LEC4_GRISI
ID LEC4_GRISI Reviewed; 243 AA.
AC P24146;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 3.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Lectin-4;
DE AltName: Full=GS4;
DE AltName: Full=Lectin IV;
OS Griffonia simplicifolia (Bandeiraea simplicifolia).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Cercidoideae; Cercideae; Cercidinae;
OC Griffonia.
OX NCBI_TaxID=3850;
RN [1]
RP PROTEIN SEQUENCE, AND X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH
RP CARBOHYDRATE; CALCIUM AND MANGANESE IONS.
RX PubMed=8478943; DOI=10.1006/jmbi.1993.1212;
RA Delbaere L.T.J., Vandonselaar M., Prasad L., Quail J.W., Wilson K.S.,
RA Dauter Z.;
RT "Structures of the lectin IV of Griffonia simplicifolia and its complex
RT with the Lewis b human blood group determinant at 2.0-A resolution.";
RL J. Mol. Biol. 230:950-965(1993).
RN [2]
RP PROTEIN SEQUENCE OF 1-62, AND PYROGLUTAMATE FORMATION AT GLN-1.
RC TISSUE=Seed;
RX PubMed=2268264; DOI=10.1042/bj2720343;
RA Nikrad P.V., Pearlstone J.R., Carpenter M.R., Lemieux R.U., Smillie L.B.;
RT "Molecular-mass heterogeneity of Griffonia simplicifolia lectin IV
RT subunits. Differences in the oligosaccharide moieties in the N-terminal
RT region.";
RL Biochem. J. 272:343-350(1990).
CC -!- FUNCTION: Lectin which has a strong affinity for both the Lewis b and y
CC human blood-group determinants. {ECO:0000269|PubMed:8478943}.
CC -!- SUBUNIT: Homodimer of Alpha and Beta forms.
CC {ECO:0000269|PubMed:8478943}.
CC -!- PTM: N-glycosylation of Asn-5 converts form Beta to form Alpha.
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:0000269|PubMed:8478943}.
CC -!- SIMILARITY: Belongs to the leguminous lectin family. {ECO:0000305}.
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DR PIR; S13389; S13389.
DR PDB; 1GSL; X-ray; 2.00 A; A=2-243.
DR PDB; 1LEC; X-ray; 2.00 A; A=2-243.
DR PDB; 1LED; X-ray; 2.00 A; A=2-243.
DR PDBsum; 1GSL; -.
DR PDBsum; 1LEC; -.
DR PDBsum; 1LED; -.
DR AlphaFoldDB; P24146; -.
DR SMR; P24146; -.
DR UniLectin; P24146; -.
DR EvolutionaryTrace; P24146; -.
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; 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; Glycoprotein; Lectin;
KW Manganese; Metal-binding; Pyrrolidone carboxylic acid.
FT CHAIN 1..243
FT /note="Lectin-4"
FT /id="PRO_0000105099"
FT BINDING 129
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000269|PubMed:8478943"
FT BINDING 131
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:8478943"
FT BINDING 131
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000269|PubMed:8478943"
FT BINDING 133
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:8478943"
FT BINDING 135
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:8478943"
FT BINDING 140
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:8478943"
FT BINDING 140
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000269|PubMed:8478943"
FT BINDING 145
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000269|PubMed:8478943"
FT MOD_RES 1
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000269|PubMed:8478943"
FT CARBOHYD 5
FT /note="N-linked (GlcNAc...) asparagine; in alpha chain"
FT CARBOHYD 18
FT /note="N-linked (GlcNAc...) asparagine"
FT STRAND 5..9
FT /evidence="ECO:0007829|PDB:1GSL"
FT STRAND 20..26
FT /evidence="ECO:0007829|PDB:1GSL"
FT STRAND 29..31
FT /evidence="ECO:0007829|PDB:1GSL"
FT STRAND 34..36
FT /evidence="ECO:0007829|PDB:1GSL"
FT STRAND 48..58
FT /evidence="ECO:0007829|PDB:1GSL"
FT STRAND 71..86
FT /evidence="ECO:0007829|PDB:1GSL"
FT STRAND 90..97
FT /evidence="ECO:0007829|PDB:1GSL"
FT HELIX 106..108
FT /evidence="ECO:0007829|PDB:1GSL"
FT TURN 109..111
FT /evidence="ECO:0007829|PDB:1GSL"
FT TURN 114..118
FT /evidence="ECO:0007829|PDB:1GSL"
FT HELIX 120..122
FT /evidence="ECO:0007829|PDB:1GSL"
FT STRAND 126..131
FT /evidence="ECO:0007829|PDB:1GSL"
FT HELIX 136..138
FT /evidence="ECO:0007829|PDB:1GSL"
FT STRAND 145..154
FT /evidence="ECO:0007829|PDB:1GSL"
FT STRAND 156..160
FT /evidence="ECO:0007829|PDB:1GSL"
FT HELIX 163..166
FT /evidence="ECO:0007829|PDB:1GSL"
FT STRAND 171..179
FT /evidence="ECO:0007829|PDB:1GSL"
FT TURN 180..183
FT /evidence="ECO:0007829|PDB:1GSL"
FT STRAND 184..191
FT /evidence="ECO:0007829|PDB:1GSL"
FT STRAND 196..202
FT /evidence="ECO:0007829|PDB:1GSL"
FT HELIX 205..208
FT /evidence="ECO:0007829|PDB:1GSL"
FT STRAND 211..221
FT /evidence="ECO:0007829|PDB:1GSL"
FT STRAND 223..237
FT /evidence="ECO:0007829|PDB:1GSL"
FT TURN 239..242
FT /evidence="ECO:0007829|PDB:1LED"
SQ SEQUENCE 243 AA; 26810 MW; CFEC0FA389BBBF25 CRC64;
QNTVNFTYPD FWSYSLKNGT EITFLGDATR IPGALQLTKT DANGNPVRSS AGQASYSEPV
FLWDSTGKAA SFYTSFTFLL KNYGAPTADG LAFFLAPVDS SVKDYGGFLG LFRHETAADP
SKNQVVAVEF DTWINKDWND PPYPHIGIDV NSIVSVATTR WENDDAYGSS IATAHITYDA
RSKILTVLLS YEHGRDYILS HVVDLAKVLP QKVRIGFSAG VGYDEVTYIL SWHFFSTLDG
TNK
