CONV_CANCT
ID CONV_CANCT Reviewed; 237 AA.
AC C0HJY1;
DT 05-JUL-2017, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2017, sequence version 1.
DT 03-AUG-2022, entry version 15.
DE RecName: Full=Concanavalin V {ECO:0000303|PubMed:24519628};
DE AltName: Full=ConV {ECO:0000303|PubMed:24519628};
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 {ECO:0000303|PubMed:24519628};
RN [1] {ECO:0000305}
RP PROTEIN SEQUENCE, X-RAY CRYSTALLOGRAPHY (2.52 ANGSTROMS) IN COMPLEX WITH
RP CALCIUM; MANGANESE AND CARBOHYDRATE, FUNCTION, SUBUNIT, AND IDENTIFICATION
RP BY MASS SPECTROMETRY.
RX PubMed=27737777; DOI=10.1016/j.ijbiomac.2016.10.020;
RA Osterne V.J., Silva-Filho J.C., Santiago M.Q., Pinto-Junior V.R.,
RA Almeida A.C., Barreto A.A., Wolin I.A., Nascimento A.P., Amorim R.M.,
RA Rocha B.A., Delatorre P., Nagano C.S., Leal R.B., Assreuy A.M.,
RA Nascimento K.S., Cavada B.S.;
RT "Structural characterization of a lectin from Canavalia virosa seeds with
RT inflammatory and cytotoxic activities.";
RL Int. J. Biol. Macromol. 94:271-282(2017).
RN [2] {ECO:0000305}
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND MASS SPECTROMETRY.
RC TISSUE=Seed {ECO:0000303|PubMed:24519628};
RX PubMed=24519628; DOI=10.1007/s12010-014-0751-3;
RA Osterne V.J., Santiago M.Q., Pinto-Junior V.R., Cajazeiras J.B.,
RA Correia J.L., Leitao C.C., Carneiro R.F., Pereira-Junior F.N.,
RA Vasconcelos M.A., Rocha B.A., Assreuy A.M., Bringel P.H., Nagano C.S.,
RA Nascimento K.S., Cavada B.S.;
RT "Purification, partial characterization, and CNBr-sepharose immobilization
RT of a vasorelaxant glucose/mannose lectin from Canavalia virosa seeds.";
RL Appl. Biochem. Biotechnol. 172:3342-3353(2014).
CC -!- FUNCTION: D-mannose/D-glucose-binding lectin which binds alpha-methyl-
CC D-mannoside, D-mannose and D-glucose in that order (PubMed:24519628,
CC PubMed:27737777). Also binds to serum fetuin and ovalbumin
CC (PubMed:24519628). Has hemagglutinating activity towards rabbit
CC erythrocytes (PubMed:24519628). Is not toxic towards larvae of the
CC brine shrimp Artemia (PubMed:24519628). Induces relaxation in rat
CC endothelized aorta (PubMed:24519628). Shows a transient edematogenic
CC effect in rat (PubMed:27737777). {ECO:0000269|PubMed:24519628,
CC ECO:0000269|PubMed:27737777}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 7-9 with activity decreasing quickly at higher or lower
CC pH. {ECO:0000269|PubMed:24519628};
CC Temperature dependence:
CC Hemagglutinating activity stable up to incubation at 80 degrees
CC Celsius for 1 hour but diminishes with higher temperatures and is
CC absent at 100 degrees Celsius. {ECO:0000269|PubMed:24519628};
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:27737777}.
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|PubMed:27737777}.
CC -!- MASS SPECTROMETRY: Mass=25480; Mass_error=2; Method=Electrospray;
CC Note=Alpha chain.; Evidence={ECO:0000269|PubMed:24519628};
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:27737777}.
CC -!- SIMILARITY: Belongs to the leguminous lectin family. {ECO:0000305}.
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DR PDB; 5F5Q; X-ray; 2.52 A; A/B=1-237.
DR PDB; 6GW9; X-ray; 2.10 A; A=1-237.
DR PDBsum; 5F5Q; -.
DR PDBsum; 6GW9; -.
DR AlphaFoldDB; C0HJY1; -.
DR SMR; C0HJY1; -.
DR UniLectin; C0HJY1; -.
DR GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
DR GO; GO:0005536; F:glucose binding; IDA:UniProtKB.
DR GO; GO:0030145; F:manganese ion binding; IDA:UniProtKB.
DR GO; GO:0005537; F:mannose binding; IDA:UniProtKB.
DR GO; GO:0042311; P:vasodilation; 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; Hemagglutinin; Lectin;
KW Manganese; Mannose-binding; Metal-binding; Vasoactive; Vasodilator.
FT CHAIN 1..237
FT /note="Concanavalin V"
FT /evidence="ECO:0000269|PubMed:27737777"
FT /id="PRO_0000440670"
FT BINDING 8
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000269|PubMed:27737777"
FT BINDING 10
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:27737777"
FT BINDING 10
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000269|PubMed:27737777"
FT BINDING 12
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:27737777"
FT BINDING 14
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000269|PubMed:27737777"
FT BINDING 14
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:27737777"
FT BINDING 19
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:27737777"
FT BINDING 19
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000269|PubMed:27737777"
FT BINDING 24
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000269|PubMed:27737777"
FT BINDING 70
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000269|PubMed:27737777"
FT BINDING 98..100
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000269|PubMed:27737777"
FT BINDING 208
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000269|PubMed:27737777"
FT BINDING 228
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000269|PubMed:27737777"
FT STRAND 4..10
FT /evidence="ECO:0007829|PDB:6GW9"
FT HELIX 15..17
FT /evidence="ECO:0007829|PDB:6GW9"
FT STRAND 24..33
FT /evidence="ECO:0007829|PDB:6GW9"
FT STRAND 35..39
FT /evidence="ECO:0007829|PDB:6GW9"
FT STRAND 47..55
FT /evidence="ECO:0007829|PDB:6GW9"
FT TURN 56..59
FT /evidence="ECO:0007829|PDB:6GW9"
FT STRAND 60..66
FT /evidence="ECO:0007829|PDB:6GW9"
FT STRAND 73..78
FT /evidence="ECO:0007829|PDB:6GW9"
FT HELIX 81..83
FT /evidence="ECO:0007829|PDB:6GW9"
FT STRAND 87..96
FT /evidence="ECO:0007829|PDB:6GW9"
FT STRAND 98..100
FT /evidence="ECO:0007829|PDB:5F5Q"
FT STRAND 105..117
FT /evidence="ECO:0007829|PDB:6GW9"
FT STRAND 124..132
FT /evidence="ECO:0007829|PDB:6GW9"
FT STRAND 140..144
FT /evidence="ECO:0007829|PDB:6GW9"
FT HELIX 150..152
FT /evidence="ECO:0007829|PDB:6GW9"
FT STRAND 170..177
FT /evidence="ECO:0007829|PDB:6GW9"
FT STRAND 186..198
FT /evidence="ECO:0007829|PDB:6GW9"
FT STRAND 202..205
FT /evidence="ECO:0007829|PDB:6GW9"
FT STRAND 209..216
FT /evidence="ECO:0007829|PDB:6GW9"
FT HELIX 227..229
FT /evidence="ECO:0007829|PDB:6GW9"
FT TURN 230..232
FT /evidence="ECO:0007829|PDB:6GW9"
SQ SEQUENCE 237 AA; 25480 MW; 3702EBBFC00EE79A CRC64;
ADTIVAVELD TYPNTDIGDP SYPHIGIDIK SVRSKKTAKW NMQNGKVGTA HIIYNSVGKR
LSAVVSYPNG DSATVSYDVD LDNVLPEWVR VGLSASTGLY KETNTILSWS FTSKLKSNST
HETNALHFVF NQFSKDQKDL ILQGDATTGT DGNLELTRVS SNGSPQGSSV GRALFYAPVH
IWESSAVVAS FDATFTFLIK SPDSHPADGI AFFISNIDSS IPSGSTGRLL GLFPDAN
