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 27-MAR-2024, entry version 119. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 Gene3D; 2.60.120.200; -; 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 PANTHER; PTHR32401; CONCANAVALIN A-LIKE LECTIN FAMILY PROTEIN; 1. DR PANTHER; PTHR32401:SF21; OS09G0335200 PROTEIN; 1. DR Pfam; PF00139; Lectin_legB; 1. DR PIRSF; PIRSF002690; L-type_lectin_plant; 1. DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 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 //