDB; 2A7A; X-ray; 1.75 A; A=1-237.
DR PDB; 2G4I; X-ray; 2.40 A; A=1-237.
DR PDB; 3QLQ; X-ray; 1.70 A; A/B/C/D=1-237.
DR PDB; 4CZS; X-ray; 1.73 A; A/B/C/D=1-237.
DR PDBsum; 2A7A; -.
DR PDBsum; 2G4I; -.
DR PDBsum; 3QLQ; -.
DR PDBsum; 4CZS; -.
DR AlphaFoldDB; P81461; -.
DR SMR; P81461; -.
DR UniLectin; P81461; -.
DR EvolutionaryTrace; P81461; -.
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_0000105088"
FT BINDING 8
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000269|PubMed:17327674,
FT ECO:0000269|PubMed:25860443, ECO:0000269|Ref.3,
FT ECO:0007744|PDB:2A7A, ECO:0007744|PDB:2G4I,
FT ECO:0007744|PDB:3QLQ, ECO:0007744|PDB:4CZS"
FT BINDING 10
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:17327674,
FT ECO:0000269|PubMed:25860443, ECO:0000269|Ref.3,
FT ECO:0007744|PDB:2A7A, ECO:0007744|PDB:2G4I,
FT ECO:0007744|PDB:3QLQ, ECO:0007744|PDB:4CZS"
FT BINDING 10
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000269|PubMed:17327674,
FT ECO:0000269|PubMed:25860443, ECO:0000269|Ref.3,
FT ECO:0007744|PDB:2A7A, ECO:0007744|PDB:2G4I,
FT ECO:0007744|PDB:3QLQ, ECO:0007744|PDB:4CZS"
FT BINDING 12
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:17327674,
FT ECO:0000269|PubMed:25860443, ECO:0000269|Ref.3,
FT ECO:0007744|PDB:2A7A, ECO:0007744|PDB:2G4I,
FT ECO:0007744|PDB:3QLQ, ECO:0007744|PDB:4CZS"
FT BINDING 14
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000269|PubMed:25860443, ECO:0000269|Ref.3,
FT ECO:0007744|PDB:3QLQ, ECO:0007744|PDB:4CZS"
FT BINDING 14
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:17327674,
FT ECO:0000269|PubMed:25860443, ECO:0000269|Ref.3,
FT ECO:0007744|PDB:2A7A, ECO:0007744|PDB:2G4I,
FT ECO:0007744|PDB:3QLQ, ECO:0007744|PDB:4CZS"
FT BINDING 19
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:17327674,
FT ECO:0000269|PubMed:25860443, ECO:0000269|Ref.3,
FT ECO:0007744|PDB:2A7A, ECO:0007744|PDB:2G4I,
FT ECO:0007744|PDB:3QLQ, ECO:0007744|PDB:4CZS"
FT BINDING 19
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000269|PubMed:17327674,
FT ECO:0000269|PubMed:25860443, ECO:0000269|Ref.3,
FT ECO:0007744|PDB:2A7A, ECO:0007744|PDB:2G4I,
FT ECO:0007744|PDB:3QLQ, ECO:0007744|PDB:4CZS"
FT BINDING 24
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000269|PubMed:17327674,
FT ECO:0000269|PubMed:25860443, ECO:0000269|Ref.3,
FT ECO:0007744|PDB:2A7A, ECO:0007744|PDB:2G4I,
FT ECO:0007744|PDB:3QLQ, ECO:0007744|PDB:4CZS"
FT BINDING 98..100
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000269|PubMed:25860443, ECO:0000269|Ref.3,
FT ECO:0007744|PDB:3QLQ, ECO:0007744|PDB:4CZS"
FT BINDING 208
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000269|PubMed:25860443, ECO:0000269|Ref.3,
FT ECO:0007744|PDB:3QLQ, ECO:0007744|PDB:4CZS"
FT BINDING 228
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000269|PubMed:25860443, ECO:0000269|Ref.3,
FT ECO:0007744|PDB:3QLQ, ECO:0007744|PDB:4CZS"
FT STRAND 4..10
FT /evidence="ECO:0007829|PDB:3QLQ"
FT HELIX 15..17
FT /evidence="ECO:0007829|PDB:3QLQ"
FT STRAND 24..33
FT /evidence="ECO:0007829|PDB:3QLQ"
FT STRAND 35..39
FT /evidence="ECO:0007829|PDB:3QLQ"
FT STRAND 46..55
FT /evidence="ECO:0007829|PDB:3QLQ"
FT TURN 56..59
FT /evidence="ECO:0007829|PDB:3QLQ"
FT STRAND 60..66
FT /evidence="ECO:0007829|PDB:3QLQ"
FT STRAND 73..78
FT /evidence="ECO:0007829|PDB:3QLQ"
FT HELIX 81..83
FT /evidence="ECO:0007829|PDB:3QLQ"
FT STRAND 87..96
FT /evidence="ECO:0007829|PDB:3QLQ"
FT STRAND 98..100
FT /evidence="ECO:0007829|PDB:4CZS"
FT STRAND 105..118
FT /evidence="ECO:0007829|PDB:3QLQ"
FT STRAND 123..132
FT /evidence="ECO:0007829|PDB:3QLQ"
FT STRAND 140..144
FT /evidence="ECO:0007829|PDB:3QLQ"
FT HELIX 150..152
FT /evidence="ECO:0007829|PDB:3QLQ"
FT STRAND 154..157
FT /evidence="ECO:0007829|PDB:4CZS"
FT STRAND 170..177
FT /evidence="ECO:0007829|PDB:3QLQ"
FT STRAND 186..198
FT /evidence="ECO:0007829|PDB:3QLQ"
FT STRAND 202..205
FT /evidence="ECO:0007829|PDB:3QLQ"
FT STRAND 209..215
FT /evidence="ECO:0007829|PDB:3QLQ"
FT HELIX 227..229
FT /evidence="ECO:0007829|PDB:3QLQ"
FT TURN 230..232
FT /evidence="ECO:0007829|PDB:3QLQ"
SQ SEQUENCE 237 AA; 25539 MW; DD31D2BFCC6EDD07 CRC64;
ADTIVAVELD TYPNTDIGDP SYPHIGIDIK SVRSKKTAKW NMQNGKVGTA HIIYNSVGKR
LSAVVSYPNG DSATVSYDVD LDNVLPEWVR VGLSASTGLY KETNTILSWS FTSKLKSNST
HETNALHFMF NQFSKDQKDL ILQGDATTGT DGNLELTRVS SNGSPQGNSV GRALFYAPVH
IWESSAVVAS FDATFTFLIK SPDSHPADGI AFFISNIDSS IPSGSTGRLL GLFPDAN
