LECA_CANGR
ID LECA_CANGR Reviewed; 237 AA.
AC A0A067XG71; C0HJC6;
DT 07-JUN-2017, integrated into UniProtKB/Swiss-Prot.
DT 03-SEP-2014, sequence version 1.
DT 03-AUG-2022, entry version 31.
DE RecName: Full=Lectin ConGF {ECO:0000303|PubMed:22368061};
OS Canavalia grandiflora (Jackbean).
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=232301 {ECO:0000312|PDB:4L8Q};
RN [1] {ECO:0000312|PDB:4L8Q}
RP PROTEIN SEQUENCE, X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) IN COMPLEX WITH
RP CARBOHYDRATE; CALCIUM AND MANGANESE, FUNCTION, SUBUNIT, MASS SPECTROMETRY,
RP AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Seed {ECO:0000303|PubMed:24361256};
RX PubMed=24361256; DOI=10.1016/j.abb.2013.12.006;
RA Barroso-Neto I.L., Simoes R.C., Rocha B.A., Bezerra M.J.,
RA Pereira-Junior F.N., Silva Osterne V.J., Nascimento K.S., Nagano C.S.,
RA Delatorre P., Pereira M.G., Freitas Pires A., Sampaio A.H., Assreuy A.M.,
RA Cavada B.S.;
RT "Vasorelaxant activity of Canavalia grandiflora seed lectin: A structural
RT analysis.";
RL Arch. Biochem. Biophys. 543:31-39(2014).
RN [2] {ECO:0000305}
RP PROTEIN SEQUENCE OF 39-128; 152-162; 177-203 AND 214-237, FUNCTION,
RP CRYSTALLIZATION, MASS SPECTROMETRY, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC TISSUE=Seed {ECO:0000303|PubMed:22368061};
RX PubMed=22368061; DOI=10.1002/rcm.6171;
RA Simoes R.C., Rocha B.A., Bezerra M.J., Barroso-Neto I.L.,
RA Pereira-Junior F.N., da Mata Moura R., do Nascimento K.S., Nagano C.S.,
RA Delatorre P., de Freitas Pires A., Assreuy A.M., Sampaio A.H., Cavada B.S.;
RT "Protein crystal content analysis by mass spectrometry and preliminary X-
RT ray diffraction of a lectin from Canavalia grandiflora seeds with
RT modulatory role in inflammation.";
RL Rapid Commun. Mass Spectrom. 26:811-818(2012).
RN [3] {ECO:0000305}
RP FUNCTION.
RC TISSUE=Seed {ECO:0000303|PubMed:19153712};
RX PubMed=19153712; DOI=10.1007/s00210-009-0397-9;
RA Nunes B.S., Rensonnet N.S., Dal-Secco D., Vieira S.M., Cavada B.S.,
RA Teixeira E.H., Moura T.R., Teixeira C.S., Clemente-Napimoga J.T.,
RA Cunha F.Q., Napimoga M.H.;
RT "Lectin extracted from Canavalia grandiflora seeds presents potential anti-
RT inflammatory and analgesic effects.";
RL Naunyn Schmiedebergs Arch. Pharmacol. 379:609-616(2009).
CC -!- FUNCTION: Lectin (PubMed:24361256). Induces paw edema in mice
CC (PubMed:22368061). Has a weak vasorelaxant effect on rat aorta
CC (PubMed:24361256). Has anti-inflammatory and anti-nociceptive effects
CC (PubMed:19153712). {ECO:0000269|PubMed:19153712,
CC ECO:0000269|PubMed:22368061, ECO:0000269|PubMed:24361256}.
CC -!- SUBUNIT: Homotetramer; dimer of dimers. {ECO:0000269|PubMed:24361256}.
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. Residues 1-118 of the mature chain,
CC as displayed here, probably constitute the beta chain in the
CC propeptide, residues 119-237 the gamma chain.
CC {ECO:0000305|PubMed:22368061, ECO:0000305|PubMed:24361256}.
CC -!- MASS SPECTROMETRY: Mass=25606; Mass_error=2; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:24361256};
CC -!- MASS SPECTROMETRY: Mass=25612; Mass_error=2; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:22368061};
CC -!- MISCELLANEOUS: Binds one manganese (or other transition metal) ion and
CC one calcium ion (PubMed:24361256). The metal ions are essential for the
CC saccharide-binding and cell-agglutinating activities (Probable).
CC {ECO:0000269|PubMed:24361256, ECO:0000305}.
CC -!- SIMILARITY: Belongs to the leguminous lectin family. {ECO:0000255}.
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DR PDB; 4L8Q; X-ray; 2.30 A; A=1-237.
DR PDBsum; 4L8Q; -.
DR AlphaFoldDB; A0A067XG71; -.
DR SMR; A0A067XG71; -.
DR UniLectin; A0A067XG71; -.
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="Lectin ConGF"
FT /evidence="ECO:0000269|PubMed:24361256"
FT /id="PRO_0000440069"
FT BINDING 8
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000269|PubMed:24361256,
FT ECO:0007744|PDB:4L8Q"
FT BINDING 10
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:24361256,
FT ECO:0007744|PDB:4L8Q"
FT BINDING 10
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000269|PubMed:24361256,
FT ECO:0007744|PDB:4L8Q"
FT BINDING 12
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:24361256,
FT ECO:0007744|PDB:4L8Q"
FT BINDING 14
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000269|PubMed:24361256,
FT ECO:0007744|PDB:4L8Q"
FT BINDING 14
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:24361256,
FT ECO:0007744|PDB:4L8Q"
FT BINDING 19
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:24361256,
FT ECO:0007744|PDB:4L8Q"
FT BINDING 19
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000269|PubMed:24361256,
FT ECO:0007744|PDB:4L8Q"
FT BINDING 24
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000269|PubMed:24361256,
FT ECO:0007744|PDB:4L8Q"
FT BINDING 99
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000269|PubMed:24361256,
FT ECO:0007744|PDB:4L8Q"
FT BINDING 100
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000269|PubMed:24361256,
FT ECO:0007744|PDB:4L8Q"
FT BINDING 208
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000269|PubMed:24361256,
FT ECO:0007744|PDB:4L8Q"
FT BINDING 228
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000269|PubMed:24361256,
FT ECO:0007744|PDB:4L8Q"
FT STRAND 4..10
FT /evidence="ECO:0007829|PDB:4L8Q"
FT HELIX 15..17
FT /evidence="ECO:0007829|PDB:4L8Q"
FT STRAND 24..33
FT /evidence="ECO:0007829|PDB:4L8Q"
FT STRAND 35..39
FT /evidence="ECO:0007829|PDB:4L8Q"
FT STRAND 47..55
FT /evidence="ECO:0007829|PDB:4L8Q"
FT TURN 56..59
FT /evidence="ECO:0007829|PDB:4L8Q"
FT STRAND 60..66
FT /evidence="ECO:0007829|PDB:4L8Q"
FT STRAND 72..78
FT /evidence="ECO:0007829|PDB:4L8Q"
FT TURN 82..84
FT /evidence="ECO:0007829|PDB:4L8Q"
FT STRAND 87..96
FT /evidence="ECO:0007829|PDB:4L8Q"
FT STRAND 105..116
FT /evidence="ECO:0007829|PDB:4L8Q"
FT STRAND 124..132
FT /evidence="ECO:0007829|PDB:4L8Q"
FT STRAND 140..144
FT /evidence="ECO:0007829|PDB:4L8Q"
FT STRAND 154..157
FT /evidence="ECO:0007829|PDB:4L8Q"
FT STRAND 170..177
FT /evidence="ECO:0007829|PDB:4L8Q"
FT STRAND 187..198
FT /evidence="ECO:0007829|PDB:4L8Q"
FT STRAND 202..205
FT /evidence="ECO:0007829|PDB:4L8Q"
FT STRAND 209..216
FT /evidence="ECO:0007829|PDB:4L8Q"
FT HELIX 227..229
FT /evidence="ECO:0007829|PDB:4L8Q"
FT TURN 230..232
FT /evidence="ECO:0007829|PDB:4L8Q"
SQ SEQUENCE 237 AA; 25607 MW; F01C170425797F16 CRC64;
ADTIVAVELD TYPNTDIGDP NYPHIGIDIK SIRSKKIAKW NMQDGKVATA HIIYNSVGKR
LSAVVSYPNA DSATVSYDVD LDNVLPEWVR VGLSATTGLY KETNTILSWS FTSKLKSNST
AETNALHFTF NQFTKDQKDL ILQGDATTDS DGNLQLTRVS SDGTPQGNSV GRALFYAPVH
IWESSAVVAS FDATFTFLIK SPDSDPADGI TFFISNMDST IPSGSGGRLL GLFPDAN
