LEC_VICVI
ID LEC_VICVI Reviewed; 185 AA.
AC P56625;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-1998, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Lectin B4;
DE AltName: Full=VVLB4;
DE Flags: Fragments;
OS Vicia villosa (Hairy vetch).
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; Hologalegina; IRL clade; Fabeae; Vicia.
OX NCBI_TaxID=3911;
RN [1]
RP PROTEIN SEQUENCE, AND X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS).
RC TISSUE=Seed;
RX PubMed=9257718; DOI=10.1016/s0014-5793(97)00677-7;
RA Osinaga E., Tello D., Batthyany C., Bianchet M., Tavares G., Duran R.,
RA Cervenansky C., Camoin L., Roseto A., Alzari P.M.;
RT "Amino acid sequence and three-dimensional structure of the Tn-specific
RT isolectin B4 from Vicia villosa.";
RL FEBS Lett. 412:190-196(1997).
RN [2]
RP CHARACTERIZATION.
RC TISSUE=Seed;
RX PubMed=6833294; DOI=10.1016/s0021-9258(18)32553-5;
RA Tollefsen S.E., Kornfeld R.;
RT "Isolation and characterization of lectins from Vicia villosa. Two distinct
RT carbohydrate binding activities are present in seed extracts.";
RL J. Biol. Chem. 258:5165-5171(1983).
CC -!- FUNCTION: N-acetyl-D-galactosamine specific lectin. Binds the Tn
CC determinant (GalNAc-alpha-O-Ser/Thr) of the tumor-associated
CC glycopeptide. Could be required for agglutinating cells such as Tn-
CC exposed erythrocytes.
CC -!- SUBUNIT: Homo- or heterotetramer. V.villosa isolectins are composed of
CC either two subunits a and two subunits B (A2B2), four subunits A (A4),
CC or four subunits B (B4). The predominant form, isolectin B4, has no A1
CC erythrocyte agglutinating activity.
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 (By similarity).
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the leguminous lectin family. {ECO:0000305}.
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DR PDB; 1N47; X-ray; 2.70 A; A/B/C/D=2-185.
DR PDBsum; 1N47; -.
DR AlphaFoldDB; P56625; -.
DR SMR; P56625; -.
DR IntAct; P56625; 1.
DR UniLectin; P56625; -.
DR EvolutionaryTrace; P56625; -.
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; 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; Glycoprotein; Lectin;
KW Manganese; Metal-binding.
FT CHAIN 1..>185
FT /note="Lectin B4"
FT /id="PRO_0000105118"
FT BINDING 111
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 113
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 113
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 115
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 117
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 120
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 120
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 125
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT CARBOHYD 48
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 122
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT NON_CONS 47..48
FT /evidence="ECO:0000305"
FT NON_CONS 148..149
FT /evidence="ECO:0000305"
FT NON_CONS 160..161
FT /evidence="ECO:0000305"
FT NON_TER 185
FT STRAND 2..10
FT /evidence="ECO:0007829|PDB:1N47"
FT STRAND 18..22
FT /evidence="ECO:0007829|PDB:1N47"
FT STRAND 32..35
FT /evidence="ECO:0007829|PDB:1N47"
FT STRAND 37..40
FT /evidence="ECO:0007829|PDB:1N47"
FT STRAND 45..47
FT /evidence="ECO:0007829|PDB:1N47"
FT STRAND 54..62
FT /evidence="ECO:0007829|PDB:1N47"
FT STRAND 73..80
FT /evidence="ECO:0007829|PDB:1N47"
FT HELIX 90..92
FT /evidence="ECO:0007829|PDB:1N47"
FT TURN 93..95
FT /evidence="ECO:0007829|PDB:1N47"
FT STRAND 97..100
FT /evidence="ECO:0007829|PDB:1N47"
FT HELIX 103..105
FT /evidence="ECO:0007829|PDB:1N47"
FT STRAND 108..113
FT /evidence="ECO:0007829|PDB:1N47"
FT STRAND 125..134
FT /evidence="ECO:0007829|PDB:1N47"
FT STRAND 136..140
FT /evidence="ECO:0007829|PDB:1N47"
FT STRAND 149..156
FT /evidence="ECO:0007829|PDB:1N47"
FT TURN 157..160
FT /evidence="ECO:0007829|PDB:1N47"
FT STRAND 165..175
FT /evidence="ECO:0007829|PDB:1N47"
SQ SEQUENCE 185 AA; 20328 MW; E375F10559F29A8C CRC64;
SESTSFSFTN FNPNQENLIL QEDALVNSKG TLELTKNGKP VPESLGRNCT TLASFTTSFS
FVMSAPNSLD VADGLAFFLA PPDTQPQKRG GFLGLFKDRK HDISYQSVAV EFDTYSNVWD
PNTTHIGIDT NTIESKKITP FDMVYGEKIL FASLVFPVSQ DILPEYVRVG FSATTGLNEG
VVETH
