ID LEC1_VIGUC Reviewed; 275 AA. AC P05045; Q39666; DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot. DT 15-JUL-1999, sequence version 2. DT 27-MAR-2024, entry version 107. DE RecName: Full=Seed lectin subunit I; DE Short=SL; DE Contains: DE RecName: Full=Seed lectin subunit II; DE Flags: Precursor; OS Vigna unguiculata subsp. cylindrica (Horse gram) (Dolichos biflorus). 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; Vigna. OX NCBI_TaxID=3091605; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=3584113; DOI=10.1016/s0021-9258(18)48226-9; RA Schnell D.J., Etzler M.E.; RT "Primary structure of the Dolichos biflorus seed lectin."; RL J. Biol. Chem. 262:7220-7225(1987). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=2318879; DOI=10.1016/s0021-9258(19)34074-8; RA Harada J.J., Spadoro-Tank J., Maxwell J.C., Schnell D.J., Etzler M.E.; RT "Two lectin genes differentially expressed in Dolichos biflorus differ RT primarily by a 116-base pair sequence in their 5' flanking regions."; RL J. Biol. Chem. 265:4997-5001(1990). RN [3] RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS). RX PubMed=10047489; DOI=10.1006/jmbi.1998.2534; RA Hamelryck T.W., Loris R., Bouckaert J., Dao-Thi M.-H., Strecker G., RA Imberty A., Fernandez E., Wyns L., Etzler M.E.; RT "Carbohydrate binding, quaternary structure and a novel hydrophobic binding RT site in two legume lectin oligomers from Dolichos biflorus."; RL J. Mol. Biol. 286:1161-1177(1999). CC -!- FUNCTION: Metalloglycoprotein, containing Ca, Mg, Mn, and Zn and the CC carbohydrates galactose, glucosamine, mannose, and fucose. It CC agglutinates erythrocytes of blood group A1. Has a high preference for CC GalNAc over Gal. CC -!- SUBUNIT: Homotetramer. CC -!- PTM: Subunit II may arise from subunit I by proteolytic cleavage at the CC C-terminal end. 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 EMBL; J02721; AAA33141.1; -; mRNA. DR EMBL; M34270; AAA33143.1; -; Genomic_DNA. DR PIR; A29572; A29572. DR PDB; 1BJQ; X-ray; 2.65 A; A/B/C/D/E/F/G/H=23-275. DR PDB; 1LU1; X-ray; 2.60 A; A=23-275. DR PDB; 1LU2; X-ray; 2.80 A; A/B=23-275. DR PDBsum; 1BJQ; -. DR PDBsum; 1LU1; -. DR PDBsum; 1LU2; -. DR AlphaFoldDB; P05045; -. DR SMR; P05045; -. DR Allergome; 3011; Dol b Agglutinin. DR UniLectin; P05045; -. DR EvolutionaryTrace; P05045; -. DR GO; GO:0005537; F:mannose 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:SF45; LECTIN; 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; Glycoprotein; Lectin; Mannose-binding; Signal. FT SIGNAL 1..22 FT CHAIN 23..275 FT /note="Seed lectin subunit I" FT /id="PRO_0000017611" FT CHAIN 23..265 FT /note="Seed lectin subunit II" FT /id="PRO_0000017612" FT SITE 265..266 FT /note="Cleavage" FT CARBOHYD 136 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CONFLICT 61..67 FT /note="IPTPSSL -> FPLRFPS (in Ref. 1; AAA33141)" FT /evidence="ECO:0000305" FT CONFLICT 82 FT /note="S -> F (in Ref. 1; AAA33141)" FT /evidence="ECO:0000305" FT CONFLICT 149 FT /note="F -> L (in Ref. 1; AAA33141)" FT /evidence="ECO:0000305" FT CONFLICT 199 FT /note="A -> V (in Ref. 1; AAA33141)" FT /evidence="ECO:0000305" FT CONFLICT 227 FT /note="S -> G (in Ref. 1; AAA33141)" FT /evidence="ECO:0000305" FT CONFLICT 254 FT /note="K -> R (in Ref. 1; AAA33141)" FT /evidence="ECO:0000305" FT CONFLICT 268 FT /note="S -> R (in Ref. 1; AAA33141)" FT /evidence="ECO:0000305" FT STRAND 24..32 FT /evidence="ECO:0007829|PDB:1LU1" FT HELIX 35..37 FT /evidence="ECO:0007829|PDB:1LU1" FT STRAND 38..42 FT /evidence="ECO:0007829|PDB:1LU1" FT STRAND 45..47 FT /evidence="ECO:0007829|PDB:1LU1" FT STRAND 50..52 FT /evidence="ECO:0007829|PDB:1LU1" FT STRAND 67..74 FT /evidence="ECO:0007829|PDB:1LU1" FT TURN 81..84 FT /evidence="ECO:0007829|PDB:1LU1" FT STRAND 88..96 FT /evidence="ECO:0007829|PDB:1LU1" FT STRAND 107..115 FT /evidence="ECO:0007829|PDB:1LU1" FT HELIX 124..126 FT /evidence="ECO:0007829|PDB:1LU1" FT TURN 127..129 FT /evidence="ECO:0007829|PDB:1LU1" FT HELIX 137..139 FT /evidence="ECO:0007829|PDB:1LU1" FT STRAND 142..147 FT /evidence="ECO:0007829|PDB:1LU1" FT TURN 152..154 FT /evidence="ECO:0007829|PDB:1LU1" FT STRAND 160..169 FT /evidence="ECO:0007829|PDB:1LU1" FT STRAND 171..175 FT /evidence="ECO:0007829|PDB:1LU1" FT STRAND 184..191 FT /evidence="ECO:0007829|PDB:1LU1" FT TURN 192..195 FT /evidence="ECO:0007829|PDB:1LU1" FT STRAND 196..202 FT /evidence="ECO:0007829|PDB:1LU1" FT HELIX 204..206 FT /evidence="ECO:0007829|PDB:1LU1" FT STRAND 209..215 FT /evidence="ECO:0007829|PDB:1LU1" FT HELIX 218..221 FT /evidence="ECO:0007829|PDB:1LU1" FT STRAND 224..234 FT /evidence="ECO:0007829|PDB:1LU1" FT STRAND 245..255 FT /evidence="ECO:0007829|PDB:1LU1" FT STRAND 257..259 FT /evidence="ECO:0007829|PDB:1LU1" FT HELIX 266..273 FT /evidence="ECO:0007829|PDB:1LU1" SQ SEQUENCE 275 AA; 29406 MW; D313D73860661A83 CRC64; MASSTVSVVL SLFLLLLTQA NSANIQSFSF KNFNSPSFIL QGDATVSSGK LQLTKVKENG IPTPSSLGRA FYSSPIQIYD KSTGAVASWA TSFTVKISAP SKASFADGIA FALVPVGSEP RRNGGYLGVF DSDVYNNSAQ TVAVEFDTFS NSGWDPSMKH IGIDVNSIKS IATVSWDLAN GENAEILITY NAATSLLVAS LVHPSRRTSY ILSERVDITN ELPEYVSVGF SATTGLSEGY IETHDVLSWS FASKLPDDST AEPLDLASYL VRNVL //