LECA_CANBN
ID LECA_CANBN Reviewed; 281 AA.
AC P58906;
DT 26-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT 30-NOV-2016, sequence version 2.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=Lectin CaBo {ECO:0000303|Ref.1};
DE AltName: Full=Lectin Cbo {ECO:0000303|PubMed:10082964};
DE Flags: Precursor; Fragment;
OS Canavalia bonariensis.
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=192414 {ECO:0000303|PubMed:10082964};
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-251, PROTEIN SEQUENCE OF 50-83;
RP 102-110; 124-139; 164-193; 210-222 AND 238-281, PTM, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC TISSUE=Seed {ECO:0000303|Ref.1};
RA da Silva M.T.L., da Silva Osterne V.J., Simplicio Nobre C.A., Chaves R.P.,
RA da Silva I.B., Moreira C.G., de Andrade M.L.L., Nagano C.S., Rocha C.R.C.,
RA Leal R.B., Martins J.L., Cavada B.S., do Nascimento K.S.;
RT "Structural characterization, docking and dynamics simulations of Canavalia
RT bonariensis lectin.";
RL J. Drug Des. Res. 3:1023-1023(2016).
RN [2]
RP PROTEIN SEQUENCE OF 30-51 AND 164-188, AND SUBUNIT.
RC TISSUE=Seed {ECO:0000303|PubMed:10082964};
RX PubMed=10082964; DOI=10.1016/s0167-4838(99)00020-5;
RA Calvete J.J., Thole H.H., Raida M., Urbanke C., Romero A., Grangeiro T.B.,
RA Ramos M.V., Almeida da Rocha I.M., Guimaraes F.N., Cavada B.S.;
RT "Molecular characterization and crystallization of Diocleinae lectins.";
RL Biochim. Biophys. Acta 1430:367-375(1999).
CC -!- FUNCTION: D-mannose-specific lectin. {ECO:0000303|Ref.1}.
CC -!- SUBUNIT: Equilibrium between homodimer and homotetramer.
CC {ECO:0000269|PubMed:10082964}.
CC -!- PTM: The mature chain consists of residues 164-281 followed by residues
CC 30-148. 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. {ECO:0000269|Ref.1}.
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:0000250|UniProtKB:P14894}.
CC -!- MISCELLANEOUS: Several isolectin forms may exist.
CC {ECO:0000269|PubMed:10082964}.
CC -!- SIMILARITY: Belongs to the leguminous lectin family. {ECO:0000305}.
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DR PDB; 5U3E; X-ray; 2.30 A; A=1-148.
DR PDBsum; 5U3E; -.
DR AlphaFoldDB; P58906; -.
DR SMR; P58906; -.
DR UniLectin; P58906; -.
DR GO; GO:0030246; F:carbohydrate binding; IDA:UniProtKB.
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; IPR016363; L-lectin.
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 PIRSF; PIRSF002690; L-type_lectin_plant; 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; Signal.
FT SIGNAL 1..29
FT /evidence="ECO:0000255"
FT CHAIN 30..148
FT /note="Lectin CaBo, 2nd part"
FT /evidence="ECO:0000305|Ref.1"
FT /id="PRO_0000017585"
FT PROPEP 149..163
FT /note="Removed in mature form"
FT /evidence="ECO:0000269|Ref.1"
FT /id="PRO_0000438365"
FT CHAIN 164..281
FT /note="Lectin CaBo, 1st part"
FT /evidence="ECO:0000305|Ref.1"
FT /id="PRO_0000017587"
FT BINDING 119
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 139
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000250|UniProtKB:P86624"
FT BINDING 171
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:P86624"
FT BINDING 173
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P86624"
FT BINDING 173
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:P86624"
FT BINDING 175
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000250|UniProtKB:P86624"
FT BINDING 175
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P86624"
FT BINDING 177
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P86624"
FT BINDING 182
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P86624"
FT BINDING 182
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:P86624"
FT BINDING 187
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:P86624"
FT BINDING 262..263
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000250|UniProtKB:P86624"
FT SITE 148..149
FT /note="Cleavage"
FT /evidence="ECO:0000269|Ref.1"
FT SITE 163..164
FT /note="Cleavage"
FT /evidence="ECO:0000269|Ref.1"
FT CONFLICT 36
FT /note="A -> S (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 46..48
FT /note="KDQ -> QNP (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT NON_TER 281
FT /evidence="ECO:0000305"
FT STRAND 1..6
FT /evidence="ECO:0007829|PDB:5U3E"
FT STRAND 15..25
FT /evidence="ECO:0007829|PDB:5U3E"
FT STRAND 35..43
FT /evidence="ECO:0007829|PDB:5U3E"
FT STRAND 51..55
FT /evidence="ECO:0007829|PDB:5U3E"
FT HELIX 61..63
FT /evidence="ECO:0007829|PDB:5U3E"
FT STRAND 81..88
FT /evidence="ECO:0007829|PDB:5U3E"
FT STRAND 100..109
FT /evidence="ECO:0007829|PDB:5U3E"
FT STRAND 113..115
FT /evidence="ECO:0007829|PDB:5U3E"
FT STRAND 119..127
FT /evidence="ECO:0007829|PDB:5U3E"
FT HELIX 138..140
FT /evidence="ECO:0007829|PDB:5U3E"
FT TURN 141..143
FT /evidence="ECO:0007829|PDB:5U3E"
SQ SEQUENCE 281 AA; 30440 MW; E977C8C59667BA9D CRC64;
MAISKKSSLY LPIFTFITML LMVVNKVSSS TADANALHFT FNQFSKDQKD LILQGDATTG
TDGNLELTRV SSNGSPQGNS VGRALFYAPV HIWESSAVVA SFDATFKFLI KSPDSEPADG
ITFFIANIDS SIPSGSGGRL LGLFPDANII KNSTTIDFNA AYNADTIVAV ELDTYPNTDI
GDPNYPHIGI DIKSIRSKKT TRWNIQNGKV GTAHINYNSV GKRLSAIVSY PNSDSATVSY
DVDLDNVLPE WVRVGLSATT GLYKETNTIL SWSFTSKLKS N
