LECA_BIOPE
ID LECA_BIOPE Reviewed; 236 AA.
AC J9PBR3; P86894;
DT 12-APR-2017, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2012, sequence version 1.
DT 03-AUG-2022, entry version 40.
DE RecName: Full=Lectin CPL {ECO:0000303|PubMed:22554687};
OS Bionia pedicellata (Camptosema pedicellatum).
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; Bionia.
OX NCBI_TaxID=232302;
RN [1] {ECO:0000312|PDB:3U4X, ECO:0007744|PDB:3U4X}
RP PROTEIN SEQUENCE, FUNCTION, SUBUNIT, MASS SPECTROMETRY, AND X-RAY
RP CRYSTALLOGRAPHY (2.16 ANGSTROMS) IN COMPLEX WITH CALCIUM AND MANGANESE.
RC TISSUE=Seed {ECO:0000303|PubMed:22554687};
RX PubMed=22554687; DOI=10.1093/jb/mvs047;
RA Souza Teixeira C., da Silva H.C., de Moura T.R., Pereira-Junior F.N.,
RA do Nascimento K.S., Nagano C.S., Sampaio A.H., Delatorre P., Rocha B.A.,
RA Cavada B.S.;
RT "Crystal structure of the lectin of Camptosema pedicellatum: implications
RT of a conservative substitution at the hydrophobic subsite.";
RL J. Biochem. 152:87-98(2012).
CC -!- FUNCTION: D-mannose/D-glucose-binding lectin that also binds derivative
CC alpha-methyl-D-mannppyranoside. Has hemagglutinating activity towards
CC rabbit erythrocytes. {ECO:0000269|PubMed:22554687}.
CC -!- SUBUNIT: Homotetramer; dimer of dimers. {ECO:0000269|PubMed:22554687}.
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 119-236 the gamma chain.
CC {ECO:0000303|PubMed:22554687, ECO:0000305}.
CC -!- MASS SPECTROMETRY: Mass=25298; Mass_error=2; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:22554687};
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:22554687}.
CC -!- SIMILARITY: Belongs to the leguminous lectin family. {ECO:0000255}.
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DR PDB; 3U4X; X-ray; 2.16 A; A=1-236.
DR PDBsum; 3U4X; -.
DR AlphaFoldDB; J9PBR3; -.
DR SMR; J9PBR3; -.
DR UniLectin; J9PBR3; -.
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 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; 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; Calcium; Direct protein sequencing; Lectin; Manganese;
KW Mannose-binding; Metal-binding.
FT CHAIN 1..236
FT /note="Lectin CPL"
FT /evidence="ECO:0000269|PubMed:22554687"
FT /id="PRO_0000439558"
FT BINDING 8
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000269|PubMed:22554687,
FT ECO:0007744|PDB:3U4X"
FT BINDING 10
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:22554687,
FT ECO:0007744|PDB:3U4X"
FT BINDING 10
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000269|PubMed:22554687,
FT ECO:0007744|PDB:3U4X"
FT BINDING 12
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:22554687,
FT ECO:0007744|PDB:3U4X"
FT BINDING 14
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0007744|PDB:3U4X"
FT BINDING 14
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:22554687,
FT ECO:0007744|PDB:3U4X"
FT BINDING 19
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:22554687,
FT ECO:0007744|PDB:3U4X"
FT BINDING 19
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000269|PubMed:22554687,
FT ECO:0007744|PDB:3U4X"
FT BINDING 24
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000269|PubMed:22554687,
FT ECO:0007744|PDB:3U4X"
FT BINDING 99..100
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000269|PubMed:22554687,
FT ECO:0007744|PDB:3U4X"
FT BINDING 207
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0007744|PDB:3U4X"
FT BINDING 227
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000269|PubMed:22554687,
FT ECO:0007744|PDB:3U4X"
FT STRAND 4..10
FT /evidence="ECO:0007829|PDB:3U4X"
FT HELIX 15..17
FT /evidence="ECO:0007829|PDB:3U4X"
FT STRAND 24..33
FT /evidence="ECO:0007829|PDB:3U4X"
FT STRAND 35..39
FT /evidence="ECO:0007829|PDB:3U4X"
FT STRAND 47..55
FT /evidence="ECO:0007829|PDB:3U4X"
FT TURN 56..59
FT /evidence="ECO:0007829|PDB:3U4X"
FT STRAND 60..66
FT /evidence="ECO:0007829|PDB:3U4X"
FT STRAND 73..78
FT /evidence="ECO:0007829|PDB:3U4X"
FT HELIX 81..83
FT /evidence="ECO:0007829|PDB:3U4X"
FT STRAND 87..96
FT /evidence="ECO:0007829|PDB:3U4X"
FT STRAND 98..100
FT /evidence="ECO:0007829|PDB:3U4X"
FT STRAND 105..120
FT /evidence="ECO:0007829|PDB:3U4X"
FT STRAND 124..132
FT /evidence="ECO:0007829|PDB:3U4X"
FT STRAND 140..144
FT /evidence="ECO:0007829|PDB:3U4X"
FT STRAND 154..157
FT /evidence="ECO:0007829|PDB:3U4X"
FT STRAND 169..176
FT /evidence="ECO:0007829|PDB:3U4X"
FT STRAND 185..197
FT /evidence="ECO:0007829|PDB:3U4X"
FT STRAND 201..204
FT /evidence="ECO:0007829|PDB:3U4X"
FT STRAND 208..215
FT /evidence="ECO:0007829|PDB:3U4X"
FT HELIX 226..228
FT /evidence="ECO:0007829|PDB:3U4X"
FT TURN 229..231
FT /evidence="ECO:0007829|PDB:3U4X"
SQ SEQUENCE 236 AA; 25298 MW; 9AC924B5BAA662BB CRC64;
ADTIVAVELD TYPNTDIGDP NYQHIGINIK SIRSKATTRW NVQDGKVGTA HISYNSVAKR
LSAIVSYPGG SSATVSYDVD LNNILPEWVR VGLSASTGVY KETNTILSWS FTSKLKTNST
ADAQSLHFTF NQFSQSPKDL ILQGDASTDS DGNLQLTRVS NGSPQSNSVG RALYYAPVHV
WDKSAVVASF DATFTFLIKS PDSDPADGIA FFIANTDSSI PHGSGGRLLG LFPDAN
