LECT_BAUFO
ID LECT_BAUFO Reviewed; 233 AA.
AC P86993;
DT 16-MAR-2016, integrated into UniProtKB/Swiss-Prot.
DT 16-MAR-2016, sequence version 1.
DT 03-AUG-2022, entry version 19.
DE RecName: Full=Lectin {ECO:0000303|Ref.1};
DE Short=BfL {ECO:0000303|Ref.1};
OS Bauhinia forficata (Brazilian orchid-tree) (Cow's-foot).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Cercidoideae; Cercideae; Bauhiniinae;
OC Bauhinia.
OX NCBI_TaxID=413686 {ECO:0000303|Ref.1};
RN [1] {ECO:0000305}
RP PROTEIN SEQUENCE, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT,
RP GLYCOSYLATION AT ASN-26 AND ASN-108, AND MASS SPECTROMETRY.
RC TISSUE=Seed {ECO:0000303|Ref.1};
RA Silva M.C.C., Santana L.A., Mentelee R., Ferreira R.S., Miranda A.,
RA Silva-Lucca R.A., Sampaio M.U., Correia M.T.S., Oliva M.L.V.;
RT "Purification, primary structure and potential functions of a novel lectin
RT from Bauhinia forficata seeds.";
RL Process Biochem. 47:1049-1059(2012).
CC -!- FUNCTION: Has metal-independent hemagglutinating activity towards
CC erythrocytes from rabbit and human. Hemagglutinating activity is
CC inhibited by glycoproteins fetuin, asialo-fetuin, thyroglobulin and
CC azocasein but not by free carbohydrates. Inhibits ADP- and epinephrin-
CC induced but not collagen-, fibrinogen, thrombin- or arachidonic acid-
CC induced platelet aggregation in vitro. Has anticoagulant activity in
CC vitro. {ECO:0000269|Ref.1}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 6 for hemagglutinating activity. {ECO:0000269|Ref.1};
CC Temperature dependence:
CC Heat stable. Retains hemagglutinating activity after incubation at
CC 100 degrees Celsius for 30 minutes. {ECO:0000269|Ref.1};
CC -!- SUBUNIT: Monomer. {ECO:0000269|Ref.1}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|Ref.1}.
CC -!- MASS SPECTROMETRY: Mass=27850; Mass_error=2.926; Method=Electrospray;
CC Evidence={ECO:0000269|Ref.1};
CC -!- MISCELLANEOUS: Hemagglutinating activity is independent of divalent
CC metal ions. {ECO:0000269|Ref.1}.
CC -!- SIMILARITY: Belongs to the leguminous lectin family. {ECO:0000305}.
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DR PDB; 5T50; X-ray; 1.43 A; A/B=1-233.
DR PDB; 5T52; X-ray; 1.70 A; A/B=1-233.
DR PDB; 5T54; X-ray; 1.65 A; A/B=1-233.
DR PDB; 5T55; X-ray; 1.43 A; A/B=1-233.
DR PDB; 5T5J; X-ray; 1.35 A; A/B=1-233.
DR PDB; 5T5L; X-ray; 1.17 A; A/B=1-233.
DR PDB; 5T5O; X-ray; 2.75 A; A/B/C/D/E/F/G/H/I/J=1-233.
DR PDB; 5T5P; X-ray; 1.66 A; A/B=1-233.
DR PDBsum; 5T50; -.
DR PDBsum; 5T52; -.
DR PDBsum; 5T54; -.
DR PDBsum; 5T55; -.
DR PDBsum; 5T5J; -.
DR PDBsum; 5T5L; -.
DR PDBsum; 5T5O; -.
DR PDBsum; 5T5P; -.
DR AlphaFoldDB; P86993; -.
DR SMR; P86993; -.
DR UniLectin; P86993; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0030246; F:carbohydrate 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; 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.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium; Direct protein sequencing; Glycoprotein;
KW Hemagglutinin; Lectin; Manganese; Metal-binding; Secreted.
FT CHAIN 1..233
FT /note="Lectin"
FT /id="PRO_0000435798"
FT BINDING 118
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:P24146"
FT BINDING 120
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P24146"
FT BINDING 120
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:P24146"
FT BINDING 122
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P24146"
FT BINDING 124
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P24146"
FT BINDING 129
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P24146"
FT BINDING 129
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:P24146"
FT BINDING 134
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:P24146"
FT CARBOHYD 26
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|Ref.1"
FT CARBOHYD 108
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|Ref.1"
FT STRAND 3..11
FT /evidence="ECO:0007829|PDB:5T5L"
FT STRAND 16..20
FT /evidence="ECO:0007829|PDB:5T5L"
FT STRAND 23..25
FT /evidence="ECO:0007829|PDB:5T5L"
FT STRAND 28..30
FT /evidence="ECO:0007829|PDB:5T5L"
FT STRAND 45..52
FT /evidence="ECO:0007829|PDB:5T5L"
FT STRAND 59..75
FT /evidence="ECO:0007829|PDB:5T5L"
FT STRAND 77..85
FT /evidence="ECO:0007829|PDB:5T5L"
FT HELIX 95..97
FT /evidence="ECO:0007829|PDB:5T5L"
FT TURN 98..100
FT /evidence="ECO:0007829|PDB:5T5L"
FT TURN 103..107
FT /evidence="ECO:0007829|PDB:5T5L"
FT HELIX 109..111
FT /evidence="ECO:0007829|PDB:5T5L"
FT STRAND 115..120
FT /evidence="ECO:0007829|PDB:5T5L"
FT STRAND 125..127
FT /evidence="ECO:0007829|PDB:5T5L"
FT STRAND 134..143
FT /evidence="ECO:0007829|PDB:5T5L"
FT STRAND 145..149
FT /evidence="ECO:0007829|PDB:5T5L"
FT HELIX 152..155
FT /evidence="ECO:0007829|PDB:5T5L"
FT STRAND 161..168
FT /evidence="ECO:0007829|PDB:5T5L"
FT TURN 169..172
FT /evidence="ECO:0007829|PDB:5T5L"
FT STRAND 173..179
FT /evidence="ECO:0007829|PDB:5T5L"
FT STRAND 185..191
FT /evidence="ECO:0007829|PDB:5T5L"
FT HELIX 194..197
FT /evidence="ECO:0007829|PDB:5T5L"
FT STRAND 199..227
FT /evidence="ECO:0007829|PDB:5T5L"
SQ SEQUENCE 233 AA; 26007 MW; 640FE0B934C0890C CRC64;
SELSFNYPNF QSVEDITFQG GASPRNETLQ LTPTDSNGIP IRQRAGHAVY SQPFQLRDTS
FYTTFTFVIR TTSNSPADGF AIFIAPPDFP VKRYGGYLGL FEPNTATNTS ANKVVAVEFD
TWVNTEWKEP RYRHIGIDVN SIVSVRVTRW QDKDVFSRSI ATAHVGYDGI SKILTAFVTY
PDGGNYVLSH VVDLAEIFPG DVRIGFSGAT GQYETQYIHS WSFSSTSTNL LRD
